A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
A phenothiazine with actions similar to CHLORPROMAZINE. It is used as an antipsychotic and an antiemetic.
Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.
A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A group of compounds that contain the structure SO2NH2.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The rate dynamics in chemical or physical systems.
A chelating agent relatively more specific for calcium and less toxic than EDETIC ACID.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
Nucleoside-2',3'-cyclic phosphate nucleotidohydrolase. Enzymes that catalyze the hydrolysis of the 2'- or 3'- phosphate bonds of 2',3'-cyclic nucleotides. Also hydrolyzes nucleoside monophosphates. Includes EC 3.1.4.16 and EC 3.1.4.37. EC 3.1.4.-.
The prototypical phenothiazine antipsychotic drug. Like the other drugs in this class chlorpromazine's antipsychotic actions are thought to be due to long-term adaptation by the brain to blocking DOPAMINE RECEPTORS. Chlorpromazine has several other actions and therapeutic uses, including as an antiemetic and in the treatment of intractable hiccup.
Cation-transporting proteins that utilize the energy of ATP hydrolysis for the transport of CALCIUM. They differ from CALCIUM CHANNELS which allow calcium to pass through a membrane without the use of energy.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Enzymes that catalyze the hydrolysis of CYCLIC AMP to form adenosine 5'-phosphate. The enzymes are widely distributed in animal tissue and control the level of intracellular cyclic AMP. Many specific enzymes classified under this heading demonstrate additional spcificity for 3',5'-cyclic IMP and CYCLIC GMP.
A BRAIN-specific substrate for PROTEIN KINASE C that binds CALMODULIN and is involved in regulation of CALCIUM SIGNALING.
Terpenes of five units of HEMITERPENES, formed from geranylfarnesyl pyrophosphate.
Basic polypeptide from the venom of the honey bee (Apis mellifera). It contains 26 amino acids, has cytolytic properties, causes contracture of muscle, releases histamine, and disrupts surface tension, probably due to lysis of cell and mitochondrial membranes.
A CALCIUM and CALMODULIN-dependent cyclic nucleotide phosphodiesterase subfamily. The three members of this family are referred to as type 1A, type 1B, and type 1C and are each product of a distinct gene. In addition, multiple enzyme variants of each subtype can be produced due to multiple alternative mRNA splicing. Although the type 1 enzymes are classified as 3',5'-cyclic-AMP phosphodiesterases (EC 3.1.4.17), some members of this class have additional specificity for CYCLIC GMP.
A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.
A monomeric calcium-calmodulin-dependent protein kinase subtype that is expressed in a broad variety of mammalian cell types. Its expression is regulated by the action of CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. Several isoforms of this enzyme subtype are encoded by distinct genes.
Compounds containing dibenzo-1,4-thiazine. Some of them are neuroactive.
A genus of ciliate protozoa that is often large enough to be seen by the naked eye. Paramecia are commonly used in genetic, cytological, and other research.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Calcium-binding motifs composed of two helices (E and F) joined by a loop. Calcium is bound by the loop region. These motifs are found in many proteins that are regulated by calcium.
A drug formerly used in the treatment of angina pectoris but superseded by less hazardous drugs. Prenylamine depletes myocardial catecholamine stores and has some calcium channel blocking activity. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1406)
Venoms produced by the wasp (Vespid) family of stinging insects, including hornets; the venoms contain enzymes, biogenic amines, histamine releasing factors, kinins, toxic polypeptides, etc., and are similar to bee venoms.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
An enzyme that catalyzes the conversion of ATP and PHOSPHORYLASE B to ADP and PHOSPHORYLASE A.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.
A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.
'Gizzard', in a medical context, is a term rarely used but can refer to the muscular stomach of a bird, responsible for grinding and macerating food with the aid of ingested pebbles or grit.
One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Measurement of the intensity and quality of fluorescence.
Toluenes in which one hydrogen of the methyl group is substituted by an amino group. Permitted are any substituents on the benzene ring or the amino group.
A phenothiazine used in the treatment of PSYCHOSES. Its properties and uses are generally similar to those of CHLORPROMAZINE.
The sum of the weight of all the atoms in a molecule.
One of the three polypeptide chains that make up the TROPONIN complex of skeletal muscle. It is a calcium-binding protein.
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Proteins prepared by recombinant DNA technology.
A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in their tails and therefore do not dimerize.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Venoms obtained from Apis mellifera (honey bee) and related species. They contain various enzymes, polypeptide toxins, and other substances, some of which are allergenic or immunogenic or both. These venoms were formerly used in rheumatism to stimulate the pituitary-adrenal system.
The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

AMP-activated protein kinase phosphorylation of endothelial NO synthase. (1/4572)

The AMP-activated protein kinase (AMPK) in rat skeletal and cardiac muscle is activated by vigorous exercise and ischaemic stress. Under these conditions AMPK phosphorylates and inhibits acetyl-coenzyme A carboxylase causing increased oxidation of fatty acids. Here we show that AMPK co-immunoprecipitates with cardiac endothelial NO synthase (eNOS) and phosphorylates Ser-1177 in the presence of Ca2+-calmodulin (CaM) to activate eNOS both in vitro and during ischaemia in rat hearts. In the absence of Ca2+-calmodulin, AMPK also phosphorylates eNOS at Thr-495 in the CaM-binding sequence, resulting in inhibition of eNOS activity but Thr-495 phosphorylation is unchanged during ischaemia. Phosphorylation of eNOS by the AMPK in endothelial cells and myocytes provides a further regulatory link between metabolic stress and cardiovascular function.  (+info)

Calmodulin mediates calcium-dependent activation of the intermediate conductance KCa channel, IKCa1. (2/4572)

Small and intermediate conductance Ca2+-activated K+ channels play a crucial role in hyperpolarizing the membrane potential of excitable and nonexcitable cells. These channels are exquisitely sensitive to cytoplasmic Ca2+, yet their protein-coding regions do not contain consensus Ca2+-binding motifs. We investigated the involvement of an accessory protein in the Ca2+-dependent gating of hIKCa1, a human intermediate conductance channel expressed in peripheral tissues. Cal- modulin was found to interact strongly with the cytoplasmic carboxyl (C)-tail of hIKCa1 in a yeast two-hybrid system. Deletion analyses defined a requirement for the first 62 amino acids of the C-tail, and the binding of calmodulin to this region did not require Ca2+. The C-tail of hSKCa3, a human neuronal small conductance channel, also bound calmodulin, whereas that of a voltage-gated K+ channel, mKv1.3, did not. Calmodulin co-precipitated with the channel in cell lines transfected with hIKCa1, but not with mKv1. 3-transfected lines. A mutant calmodulin, defective in Ca2+ sensing but retaining binding to the channel, dramatically reduced current amplitudes when co-expressed with hIKCa1 in mammalian cells. Co-expression with varying amounts of wild-type and mutant calmodulin resulted in a dominant-negative suppression of current, consistent with four calmodulin molecules being associated with the channel. Taken together, our results suggest that Ca2+-calmodulin-induced conformational changes in all four subunits are necessary for the channel to open.  (+info)

Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90. A possible regulatory role in molecular clustering at synaptic sites. (3/4572)

NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase family protein, is known to bind to C-terminal ends of N-methyl-D-aspartate receptor 2B (NR2B) through its PDZ (PSD-95/Dlg/ZO-1) domains. NE-dlg/SAP102 and NR2B colocalize at synaptic sites in cultured rat hippocampal neurons, and their expressions increase in parallel with the onset of synaptogenesis. We have identified that NE-dlg/SAP102 interacts with calmodulin in a Ca2+-dependent manner. The binding site for calmodulin has been determined to lie at the putative basic alpha-helix region located around the src homology 3 (SH3) domain of NE-dlg/SAP102. Using a surface plasmon resonance measurement system, we detected specific binding of recombinant NE-dlg/SAP102 to the immobilized calmodulin with a Kd value of 44 nM. However, the binding of Ca2+/calmodulin to NE-dlg/SAP102 did not modulate the interaction between PDZ domains of NE-dlg/SAP102 and the C-terminal end of rat NR2B. We have also identified that the region near the calmodulin binding site of NE-dlg/SAP102 interacts with the GUK-like domain of PSD-95/SAP90 by two-hybrid screening. Pull down assay revealed that NE-dlg/SAP102 can interact with PSD-95/SAP90 in the presence of both Ca2+ and calmodulin. These findings suggest that the Ca2+/calmodulin modulates interaction of neuronal membrane-associated guanylate kinase proteins and regulates clustering of neurotransmitter receptors at central synapses.  (+info)

Properties of filament-bound myosin light chain kinase. (4/4572)

Myosin light chain kinase binds to actin-containing filaments from cells with a greater affinity than to F-actin. However, it is not known if this binding in cells is regulated by Ca2+/calmodulin as it is with F-actin. Therefore, the binding properties of the kinase to stress fibers were examined in smooth muscle-derived A7r5 cells. Full-length myosin light chain kinase or a truncation mutant lacking residues 2-142 was expressed as chimeras containing green fluorescent protein at the C terminus. In intact cells, the full-length kinase bound to stress fibers, whereas the truncated kinase showed diffuse fluorescence in the cytoplasm. After permeabilization with saponin, the fluorescence from the truncated kinase disappeared, whereas the fluorescence of the full-length kinase was retained on stress fibers. Measurements of fluorescence intensities and fluorescence recovery after photobleaching of the full-length myosin light chain kinase in saponin-permeable cells showed that Ca2+/calmodulin did not dissociate the kinase from these filaments. However, the filament-bound kinase was sufficient for Ca2+-dependent phosphorylation of myosin regulatory light chain and contraction of stress fibers. Thus, dissociation of myosin light chain kinase from actin-containing thin filaments is not necessary for phosphorylation of myosin light chain in thick filaments. We note that the distance between the N terminus and the catalytic core of the kinase is sufficient to span the distance between thin and thick filaments.  (+info)

cAMP inhibits translation by inducing Ca2+/calmodulin-independent elongation factor 2 kinase activity in IPC-81 cells. (5/4572)

Treatment of IPC-81 cells led to inhibition of protein synthesis, which was accompanied by an increase in the average size of polysomes and a decreased rate of elongation, indicating that it involved inhibition of peptide chain elongation. This inhibition was also associated with increased phosphorylation of elongation factor eEF2 (which inhibits its activity) and enhanced Ca2+/calmodulin-independent activity of eEF2 kinase. Previous work has shown that phosphorylation of eEF2 kinase by cAMP-dependent protein kinase (cAPK) in vitro induces such activator-independent activity, and the present data show that such a mechanism can occur in intact cells to link physiological levels of cAPK activation with inhibition of protein synthesis.  (+info)

T-cell stimulation through the T-cell receptor/CD3 complex regulates CD2 lateral mobility by a calcium/calmodulin-dependent mechanism. (6/4572)

T lymphocyte activation through the T cell receptor (TCR)/CD3 complex alters the avidity of the cell surface adhesion receptor CD2 for its ligand CD58. Based on the observations that activation-associated increases in intracellular [Ca2+] ([Ca2+]i) strengthen interactions between T cells and antigen-presenting cells, and that the lateral mobility of cell surface adhesion receptors is an important regulator of cellular adhesion strength, we postulated that [Ca2+]i controls CD2 lateral mobility at the T cell surface. Human Jurkat T leukemia cells were stimulated by antibody-mediated cross-linking of the TCR/CD3 complex. CD2 was labeled with a fluorescently conjugated monoclonal antibody. Quantitative fluorescence microscopy techniques were used to measure [Ca2+]i and CD2 lateral mobility. Cross-linking of the TCR/CD3 complex caused an immediate increase in [Ca2+]i and, 10-20 min later, a decrease in the fractional mobility of CD2 from the control value of 68 +/- 1% to 45 +/- 2% (mean +/- SEM). One to two hours after cell stimulation the fractional mobility spontaneously returned to the control level. Under these and other treatment conditions, the fraction of cells with significantly elevated [Ca2+]i was highly correlated with the fraction of cells manifesting significantly reduced CD2 mobility. Pretreatment of cells with a calmodulin inhibitor or a calmodulin-dependent kinase inhibitor prevented Ca2+-mediated CD2 immobilization, and pretreatment of cells with a calcineurin phosphatase inhibitor prevented the spontaneous reversal of CD2 immobilization. These data suggest that T cell activation through the TCR/CD3 complex controls CD2 lateral mobility by a Ca2+/calmodulin-dependent mechanism, and that this mechanism may involve regulated phosphorylation and dephosphorylation of CD2 or a closely associated protein.  (+info)

Suramin and suramin analogs activate skeletal muscle ryanodine receptor via a calmodulin binding site. (7/4572)

Contraction of skeletal muscle is triggered by the rapid release of Ca2+ from the sarcoplasmic reticulum via the ryanodine receptor/calcium-release channel. The trypanocidal drug suramin is an efficient activator of the ryanodine receptor. Here, we used high-affinity [3H]ryanodine binding to sarcoplasmic reticulum from rabbit skeletal muscle to screen for more potent analogs of suramin. This approach resulted in the identification of NF307, which accelerates the association rate of [3H]ryanodine binding with an EC50 = 91 +/- 7 microM at 0.19 microM calculated free Ca2+. In single-channel recordings with the purified ryanodine receptor, NF307 increased mean open probability at 0.6 microM Ca2+ from 0.020 +/- 0.006 to 0.53 +/- 0.07 with no effect on current amplitude and unitary conductance. Like caffeine, NF307 exerts a very pronounced Ca2+-sensitizing effect (EC50 of Ca2+ shifted approximately 10-fold by saturating NF307 concentrations). Conversely, increasing concentrations of free Ca2+ sensitized the receptor for NF307 (EC50 = 14.6 +/- 3.5 microM at 0.82 microM estimated free Ca2+). The effects of NF307 and caffeine on [3H]ryanodine binding were additive, irrespective of the Ca2+ concentration. In contrast, the effects of calmodulin, which activates and inhibits the ryanodine receptor in the absence and presence of Ca2+, respectively, and of NF307 were mutually antagonistic. If the purified ryanodine receptor was prebound to a calmodulin-Sepharose matrix, 100 microM NF307 and 300 microM suramin eluted the purified ryanodine receptor to an extent that was comparable to the effect of 10 microM calmodulin. We conclude that NF307 and suramin interact directly with a calmodulin binding domain of the ryanodine receptor. Because of its potent calcium-sensitizing effect, NF307 may represent a lead compound in the search of synthetic ryanodine receptor ligands.  (+info)

Dynamic and quantitative Ca2+ measurements using improved cameleons. (8/4572)

Cameleons are genetically-encoded fluorescent indicators for Ca2+ based on green fluorescent protein variants and calmodulin (CaM). Because cameleons can be targeted genetically and imaged by one- or two-photon excitation microscopy, they offer great promise for monitoring Ca2+ in whole organisms, tissues, organelles, and submicroscopic environments in which measurements were previously impossible. However, the original cameleons suffered from significant pH interference, and their Ca2+-buffering and cross-reactivity with endogenous CaM signaling pathways was uncharacterized. We have now greatly reduced the pH-sensitivity of the cameleons by introducing mutations V68L and Q69K into the acceptor yellow green fluorescent protein. The resulting new cameleons permit Ca2+ measurements despite significant cytosolic acidification. When Ca2+ is elevated, the CaM and CaM-binding peptide fused together in a cameleon predominantly interact with each other rather than with free CaM and CaM-dependent enzymes. Therefore, if cameleons are overexpressed, the primary effect is likely to be the unavoidable increase in Ca2+ buffering rather than specific perturbation of CaM-dependent signaling.  (+info)

Calmodulin is a small, ubiquitous calcium-binding protein that plays a critical role in various intracellular signaling pathways. It functions as a calcium sensor, binding to and regulating the activity of numerous target proteins upon calcium ion (Ca^2+^) binding. Calmodulin is expressed in all eukaryotic cells and participates in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, metabolism, and cell cycle progression.

The protein contains four EF-hand motifs that can bind Ca^2+^ ions. Upon calcium binding, conformational changes occur in the calmodulin structure, exposing hydrophobic surfaces that facilitate its interaction with target proteins. Calmodulin's targets include enzymes (such as protein kinases and phosphatases), ion channels, transporters, and cytoskeletal components. By modulating the activity of these proteins, calmodulin helps regulate essential cellular functions in response to changes in intracellular Ca^2+^ concentrations.

Calmodulin's molecular weight is approximately 17 kDa, and it consists of a single polypeptide chain with 148-150 amino acid residues. The protein can be found in both the cytoplasm and the nucleus of cells. In addition to its role as a calcium sensor, calmodulin has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and cardiovascular disorders.

Trifluoperazine is an antipsychotic medication that belongs to the class of drugs called phenothiazines. It works by blocking the action of dopamine, a neurotransmitter in the brain, and helps to reduce symptoms of schizophrenia such as hallucinations, delusions, paranoia, and disordered thought. Trifluoperazine may also be used to manage anxiety or agitation in certain medical conditions. It is available in the form of tablets for oral administration. As with any medication, trifluoperazine should be taken under the supervision of a healthcare provider due to potential side effects and risks associated with its use.

Calmodulin-binding proteins are a diverse group of proteins that have the ability to bind to calmodulin, a ubiquitous calcium-binding protein found in eukaryotic cells. Calmodulin plays a critical role in various cellular processes by regulating the activity of its target proteins in a calcium-dependent manner.

Calmodulin-binding proteins contain specific domains or motifs that enable them to interact with calmodulin. These domains can be classified into two main categories: IQ motifs and CaM motifs. The IQ motif is a short amino acid sequence that contains the consensus sequence IQXXXRGXXR, where X represents any amino acid. This motif binds to the C-lobe of calmodulin in a calcium-dependent manner. On the other hand, CaM motifs are longer sequences that can bind to both lobes of calmodulin with high affinity and in a calcium-dependent manner.

Calmodulin-binding proteins play crucial roles in various cellular functions, including signal transduction, gene regulation, cytoskeleton organization, and ion channel regulation. For example, calmodulin-binding proteins such as calcineurin and CaM kinases are involved in the regulation of immune responses, learning, and memory. Similarly, myosin regulatory light chains, which contain IQ motifs, play a critical role in muscle contraction by regulating the interaction between actin and myosin filaments.

In summary, calmodulin-binding proteins are a diverse group of proteins that interact with calmodulin to regulate various cellular processes. They contain specific domains or motifs that enable them to bind to calmodulin in a calcium-dependent manner, thereby modulating the activity of their target proteins.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

Calcium-binding proteins (CaBPs) are a diverse group of proteins that have the ability to bind calcium ions (Ca^2+^) with high affinity and specificity. They play crucial roles in various cellular processes, including signal transduction, muscle contraction, neurotransmitter release, and protection against oxidative stress.

The binding of calcium ions to these proteins induces conformational changes that can either activate or inhibit their functions. Some well-known CaBPs include calmodulin, troponin C, S100 proteins, and parvalbumins. These proteins are essential for maintaining calcium homeostasis within cells and for mediating the effects of calcium as a second messenger in various cellular signaling pathways.

Myosin-Light-Chain Kinase (MLCK) is an enzyme that plays a crucial role in muscle contraction. It phosphorylates the regulatory light chains of myosin, a protein involved in muscle contraction, leading to the activation of myosin and the initiation of the contractile process. MLCK is activated by calcium ions and calmodulin, and its activity is essential for various cellular processes, including cytokinesis, cell motility, and maintenance of cell shape. In addition to its role in muscle contraction, MLCK has been implicated in several pathological conditions, such as hypertension, atherosclerosis, and cancer.

Calcium-calmodulin-dependent protein kinase type 2 (CAMK2) is a type of serine/threonine protein kinase that plays a crucial role in signal transduction pathways related to synaptic plasticity, learning, and memory. It is composed of four subunits, each with a catalytic domain and a regulatory domain that contains an autoinhibitory region and a calmodulin-binding site.

The activation of CAMK2 requires the binding of calcium ions (Ca^2+^) to calmodulin, which then binds to the regulatory domain of CAMK2, relieving the autoinhibition and allowing the kinase to phosphorylate its substrates. Once activated, CAMK2 can also undergo a process called autophosphorylation, which results in a persistent activation state that can last for hours or even days.

CAMK2 has many downstream targets, including ion channels, transcription factors, and other protein kinases. Dysregulation of CAMK2 signaling has been implicated in various neurological disorders, such as Alzheimer's disease, Parkinson's disease, and epilepsy.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Sulfonamides are a group of synthetic antibacterial drugs that contain the sulfonamide group (SO2NH2) in their chemical structure. They are bacteriostatic agents, meaning they inhibit bacterial growth rather than killing them outright. Sulfonamides work by preventing the bacteria from synthesizing folic acid, which is essential for their survival.

The first sulfonamide drug was introduced in the 1930s and since then, many different sulfonamides have been developed with varying chemical structures and pharmacological properties. They are used to treat a wide range of bacterial infections, including urinary tract infections, respiratory tract infections, skin and soft tissue infections, and ear infections.

Some common sulfonamide drugs include sulfisoxazole, sulfamethoxazole, and trimethoprim-sulfamethoxazole (a combination of a sulfonamide and another antibiotic called trimethoprim). While sulfonamides are generally safe and effective when used as directed, they can cause side effects such as rash, nausea, and allergic reactions. It is important to follow the prescribing physician's instructions carefully and to report any unusual symptoms or side effects promptly.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

I apologize, but I am not able to provide a medical definition for "Egtazic Acid" because it is not a term that is recognized in the field of medicine or pharmacology. It is possible that you may have meant "Egтарic Acid," which also does not have a specific medical meaning, or "Ethylene Glycol Tetraacetic Acid (EGTA)," which is a chemical compound used in research and medicine for its ability to bind calcium ions. If you have any other questions, I would be happy to try to help answer them.

Calcium-calmodulin-dependent protein kinases (CAMKs) are a family of enzymes that play a crucial role in intracellular signaling pathways. They are activated by the binding of calcium ions and calmodulin, a ubiquitous calcium-binding protein, to their regulatory domain.

Once activated, CAMKs phosphorylate specific serine or threonine residues on target proteins, thereby modulating their activity, localization, or stability. This post-translational modification is essential for various cellular processes, including synaptic plasticity, gene expression, metabolism, and cell cycle regulation.

There are several subfamilies of CAMKs, including CaMKI, CaMKII, CaMKIII (also known as CaMKIV), and CaMK kinase (CaMKK). Each subfamily has distinct structural features, substrate specificity, and regulatory mechanisms. Dysregulation of CAMK signaling has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and cardiovascular disorders.

2,3'-Cyclic-nucleotide phosphodiesterases (PDEs) are a subclass of enzymes that belong to the family of phosphodiesterases. These enzymes are responsible for the hydrolysis of 2,3'-cyclic nucleotides, which are cyclic forms of nucleotides that act as second messengers in various cellular signaling pathways.

The two primary types of 2,3'-cyclic nucleotides are 2',3'-cGMP and 2',3'-cAMP, which are produced by the action of certain enzymes on their respective precursors, guanosine triphosphate (GTP) and adenosine triphosphate (ATP). These cyclic nucleotides play important roles in regulating various cellular processes, including metabolism, gene expression, and ion channel activity.

2,3'-Cyclic-nucleotide phosphodiesterases catalyze the hydrolysis of these cyclic nucleotides to their corresponding 5'-monophosphates, thereby terminating their signaling activity. There are several isoforms of 2,3'-cyclic-nucleotide PDEs that have been identified, each with distinct substrate specificities and regulatory properties.

Dysregulation of 2,3'-cyclic-nucleotide PDE activity has been implicated in various diseases, including cancer, cardiovascular disease, and neurological disorders. Therefore, these enzymes have emerged as important targets for the development of therapeutic agents that can modulate their activity and restore normal cellular function.

Chlorpromazine is a type of antipsychotic medication, also known as a phenothiazine. It works by blocking dopamine receptors in the brain, which helps to reduce the symptoms of psychosis such as hallucinations, delusions, and disordered thinking. Chlorpromazine is used to treat various mental health conditions including schizophrenia, bipolar disorder, and severe behavioral problems in children. It may also be used for the short-term management of severe anxiety or agitation, and to control nausea and vomiting.

Like all medications, chlorpromazine can have side effects, which can include drowsiness, dry mouth, blurred vision, constipation, weight gain, and sexual dysfunction. More serious side effects may include neurological symptoms such as tremors, rigidity, or abnormal movements, as well as cardiovascular problems such as low blood pressure or irregular heart rhythms. It is important for patients to be monitored closely by their healthcare provider while taking chlorpromazine, and to report any unusual symptoms or side effects promptly.

Calcium-transporting ATPases, also known as calcium pumps, are a type of enzyme that use the energy from ATP (adenosine triphosphate) hydrolysis to transport calcium ions across membranes against their concentration gradient. This process helps maintain low intracellular calcium concentrations and is essential for various cellular functions, including muscle contraction, neurotransmitter release, and gene expression.

There are two main types of calcium-transporting ATPases: the sarcoplasmic/endoplasmic reticulum Ca^2+^-ATPase (SERCA) and the plasma membrane Ca^2+^-ATPase (PMCA). SERCA is found in the sarcoplasmic reticulum of muscle cells and endoplasmic reticulum of other cell types, where it pumps calcium ions into these organelles to initiate muscle relaxation or signal transduction. PMCA, on the other hand, is located in the plasma membrane and extrudes calcium ions from the cell to maintain low cytosolic calcium concentrations.

Calcium-transporting ATPases play a crucial role in maintaining calcium homeostasis in cells and are important targets for drug development in various diseases, including heart failure, hypertension, and neurological disorders.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

3',5'-Cyclic-AMP (cyclic adenosine monophosphate) phosphodiesterases are a group of enzymes that catalyze the breakdown of cyclic AMP to 5'-AMP. These enzymes play a crucial role in regulating the levels of intracellular second messengers, such as cyclic AMP, which are involved in various cellular signaling pathways.

There are several subtypes of phosphodiesterases (PDEs) that specifically target cyclic AMP, including PDE1, PDE2, PDE3, PDE4, PDE7, PDE8, and PDE10. Each subtype has distinct regulatory and catalytic properties, allowing for specific regulation of cyclic AMP levels in different cellular compartments and signaling pathways.

Inhibition of these enzymes can lead to an increase in intracellular cyclic AMP levels, which can have therapeutic effects in various diseases, such as cardiovascular disease, pulmonary hypertension, and central nervous system disorders. Therefore, PDE inhibitors are a valuable class of drugs for the treatment of these conditions.

Neurogranin is a protein that is primarily found in the postsynaptic density of excitatory neurons in the brain. It is a calmodulin-binding protein and plays a significant role in synaptic plasticity, which is the ability of synapses to strengthen or weaken over time, in response to increases or decreases in their activity. Neurogranin has been identified as a potential biomarker for Alzheimer's disease and other neurodegenerative disorders due to its susceptibility to proteolytic cleavage by enzymes such as caspases, which are activated during apoptosis or programmed cell death. Increased levels of neurogranin fragments in cerebrospinal fluid have been associated with cognitive decline and neurodegeneration in Alzheimer's disease.

Sesterterpenes are a class of naturally occurring compounds derived from five units of isoprene, consisting of 25 carbon atoms. They are characterized by a unique carbon skeleton and can be found in various plants, fungi, and marine organisms. Some sesterterpenes have been identified to possess biological activities, such as antimicrobial, cytotoxic, and anti-inflammatory properties. However, they are not widely studied or used in medical contexts compared to other classes of terpenes.

I'm sorry for any confusion, but the term "Melitten" does not appear to be a recognized medical term or condition. It is possible that there may be a spelling mistake or typo in the term you are looking for. Please double-check the spelling and try again, or provide more context so I can try to help you find the information you're looking for.

Cyclic nucleotide phosphodiesterases (PDEs) are a family of enzymes that regulate intracellular levels of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP), which are important second messengers involved in various cellular processes.

Type 1 PDEs (PDE1A, PDE1B, PDE1C) are calcium/calmodulin-regulated enzymes that hydrolyze both cAMP and cGMP with similar catalytic efficiency. They play a crucial role in the regulation of vascular smooth muscle contraction, platelet aggregation, and neuronal excitability.

Dysregulation of PDE1 activity has been implicated in various pathological conditions, including hypertension, cardiovascular diseases, and neurological disorders. Therefore, PDE1 inhibitors have emerged as potential therapeutic agents for the treatment of these conditions.

Calcineurin is a calcium-calmodulin-activated serine/threonine protein phosphatase that plays a crucial role in signal transduction pathways involved in immune response and neuronal development. It consists of two subunits: the catalytic A subunit (calcineurin A) and the regulatory B subunit (calcineurin B). Calcineurin is responsible for dephosphorylating various substrates, including transcription factors, which leads to changes in their activity and ultimately affects gene expression. In the immune system, calcineurin plays a critical role in T-cell activation by dephosphorylating the nuclear factor of activated T-cells (NFAT), allowing it to translocate into the nucleus and induce the expression of cytokines and other genes involved in the immune response. Inhibitors of calcineurin, such as cyclosporine A and tacrolimus, are commonly used as immunosuppressive drugs to prevent organ rejection after transplantation.

Calcium-calmodulin-dependent protein kinase type 1 (CAMK1) is a type of serine/threonine protein kinase that plays a crucial role in signal transduction pathways involved in various cellular processes, including synaptic plasticity, learning, and memory. It is activated by the binding of calcium ions (Ca2+) and calmodulin, a ubiquitous calcium-binding protein, to its regulatory domain.

Once activated, CAMK1 phosphorylates various downstream target proteins, leading to changes in their activity or function. In the brain, CAMK1 is primarily expressed in neurons and has been implicated in the regulation of synaptic strength and transmission, as well as in the modulation of gene expression and cell survival. Dysregulation of CAMK1 has been associated with several neurological disorders, including Alzheimer's disease, Parkinson's disease, and epilepsy.

Phenothiazines are a class of heterocyclic organic compounds that contain a phenothiazine nucleus, which consists of a pair of benzene rings fused to a thiazine ring. They have been widely used in medicine as antipsychotic drugs for the treatment of various mental disorders such as schizophrenia and bipolar disorder.

Phenothiazines work by blocking dopamine receptors in the brain, which helps to reduce the symptoms of psychosis such as hallucinations, delusions, and disordered thinking. They also have sedative and antiemetic (anti-nausea) effects. However, they can cause a range of side effects including extrapyramidal symptoms (involuntary muscle movements), tardive dyskinesia (irreversible movement disorder), and neuroleptic malignant syndrome (a rare but potentially fatal reaction to antipsychotic drugs).

Examples of phenothiazine drugs include chlorpromazine, thioridazine, and promethazine. While they have been largely replaced by newer atypical antipsychotics, phenothiazines are still used in some cases due to their lower cost and effectiveness in treating certain symptoms.

I'm sorry for any confusion, but "Paramecium" is not a medical term. It is a genus of unicellular organisms commonly found in freshwater environments. Paramecia are classified as ciliates due to the presence of hair-like structures called cilia on their surface. They use these cilia for locomotion and feeding. If you have any questions about biology or another topic, I'd be happy to try to help!

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

"EF hand motifs" are structural domains found in proteins that bind calcium ions. The name "EF hand" comes from the initials of the parvalbumin protein, where these structures were first identified, and the shape of the domain, which resembles the capital letters 'E' and 'F' lying on their sides when viewed in a certain orientation.

Each EF hand motif is composed of a helix-loop-helix structure, with the calcium-binding site located in the loop region. When calcium binds to the EF hand, it causes a conformational change in the protein, which can then activate or inhibit various cellular processes.

EF hand motifs are found in many different types of proteins, including calmodulin, troponin C, and S100 proteins. They play important roles in calcium signaling pathways, muscle contraction, and other physiological processes.

Prenylamine is not a medical term in and of itself, but it is the chemical name for a medication that is sometimes used in the medical field. The drug is known as Phenelzine sulfate in its brand name form, with trade names including Nardil.

Phenelzine sulfate (Prenylamine) is a type of medication called a monoamine oxidase inhibitor (MAOI). It works by blocking the action of an enzyme called monoamine oxidase, which helps break down certain chemicals in the brain called neurotransmitters. By blocking this enzyme's action, phenelzine sulfate increases the levels of these neurotransmitters in the brain, which can help to improve mood and alleviate symptoms of depression.

Phenelzine sulfate is used primarily to treat depression that has not responded to other treatments. It may also be used off-label for other conditions, such as anxiety disorders or panic attacks. However, it is important to note that phenelzine sulfate can have serious side effects and interactions with certain foods and medications, so it should only be taken under the close supervision of a healthcare provider.

Wasp venoms are complex mixtures of bioactive molecules produced by wasps (Hymenoptera: Vespidae) to defend themselves and paralyze prey. The main components include:

1. Phospholipases A2 (PLA2): Enzymes that can cause pain, inflammation, and damage to cell membranes.
2. Hyaluronidase: An enzyme that helps spread the venom by breaking down connective tissues.
3. Proteases: Enzymes that break down proteins and contribute to tissue damage and inflammation.
4. Antigen 5: A major allergen that can cause severe allergic reactions (anaphylaxis) in sensitive individuals.
5. Mastoparan: A peptide that induces histamine release, leading to localized inflammation and pain.
6. Neurotoxins: Some wasp venoms contain neurotoxins that can cause paralysis or neurological symptoms.

The composition of wasp venoms may vary among species, and individual sensitivity to the components can result in different reactions ranging from localized pain, swelling, and redness to systemic allergic responses.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

The brain is the central organ of the nervous system, responsible for receiving and processing sensory information, regulating vital functions, and controlling behavior, movement, and cognition. It is divided into several distinct regions, each with specific functions:

1. Cerebrum: The largest part of the brain, responsible for higher cognitive functions such as thinking, learning, memory, language, and perception. It is divided into two hemispheres, each controlling the opposite side of the body.
2. Cerebellum: Located at the back of the brain, it is responsible for coordinating muscle movements, maintaining balance, and fine-tuning motor skills.
3. Brainstem: Connects the cerebrum and cerebellum to the spinal cord, controlling vital functions such as breathing, heart rate, and blood pressure. It also serves as a relay center for sensory information and motor commands between the brain and the rest of the body.
4. Diencephalon: A region that includes the thalamus (a major sensory relay station) and hypothalamus (regulates hormones, temperature, hunger, thirst, and sleep).
5. Limbic system: A group of structures involved in emotional processing, memory formation, and motivation, including the hippocampus, amygdala, and cingulate gyrus.

The brain is composed of billions of interconnected neurons that communicate through electrical and chemical signals. It is protected by the skull and surrounded by three layers of membranes called meninges, as well as cerebrospinal fluid that provides cushioning and nutrients.

Protein kinases are a group of enzymes that play a crucial role in many cellular processes by adding phosphate groups to other proteins, a process known as phosphorylation. This modification can activate or deactivate the target protein's function, thereby regulating various signaling pathways within the cell. Protein kinases are essential for numerous biological functions, including metabolism, signal transduction, cell cycle progression, and apoptosis (programmed cell death). Abnormal regulation of protein kinases has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

Phosphorylase Kinase (PhK) is a key enzyme in the regulation of glycogen metabolism, primarily involved in the breakdown of glycogen to glucose-1-phosphate. It is a serine/threonine protein kinase that catalyzes the phosphorylation of glycogen phosphorylase b, an isoform of glycogen phosphorylase, converting it into its active form, glycogen phosphorylase a.

PhK is composed of four different subunits: α, β, γ, and δ. The γ subunit contains the catalytic site, while the other subunits play regulatory roles. PhK itself can be activated by calcium ions (Ca2+) and protein kinase A (PKA)-mediated phosphorylation.

Phosphorylase Kinase is primarily located in the sarcoplasmic reticulum of muscle cells, where it plays a crucial role in regulating energy production during muscle contraction and relaxation. Dysregulation or mutations in PhK have been implicated in several genetic disorders, such as Debré-akaki syndrome, which is characterized by muscle weakness and cardiac abnormalities.

"Chickens" is a common term used to refer to the domesticated bird, Gallus gallus domesticus, which is widely raised for its eggs and meat. However, in medical terms, "chickens" is not a standard term with a specific definition. If you have any specific medical concern or question related to chickens, such as food safety or allergies, please provide more details so I can give a more accurate answer.

Calcium signaling is the process by which cells regulate various functions through changes in intracellular calcium ion concentrations. Calcium ions (Ca^2+^) are crucial second messengers that play a critical role in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, and programmed cell death (apoptosis).

Intracellular calcium levels are tightly regulated by a complex network of channels, pumps, and exchangers located on the plasma membrane and intracellular organelles such as the endoplasmic reticulum (ER) and mitochondria. These proteins control the influx, efflux, and storage of calcium ions within the cell.

Calcium signaling is initiated when an external signal, such as a hormone or neurotransmitter, binds to a specific receptor on the plasma membrane. This interaction triggers the opening of ion channels, allowing extracellular Ca^2+^ to flow into the cytoplasm. In some cases, this influx of calcium ions is sufficient to activate downstream targets directly. However, in most instances, the increase in intracellular Ca^2+^ serves as a trigger for the release of additional calcium from internal stores, such as the ER.

The release of calcium from the ER is mediated by ryanodine receptors (RyRs) and inositol trisphosphate receptors (IP3Rs), which are activated by specific second messengers generated in response to the initial external signal. The activation of these channels leads to a rapid increase in cytoplasmic Ca^2+^, creating a transient intracellular calcium signal known as a "calcium spark" or "calcium puff."

These localized increases in calcium concentration can then propagate throughout the cell as waves of elevated calcium, allowing for the spatial and temporal coordination of various cellular responses. The duration and amplitude of these calcium signals are finely tuned by the interplay between calcium-binding proteins, pumps, and exchangers, ensuring that appropriate responses are elicited in a controlled manner.

Dysregulation of intracellular calcium signaling has been implicated in numerous pathological conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer. Therefore, understanding the molecular mechanisms governing calcium homeostasis and signaling is crucial for the development of novel therapeutic strategies targeting these diseases.

Phosphoric diester hydrolases are a class of enzymes that catalyze the hydrolysis of phosphoric diester bonds. These enzymes are also known as phosphatases or nucleotidases. They play important roles in various biological processes, such as signal transduction, metabolism, and regulation of cellular activities.

Phosphoric diester hydrolases can be further classified into several subclasses based on their substrate specificity and catalytic mechanism. For example, alkaline phosphatases (ALPs) are a group of phosphoric diester hydrolases that preferentially hydrolyze phosphomonoester bonds in a variety of organic molecules, releasing phosphate ions and alcohols. On the other hand, nucleotidases are a subclass of phosphoric diester hydrolases that specifically hydrolyze the phosphodiester bonds in nucleotides, releasing nucleosides and phosphate ions.

Overall, phosphoric diester hydrolases are essential for maintaining the balance of various cellular processes by regulating the levels of phosphorylated molecules and nucleotides.

In human anatomy, a "gizzard" does not exist as it is not part of the human digestive system. However, in veterinary medicine, the gizzard refers to a part of the stomach in birds and some other animals, such as crocodiles and alligators. It is a muscular, thick-walled portion where food is stored and mechanically broken down by grinding and mixing it with grit that the animal has swallowed. This action helps in the digestion process, especially for birds that do not have teeth to chew their food.

Troponin is a protein complex found in cardiac and skeletal muscle cells that plays a critical role in muscle contraction. It consists of three subunits: troponin C, which binds calcium ions; troponin I, which inhibits the interaction between actin and myosin in the absence of calcium; and troponin T, which binds to tropomyosin and helps anchor the complex to the muscle filament.

In clinical medicine, "troponin" usually refers to cardiac-specific isoforms of these proteins (cTnI and cTnT) that are released into the bloodstream following damage to the heart muscle, such as occurs in myocardial infarction (heart attack). Measurement of troponin levels in the blood is a sensitive and specific biomarker for the diagnosis of acute myocardial infarction.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.

The process typically involves the following steps:

1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.

Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

Benzylamines are a class of organic compounds that consist of a benzene ring attached to an amine group. The amine group (-NH2) can be primary, secondary, or tertiary, depending on the number of hydrogen atoms bonded to the nitrogen atom. Benzylamines are used in the synthesis of various pharmaceuticals, agrochemicals, and other organic compounds. They have a variety of biological activities and can act as central nervous system depressants, local anesthetics, and muscle relaxants. However, some benzylamines can also be toxic or carcinogenic, so they must be handled with care.

Fluphenazine is an antipsychotic medication that belongs to the class of phenothiazines. It works by blocking the action of dopamine, a neurotransmitter in the brain, which helps to reduce the symptoms of psychosis such as delusions, hallucinations, and disordered thought.

Fluphenazine is available in several forms, including oral tablets, orally disintegrating tablets, and injectable solutions. It may be used for the treatment of schizophrenia, psychotic disorders, and other conditions associated with elevated levels of dopamine in the brain.

Like all antipsychotic medications, fluphenazine can cause side effects, including extrapyramidal symptoms (EPS), such as stiffness, tremors, and spasms of the face and neck muscles, as well as other systemic side effects like weight gain, sedation, and orthostatic hypotension. It is essential to use fluphenazine under the close supervision of a healthcare provider who can monitor for side effects and adjust the dosage accordingly.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Troponin C is a subunit of the troponin complex, which is a protein complex that plays a crucial role in muscle contraction. In the heart, the troponin complex is found in the myofibrils of cardiac muscle cells (cardiomyocytes). It is composed of three subunits: troponin C, troponin T, and troponin I.

Troponin C has the ability to bind calcium ions (Ca²+), which is essential for muscle contraction. When Ca²+ binds to troponin C, it causes a conformational change that leads to the exposure of binding sites on troponin I for another protein called actin. This interaction allows for the cross-bridge formation between actin and myosin, generating the force needed for muscle contraction.

In clinical settings, cardiac troponins (including troponin T and troponin I) are commonly measured in blood tests to diagnose and monitor heart damage, particularly in conditions like myocardial infarction (heart attack). However, Troponin C is not typically used as a biomarker for heart injury because it is less specific to the heart than troponin T and troponin I. Increased levels of Troponin C in the blood can be found in various conditions involving muscle damage or disease, making it less useful for diagnosing heart-specific issues.

Myosins are a large family of motor proteins that play a crucial role in various cellular processes, including muscle contraction and intracellular transport. They consist of heavy chains, which contain the motor domain responsible for generating force and motion, and light chains, which regulate the activity of the myosin. Based on their structural and functional differences, myosins are classified into over 35 classes, with classes II, V, and VI being the most well-studied.

Class II myosins, also known as conventional myosins, are responsible for muscle contraction in skeletal, cardiac, and smooth muscles. They form filaments called thick filaments, which interact with actin filaments to generate force and movement during muscle contraction.

Class V myosins, also known as unconventional myosins, are involved in intracellular transport and organelle positioning. They have a long tail that can bind to various cargoes, such as vesicles, mitochondria, and nuclei, and a motor domain that moves along actin filaments to transport the cargoes to their destinations.

Class VI myosins are also unconventional myosins involved in intracellular transport and organelle positioning. They have two heads connected by a coiled-coil tail, which can bind to various cargoes. Class VI myosins move along actin filaments in a unique hand-over-hand motion, allowing them to transport their cargoes efficiently.

Overall, myosins are essential for many cellular functions and have been implicated in various diseases, including cardiovascular diseases, neurological disorders, and cancer.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Myosin Type I, also known as myosin-IA, is a type of motor protein found in non-muscle cells. It is involved in various cellular processes such as organelle transport, cell division, and maintenance of cell shape. Myosin-IA consists of a heavy chain, light chains, and a cargo-binding tail domain. The heavy chain contains the motor domain that binds to actin filaments and hydrolyzes ATP to generate force and movement along the actin filament.

Myosin-I is unique among myosins because it can move in both directions along the actin filament, whereas most other myosins can only move in one direction. Additionally, myosin-I has a high duty ratio, meaning that it spends a larger proportion of its ATP hydrolysis cycle bound to the actin filament, making it well-suited for processes requiring sustained force generation or precise positioning.

Phosphoprotein phosphatases (PPPs) are a family of enzymes that play a crucial role in the regulation of various cellular processes by removing phosphate groups from serine, threonine, and tyrosine residues on proteins. Phosphorylation is a post-translational modification that regulates protein function, localization, and stability, and dephosphorylation by PPPs is essential for maintaining the balance of this regulation.

The PPP family includes several subfamilies, such as PP1, PP2A, PP2B (also known as calcineurin), PP4, PP5, and PP6. Each subfamily has distinct substrate specificities and regulatory mechanisms. For example, PP1 and PP2A are involved in the regulation of metabolism, signal transduction, and cell cycle progression, while PP2B is involved in immune response and calcium signaling.

Dysregulation of PPPs has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Therefore, understanding the function and regulation of PPPs is important for developing therapeutic strategies to target these diseases.

Adenylate cyclase is an enzyme that catalyzes the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP). It plays a crucial role in various cellular processes, including signal transduction and metabolism. Adenylate cyclase is activated by hormones and neurotransmitters that bind to G-protein-coupled receptors on the cell membrane, leading to the production of cAMP, which then acts as a second messenger to regulate various intracellular responses. There are several isoforms of adenylate cyclase, each with distinct regulatory properties and subcellular localization.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Bee venom is a poisonous substance that a honeybee (Apis mellifera) injects into the skin of a person or animal when it stings. It's produced in the venom gland and stored in the venom sac of the bee. Bee venom is a complex mixture of proteins, peptides, and other compounds. The main active components of bee venom include melittin, apamin, and phospholipase A2.

Melittin is a toxic peptide that causes pain, redness, and swelling at the site of the sting. It also has hemolytic (red blood cell-destroying) properties. Apamin is a neurotoxin that can affect the nervous system and cause neurological symptoms in severe cases. Phospholipase A2 is an enzyme that can damage cell membranes and contribute to the inflammatory response.

Bee venom has been used in traditional medicine for centuries, particularly in China and other parts of Asia. It's believed to have anti-inflammatory, analgesic (pain-relieving), and immunomodulatory effects. Some studies suggest that bee venom may have therapeutic potential for a variety of medical conditions, including rheumatoid arthritis, multiple sclerosis, and chronic pain. However, more research is needed to confirm these findings and to determine the safety and efficacy of bee venom therapy.

It's important to note that bee stings can cause severe allergic reactions (anaphylaxis) in some people, which can be life-threatening. If you experience symptoms such as difficulty breathing, rapid heartbeat, or hives after being stung by a bee, seek medical attention immediately.

An erythrocyte, also known as a red blood cell, is a type of cell that circulates in the blood and is responsible for transporting oxygen throughout the body. The erythrocyte membrane refers to the thin, flexible barrier that surrounds the erythrocyte and helps to maintain its shape and stability.

The erythrocyte membrane is composed of a lipid bilayer, which contains various proteins and carbohydrates. These components help to regulate the movement of molecules into and out of the erythrocyte, as well as provide structural support and protection for the cell.

The main lipids found in the erythrocyte membrane are phospholipids and cholesterol, which are arranged in a bilayer structure with the hydrophilic (water-loving) heads facing outward and the hydrophobic (water-fearing) tails facing inward. This arrangement helps to maintain the integrity of the membrane and prevent the leakage of cellular components.

The proteins found in the erythrocyte membrane include integral proteins, which span the entire width of the membrane, and peripheral proteins, which are attached to the inner or outer surface of the membrane. These proteins play a variety of roles, such as transporting molecules across the membrane, maintaining the shape of the erythrocyte, and interacting with other cells and proteins in the body.

The carbohydrates found in the erythrocyte membrane are attached to the outer surface of the membrane and help to identify the cell as part of the body's own immune system. They also play a role in cell-cell recognition and adhesion.

Overall, the erythrocyte membrane is a complex and dynamic structure that plays a critical role in maintaining the function and integrity of red blood cells.

Actin is a type of protein that forms part of the contractile apparatus in muscle cells, and is also found in various other cell types. It is a globular protein that polymerizes to form long filaments, which are important for many cellular processes such as cell division, cell motility, and the maintenance of cell shape. In muscle cells, actin filaments interact with another type of protein called myosin to enable muscle contraction. Actins can be further divided into different subtypes, including alpha-actin, beta-actin, and gamma-actin, which have distinct functions and expression patterns in the body.

Protein Kinase C (PKC) is a family of serine-threonine kinases that play crucial roles in various cellular signaling pathways. These enzymes are activated by second messengers such as diacylglycerol (DAG) and calcium ions (Ca2+), which result from the activation of cell surface receptors like G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs).

Once activated, PKC proteins phosphorylate downstream target proteins, thereby modulating their activities. This regulation is involved in numerous cellular processes, including cell growth, differentiation, apoptosis, and membrane trafficking. There are at least 10 isoforms of PKC, classified into three subfamilies based on their second messenger requirements and structural features: conventional (cPKC; α, βI, βII, and γ), novel (nPKC; δ, ε, η, and θ), and atypical (aPKC; ζ and ι/λ). Dysregulation of PKC signaling has been implicated in several diseases, such as cancer, diabetes, and neurological disorders.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

... 1 (CALM1) Calmodulin 2 (CALM2) Calmodulin 3 (CALM3) calmodulin 1 pseudogene 1 (CALM1P1) Calmodulin-like 3 (CALML3) ... Calmodulin-like 4 (CALML4) Calmodulin-like 5 (CALML5) Calmodulin-like 6 (CALML6) Calmodulin belongs to one of the two main ... Calmodulin can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum. Calmodulin can ... Calcium binding by calmodulin exhibits considerable cooperativity, making calmodulin an unusual example of a monomeric (single- ...
... is a protein that in humans is encoded by the CALM1 gene. Calmodulin 1 is the archetype of the family of calcium- ... Calmodulin contains 149 amino acids and has 4 calcium-binding EF hand motifs. Its functions include roles in growth and the ... "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)". Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002 ... Calmodulin 1 has been shown to interact with: AKAP9, Androgen receptor, IQGAP1, PPEF1, and TRPV1. GRCh38: Ensembl release 89: ...
Other names in common use include ubiquityl-calmodulin synthase, ubiquitin-calmodulin synthetase, ubiquityl-calmodulin ... n-calmodulin The 3 substrates of this enzyme are ATP, calmodulin, and ubiquitin, whereas its 3 products are AMP, diphosphate, ... "Multiple ubiquitination of vertebrate calmodulin by reticulocyte lysate and inhibition of calmodulin conjugation by ... In enzymology, an ubiquitin-calmodulin ligase (EC 6.3.2.21) is an enzyme that catalyzes the chemical reaction n ATP + ...
In molecular biology, calmodulin binding domain (CaMBD) is a protein domain found in small-conductance calcium-activated ... They are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM ... "Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin". Nature. 410 (6832): 1120-4. ...
... are, as their name implies, proteins which bind calmodulin. Calmodulin can bind to a variety of ... Studies have proven that calmodulin's affinity for Ca2+ increases when it is bound to a calmodulin-binding protein, which ... This binding of the calmodulin to GAP-43 is allowed by the electrostatic interaction between the negatively-charged calmodulin ... Zielinski, Raymond E. (1998). "Calmodulin and Calmodulin-Binding Proteins in Plants". Annual Review of Plant Physiology and ...
The IQ calmodulin-binding motif is an amino acid sequence motif containing the following sequence: [FILV]Qxxx[RK]Gxxx[RK]xx[ ... Rhoads AR, Friedberg F (April 1997). "Sequence motifs for calmodulin recognition". FASEB J. 11 (5): 331-40. doi:10.1096/fasebj. ... Calmodulin (CaM) is recognized as a major calcium (Ca2+) sensor and orchestrator of regulatory events through its interaction ...
In molecular biology, the plant calmodulin-binding domain is a protein domain found repeated in a number of plant calmodulin- ... These domains are thought to constitute the calmodulin-binding domains of these proteins. Binding of the proteins to calmodulin ... Reddy VS, Ali GS, Reddy AS (May 2003). "Characterization of a pathogen-induced calmodulin-binding protein: mapping of four Ca2+ ... "Isolation and characterization of a novel calmodulin-binding protein from potato". J. Biol. Chem. 277 (6): 4206-14. doi:10.1074 ...
... calmodulin N6-methyl-L-lysine Thus, the two substrates of this enzyme are S-adenosyl methionine and calmodulin L-lysine, ... In enzymology, a calmodulin-lysine N-methyltransferase (EC 2.1.1.60) is an enzyme that catalyzes the chemical reaction S- ... The systematic name of this enzyme class is S-adenosyl-L-methionine:calmodulin-L-lysine N6-methyltransferase. Other names in ... Sitaramayya A, Wright LS, Siegel FL (1980). "Enzymatic methylation of calmodulin in rat brain cytosol". J. Biol. Chem. 255 (18 ...
... is a protein that in humans is encoded by the CAMTA1 gene. GRCm38: Ensembl release ... Bouche N, Scharlat A, Snedden W, Bouchez D, Fromm H (Jun 2002). "A novel family of calmodulin-binding transcription activators ... "Entrez Gene: CAMTA1 calmodulin binding transcription activator 1". Katoh M, Katoh M (2004). "Identification and ... 2007). "Calmodulin-binding transcription activator 1 (CAMTA1) alleles predispose human episodic memory performance" (PDF). ...
In molecular biology, the calmodulin-regulated spectrin-associated CKK domain (also known as the CKK domain) is a domain which ... occurs at the C-terminus of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, ...
Benaim G, Villalobo A (August 2002). "Phosphorylation of calmodulin. Functional implications". European Journal of Biochemistry ...
Application to calmodulin". Biochemistry. 29 (19): 4659-67. doi:10.1021/bi00471a022. PMID 2372549. Lewis E Kay; Mitsuhiko Ikura ...
Benaim G, Villalobo A (August 2002). "Phosphorylation of calmodulin. Functional implications" (PDF). European Journal of ...
Reis, J. (2011). Video: Calmodulin Synthesis ; Lisbon Ensemble 20/21 ; M.: Pedro Pinto Figueiredo; Marco Fernandes, Miguel ... 2 percussionists 2003/2004 Phonopolis Electronics 2003 Síntese Orchestra 2003 Lysozyme Synthesis Piano 2002 Calmodulin ... Retrieved from https://itunes.apple.com/pt/album/portuguese-contemporary-music/id957574297 Reis, J. (2016). Calmodulin ...
Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene. A member of the calmodulin family of signaling molecules ... "Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin- ... "Entrez Gene: CALM2 Calmodulin 2 (phosphorylase kinase, delta)". SenGupta B, Friedberg F, Detera-Wadleigh SD (December 1987). " ... Pan Z, Radding W, Zhou T, Hunter E, Mountz J, McDonald JM (September 1996). "Role of calmodulin in HIV-potentiated Fas-mediated ...
Calmodulin participates in an intracellular signaling system by acting as a diffusible second messenger to the initial stimuli ... Pb2+ (lead) can replace Ca2+ (calcium) as, for example, with calmodulin or Zn2+ (zinc) as with metallocarboxypeptidases Some ... Chin D, Means AR (August 2000). "Calmodulin: a prototypical calcium sensor". Trends in Cell Biology. 10 (8): 322-8. doi:10.1016 ... Stevens FC (August 1983). "Calmodulin: an introduction". Canadian Journal of Biochemistry and Cell Biology. 61 (8): 906-10. doi ...
Benaim G, Villalobo A (August 2002). "Phosphorylation of calmodulin. Functional implications". European Journal of Biochemistry ...
Application to calmodulin". Biochemistry. 29 (19): 4659-67. doi:10.1021/bi00471a022. PMID 2372549. Lewis E Kay; Mitsuhiko Ikura ...
This domain binds calmodulin, a protein known as a calcium sensor that can bind and regulate many target proteins. A GRD ( ... Hart MJ, Callow MG, Souza B, Polakis P (Aug 1996). "IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a ... Li Z, Sacks DB (February 2003). "Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1". J. Biol. Chem. 278 ... Li Z, Kim SH, Higgins JM, Brenner MB, Sacks DB (December 1999). "IQGAP1 and calmodulin modulate E-cadherin function". J. Biol. ...
For this reason protein kinases are named based on what regulates their activity (i.e. Calmodulin-dependent protein kinases). ... The 1970s included the discovery of calmodulin-dependent protein kinases and the finding that proteins can be phosphorylated on ... Activation loop Autophosphorylation Ca2+/calmodulin-dependent protein kinase Cell signaling Cyclin-dependent kinase G protein- ...
Proteins with calcium binding sites consisting of two tyrosine residues, such as calmodulin and troponin C, are especially ... Malencik, Dean A.; Anderson, Sonia R. (1987). "Dityrosine formation in calmodulin". Biochemistry. 26 (3): 695-704. doi:10.1021/ ...
Tuberculosis toxin blocking phagosome maturation inhibits a novel Ca2!/calmodulin-PI3K hVPS34 cascade. J. Exp. Med. 198:653-659 ...
An IQ motif provides a binding site for calmodulin (CaM) or CaM-like proteins. LRRIQ3 is predicted to be mostly alpha-helical ... In total, there are 4 conserved domains within LRRIQ3: 3 leucine-rich repeats and 1 IQ calmodulin-binding motif. Leucine-rich ... Rhoads AR, Friedberg F (April 1997). "Sequence motifs for calmodulin recognition". FASEB J. 11 (5): 331-40. doi:10.1096/fasebj. ...
They are used in Calmodulin. Rouse, G.W.; Goffredi, S.K. & Vrijenhoek, R.C. (2004). "Osedax rubiplumus Rouse, Goffredi & ...
... produces Calmodulin inhibitors. Many of the strains of Aspergillus stromatoides have been isolated in ... "Calmodulin inhibitors from Aspergillus stromatoides". Chemistry & Biodiversity. 10 (3): 328-37. doi:10.1002/cbdv.201200321. ...
First, the calcium will bind to calmodulin. After the influx of calcium ions and the binding to calmodulin, pp60 SRC (a protein ... Kim MT, Kim BJ, Lee JH, Kwon SC, Yeon DS, Yang DK, So I, Kim KW (April 2006). "Involvement of calmodulin and myosin light chain ... On either sides of the catalytic core sit calcium ion/calmodulin binding sites. Binding of calcium ion to this domain increases ... Robinson A, Colbran R (2013). "Calcium/Calmodulin-Dependent Protein Kinases". In Lennarz W, Lane D (eds.). Encyclopedia of ...
"New nuclear functions for calmodulin". Cell Calcium. 23 (2-3): 115-21. doi:10.1016/S0143-4160(98)90109-9. PMID 9601606. ...
One such example is calmodulin. One molecule of calmodulin binds four calcium ions cooperatively. Its structure presents four ... DAPK and EGFR calmodulin binding domains interact with different calmodulin-calcium complexes". Biochimica et Biophysica Acta ( ... Babu YS, Sack JS, Greenhough TJ, Bugg CE, Means AR, Cook WJ (1985). "Three-dimensional structure of calmodulin". Nature. 315 ( ... "A general strategy to characterize calmodulin-calcium complexes involved in CaM-target recognition: ...
Joyal JL, Burks DJ, Pons S, Matter WF, Vlahos CJ, White MF, Sacks DB (November 1997). "Calmodulin activates ...
Ca2+-bound calmodulin (CaM) interacts with Cav1.3 to induce calcium-dependent inactivation (CDI). Recently, it has been shown ... but weakens the pre-binding of Ca2+-free calmodulin (apoCaM) to channels. The upshot is that CDI is continuously tuneable by ... "Calcium calmodulin and hormone secretion". Clinical Endocrinology. 23 (2): 201-18. doi:10.1111/j.1365-2265.1985.tb00216.x. PMID ...
Calmodulin 1 (CALM1) Calmodulin 2 (CALM2) Calmodulin 3 (CALM3) calmodulin 1 pseudogene 1 (CALM1P1) Calmodulin-like 3 (CALML3) ... Calmodulin-like 4 (CALML4) Calmodulin-like 5 (CALML5) Calmodulin-like 6 (CALML6) Calmodulin belongs to one of the two main ... Calmodulin can also make use of the calcium stores in the endoplasmic reticulum, and the sarcoplasmic reticulum. Calmodulin can ... Calcium binding by calmodulin exhibits considerable cooperativity, making calmodulin an unusual example of a monomeric (single- ...
calmodulin-1. Names. Calmodulin-2. Calmodulin-3. calmodulin 1 (phosphorylase kinase, delta). phosphorylase kinase subunit delta ... Calmodulin and calmodulin-dependent protein kinase-II (CaMK-II)-activated p38 MAPK play a role in extracellular Tat-induced IL- ... Calmodulin binds to both HIV-1 Gag and Matrix proteins through an extended calmodulin-binding domain in Matrix (amino acids 11- ... Calmodulin disrupts plasma membrane localization of farnesylated KRAS4b by sequestering its lipid moiety. Title: Calmodulin ...
Calmodulin-like. Timeline for Protein Calmodulin from a.39.1.5: Calmodulin-like: *Protein Calmodulin from a.39.1.5: Calmodulin- ... Protein Calmodulin from a.39.1.5: Calmodulin-like appears in SCOPe 2.05. *Protein Calmodulin from a.39.1.5: Calmodulin-like ... complexed with calmodulin-binding domain of calmodulin-dependent protein kinase. complexed with ca. ... Protein Calmodulin from a.39.1.5: Calmodulin-like appears in the current release, SCOPe 2.08. ...
Expression of type I adenylyl cyclase activity in animal cells has established that this enzyme is stimulated by calmodulin and ... Stimulation of the type III olfactory adenylyl cyclase by calcium and calmodulin Biochemistry. 1992 Jul 21;31(28):6492-8. doi: ... The sensitivity of the type III adenylyl cyclase to Ca2+ and calmodulin has not been reported. In this study, type III adenylyl ... The type III enzyme was not stimulated by Ca2+ and calmodulin in the absence of other effectors. It was, however, stimulated by ...
The complex Structure of Calmodulin Bound to a Calcineurin Peptide ... Calmodulin. A,. C [auth B]. 149. Homo sapiens. Mutation(s): 0 Gene Names: CALM1, CALM, CAM, CAM1. ... including the calmodulin binding domain (CaMBD), block access to its active site. Upon binding of Ca2+ and calmodulin (Ca2+/CaM ... The complex structure of calmodulin bound to a calcineurin peptide.. Ye, Q., Wang, H., Zheng, J., Wei, Q., Jia, Z.. (2008) ...
J:37553 Yan C, et al., Molecular cloning and characterization of a calmodulin-dependent phosphodiesterase enriched in olfactory ... PR:000012466 dual specificity calcium/calmodulin-dependent 3,5-cyclic nucleotide phosphodiesterase 1A ...
Ca2+/Calmodulin dependent protein kinase (CaMK) are mammalian calmodulin-dependent calcium-dependent protein kinases activated ... 3D Structures of Calcium/calmodulin dependent protein kinase Calcium/calmodulin dependent protein kinase 3D structures ... Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, Knapp S. Structure of the CaMKIIdelta/calmodulin complex reveals ... Retrieved from "http://proteopedia.org/wiki/index.php/Calcium/Calmodulin-dependent_protein_kinase" ...
Protein target information for Calmodulin (Stylonychia lemnae). Find diseases associated with this biological target and ...
Solution NMR-derived structure of calmodulin N-lobe bound with ER alpha peptide ... Structural basis for Ca2+-induced activation and dimerization of estrogen receptor alpha by calmodulin.. Zhang, Y., Li, Z., ... Calcium-dependent regulation of ER-α is critical for activating gene expression and is controlled by calmodulin (CaM). Here, we ... Calcium-dependent regulation of ER-α is critical for activating gene expression and is controlled by calmodulin (CaM). Here, we ...
So what is calmodulin, and what can a mutation in the gene that codes for it do to the heart? ... So what is calmodulin, and what can a mutation in the gene that codes for it do to the heart? Paul Biegler explains in this ... Calmodulin closes the ion channels through which calcium flits in and out of the heart muscle cells. But if you have the CALM2 ... Calmodulin regulates your heartbeat. Mutations in it could have been fatal for Kathleen Folbiggs daughters. Human cardiac ...
Invitrogen Anti-Calmodulin 1/2/3 Polyclonal, Catalog # PA5-102378. Tested in Western Blot (WB), Immunocytochemistry (ICC/IF) ... calmodulin 3 (phosphorylase kinase, delta); Calmodulin III; Calmodulin-1; Calmodulin-2; Calmodulin-3; caM; epididymis secretory ... Protein Aliases: calmodulin; Calmodulin 1 (phosphorylase kinase, delta); calmodulin 2 (phosphorylase kinase, delta); ... Cite Calmodulin 1/2/3 Polyclonal Antibody. The following product was used in this experiment: Calmodulin 1/2/3 Polyclonal ...
However, their calcium-binding domain is restricted by calmodulin from metazoans. In this study, we developed red GECI, called ... FRCaMP, using calmodulin (CaM) from Schizosaccharomyces pombe fungus as a calcium binding domain. Compared to the R-GECO1 ... Because of calmodulins lower amino acid sequence homology to metazoa orthologues, the utilization of calmodulin from ... The amino acid sequence of calmodulin (CaM) from S. pombe is 75% identical to those of CaMs from H. sapiens and M. musculus ( ...
2005) Visualization of synaptic Ca2+/calmodulin-dependent protein kinase II activity in living neurons. J Neurosci 25:3107-3112 ... 1998) Definition of optimal substrate recognition motifs of Ca2+-calmodulin-dependent protein kinases IV and II reveals shared ... 1991) The newly synthesized selective Ca2+/calmodulin dependent protein kinase II inhibitor KN-93 reduces dopamine contents in ... 1988) Cell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in ...
A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve ... differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN ... Calcium-Calmodulin Protein Kinase II; Calcium-Calmodulin-Dependent PK Type II; Calcium-Calmodulin-Dependent Protein Kinase Type ... Calmodulin Kinase IIalpha; Calmodulin-Dependent Protein Kinase II; CaM Kinase IIalpha; Calcium Calmodulin Dependent PK Type II ...
Ca2+-binding protein calmodulin (CaM) serves as a primary effector of calcium function. Ca2+/CaM binds to the death-associated ... Ca2+-binding protein calmodulin (CaM) serves as a primary effector of calcium function. Ca2+/CaM binds to the death-associated ... 2018). Calmodulin (CaM) activates PI3Kα by targeting the "soft" CaM-binding motifs in both the nSH2 and cSH2 domains of p85α. J ... Keywords: calcium, calmodulin, death-associated protein kinase, allostery, molecular dynamics simulation. Citation: Li X, Li B ...
... ... "Neuroprotective Effects of Calmodulin Peptide 76-121aa: Disruption of Calmodulin Binding to Mutant Huntingtin." Brain Pathology ... which may cause abnormal protein-protein interactions such as increased association with calmodulin (CaM). We previously ...
Increment of calmodulin in proportion to enhancement of non-nicotinic responses after preganglionic stimulation of the dog ... Increment of calmodulin in proportion to enhancement of non-nicotinic responses after preganglionic stimulation of the dog ... Increment of calmodulin in proportion to enhancement of non-nicotinic responses after preganglionic stimulation of the dog ... Increment of calmodulin in proportion to enhancement of non-nicotinic responses after preganglionic stimulation of the dog ...
Calmodulin (CaM)-mediated Ca2+-induced inactivation is an ion channel regulatory mechanism that protects cells against the ... Mechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6. Singh, Appu K.; McGoldrick, Luke Lawrence ... Calmodulin (CaM)-mediated Ca2+-induced inactivation is an ion channel regulatory mechanism that protects cells against the ...
The C-terminal tail of Dfi1p has a calmodulin binding motif, suggesting that Dfi1p binding to calmodulin may affect Cek1p ... We show that the C-terminal tail of Dfi1p binds to calmodulin in vitro, and mutations that affect this region affect both ... The goal of this work was to determine the importance of the calmodulin binding motif of Dfi1p in filamentation and signaling. ... Dfi1p Binding to Calmodulin Promotes Filamentation and Cek1p Activation in Candida albicans. Davis, Talya. ...
In this study, we found that activation of D4 receptors in PFC exerts a complex regulation of Ca2+/calmodulin-dependent protein ... Bidirectional Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II Activity by Dopamine D4 Receptors in Prefrontal Cortex ... Bidirectional Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II Activity by Dopamine D4 Receptors in Prefrontal Cortex ... Bidirectional Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II Activity by Dopamine D4 Receptors in Prefrontal Cortex ...
Calcium drives interactions for both calcium-binding domains of calmodulin in complex with KCa2.1 peptides and both domains are ... Calcium dependence of both lobes of calmodulin is involved in binding to a cytoplasmic domain of SK channels. ... Calcium dependence of both lobes of calmodulin is involved in binding to a cytoplasmic domain of SK channels ... Calcium dependence of both lobes of calmodulin is involved in binding to a cytoplasmic domain of SK channels ...
pThr286]Ca2+/calmodulin-dependent protein kinase II (rat) (α subunit) monoclonal antibody (22B1) - ALX-802-009 ... Cytoplasmic polyadenylation element binding protein-dependent protein synthesis is regulated by calcium/calmodulin-dependent ... pThr286]Ca2+/calmodulin-dependent protein kinase II (rat) (α subunit) monoclonal antibody (22B1). ... Ca2+/Calmodulin-dependent Protein Kinase II) thiophosphorylated at (Thr286).. ...
Human CALML5(Calmodulin Like Protein 5) ELISA Kit. Human CALML5(Calmodulin Like Protein 5) ELISA Kit ... Human Calmodulin Like Protein 5 (CALML5) ELISA Kit. SEF897Hu-10x96wellstestplate Cloud-Clone 10x96-wells test plate. 5677.8 EUR ... Description: A sandwich ELISA kit for detection of Calmodulin Like Protein 5 from Human in samples from blood, serum, plasma, ... Description: A sandwich quantitative ELISA assay kit for detection of Human Calmodulin Like Protein 3 (CALML3) in samples from ...
A Triton X-100-lysed cell system has been used to identify calmodulin on the cytoskeleton of 3T3 and transformed SV3T3 cells. ... Calmodulin-microtubule association in cultured mammalian cells.. J Cell Biol (1984) 98 (3): 904-910. ...
... a mutant calmodulin led to the loss of Ca-activated K conductance, which could be restored by injection of wild type calmodulin ... in which neither the injection of calmodulin, nor of the calmodulin-antagonist, trifluoperazine, were able to modify Ca- ... but have calmodulin-binding domains near their intracellular carboxy-terminal regions to which calmodulin binds tightly and ... potassium conductance has an altered calmodulin: a nonlethal selective alteration in calmodulin regulation. Proc Natl Acad Sci ...
Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat. Struct. ... Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat. Struct. ... Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin Marc Fivaz, ... Calmodulin binds RalA and RalB and is required for the thrombin-induced activation of Ral in human platelets. J. Biol. Chem. ...
Yuan K, Jing G, Chen J, Liu H, Zhang K, Li Y, Wu H, McDonald JM, Chen Y. Calmodulin mediates Fas-induced FADD-independent ... Calmodulin binding to the Fas death domain. Regulation by Fas activation. The Journal of biological chemistry. 2004; 279:5661- ... Calmodulin binding to the Fas-mediated death-inducing signaling complex in cholangiocarcinoma cells. Journal of cellular ... Calmodulin binding to cellular FLICE-like inhibitory protein modulates Fas-induced signalling. The Biochemical journal. 2008; ...
Calcium-dependent and independent calmodulin binding motifs. CaM, calmodulin; CaMBPs, CaM-binding proteins; CaMBDs, CaM-binding ... Detection of putative calmodulin binding domains in proteins associated with neuroinflammation. Using the Calmodulin Target ... Neuroprotective effects of calmodulin peptide 76-121aa: disruption of calmodulin binding to mutant huntingtin. Brain Pathol. ... were scanned for calmodulin binding domains using the Calmodulin Target Database. This analysis revealed the presence of at ...
Structural dynamics of calmodulin in regulation of cardi. *McCarthy, Megan R (PI) ...
  • Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases. (wikipedia.org)
  • Together, these features allow calmodulin to recognize some 300 target proteins exhibiting a variety of CaM-binding sequence motifs. (wikipedia.org)
  • Canonical" targets of calmodulin, such as myosin light-chain kinases and CaMKII, bind only to the Ca2+-bound protein, whereas some proteins, such as NaV channels and IQ-motif proteins, also bind to calmodulin in the absence of Ca2+. (wikipedia.org)
  • This influence of target binding on Ca2+ affinity is believed to allow for Ca2+ activation of proteins that are constitutively bound to calmodulin, such as small-conductance Ca2+-activated potassium (SK) channels. (wikipedia.org)
  • This gene encodes one of three calmodulin proteins which are members of the EF-hand calcium-binding protein family. (nih.gov)
  • As it binds calcium, calmodulin undergoes conformational changes which can increase its affinity for target proteins. (thermofisher.com)
  • Calcium binds to and regulates the small regulatory protein calmodulin that in turn binds to and regulates several hundred calmodulin binding proteins. (biomedcentral.com)
  • Many of these proteins are linked to multiple neurodegenerative diseases indicating that calmodulin binding proteins lie at the heart of neuroinflammatory events associated with multiple neurodegenerative diseases. (biomedcentral.com)
  • The small calcium-binding protein calmodulin (CaM) is a primary effector of calcium function and works in turn by binding to and regulating CaM-binding proteins (CaMBPs) [ 53 ]. (biomedcentral.com)
  • The Calcium Hypothesis was thus extended as the Calmodulin Hypothesis since CaM not only binds to and regulates CaMBPs critical to learning and memory but also proteins involved in the formation of amyloid plaques and tangles, hallmarks of AD [ 41 ]. (biomedcentral.com)
  • The intimate role of CaMBPs in AD was recently reviewed reinforcing the role of CaM in binding to and regulating multiple key proteins adding further support for the Calmodulin Hypothesis of O'Day and Myre [ 41 , 47 ]. (biomedcentral.com)
  • Calmodulin is an important multifunctional molecule that regulates the activities of a large number of proteins in the cell. (biomedcentral.com)
  • Calcium binding induces conformational transitions in calmodulin that make it specifically active to particular target proteins. (biomedcentral.com)
  • Many proteins use Calmodulin as a calcium sensor and signal transducer, as the proteins themselves are not able to bind calcium. (genaxxon.com)
  • Troponin and calmodulin are two proteins. (differencebetween.com)
  • Troponin is a complex of three proteins, while calmodulin is a small protein made up of two globular domains connected by a central alpha helix. (differencebetween.com)
  • Structurally, troponin is a complex of three proteins, while calmodulin is composed of two globular domains connected by a central alpha-helix. (differencebetween.com)
  • 140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry. (lu.se)
  • We describe the proteomic characterization of mouse brain Ca2+-calmodulin-binding proteins that were purified using calmodulin affinity chromatography. (lu.se)
  • A total of 140 putative Ca2+-calmodulin-binding proteins were identified of which 87 proteins contained calmodulin-binding motifs. (lu.se)
  • Among the 87 proteins that contained calmodulin-binding motifs, 48 proteins have not previously been shown to interact with calmodulin and 39 proteins were known calmodulin-binding proteins. (lu.se)
  • Ca2+/Calmodulin-dependent protein kinase 2 (CAMK2) family proteins are involved in regulation of cellular processes in a variety of tissues including brain, heart, liver and kidney. (bvsalud.org)
  • Ca2+/Calmodulin dependent protein kinase (CaMK) are mammalian calmodulin-dependent calcium-dependent protein kinases activated by elevation of Ca+2 and calmodulin concentration to phosphorylate Ser and Thr. (proteopedia.org)
  • Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, Knapp S. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. (proteopedia.org)
  • We found that Homer3, the predominant isoform in Purkinje cells, is phosphorylated by calcium/calmodulin-dependent protein kinase II (CaMKII) both in vitro and in vivo . (jneurosci.org)
  • In this study, we revealed that Homer3 was phosphorylated by calcium/calmodulin-dependent protein kinase II (CaMKII) in Purkinje cells, and the phosphorylation reduces the affinity for Homer target molecules, resulting in change of the solubility. (jneurosci.org)
  • A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. (curehunter.com)
  • It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. (curehunter.com)
  • In this study, we found that activation of D 4 receptors in PFC exerts a complex regulation of Ca 2+ /calmodulin-dependent protein kinase II (CaMKII), a multifunctional enzyme critically involved in synaptic plasticity that is fundamental for cognitive and emotional processes. (aspetjournals.org)
  • Synthetic peptide corresponding to aa 281-294 (M 281 HRQET(PSO 3 )VDCLKKFN 294 ) of the α-subunit of mouse and rat CaM kinase II (Ca 2+ /Calmodulin-dependent Protein Kinase II) thiophosphorylated at (Thr 286 ). (enzolifesciences.com)
  • Ca 2+ /calmodulin-dependent protein kinase kinases (CaMKKα and β) are regulatory kinases for multiple downstream kinases, including CaMKI, CaMKIV, PKB/Akt, and AMP-activated protein kinase (AMPK) through phosphorylation of each activation-loop Thr residue. (elsevierpure.com)
  • It is shown that increasing of intracellular calcium concentration in rotavirus infected cells is associated with the activation of some members of protein kinases family such as calcium/calmodulin-dependent kinase II, which plays a crucial role in replication and pathogenesis of the virus. (ac.ir)
  • The aim of this study was to expression bovine rotavirus NSP4 gene in HEK293 cell and evaluation of its biological effect related to activation of calcium/calmodulin-dependent kinase II in cell culture. (ac.ir)
  • Western blot analysis was performed as a confirmation test for both expression of NSP4 protein and activation of calcium/calmodulin-dependent kinase II. (ac.ir)
  • Expression of NSP4 and activated form of calcium/calmodulin-dependent kinase II were demonstrated by western blotting. (ac.ir)
  • Autophagy hijacked through viroporin-activated calcium/calmodulin-dependent kinase kinase-β signaling is required for rotavirus replication. (ac.ir)
  • Autophosphorylation at Thr286 of the α calcium-calmodulin kinase II in LTP and learning. (ac.ir)
  • 12. Braun AP, Schulman H. The multifunctional calcium/calmodulin-dependent protein kinase: from form to function. (ac.ir)
  • 13. Meyer T, Hanson PI, Stryer L, Schulman H. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. (ac.ir)
  • Calcium-induced activation of calmodulin regulates and modulates the function of cardiac ion channels. (nih.gov)
  • Calmodulin regulates your heartbeat. (cosmosmagazine.com)
  • CALM2 G114R is a variation in the gene CALM2 that codes for a protein called calmodulin ( read our genetics explainer ) which, in turn, regulates the movement of calcium in heart muscle cells. (cosmosmagazine.com)
  • In contrast, calmodulin regulates many cellular processes. (differencebetween.com)
  • troponin regulates the contractions of the heart and skeletal muscles while calmodulin mediates Ca 2+ -dependent signalling. (differencebetween.com)
  • On the other hand, these recent studies apparently also support the lack of involvement of calmodulin in the gating of the BK channels studied in Helix neurons by Levitan and Levitan (1986) . (conicyt.cl)
  • To gain insight into the general applicability of this hypothesis, the involvement of calmodulin in neuroinflammation in Alzheimer's, amyotrophic lateral sclerosis, Huntington's disease, Parkinson's disease, frontotemporal dementia, and other dementias was explored. (biomedcentral.com)
  • Calmodulin variant E140G associated with long QT syndrome impairs CaMKIIδ autophosphorylation and L-type calcium channel inactivation. (nih.gov)
  • Calmodulin Mutations in Human Disease. (nih.gov)
  • We show that the C-terminal tail of Dfi1p binds to calmodulin in vitro, and mutations that affect this region affect both calmodulin binding in vitro and invasive filamentation when incorporated into the full length Dfi1p protein. (tufts.edu)
  • Guillemette, J. G., Structural Consequences of Calmodulin EF Hand Mutations. (nicoyalife.com)
  • Calmodulin is structurally quite similar to troponin C, another Ca2+-binding protein containing four EF-hand motifs. (wikipedia.org)
  • Calmodulin is similar to troponin C. (differencebetween.com)
  • It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. (wikipedia.org)
  • Studies have found that calmodulin participates in the regulation of several biological processes including energy and biosynthetic metabolism, cell motility, exocytosis, cytoskeletal assembly, and intracellular modulation of both cAMP and calcium concentrations. (thermofisher.com)
  • The results of our analysis reduce the gap between current understanding of intracellular calmodulin function at the structural level and physiological calcium-dependent calmodulin target activation experiments. (biomedcentral.com)
  • In order to examine the consequences of a transient increase or decrease in intracellular calmodulin (CaM) levels, two bovine-papilloma-virus (BPV)-based expression vectors capable of inducibly synthesizing CaM sense (BPV-MCM) or anti-sense (BPV-CaMAS) RNA have been constructed and used to stably transform mouse C127 cells. (duke.edu)
  • Binding of calmodulin induces conformational rearrangements in the target protein via "mutually induced fit", leading to changes in the target protein's function. (wikipedia.org)
  • These conclusions were, however, apparently contradicted by elegant experiments done on internally-perfused snail neurons, in which neither the injection of calmodulin, nor of the calmodulin-antagonist, trifluoperazine, were able to modify Ca-activated K currents ( Levitan and Levitan, 1986 ). (conicyt.cl)
  • We investigated the effects of calmodulin(CaM) antagonists, trifluoperazine(TFP) and tamoxifen(TMX), on TRA-8-induced apoptosis and tumorigenesis of TRA-8-resistant pancreatic cancer cells, and underlying mechanisms. (oncotarget.com)
  • Using cells of the human lymphoblastoid line WiL2, we have previously shown that receptor-mediated endocytosis occurring at caps involves clathrin-coated vesicles and that the formation of such vesicles is sensitive to drugs such as trifluoperazine dihydrochloride (TFP) that affect calmodulin (CaM), the calcium-dependent regulatory protein of cells 3 . (elsevierpure.com)
  • The activity of the protein phosphatase calcineurin (CN) is regulated by an autoinhibition mechanism wherein several domains from its catalytic A subunit, including the calmodulin binding domain (CaMBD), block access to its active site. (rcsb.org)
  • Calcium-dependent regulation of ER-α is critical for activating gene expression and is controlled by calmodulin (CaM). (rcsb.org)
  • Though such ions distort calmodulin's structure and are generally not physiologically relevant due to their scarcity in vitro, they have nonetheless seen wide scientific use as reporters of calmodulin structure and function. (wikipedia.org)
  • 1983. Correlation of metal toxicity with in vitro calmodulin inhibition. (cdc.gov)
  • However, troponin C contains an additional alpha-helix at its N-terminus, and is constitutively bound to its target, troponin I. It therefore does not exhibit the same diversity of target recognition as does calmodulin. (wikipedia.org)
  • Troponin C is similar to calmodulin both in amino acid sequence and in three-dimensional structure. (differencebetween.com)
  • Similar to calmodulin, troponin C has calcium-binding sites. (differencebetween.com)
  • What are the Similarities Between Troponin and Calmodulin? (differencebetween.com)
  • Troponin is a protein present in cardiac and skeletal muscles, while calmodulin is a protein present in the cytoplasm of all eukaryotic cells. (differencebetween.com)
  • So, this is the key difference between troponin and calmodulin. (differencebetween.com)
  • Below infographic summarizes the difference between troponin and calmodulin. (differencebetween.com)
  • Thus, this summarizes the difference between troponin and calmodulin. (differencebetween.com)
  • Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. (wikipedia.org)
  • Calmodulin is a small, highly conserved calcium binding protein found in all eukaryotic cells. (thermofisher.com)
  • Calmodulin is a calcium-binding protein expressed in many eukaryotic cells. (genaxxon.com)
  • Calmodulin is a small dumbbell-shaped protein which is present in the cytoplasm of all eukaryotic cells. (differencebetween.com)
  • Calmodulin also exhibits great structural variability, and undergoes considerable conformational fluctuations, when bound to targets. (wikipedia.org)
  • Moreover, the predominantly hydrophobic nature of binding between calmodulin and most of its targets allows for recognition of a broad range of target protein sequences. (wikipedia.org)
  • The flexible central domain of calmodulin allows the protein to wrap around its target, although alternate modes of binding are known. (wikipedia.org)
  • Calcium binding by calmodulin exhibits considerable cooperativity, making calmodulin an unusual example of a monomeric (single-chain) cooperative binding protein. (wikipedia.org)
  • Furthermore, target binding alters the binding affinity of calmodulin toward Ca2+ ions, which allows for complex allosteric interplay between Ca2+ and target binding interactions. (wikipedia.org)
  • Although calmodulin principally operates as a Ca2+ binding protein, it also coordinates other metal ions. (wikipedia.org)
  • Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca(2+)-ligated calmodulin. (nih.gov)
  • Upon binding of Ca2+ and calmodulin (Ca2+/CaM) to CaMBD, the autoinhibitory domains dissociate from the catalytic groove, thus activating the enzyme. (rcsb.org)
  • However, their calcium-binding domain is restricted by calmodulin from metazoans. (mdpi.com)
  • In this study, we developed red GECI, called FRCaMP, using calmodulin (CaM) from Schizosaccharomyces pombe fungus as a calcium binding domain. (mdpi.com)
  • Ca 2+ -binding protein calmodulin (CaM) serves as a primary effector of calcium function. (frontiersin.org)
  • The small and highly expressed Ca 2+ -binding protein calmodulin (CaM) acts as a primary effector of calcium function ( Soderling and Stull, 2001 ). (frontiersin.org)
  • Dfi1p Binding to Calmodulin Promotes Filamentation and Cek1p Activation in Candida albicans. (tufts.edu)
  • The C-terminal tail of Dfi1p has a calmodulin binding motif, suggesting that Dfi1p binding to calmodulin may affect Cek1p activation and invasive filamentation. (tufts.edu)
  • The goal of this work was to determine the importance of the calmodulin binding motif of Dfi1p in filamentation and signaling. (tufts.edu)
  • The precise mechanisms underlying calcium binding to calmodulin are still, however, quite poorly understood. (biomedcentral.com)
  • Full CaN activation requires binding of calcium-loaded calmodulin (CaM), however little is known about how CaM binding releases CaN's autoinhibitory domain from the active site. (uky.edu)
  • According to the most current studies, the most important CBP (Calcium Binding Protein) in the human body is Calmodulin. (lcngrain.com)
  • 2. "Calmodulin Binding sites" By PDB - from the Molecule of the Month feature by David Goodsell at the RCSB Protein Data Bank . (differencebetween.com)
  • Structural Basis for Simultaneous Binding of Two Carboxy-terminal Peptidesof Plant Glutamate Decarboxylase to Calmodulin. (expasy.org)
  • Calmodulin (CaM) is a cytosolic Ca 2+ -binding protein that serves as a control element for many enzymes. (nicoyalife.com)
  • Calmodulin is an essential Ca2+-binding protein that binds to a variety of targets that carry out critical signaling functions. (lu.se)
  • cDNA encoding calmodulin, a calcium sensor protein, (rEgCaM) may play an essential role in the biologic function of E granulosus as a calcium binding protein. (medscape.com)
  • We compare the predictions of our analysis with physiological dose-response curves taken from the literature, in order to provide a quantitative comparison of the effects of different mechanisms of cooperativity on calcium-calmodulin interactions. (biomedcentral.com)
  • The major function of calmodulin is to mediate Ca 2+ dependent signalling. (differencebetween.com)
  • The authors conclude that A23187 chemiluminescence is dependent on calmodulin, independent of the oxidative burst, and attributable to arachidonate release from cellular phospholipids. (cdc.gov)
  • Calmodulin-microtubule association in cultured mammalian cells. (rupress.org)
  • Description: A sandwich ELISA kit for detection of Calmodulin Like Protein 5 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (glideruniversity.org)
  • In this study, we adopt a structural systems biology approach and develop a mathematical model to investigate various types of cooperative calcium-calmodulin interactions. (biomedcentral.com)
  • The following product was used in this experiment: Calmodulin 1/2/3 Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-102378, RRID AB_2851785. (thermofisher.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Calmodulin Like Protein 5 (CALML5) in Tissue homogenates, cell lysates and other biological fluids. (glideruniversity.org)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Calmodulin Like Protein 5 (CALML5) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (glideruniversity.org)
  • Huntington's disease (HD) is a neurodegenerative disease caused by mutant huntingtin protein containing an expanded polyglutamine tract, which may cause abnormal protein-protein interactions such as increased association with calmodulin (CaM). (ku.edu)
  • We propose that conformational changes in Dfi1p in response to environmental conditions encountered during growth allow the protein to bind calmodulin and initiate a signaling cascade that activates Cek1p. (tufts.edu)
  • Calmodulin Interactions with Voltage-Gated Sodium Channels. (nih.gov)
  • So what is calmodulin, and what can a mutation in the gene that codes for it do to the heart? (cosmosmagazine.com)
  • Calmodulin is a bioactive protein isolated from bovine testes with a molecular weight of 16,7. (genaxxon.com)
  • Calmodulin (CaM)-mediated Ca2+-induced inactivation is an ion channel regulatory mechanism that protects cells against the toxic effects of Ca2+ overload. (columbia.edu)
  • Expression of type I adenylyl cyclase activity in animal cells has established that this enzyme is stimulated by calmodulin and Ca2+. (nih.gov)
  • In this study, type III adenylyl cyclase was expressed in human kidney 293 cells to determine if the enzyme is stimulated by Ca2+ and calmodulin. (nih.gov)
  • The type III enzyme was not stimulated by Ca2+ and calmodulin in the absence of other effectors. (nih.gov)
  • It was, however, stimulated by Ca2+ through calmodulin when the enzyme was concomitantly activated by either GppNHp or forskolin. (nih.gov)
  • Later experiments, in which six different calmodulin-inhibitory drugs were tested on the Ca-activated K conductance of human RBCs, showed that all were potent inhibitors of this conductance and that their effect showed a correlation coefficient of 0.98 with that found on RBC Ca-ATPase, a membrane enzyme known to be activated by calmodulin ( Lackington and Orrego, 1981 ). (conicyt.cl)
  • But if you have the CALM2 G114R variant, calmodulin gets bad at closing the channel - it stays open and calcium can come and go as it pleases. (cosmosmagazine.com)
  • Calmodulin - A new domain in osteoporosis treatment. (lcngrain.com)
  • Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions. (nih.gov)
  • Increment of calmodulin in proportion to enhancement of non-nicotinic responses after preganglionic stimulation of the dog cardiac sympathetic ganglia. (aspetjournals.org)
  • Calmodulin closes the ion channels through which calcium flits in and out of the heart muscle cells. (cosmosmagazine.com)
  • All these findings thus seemed to firmly support a role for calmodulin in the gating of these Ca-activated K channels. (conicyt.cl)
  • At the time, this seemed to tip the balance against a participation of calmodulin in these channels. (conicyt.cl)
  • Very recently, the sequencing of the genes that code for SK, IK and BK channels has allowed a definition of the mechanisms of channel gating and of the participation of calmodulin in it. (conicyt.cl)
  • Recombinant human Calmodulin (1-149aa) purified from E. coli. (covalab.com)
  • Reacts with human Calmodulin. (covalab.com)
  • Description: A competitive ELISA for quantitative measurement of Human Calmodulin like protein 5(CALML5) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (glideruniversity.org)
  • We provide evidence that KRas translocation occurs through sequestration of the polybasic-prenyl motif by Ca 2+ /calmodulin (Ca 2+ /CaM) and subsequent release of KRas from the PM, in a process reminiscent of GDP dissociation inhibitor-mediated membrane recycling of Rab and Rho GTPases. (rupress.org)