A 17-KDa cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE.
A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
A cyclic undecapeptide from an extract of soil fungi. It is a powerful immunosupressant with a specific action on T-lymphocytes. It is used for the prophylaxis of graft rejection in organ and tissue transplantation. (From Martindale, The Extra Pharmacopoeia, 30th ed).
Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases (PEPTIDYLPROLYL ISOMERASE). They bind the immunosuppressant drugs CYCLOSPORINE; TACROLIMUS and SIROLIMUS. They possess rotamase activity, which is inhibited by the immunosuppressant drugs that bind to them.
A group of closely related cyclic undecapeptides from the fungi Trichoderma polysporum and Cylindocarpon lucidum. They have some antineoplastic and antifungal action and significant immunosuppressive effects. Cyclosporins have been proposed as adjuvants in tissue and organ transplantation to suppress graft rejection.
Transport proteins that carry specific substances in the blood or across cell membranes.
A widely distributed cell surface transmembrane glycoprotein that stimulates the synthesis of MATRIX METALLOPROTEINASES. It is found at high levels on the surface of malignant NEOPLASMS and may play a role as a mediator of malignant cell behavior.
Proteins involved in the transport of specific substances across the membranes of the MITOCHONDRIA.
A tumor necrosis factor receptor superfamily member found expressed on peripheral B-LYMPHOCYTES. It has specificity for B-CELL MATURATION ANTIGEN and TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
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.
A family of the New World monkeys inhabiting the forests of South and Central America. There is a single genus and several species occurring in this family, including AOTUS TRIVIRGATUS (Northern night monkeys).
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.
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 member of tumor necrosis factor superfamily found on MACROPHAGES; DENDRITIC CELLS and T-LYMPHOCYTES. It occurs as transmembrane protein that can be cleaved to release a secreted form that specifically binds to TRANSMEMBRANE ACTIVATOR AND CAML INTERACTOR PROTEIN; and B CELL MATURATION ANTIGEN.
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.
The type species of LENTIVIRUS and the etiologic agent of AIDS. It is characterized by its cytopathic effect and affinity for the T4-lymphocyte.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
Clinical sign or symptom manifested as debility, or lack or loss of strength and energy.
A group of compounds consisting in part of two rings sharing one atom (usually a carbon) in common.
A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. It also hydrolyzes peptide amides. (From Enzyme Nomenclature, 1992) EC 3.4.21.62.
The process of intracellular viral multiplication, consisting of the synthesis of PROTEINS; NUCLEIC ACIDS; and sometimes LIPIDS, and their assembly into a new infectious particle.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A member of the tumor necrosis factor receptor superfamily found on mature B-LYMPHOCYTES. It has specificity for B CELL ACTIVATING FACTOR and TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13. Signaling of the receptor occurs through its association with TNF RECEPTOR-ASSOCIATED FACTORS.
A plant family of the order Sapindales, subclass Rosidae, class Magnoliopsida.
A subtype of mitochondrial ADP, ATP translocase found primarily in heart muscle (MYOCARDIUM) and skeletal muscle (MUSCLE, SKELETAL).
A macrolide isolated from the culture broth of a strain of Streptomyces tsukubaensis that has strong immunosuppressive activity in vivo and prevents the activation of T-lymphocytes in response to antigenic or mitogenic stimulation in vitro.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Oxazepines are a class of benzodiazepine-like drugs that have a oxazepine ring in their chemical structure, and are used as anticonvulsants and anxiolytics due to their ability to modulate GABAergic neurotransmission.
The infective system of a virus, composed of the viral genome, a protein core, and a protein coat called a capsid, which may be naked or enclosed in a lipoprotein envelope called the peplos.
Proteins coded by the retroviral gag gene. The products are usually synthesized as protein precursors or POLYPROTEINS, which are then cleaved by viral proteases to yield the final products. Many of the final products are associated with the nucleoprotein core of the virion. gag is short for group-specific antigen.
Established cell cultures that have the potential to propagate indefinitely.
A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Agents that suppress immune function by one of several mechanisms of action. Classical cytotoxic immunosuppressants act by inhibiting DNA synthesis. Others may act through activation of T-CELLS or by inhibiting the activation of HELPER CELLS. While immunosuppression has been brought about in the past primarily to prevent rejection of transplanted organs, new applications involving mediation of the effects of INTERLEUKINS and other CYTOKINES are emerging.
A subtype of thioredoxins found primarily in CHLOROPLASTS.
A tumor necrosis factor superfamily member that plays a role in the regulation of B-LYMPHOCYTE survival. It occurs as a membrane-bound protein that is cleaved to release an biologically active soluble form with specificity to TRANSMEMBRANE ACTIVATOR AND CAML INTERACTOR PROTEIN; B-CELL ACTIVATION FACTOR RECEPTOR; and B-CELL MATURATION ANTIGEN.
The voltage difference, normally maintained at approximately -180mV, across the INNER MITOCHONDRIAL MEMBRANE, by a net movement of positive charge across the membrane. It is a major component of the PROTON MOTIVE FORCE in MITOCHONDRIA used to drive the synthesis of ATP.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
A family of RNA plant viruses infecting disparate plant families. They are transmitted by specific aphid vectors. There are three genera: LUTEOVIRUS; Polerovirus; and Enamovirus.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The family of Old World monkeys and baboons consisting of two subfamilies: CERCOPITHECINAE and COLOBINAE. They are found in Africa and part of Asia.
Proteins prepared by recombinant DNA technology.
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).
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The two lipoprotein layers in the MITOCHONDRION. The outer membrane encloses the entire mitochondrion and contains channels with TRANSPORT PROTEINS to move molecules and ions in and out of the organelle. The inner membrane folds into cristae and contains many ENZYMES important to cell METABOLISM and energy production (MITOCHONDRIAL ATP SYNTHASE).

Cyclophilin A is a secreted growth factor induced by oxidative stress. (1/314)

Reactive oxygen species have been implicated in the pathogenesis of atherosclerosis, hypertension, and restenosis, in part by promoting vascular smooth muscle cell (VSMC) growth. Many VSMC growth factors are secreted by VSMC and act in an autocrine manner. Here we demonstrate that cyclophilin A (CyPA), a member of the immunophilin family, is secreted by VSMCs in response to oxidative stress and mediates extracellular signal-regulated kinase (ERK1/2) activation and VSMC growth by reactive oxygen species. Human recombinant CyPA can mimic the effects of secreted CyPA to stimulate ERK1/2 and cell growth. The peptidyl-prolyl isomerase activity is required for ERK1/2 activation by CyPA. In vivo, CyPA expression and secretion are increased by oxidative stress and vascular injury. These findings are the first to identify CyPA as a secreted redox-sensitive mediator, establish CyPA as a VSMC growth factor, and suggest an important role for CyPA and enzymes with peptidyl-prolyl isomerase activity in the pathogenesis of vascular diseases.  (+info)

Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells. (2/314)

The human immunodeficiency virus type 1 (HIV-1) Gag polyprotein binds most members of the cyclophilin family of peptidyl-prolyl isomerases. Of 15 known human cyclophilins, cyclophilin A (CypA) has been the focus of investigation because it was detected in HIV-1 virions. To determine whether CypA promotes HIV-1 replication, we deleted the gene encoding CypA (PPIA) in human CD4(+) T cells by homologous recombination. HIV-1 replication in PPIA(-/-) cells was decreased and not inhibited further by cyclosporin or gag mutations that disrupt Gag's interaction with cyclophilins, indicating that no other cyclophilin family members promote HIV-1 replication. The defective replication phenotype was specific for wild-type HIV-1 since HIV-2/SIV isolates, as well as HIV-1 bearing a gag mutation that confers cyclosporin resistance, replicated the same in PPIA(+/+) and PPIA(-/-) cells. Stable re-expression of CypA in PPIA(-/-) cells restored HIV-1 replication to an extent that correlated with steady-state levels of CypA. Finally, virions from PPIA(-/-) cells possessed no obvious biochemical abnormalities but were less infectious than virions from wild-type cells. These data formally demonstrate that CypA regulates the infectivity of HIV-1 virions.  (+info)

Palmitoylation of caveolin-1 in endothelial cells is post-translational but irreversible. (3/314)

Caveolin-1 is a palmitoylated protein involved in assembly of signaling molecules in plasma membrane subdomains termed caveolae and in intracellular cholesterol transport. Three cysteine residues in the C terminus of caveolin-1 are subject to palmitoylation, which is not necessary for caveolar targeting of caveolin-1. Protein palmitoylation is a post-translational and reversible modification that may be regulated and that in turn may regulate conformation, membrane association, protein-protein interactions, and intracellular localization of the target protein. We have undertaken a detailed analysis of [(3)H]palmitate incorporation into caveolin-1 in aortic endothelial cells. The linkage of palmitate to caveolin-1 was hydroxylamine-sensitive and thus presumably a thioester bond. However, contrary to expectations, palmitate incorporation was blocked completely by the protein synthesis inhibitors cycloheximide and puromycin. In parallel experiments to show specificity, palmitoylation of aortic endothelial cell-specific nitric-oxide synthase was unaffected by these reagents. Inhibitors of protein trafficking, brefeldin A and monensin, blocked caveolin-1 palmitoylation, indicating that the modification was not cotranslational but rather required caveolin-1 transport from the endoplasmic reticulum and Golgi to the plasma membrane. In addition, immunophilin chaperones that form complexes with caveolin-1, i.e. FK506-binding protein 52, cyclophilin A, and cyclophilin 40, were not necessary for caveolin-1 palmitoylation because agents that bind immunophilins did not inhibit palmitoylation. Pulse-chase experiments showed that caveolin-1 palmitoylation is essentially irreversible because the release of [(3)H]palmitate was not significant even after 24 h. These results show that [(3)H]palmitate incorporation is limited to newly synthesized caveolin-1, not because incorporation only occurs during synthesis but because the continuous presence of palmitate on caveolin-1 prevents subsequent repalmitoylation.  (+info)

Structural consequences of cyclophilin A binding on maturational refolding in human immunodeficiency virus type 1 capsid protein. (4/314)

While several cellular proteins are incorporated in the human immunodeficiency virus type 1 virion, cyclophilin (CyP) A is the only one whose absence has been demonstrated to impair infectivity. Incorporation of the cytosolic protein results from interaction with a highly exposed Pro-rich loop in the N-terminal region of the capsid (CA) domain of the precursor polyprotein, Pr55(Gag). Even when prevented from interacting with CyP A, Pr55Gag still forms particles that proceed to mature into morphologically wild-type virions, suggesting that CyP A influences a postassembly event. The nature of this CyP A influence has yet to be elucidated. Here, we show that while CyP A binds both Gag and mature CA proteins, the two binding interactions are actually different. Tryptophan 121 (W121) in CyP A distinguished the two proteins: a phenylalanine substitution (W121F) impaired binding of mature CA protein but not of Gag. This indicates the occurrence of a maturation-dependent switch in the conformation of the Pro-rich loop. A structural consequence of Gag binding to CyP A was to block this maturational refolding, resulting in a 24-kDa CA protein retaining the immature Pro-rich loop conformation. Using trypsin as a structure probe, we demonstrate that the conformation of the C-terminal region in mature CA is also a product of maturational refolding. Binding to wild-type CyP A altered this conformation, as indicated by a reduction in the accessibility of Cys residue(s) in the region to chemical modification. Hence, the end result of binding to CyP A, whether the Pro-rich loop is in the context of Gag or mature CA protein, is a structurally modified mature CA protein. The postassembly role of CyP A may be mediated through these modified mature CA proteins.  (+info)

Sanglifehrin A, a novel cyclophilin-binding immunosuppressant, inhibits IL-2-dependent T cell proliferation at the G1 phase of the cell cycle. (5/314)

Sanglifehrin A (SFA) is a novel immunosuppressive natural product that binds to cyclophilin but is structurally distinct from cyclosporin A (CsA). We have investigated the cellular and molecular mechanisms of the action of SFA in T lymphocytes. We show that SFA inhibits T cell proliferation induced by IL-2 with an IC(50) of 200 nM. Distinct from CsA, which also binds to cyclophilin, SFA does not affect calcium-dependent IL-2 production, although SFA enhanced IL-2 gene transcription in the same cells. SFA blocks T cell proliferation induced by IL-2 in G(1) with no appreciable effect on IL-2 receptor expression in a manner similar to that of the immunosuppressant rapamycin. Unlike rapamycin, however, SFA has no effect on the phosphorylation or enzymatic activity of p70(s6k) kinase, distinguishing SFA from rapamycin in their mode of action. SFA inhibits hyperphosphorylation of Rb and the activity of cyclin E-cyclin-dependent kinase 2 on IL-2 signaling. These results suggest that SFA has a novel mode of action in comparison with CsA, FK506, and rapamycin, and that its use as a molecular probe may lead to the discovery of a novel target involved in T cell activation.  (+info)

CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A. (6/314)

Cyclophilin A (CyPA) is specifically incorporated into the virions of HIV-1 and has been shown to enhance significantly an early step of cellular HIV-1 infection. Our preliminary studies implicated CD147 as a receptor for extracellular CyPA. Here, we demonstrate a role for CyPA-CD147 interaction during the early steps of HIV-1 infection. Expression of human CD147 increased infection by HIV-1 under one-cycle conditions. However, susceptibility to infection by viruses lacking CyPA (simian immunodeficiency virus or HIV-1 produced in the presence of cyclosporin A) was unaffected by CD147. Virus-associated CyPA coimmunoprecipitated with CD147 from infected cells. Antibody to CD147 inhibited HIV-1 entry as evidenced by the delay in translocation of the HIV-1 core proteins from the membrane and inhibition of viral reverse transcription. Viruses whose replication did not require CyPA (SIV or mutant HIV-1) were resistant to the inhibitory effect of anti-CD147 antibody. These results suggest that HIV-1 entry depends on an interaction between virus-associated CyPA and CD147 on a target cell.  (+info)

A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding. (7/314)

The folding of apo-pseudoazurin, a 123-residue, predominantly beta-sheet protein with a complex Greek key topology, has been investigated using several biophysical techniques. Kinetic analysis of refolding using far- and near-ultraviolet circular dichroism (UV CD) shows that the protein folds slowly to the native state with rate constants of 0.04 and 0.03 min(-1), respectively, at pH 7.0 and at 15 degrees C. This process has an activation enthalpy of approximately 90 kJ/mole and is catalyzed by cyclophilin A, indicating that folding is limited by trans-cis proline isomerization, presumably around the Xaa-Pro 20 bond that is in the cis isomer in the native state. Before proline isomerization, an intermediate accumulates during folding. This species has a substantial signal in the far-UV CD, a nonnative signal in the near-UV CD, exposed hydrophobic surfaces (judged by 1-anilino naphthalenesulphonate binding), a noncooperative denaturation transition, and a dynamic structure (revealed by line broadening on the nuclear magnetic resonance time scale). We compare the properties of this intermediate with partially folded states of other proteins and discuss its role in folding of this complex Greek key protein.  (+info)

Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity. (8/314)

Six distinct peroxiredoxin (Prx) proteins (Prx I-VI) from distinct genes have been identified in mammalian tissues. Prxs are members of a group of peroxidases that have conserved reactive cysteine residue(s) in the active site(s). An immediate physiological electron donor for the peroxidase catalysis for five Prx proteins (Prx I-V) has been identified as thioredoxin (Trx), but that for Prx VI (1-Cys Prx) is still unclear. To identify an immediate electron donor and a binding protein for Prx VI, we performed a Prx VI protein overlay assay. A 20-kDa binding protein was identified by the Prx VI protein overlay assay with flow-through fractions from a High-Q column with rat lung crude extracts. Using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF) and MS-Fit, we identified the 20-kDa Prx VI-binding protein as a cyclophilin A (CyP-A). The binding of recombinant human CyP-A (hCyP-A) to Prx VI was confirmed by using the hCyP-A protein overlay assay and Western immunoblot analysis with hCyP-A-specific antibodies. hCyP-A enhanced the antioxidant activity of Prx VI, as well as the other known mammalian Prx isotypes. hCyP-A supported antioxidant activity of Prx II and Prx VI both against thiol (dithiothreitol)-containing metal-catalyzed oxidation (MCO) systems and ascorbate-containing MCO systems. Prx II was reduced by hCyP-A without help from any other reductant, and the reduction was cyclosporin A-independent. These results strongly suggest that CyP-A not only binds to Prx proteins but also supports its peroxidase activity as an immediate electron donor. In addition, Cys(115) and Cys(161) of hCyP-A were found to be involved in the activation and the reduction of Prx.  (+info)

Cyclophilin A is a type of intracellular protein that belongs to the immunophilin family. It has peptidyl-prolyl cis-trans isomerase activity, which means it helps in folding and assembling other proteins by catalyzing the cis-trans isomerization of proline residues.

Cyclophilin A is widely distributed in various tissues and cells, including immune cells such as T lymphocytes. It plays a crucial role in the immune system by binding to and activating the immunosuppressive drug cyclosporine A, which is used to prevent rejection of transplanted organs.

In addition to its role in protein folding and immunosuppression, Cyclophilin A has been implicated in various cellular processes such as signal transduction, gene expression, and apoptosis (programmed cell death). It also plays a role in viral replication, particularly of HIV-1, the virus that causes AIDS.

Cyclophilins are a family of proteins that have peptidyl-prolyl isomerase activity, which means they help with the folding and functioning of other proteins in cells. They were first identified as binding proteins for the immunosuppressive drug cyclosporine A, hence their name.

Cyclophilins are found in various organisms, including humans, and play important roles in many cellular processes such as signal transduction, protein trafficking, and gene expression. In addition to their role in normal cell function, cyclophilins have also been implicated in several diseases, including viral infections, cancer, and neurodegenerative disorders.

In medicine, the most well-known use of cyclophilins is as a target for immunosuppressive drugs used in organ transplantation. Cyclosporine A and its derivatives work by binding to cyclophilins, which inhibits their activity and subsequently suppresses the immune response.

Peptidylprolyl Isomerase (PPIase) is an enzyme that catalyzes the cis-trans isomerization of peptidyl-prolyl bonds in proteins. This isomerization process, which involves the rotation around a proline bond, is a rate-limiting step in protein folding and can be a significant factor in the development of various diseases, including neurodegenerative disorders and cancer.

PPIases are classified into three families: cyclophilins, FK506-binding proteins (FKBPs), and parvulins. These enzymes play important roles in protein folding, trafficking, and degradation, as well as in signal transduction pathways and the regulation of gene expression.

Inhibitors of PPIases have been developed as potential therapeutic agents for various diseases, including transplant rejection, autoimmune disorders, and cancer. For example, cyclosporine A and FK506 are immunosuppressive drugs that inhibit cyclophilins and FKBPs, respectively, and are used to prevent transplant rejection.

Amino acid isomerases are a class of enzymes that catalyze the conversion of one amino acid stereoisomer to another. These enzymes play a crucial role in the metabolism and biosynthesis of amino acids, which are the building blocks of proteins.

Amino acids can exist in two forms, called L- and D-stereoisomers, based on the spatial arrangement of their constituent atoms around a central carbon atom. While most naturally occurring amino acids are of the L-configuration, some D-amino acids are also found in certain proteins and peptides, particularly in bacteria and lower organisms.

Amino acid isomerases can convert one stereoisomer to another by breaking and reforming chemical bonds in a process that requires energy. This conversion can be important for the proper functioning of various biological processes, such as protein synthesis, neurotransmitter metabolism, and immune response.

Examples of amino acid isomerases include proline racemase, which catalyzes the interconversion of L-proline and D-proline, and serine hydroxymethyltransferase, which converts L-serine to D-serine. These enzymes are essential for maintaining the balance of amino acids in living organisms and have potential therapeutic applications in various diseases, including neurodegenerative disorders and cancer.

Cyclosporine is a medication that belongs to a class of drugs called immunosuppressants. It is primarily used to prevent the rejection of transplanted organs, such as kidneys, livers, and hearts. Cyclosporine works by suppressing the activity of the immune system, which helps to reduce the risk of the body attacking the transplanted organ.

In addition to its use in organ transplantation, cyclosporine may also be used to treat certain autoimmune diseases, such as rheumatoid arthritis and psoriasis. It does this by suppressing the overactive immune response that contributes to these conditions.

Cyclosporine is available in capsule, oral solution, and injectable forms. Common side effects of the medication include kidney problems, high blood pressure, tremors, headache, and nausea. Long-term use of cyclosporine can also increase the risk of certain types of cancer and infections.

It is important to note that cyclosporine should only be used under the close supervision of a healthcare provider, as it requires regular monitoring of blood levels and kidney function.

Immunophilins are a group of intracellular proteins that have peptidyl-prolyl isomerase (PPIase) activity, which enables them to catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. They play crucial roles in protein folding, trafficking, and assembly, as well as in immunoregulation and signal transduction processes.

Two major classes of immunophilins are FK506-binding proteins (FKBPs) and cyclophilins. These proteins can bind to immunosuppressive drugs like FK506 (tacrolimus) and cyclosporin A, respectively, forming complexes that inhibit the activity of calcineurin, a phosphatase involved in T-cell activation. This interaction leads to an inhibition of immune responses and is exploited in transplantation medicine to prevent graft rejection.

Immunophilins also participate in various cellular processes, such as protein trafficking, neuroprotection, and regulation of gene expression, by interacting with other proteins or acting as chaperones during protein folding. Dysregulation of immunophilin function has been implicated in several diseases, including cancer, neurological disorders, and viral infections.

Cyclosporins are a group of cyclic undecapeptides that have immunosuppressive properties. The most well-known and widely used cyclosporin is cyclosporine A, which is commonly used in organ transplantation to prevent rejection. It works by inhibiting the activation of T-cells, a type of white blood cell that plays a central role in the immune response. By suppressing the activity of T-cells, cyclosporine A reduces the risk of an immune response against the transplanted organ.

Cyclosporins are also used in the treatment of autoimmune diseases, such as rheumatoid arthritis and psoriasis, where they help to reduce inflammation and prevent damage to tissues. Like all immunosuppressive drugs, cyclosporins can increase the risk of infection and cancer, so they must be used with caution and under close medical supervision.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

CD147 (also known as basigin or EMMPRIN) is a transmembrane protein that belongs to the immunoglobulin superfamily. It is widely expressed on various cell types including immune cells, epithelial cells, and endothelial cells. CD147 plays important roles in several biological processes such as cell adhesion, migration, and activation of matrix metalloproteinases (MMPs), which are enzymes involved in extracellular matrix remodeling.

CD147 can also function as an antigen, a molecule that is recognized by the immune system and can stimulate an immune response. CD147 has been identified as a receptor for the cyclophilin A protein of several enveloped viruses, including HIV-1, dengue virus, and hepatitis C virus. The interaction between CD147 and these viral proteins is important for viral entry into host cells and can also modulate the immune response to infection.

In addition, CD147 has been implicated in various pathological conditions such as cancer, inflammation, and autoimmune diseases. It has been shown to promote tumor growth, invasion, and metastasis, and its expression is often upregulated in various types of cancer. CD147 has also been found to contribute to the pathogenesis of several inflammatory and autoimmune diseases, including rheumatoid arthritis, multiple sclerosis, and lupus erythematosus.

Overall, CD147 is a multifunctional protein that can act as an antigen and play important roles in various biological processes, pathological conditions, and infectious diseases.

Mitochondrial membrane transport proteins are a type of integral membrane proteins located in the inner and outer mitochondrial membranes. They play a crucial role in the regulation of molecule exchange between the cytosol and the mitochondrial matrix, allowing only specific ions and molecules to pass through while maintaining the structural and functional integrity of the mitochondria.

The inner mitochondrial membrane transport proteins, also known as the mitochondrial carrier proteins or the solute carriers, are a family of about 50 different types of proteins that facilitate the passage of various metabolites, such as nucleotides, amino acids, fatty acids, and inorganic ions (like calcium, sodium, and potassium). These transport proteins usually function as exchangers or uniporters, moving one type of solute in one direction in exchange for another type of solute or a proton.

The outer mitochondrial membrane is more permeable than the inner membrane due to the presence of voltage-dependent anion channels (VDACs) and other porins that allow small molecules, ions, and metabolites to pass through. VDACs are the most abundant proteins in the outer mitochondrial membrane and play a significant role in controlling the flow of metabolites between the cytosol and the intermembrane space.

In summary, mitochondrial membrane transport proteins are essential for maintaining the proper functioning of mitochondria by regulating the movement of molecules across the inner and outer membranes. They facilitate the exchange of nutrients, metabolites, and ions required for oxidative phosphorylation, energy production, and other cellular processes.

The Transmembrane Activator and CAML Interactor protein (also known as TACI or TNFRSF13B) is a type I transmembrane protein that belongs to the tumor necrosis factor receptor superfamily. It is involved in the regulation of immune responses, specifically in the activation and differentiation of B cells, which are a type of white blood cell that plays a central role in the humoral immune response.

TACI has two main ligands, or binding partners: A Proliferation-Inducing Ligand (APRIL) and B cell Activating Factor (BAFF). These ligands bind to TACI and activate downstream signaling pathways that lead to the activation and differentiation of B cells.

Mutations in the TACI gene have been associated with various immune disorders, including common variable immunodeficiency (CVID), a primary immunodeficiency disorder characterized by low levels of antibodies and recurrent infections. Additionally, variations in the TACI gene have been linked to an increased risk of developing autoimmune diseases such as systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA).

Tacrolimus binding proteins, also known as FK506 binding proteins (FKBPs), are a group of intracellular proteins that bind to the immunosuppressive drug tacrolimus (also known as FK506) and play a crucial role in its mechanism of action. Tacrolimus is primarily used in organ transplantation to prevent rejection of the transplanted organ.

FKBPs are a family of peptidyl-prolyl cis-trans isomerases (PPIases) that catalyze the conversion of proline residues from their cis to trans conformations in proteins, thereby regulating protein folding and function. FKBP12, a member of this family, has a high affinity for tacrolimus and forms a complex with it upon entry into the cell.

The formation of the tacrolimus-FKBP12 complex inhibits calcineurin, a serine/threonine phosphatase that plays a critical role in T-cell activation. Calcineurin inhibition prevents the dephosphorylation and nuclear translocation of the transcription factor NFAT (nuclear factor of activated T-cells), thereby blocking the expression of genes involved in T-cell activation, proliferation, and cytokine production.

In summary, tacrolimus binding proteins are intracellular proteins that bind to tacrolimus and inhibit calcineurin, leading to the suppression of T-cell activation and immune response, which is essential in organ transplantation and other immunological disorders.

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.

Aotidae is a family of nocturnal primates also known as lorises or slow lorises. They are native to Southeast Asia and are characterized by their small size, round head, large eyes, and a wet-nosed face. Slow lorises have a toxic bite, which they use to defend themselves against predators. They are currently listed as vulnerable or endangered due to habitat loss and hunting.

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.

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.

Tumor Necrosis Factor Ligand Superfamily Member 13 (TNFSF13), also known as APRIL (A Proliferation-Inducing Ligand), is a type II transmembrane protein and a member of the tumor necrosis factor (TNF) ligand superfamily. It plays a crucial role in the immune system, particularly in the activation, proliferation, and differentiation of B cells, which are key players in the humoral immune response.

TNFSF13 is expressed by various cell types, including macrophages, dendritic cells, and neutrophils. It binds to two receptors: TACI (Transmembrane Activator and Calcium Modulator and Cyclophilin Ligand Interactor) and BCMA (B-cell Maturation Antigen), which are primarily found on the surface of B cells. The interaction between TNFSF13 and its receptors promotes the survival, proliferation, and differentiation of B cells into plasma cells, ultimately leading to increased antibody production.

Dysregulation of TNFSF13 has been implicated in several autoimmune and inflammatory diseases, such as rheumatoid arthritis, systemic lupus erythematosus (SLE), and multiple sclerosis (MS). Therefore, targeting this molecule or its signaling pathways has been a focus of research for the development of novel therapeutic strategies in these conditions.

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.

HIV-1 (Human Immunodeficiency Virus type 1) is a species of the retrovirus genus that causes acquired immunodeficiency syndrome (AIDS). It is primarily transmitted through sexual contact, exposure to infected blood or blood products, and from mother to child during pregnancy, childbirth, or breastfeeding. HIV-1 infects vital cells in the human immune system, such as CD4+ T cells, macrophages, and dendritic cells, leading to a decline in their numbers and weakening of the immune response over time. This results in the individual becoming susceptible to various opportunistic infections and cancers that ultimately cause death if left untreated. HIV-1 is the most prevalent form of HIV worldwide and has been identified as the causative agent of the global AIDS pandemic.

Proline is an organic compound that is classified as a non-essential amino acid, meaning it can be produced by the human body and does not need to be obtained through the diet. It is encoded in the genetic code as the codon CCU, CCC, CCA, or CCG. Proline is a cyclic amino acid, containing an unusual secondary amine group, which forms a ring structure with its carboxyl group.

In proteins, proline acts as a structural helix breaker, disrupting the alpha-helix structure and leading to the formation of turns and bends in the protein chain. This property is important for the proper folding and function of many proteins. Proline also plays a role in the stability of collagen, a major structural protein found in connective tissues such as tendons, ligaments, and skin.

In addition to its role in protein structure, proline has been implicated in various cellular processes, including signal transduction, apoptosis, and oxidative stress response. It is also a precursor for the synthesis of other biologically important compounds such as hydroxyproline, which is found in collagen and elastin, and glutamate, an excitatory neurotransmitter in the brain.

Asthenia is a medical term that refers to a condition of unusual physical weakness or exhaustion that is not relieved by rest. It can be a symptom of various underlying health issues, such as infections, neurological disorders, endocrine diseases, and mental health conditions. Asthenia should not be confused with general fatigue or tiredness, as it is more severe, persistent, and debilitating.

The term "asthenia" comes from the Greek words "a" (without) and "sthenos" (strength), which together mean "without strength." In medical contexts, asthenia is often used to describe a significant decrease in muscle strength or energy levels that interferes with daily activities and reduces the overall quality of life.

Asthenia can manifest as a general feeling of weakness, fatigue, lethargy, or lack of stamina. In some cases, it may be accompanied by other symptoms such as dizziness, lightheadedness, headaches, irritability, and depression. Depending on the underlying cause, asthenia may be treated with various interventions, including medication, lifestyle changes, physical therapy, or counseling.

"Spiro compounds" are not specifically classified as medical terms, but they are a concept in organic chemistry. However, I can provide a general definition:

Spiro compounds are a type of organic compound that contains two or more rings, which share a single common atom, known as the "spiro center." The name "spiro" comes from the Greek word for "spiral" or "coiled," reflecting the three-dimensional structure of these molecules.

The unique feature of spiro compounds is that they have at least one spiro atom, typically carbon, which is bonded to four other atoms, two of which belong to each ring. This arrangement creates a specific geometry where the rings are positioned at right angles to each other, giving spiro compounds distinctive structural and chemical properties.

While not directly related to medical terminology, understanding spiro compounds can be essential in medicinal chemistry and pharmaceutical research since these molecules often exhibit unique biological activities due to their intricate structures.

Subtilisin is not strictly a medical term, but rather a term used in biochemistry and microbiology. It refers to a group of proteolytic enzymes (proteases) that are produced by certain bacteria, particularly Bacillus subtilis. These enzymes have the ability to break down other proteins into smaller peptides or individual amino acids by cleaving specific peptide bonds.

In a medical context, subtilisin might be mentioned in relation to its use in various commercial products such as detergents and contact lens cleaning solutions, where it helps to break down protein-based stains or deposits. Additionally, subtilisins have been explored for their potential applications in therapeutics, including the treatment of certain diseases caused by protein misfolding or aggregation, like cystic fibrosis and Alzheimer's disease.

However, it is important to note that direct medical definitions of 'subtilisin' are limited, as it primarily functions within the realms of biochemistry and microbiology.

Virus replication is the process by which a virus produces copies or reproduces itself inside a host cell. This involves several steps:

1. Attachment: The virus attaches to a specific receptor on the surface of the host cell.
2. Penetration: The viral genetic material enters the host cell, either by invagination of the cell membrane or endocytosis.
3. Uncoating: The viral genetic material is released from its protective coat (capsid) inside the host cell.
4. Replication: The viral genetic material uses the host cell's machinery to produce new viral components, such as proteins and nucleic acids.
5. Assembly: The newly synthesized viral components are assembled into new virus particles.
6. Release: The newly formed viruses are released from the host cell, often through lysis (breaking) of the cell membrane or by budding off the cell membrane.

The specific mechanisms and details of virus replication can vary depending on the type of virus. Some viruses, such as DNA viruses, use the host cell's DNA polymerase to replicate their genetic material, while others, such as RNA viruses, use their own RNA-dependent RNA polymerase or reverse transcriptase enzymes. Understanding the process of virus replication is important for developing antiviral therapies and vaccines.

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.

B-cell maturation antigen (BCMA) is a protein that is primarily found on the surface of mature B cells and plasma cells. It plays a crucial role in the survival and growth of these cells. BCMA is also a target for immunotherapy in certain types of cancer, such as multiple myeloma, because it is often overexpressed on the surface of malignant plasma cells.

Immunotherapies that target BCMA include monoclonal antibodies, bispecific antibodies, and chimeric antigen receptor (CAR) T-cell therapies. These treatments work by binding to BCMA on the surface of cancer cells, which can then trigger an immune response to destroy the cancer cells.

It's important to note that while these therapies have shown promise in clinical trials, they are still being studied and may have potential side effects or limitations.

I'm sorry for any confusion, but "Hippocastanaceae" is not a medical term. It is a taxonomic category used in botany to classify a family of plants, specifically the horse chestnut family. The family includes trees and shrubs that have palmate leaves and large, inflated seed pods containing one to three seeds.

If you have any questions related to medical terminology or health-related topics, I'd be happy to help!

Adenine Nucleotide Translocator 1 (ANT1) is a protein found in the inner mitochondrial membrane of cells. It plays a crucial role in cellular energy metabolism by facilitating the exchange of adenosine diphosphate (ADP) and adenosine triphosphate (ATP) across the mitochondrial membrane.

In simpler terms, ANT1 helps to transport ATP, which is a major source of energy for cells, out of the mitochondria and exchange it for ADP, which can be converted back into ATP through cellular respiration. This process is essential for maintaining the energy balance within the cell and supporting various physiological functions.

Mutations in the gene that encodes ANT1 have been associated with certain mitochondrial disorders, such as autosomal recessive progressive external ophthalmoplegia (arPEO) and maternally inherited diabetes and deafness (MIDD). These genetic conditions can result in a range of symptoms, including muscle weakness, exercise intolerance, and neurological problems.

Tacrolimus is an immunosuppressant drug that is primarily used to prevent the rejection of transplanted organs. It works by inhibiting the activity of T-cells, which are a type of white blood cell that plays a central role in the body's immune response. By suppressing the activity of these cells, tacrolimus helps to reduce the risk of an immune response being mounted against the transplanted organ.

Tacrolimus is often used in combination with other immunosuppressive drugs, such as corticosteroids and mycophenolate mofetil, to provide a comprehensive approach to preventing organ rejection. It is available in various forms, including capsules, oral solution, and intravenous injection.

The drug was first approved for use in the United States in 1994 and has since become a widely used immunosuppressant in transplant medicine. Tacrolimus is also being studied as a potential treatment for a variety of other conditions, including autoimmune diseases and cancer.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

Oxazepines are a class of benzodiazepine-related drugs that have a chemical structure containing an oxazepine ring. They act as antagonists or inverse agonists at the benzodiazepine binding site on GABA(A) receptors and are used in the treatment of anxiety disorders, insomnia, and seizures. Some examples of oxazepines include lorazepam, oxazepam, and temazepam. It is important to note that while they share some similarities with benzodiazepines, their mechanism of action and clinical effects can be different.

A virion is the complete, infectious form of a virus outside its host cell. It consists of the viral genome (DNA or RNA) enclosed within a protein coat called the capsid, which is often surrounded by a lipid membrane called the envelope. The envelope may contain viral proteins and glycoproteins that aid in attachment to and entry into host cells during infection. The term "virion" emphasizes the infectious nature of the virus particle, as opposed to non-infectious components like individual capsid proteins or naked viral genome.

"Gene products, GAG" refer to the proteins that are produced by the GAG (Group-specific Antigen) gene found in retroviruses, such as HIV (Human Immunodeficiency Virus). These proteins play a crucial role in the structure and function of the viral particle or virion.

The GAG gene encodes for a polyprotein that is cleaved by a protease into several individual proteins, including matrix (MA), capsid (CA), and nucleocapsid (NC) proteins. These proteins are involved in the formation of the viral core, which encloses the viral RNA genome and associated enzymes required for replication.

The MA protein is responsible for binding to the host cell membrane during viral entry, while the CA protein forms the capsid shell that surrounds the viral RNA and NC protein. The NC protein binds to the viral RNA and helps to package it into the virion during assembly. Overall, GAG gene products are essential for the life cycle of retroviruses and are important targets for antiretroviral therapy in HIV-infected individuals.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

HSP90 (Heat Shock Protein 90) refers to a family of highly conserved molecular chaperones that are expressed in all eukaryotic cells. They play a crucial role in protein folding, assembly, and transport, thereby assisting in the maintenance of proper protein function and cellular homeostasis. HSP90 proteins are named for their increased expression during heat shock and other stress conditions, which helps protect cells by facilitating the refolding or degradation of misfolded proteins that can accumulate under these circumstances.

HSP90 chaperones are ATP-dependent and consist of multiple domains: a N-terminal nucleotide binding domain (NBD), a middle domain, and a C-terminal dimerization domain. They exist as homodimers and interact with a wide range of client proteins, including transcription factors, kinases, and steroid hormone receptors. By regulating the activity and stability of these client proteins, HSP90 chaperones contribute to various cellular processes such as signal transduction, cell cycle progression, and stress response. Dysregulation of HSP90 function has been implicated in numerous diseases, including cancer, neurodegenerative disorders, and infectious diseases, making it an attractive target for therapeutic intervention.

Isomerism is a term used in chemistry and biochemistry, including the field of medicine, to describe the existence of molecules that have the same molecular formula but different structural formulas. This means that although these isomers contain the same number and type of atoms, they differ in the arrangement of these atoms in space.

There are several types of isomerism, including constitutional isomerism (also known as structural isomerism) and stereoisomerism. Constitutional isomers have different arrangements of atoms, while stereoisomers have the same arrangement of atoms but differ in the spatial arrangement of their atoms in three-dimensional space.

Stereoisomerism can be further divided into subcategories such as enantiomers (mirror-image stereoisomers), diastereomers (non-mirror-image stereoisomers), and conformational isomers (stereoisomers that can interconvert by rotating around single bonds).

In the context of medicine, isomerism can be important because different isomers of a drug may have different pharmacological properties. For example, some drugs may exist as pairs of enantiomers, and one enantiomer may be responsible for the desired therapeutic effect while the other enantiomer may be inactive or even harmful. In such cases, it may be important to develop methods for producing pure enantiomers of the drug in order to maximize its efficacy and minimize its side effects.

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.

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.

Immunosuppressive agents are medications that decrease the activity of the immune system. They are often used to prevent the rejection of transplanted organs and to treat autoimmune diseases, where the immune system mistakenly attacks the body's own tissues. These drugs work by interfering with the immune system's normal responses, which helps to reduce inflammation and damage to tissues. However, because they suppress the immune system, people who take immunosuppressive agents are at increased risk for infections and other complications. Examples of immunosuppressive agents include corticosteroids, azathioprine, cyclophosphamide, mycophenolate mofetil, tacrolimus, and sirolimus.

Chloroplast thioredoxins are small, heat-stable proteins located in the chloroplasts of plant cells. They play a crucial role in regulating various metabolic processes in the chloroplast, particularly those related to photosynthesis. Thioredoxins function as electron carriers and reduce disulfide bonds in target proteins, thereby activating or deactivating their enzymatic activity.

Chloroplast thioredoxins are reduced by ferredoxin-thioredoxin reductase using electrons supplied by photosystem I during light reactions of photosynthesis. This reduction process enables chloroplast thioredoxins to regulate the activity of various enzymes involved in carbon fixation, such as Rubisco (Ribulose-1,5-bisphosphate carboxylase/oxygenase), and other metabolic processes like protein folding and degradation.

There are multiple isoforms of chloroplast thioredoxins (trx), including TrxA, TrxB, TrxC, and TrxD, each with distinct roles in regulating specific target proteins and cellular processes. The regulation of chloroplast thioredoxins and their targets is critical for maintaining optimal photosynthetic efficiency and adapting to changing environmental conditions.

B-cell activating factor (BAFF) is a type of protein belonging to the tumor necrosis factor (TNF) family. Its primary function is to stimulate and activate B cells, which are a type of white blood cell that plays a crucial role in the immune system by producing antibodies. BAFF helps to promote the survival, differentiation, and activation of B cells, thereby contributing to the adaptive immune response.

BAFF binds to its receptor, known as BAFF receptor (BAFF-R), which is expressed on the surface of B cells. This interaction leads to the activation of various signaling pathways that promote B cell survival and proliferation. Overexpression or excessive production of BAFF has been implicated in several autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus (SLE), and Sjogren's syndrome, due to the abnormal activation and expansion of B cells.

In summary, B-cell activating factor is a protein that plays an essential role in the activation and survival of B cells, which are crucial for the immune response. However, its overexpression or dysregulation can contribute to the development of autoimmune diseases.

Mitochondrial membrane potential is the electric potential difference (voltage) across the inner mitochondrial membrane. It is negative inside the mitochondria and positive outside. This electrical gradient is established by the active transport of hydrogen ions (protons) out of the mitochondrial matrix and into the intermembrane space by complexes in the electron transport chain during oxidative phosphorylation. The energy stored in this electrochemical gradient is used to generate ATP, which is the main source of energy for cellular metabolism.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

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.

Molecular chaperones are a group of proteins that assist in the proper folding and assembly of other protein molecules, helping them achieve their native conformation. They play a crucial role in preventing protein misfolding and aggregation, which can lead to the formation of toxic species associated with various neurodegenerative diseases. Molecular chaperones are also involved in protein transport across membranes, degradation of misfolded proteins, and protection of cells under stress conditions. Their function is generally non-catalytic and ATP-dependent, and they often interact with their client proteins in a transient manner.

Luteoviridae is a family of positive-strand RNA viruses that primarily infect plants. The name "luteo" comes from Latin and means "yellow," which refers to the yellowing symptoms often caused by these viruses in infected plants. The virions are non-enveloped and icosahedral in shape, with a diameter of about 25-30 nanometers.

The genome of Luteoviridae viruses is monopartite and contains one molecule of linear, single-stranded, positive-sense RNA. The genome is encapsidated within the virion and protected by a capsid protein. The genome encodes several proteins, including a readthrough protein that functions as a movement protein, allowing the virus to move from cell to cell within the plant.

Luteoviridae viruses are transmitted by aphids in a persistent, circulative manner. Once an aphid ingests virus particles while feeding on an infected plant, the virus moves through the insect's body and accumulates in its salivary glands. When the aphid feeds on a healthy plant, it injects the virus into the plant tissue along with its saliva.

Some notable members of Luteoviridae include Barley yellow dwarf virus (BYDV), Cereal yellow dwarf virus (CYDV), and Potato leafroll virus (PLRV). These viruses can cause significant economic losses in agriculture, particularly in cereal crops and potatoes.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Cercopithecidae is a family of Old World primates, which includes monkeys such as baboons, macaques, and langurs. These primates are characterized by their adaptations for arboreal or terrestrial living, and they have complex social structures. The family Cercopithecidae is divided into two subfamilies: Cercopithecinae (guenons, macaques, and langurs) and Colobinae (leaf monkeys and colobus monkeys). These primates are found in Africa and Asia, and they play important ecological roles in their environments.

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.

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.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

Mitochondrial membranes refer to the double-layered structure that surrounds the mitochondrion, an organelle found in the cells of most eukaryotes. The outer mitochondrial membrane is a smooth, porous membrane that allows small molecules and ions to pass through freely, while the inner mitochondrial membrane is highly folded and selectively permeable, controlling the movement of larger molecules and maintaining the electrochemical gradient necessary for ATP synthesis. The space between the two membranes is called the intermembrane space, and the space within the inner membrane is called the matrix. Together, these membranes play a crucial role in energy production, metabolism, and cellular homeostasis.

Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/ ... Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B ... Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is ... Cyclophilin inhibitors, such as cyclosporin, are being developed to treat neurodegenerative diseases. Cyclophilin inhibition ...
Horowitz DS, Kobayashi R, Krainer AR (Dec 1997). "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a ... Horowitz DS, Lee EJ, Mabon SA, Misteli T (Feb 2002). "A cyclophilin functions in pre-mRNA splicing". The EMBO Journal. 21 (3): ... a nuclear cyclophilin" (PDF). The Journal of Biological Chemistry. 275 (11): 7439-42. doi:10.1074/jbc.275.11.7439. PMID ... "Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide". Journal of Molecular ...
Ferreira PA, Nakayama TA, Pak WL, Travis GH (Oct 1996). "Cyclophilin-related protein RanBP2 acts as chaperone for red/green ... Ferreira PA, Yunfei C, Schick D, Roepman R (Sep 1998). "The cyclophilin-like domain mediates the association of Ran-binding ... Yi H, Friedman JL, Ferreira PA (Nov 2007). "The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the ... Ferreira PA, Hom JT, Pak WL (Sep 1995). "Retina-specifically expressed novel subtypes of bovine cyclophilin". The Journal of ...
This gene is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved ... 2005). "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60". J. Biol. Chem. 280 (30): 27866-71. doi: ... "Entrez Gene: PPIL2 peptidylprolyl isomerase (cyclophilin)-like 2". Wang BB, Hayenga KJ, Payan DG, Fisher JM (1996). " ... 2010). "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. ...
This gene encodes a member of the cyclophilin family. Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide ... Huang LL, Zhao XM, Huang CQ, Yu L, Xia ZX (Mar 2005). "Structure of recombinant human cyclophilin J, a novel member of the ... "Entrez Gene: PPIL3 peptidylprolyl isomerase (cyclophilin)-like 3". Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high ... cyclophilin)-like gene (PPIL3) from human fetal brain". Cytogenetics and Cell Genetics. 92 (3-4): 231-6. doi:10.1159/000056909 ...
This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved ... "Entrez Gene: PPIL1 peptidylprolyl isomerase (cyclophilin)-like 1". Tripodis N, Mason R, Humphray SJ, et al. (1999). "Physical ... expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain". Cytogenet Cell Genet. ...
Examples include photoisomerase and immunophilins such as cyclophilin. cis-trans-Isomerases at the U.S. National Library of ...
As a cyclophilin, PPIF binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Thus, cyclophilins may function in cardioprotection during ischemia-reperfusion injury. Currently, cyclophilin expression is ... Like other cyclophilins, PPIF forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ... It has also been referred to as, but should not be confused with, cyclophilin D (CypD), which is encoded by the PPID gene. As a ...
This gene is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved family, ... "Entrez Gene: PPIL4 peptidylprolyl isomerase (cyclophilin)-like 4". Zeng L, Zhou Z, Xu J, et al. (2002). "Molecular cloning, ... structure and expression of a novel nuclear RNA-binding cyclophilin-like gene (PPIL4) from human fetal brain". Cytogenet. Cell ...
Like other cyclophilins, PPIA forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ... Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World ... Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by ... Wei Y, Jinchuan Y, Yi L, Jun W, Zhongqun W, Cuiping W (Jun 2013). "Antiapoptotic and proapoptotic signaling of cyclophilin A in ...
As a cyclophilin, PPIB binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Price ER, Zydowsky LD, Jin MJ, Baker CH, McKeon FD, Walsh CT (Apr 1991). "Human cyclophilin B: a second cyclophilin gene ... Mikol V, Kallen J, Walkinshaw MD (1994). "X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A ... As a cyclophilin, PPIB binds cyclosporin A (CsA) and can be found within the cell or secreted by the cell. PPIB is the second ...
As a cyclophilin, PPIC binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Depletion of these two cyclophilins lead to hyperoxidation of the ER. In the brain, PPIC complexes with cyclophilin C- ... Like other cyclophilins, PPIC forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ... Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World ...
As a cyclophilin, PPID binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Thus, cyclophilins may function in cardioprotection during ischemia-reperfusion injury. Currently, cyclophilin expression is ... Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene on ... Like other cyclophilins, PPID forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ...
As a cyclophilin, PPIE also binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets ... Thus, cyclophilins may function in cardioprotection during ischemia-reperfusion injury. Currently, cyclophilin expression is ... Peptidylprolyl isomerase E (cyclophilin E), also known as PPIE, is an enzyme which in humans is encoded by the PPIE gene on ... Wang Z, Liu X, Zhao Z, Xu C, Zhang K, Chen C, Sun L, Gao GF, Ye X, Liu W (2011). "Cyclophilin E functions as a negative ...
Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK (1997). "RS cyclophilins: identification of an NK-TR1-related cyclophilin ...
... which binds cyclophilin. Both the FKBP-tacrolimus complex and the cyclosporin-cyclophilin complex inhibit a phosphatase called ... Along with cyclophilin, FKBPs belong to the immunophilin family. FKBP1A (also known as FKBP12) is notable in humans for binding ... Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL (August 1991). "Calcineurin is a common target of cyclophilin- ... constitute a family of proteins that have prolyl isomerase activity and are related to the cyclophilins in function, though not ...
Lin CL, Leu S, Lu MC, Ouyang P (2004). "Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR ... Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK (Jan 1997). "RS cyclophilins: identification of an NK-TR1-related ... "Entrez Gene: PPIG peptidylprolyl isomerase G (cyclophilin G)". Lin, Chun Lun; Leu Steve; Lu Ming Chu; Ouyang Pin (Aug 2004). " ... 2004). "The human nuclear SRcyp is a cell cycle-regulated cyclophilin". J. Biol. Chem. 279 (21): 22322-30. doi:10.1074/jbc. ...
When bound to cyclophilin B, cyclosporin A binds and inactivates the key signaling intermediate calcineurin. The protein ... Bram RJ, Crabtree GR (1994). "Calcium signalling in T cells stimulated by a cyclophilin B-binding protein". Nature. 371 (6495 ... Tovey SC, Bootman MD, Lipp P, Berridge MJ, Bram RJ (2000). "Calcium-modulating cyclophilin ligand desensitizes hormone-evoked ... Guo S, Lopez-Ilasaca M, Dzau VJ (2005). "Identification of calcium-modulating cyclophilin ligand (CAML) as transducer of ...
The Role of Cyclophilin D in learning and memory. Brush, F. Robert (2003). "Selection for Differences in avoidance Learning: ...
To the end of this, necrosis occurs by physical interaction with the PTP regulator cyclophilin D (CypD). The mitochondrial p53- ... Alam, M.R.; D. Baetz; M. Ovize (2015). "Cyclophilin D and myocardial ischemia-reperfusion injury: a fresh perspective". J Mol ...
Cyclosporin A binds to cyclophilin D to block the opening of MPTP, and thus decreases the release of protein cytochrome C, ... October 2010). "Cyclophilin D controls mitochondrial pore-dependent Ca(2+) exchange, metabolic flexibility, and propensity for ... It does this by forming a complex with cyclophilin to block the phosphatase activity of calcineurin, which in turn decreases ... This cyclosporin-cyclophilin complex inhibits calcineurin, which is normally responsible for activating the transcription of ...
... (INN), or Debio 025, DEB025, (or UNIL-025) is a cyclophilin inhibitor. Its structure is reminiscent of, and ... April 2008). "Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin ... December 2008). "Debio 025, a cyclophilin binding molecule, is highly efficient in clearing HCV replicon containing cells, ... a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy". British Journal of Pharmacology ...
Sanglifehrin is a mixed polyketide / non-ribosomal peptide natural product found to be a potent cyclophilin inhibitor and ... "Biotica nominates drug candidate, BC556, a cyclophilin inhibitor to treat Hepatitis C". www.businesswire.com. 31 October 2011. ... "NeuroVive: NeuroVive acquires highly potent, novel cyclophilin inhibitors from Biotica - Abliva". abliva.com. 11 March 2013. ...
February 2009). "Developmental shift of cyclophilin D contribution to hypoxic-ischemic brain injury". The Journal of ...
... cyclophilin mutant. Cyclosporin A is a chemical inducer of dimerization (CID) of cyclophilin. This first bump-and-hole pair was ... The bumped cyclosporin A was found to interact efficiently with the hole-modified cyclophilin mutant, but not endogenous ... cyclophilin. The orthogonal CID pair was used to inhibit calcineurin-mediated dephosphorylation of nuclear factor of activated ... engineered to improve the binding efficiency between wild type cyclosporin A and cyclophilin, thereby giving more efficient CID ...
Ferreira PA, Nakayama TA, Pak WL, Travis GH (1996). "Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin ...
Examples comprise fibronectin/long chain cytokines, NEF/SH2, cyclophilin/capsid proteins. The most well-studied example is the ...
2009). "Methods for detecting a cyclophilin B SNP associated with HERDA". Retrieved September 2, 2016. Horsetalk.co.nz: HERDA a ... "Homozygosity mapping approach identifies a missense mutation in equine cyclophilin B (PPIB) associated with HERDA in the ...
Ferreira PA, Nakayama TA, Pak WL, Travis GH (1996). "Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin ...
... is a type I integral membrane receptor that has many ligands, including the cyclophilin (CyP) proteins Cyp-A and CyP-B ... June 2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". The Journal of Biological ... June 2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". The Journal of Biological ... Yurchenko V, Constant S, Bukrinsky M (March 2006). "Dealing with the family: CD147 interactions with cyclophilins". Immunology ...
Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/ ... Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B ... Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is ... Cyclophilin inhibitors, such as cyclosporin, are being developed to treat neurodegenerative diseases. Cyclophilin inhibition ...
Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still ... Hepatitis C virus exploits cyclophilin A to evade PKR Elife. 2020 Jun 16:9:e52237. doi: 10.7554/eLife.52237. ... Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still ... Keywords: cyclophilin A; hepatitis C virus; immunology; infectious disease; inflammation; innate antiviral immunity; ...
Timeline for Protein Cyclophilin 40 from a.118.8.1: Tetratricopeptide repeat (TPR): *Protein Cyclophilin 40 from a.118.8.1: ... Protein Cyclophilin 40 from a.118.8.1: Tetratricopeptide repeat (TPR) appears in SCOP 1.59. *Protein Cyclophilin 40 from a. ... Lineage for Protein: Cyclophilin 40. *Root: SCOP 1.57 *. Class a: All alpha proteins [46456] (144 folds). ... More info for Protein Cyclophilin 40 from a.118.8.1: Tetratricopeptide repeat (TPR). ...
Crystal structure of cyclophilin D in complex with CsA analogue, JW47. ... The peptidylprolyl isomerase, cyclophilin D (CypD, PPIF), is a positive regulator of the pore, and genetic down-regulation or ... The peptidylprolyl isomerase, cyclophilin D (CypD, PPIF), is a positive regulator of the pore, and genetic down-regulation or ... Current inhibitors of peptidylprolyl isomerases show no selectivity between the tightly conserved cyclophilin paralogs and ...
The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and ... The cyclophilin-like domain (CLD) of Ran-binding protein-2 (RanBP2/Nup358) associates specifically with at least one subunit, ... "The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and ... The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and ...
Recombinant Protein Cyclophilin H, his,,Cyclophilin H, his Protein ... U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, ... Cyclophilin H, his Recombinant Protein. Product code: 32-2250. *specify in mg or ml ...
Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury. Free Radic Res. 2011 Feb; 45(2 ... "Cyclophilins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Cyclophilins" by people in this website by year, and whether " ... Cyclophilin D as a drug target. Curr Med Chem. 2003 Aug; 10(16):1485-506. ...
Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. Additionally, CyP40 ameliorated silver- ... Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. Additionally, CyP40 ameliorated silver- ... "Human Cyclophilin 40 Unravels Neurotoxic Amyloids" (2017). Molecular Medicine Faculty Publications. 259. https://digitalcommons ...
Cyclophilin inhibitors on the market or in clinical trials are cyclosporin (a natural product) or cyclosporin derivatives; the ... Mike Peel, CSO of Cypralis, said: The discovery of completely synthetic and very potent cyclophilin inhibitors that fully ... Selcias collaboration with Cypralis and Gilead delivered a set of synthetic macrocyclic cyclophilin inhibitors inspired by the ... The paper describes how novel macrocyclic non-immunosuppressive cyclophilin inhibitors, with high potency in both biochemical ...
Search for abbreviations and long forms in lifescience, always up-to-date
Ermittlung der räumlichen Struktur von an Cyclophilin gebundenem Cyclosporin A mittels isotopengefilterter ... PROTONEN-KERNRESONANZSPEKTROSKOPIE; CYCLOSPORIN-A (ANTIBIOTIKA); PEPTIDYLPROLYL-ISOMERASE, CYCLOPHILIN (ENZYME); PROTON NUCLEAR ...
Cyclophilin A - A Mediator of Cardiovascular Disease Bradford C. Berk, MD, PhD. Distinguished University Professor in Medicine, ...
Peptidyl-prolyl cis-trans isomerase, cyclophilin type (NCBI) PpiB protein (EC 5.2.1.8) 1119717 1119106 - 15466049 ... MMP1128 MMP1128 Peptidyl-prolyl cis-trans isomerase, cyclophilin type (NCBI). × Error message. *Unable to create CTools CSS ... O) COG652 , Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family (5.2.1.8) Peptidylprolyl isomerase. ...
The importance of Cyclophilins and Mps1 in cancer. / Simon Serrano, Sonia. Lund: Lund University, Faculty of Medicine, 2022. 89 ... Cyclophilin overexpression is a common event in fibrotic tissues playing a key role in different stages of the fibrotic process ... Cyclophilin overexpression is a common event in fibrotic tissues playing a key role in different stages of the fibrotic process ... Cyclophilin overexpression is a common event in fibrotic tissues playing a key role in different stages of the fibrotic process ...
Cyclophilin inhibitors. Cyclophilins (cyclophilins, Cyps) belong to the peptidyl-prolyl isomerases (PPIase) family, which are ... Cyclophilins and cyclophilin inhibitors in nidovirus replication. Virology. 2018;522:46-55 ... The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors. PLoS Pathog. ... Tanaka Y, Sato Y, Sasaki T. Suppression of coronavirus replication by cyclophilin inhibitors. Viruses. 2013;5(5):1250-1260 ...
Abstract: Peptidylprolyl isomerases (PPIase) cyclophilin A (CypA, encoded by PPIA) is a typical member of the Cyclophilin ... 摘要: Cyclophilin A (简称CypA)由PPIA(Peptidylprolyl isomerase A)基因编码,是典型的Cyclophilin家族蛋白,具有肽基脯氨酰顺反异构酶活性,在蛋白质的折叠和转运、信号转导、炎症、免疫调节、细胞凋亡 ... 脊椎动物Cyclophilin A肽基脯氨酰顺反异构酶活性及遗传变异分析 任丽倩1, 2, 刘薇
Structure/epitope analysis and IgE binding activities of three cyclophilin family proteins from Dermatophagoides pteronyssinus ... Structure/epitope analysis and IgE binding activities of three cyclophilin family proteins from Dermatophagoides pteronyssinus ...
Emerging picture of host chaperone and cyclophilin roles in RNA virus replication. / Nagy, P. D.; Wang, R. Y.; Pogany, J. et al ... Nagy PD, Wang RY, Pogany J, Hafren A, Makinen K. Emerging picture of host chaperone and cyclophilin roles in RNA virus ... Nagy, PD, Wang, RY, Pogany, J, Hafren, A & Makinen, K 2011, Emerging picture of host chaperone and cyclophilin roles in RNA ... Nagy, P. D., Wang, R. Y., Pogany, J., Hafren, A., & Makinen, K. (2011). Emerging picture of host chaperone and cyclophilin ...
Twelve of the 17 human cyclophilins and both human parvulins, but only one of the 13 human FKBPs, identified orthologues within ... whilst the cyclophilins and parvulins have evolved to perform conserved functions, the FKBPs have evolved to perform more ... multiple roles for the cyclophilins within pre-mRNA splicing and cellular signalling, and within transcription and cell cycle ... whereas the multi-domain cyclophilins appear to evolve throughout cyclophilin evolution. A comparison of their known functions ...
Endothelial Specific Redox Signalling Regulates Susceptibility to Aortic Dissection Through Endothelial Cyclophilin A secretion ... Endothelial Specific Redox Signalling Regulates Susceptibility to Aortic Dissection Through Endothelial Cyclophilin A secretion ...
CYCLOPHILIN APEPTIDE FROM THE HIV-1 CAPSID PROTEIN ...
Ontario, QC, Canada). Although normalization to Cyclophilin A was performed, RPL13 and Ubiquitin C showed similar trends and ... all values were normalized to Cyclophilin A (Table 7). The 2−ΔΔCT method was used for relative quantification of RT-qPCR ... Cyclophilin A. 5′-ACAGCTCAAAGGAGACGCGGCCCA-3′. F 5′-CCCACCGTGTTCTTCGACAT-3′. R 5′-TTTCTGCTGTCTTTGGGACCTT-3′. ...
The standard curves, multiplexed with cyclophilin, showed the following reaction efficiencies: Gimap8: , Gimap7: , Gimap4: , ... after normalization to cyclophilin. Black columns represent and grey hatched columns represent . Data is expressed as a ... To compare Gimap and Lr8 gene expression across multiple tissues, data was first normalized to cyclophilin then scaled and ... Figure 4). We observed the same expression pattern whether the data were normalized to cyclophilin or to total RNA (data not ...
Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site ... Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site ...
Launch Cyclophilins and FK506 binding protein (FKBPs) are mobile goals TKI-258 for the immunosuppressive medications ... Within steroid receptor heterocomplexes the large tetratricopeptide repeat-containing immunophilins cyclophilin 40. Within ... Individual cyclophilin 40 (CyP40; Kieffer et al 1993) and its own bovine homolog (Ratajczak et al 1993) had been cloned from ... steroid receptor heterocomplexes the large tetratricopeptide repeat-containing immunophilins cyclophilin 40 (CyP40) FKBP51 and ...
Another human protein, cyclophilin A (CypA), can shield HIV capsid from premature binding to CPSF6, which can differ in CD4+ T ... and cyclophilin A (CypA). We observe that HIV-1 infection induces higher-order CPSF6 formation, and capsid-CPSF6 complexes ... Another human protein, cyclophilin A (CypA), can shield HIV capsid from premature binding to CPSF6, which can differ in CD4+ T ... Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner. ...
Beim Quarter Horse ist HERDA mit einer Mutation im Cyclophilin B Gen (PPIB) assoziiert. Cyclophilin B ist ein Enzym, welches ... Schweizer Warmblutfohlen mit Symptomen von hereditärer dermaler Asthenie (HERDA) ohne Mutation im Cyclophilin B-Gen (PPIB). ... Schweizer Warmblutfohlen mit Symptomen von hereditärer dermaler Asthenie (HERDA) ohne Mutation im Cyclophilin B-Gen (PPIB). S. ... In the Quarter Horse, HERDA is associated with a mutation in cyclophilin B (PPIB), an enzyme involved in triple helix formation ...
... we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. ... Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. ... Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. ... we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. ...
HUMAN CYCLOPHILIN A BOUND TO A SERIES OF ACYLCIC AND MACROCYCLIC INHIBITORS - 6X3Y , canSARS ... HUMAN CYCLOPHILIN A BOUND TO A SERIES OF ACYLCIC AND MACROCYCLIC INHIBITORS ... HUMAN CYCLOPHILIN A BOUND TO A SERIES OF ACYLCIC AND MACROCYCLIC INHIBITORS ...
Huang, C. H., Chang, C. C., Kuo, C. L., Huang, C. S., Lin, C-S., & Liu, C. S. (2015). Decrease in plasma cyclophilin a ... Huang, CH, Chang, CC, Kuo, CL, Huang, CS, Lin, C-S & Liu, CS 2015, Decrease in plasma cyclophilin a concentration at 1 month ... Background: Cyclophilin A (CyPA) concentration increases in acute coronary syndrome. In an animal model of acute myocardial ... abstract = "Background: Cyclophilin A (CyPA) concentration increases in acute coronary syndrome. In an animal model of acute ...
  • Peptidylprolyl isomerases (PPIase) cyclophilin A (CypA, encoded by PPIA ) is a typical member of the Cyclophilin family and is involved in protein folding/translocation, signal transduction, inflammation, immune system regulation, apoptosis and virus replication. (chinagene.cn)
  • Human immunodeficiency virus type 1 (HIV-1) capsid binds host proteins during infection, including cleavage and polyadenylation specificity factor 6 (CPSF6) and cyclophilin A (CypA). (ox.ac.uk)
  • Another human protein, cyclophilin A (CypA), can shield HIV capsid from premature binding to CPSF6, which can differ in CD4+ T cells and macrophages. (ox.ac.uk)
  • By devising cryo-EM methodologies for exceedingly flexible and pleomorphic assemblies, we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. (ox.ac.uk)
  • Background: Cyclophilin A (CyPA) concentration increases in acute coronary syndrome. (nycu.edu.tw)
  • Cyclophilins (CYPs) are a family of proteins named after their ability to bind to ciclosporin (cyclosporin A), an immunosuppressant which is usually used to suppress rejection after internal organ transplants. (wikipedia.org)
  • Cyclophilins are intracellular proteins with the capacity to catalyse the cis/trans isomerization of the peptide bonds at the proline residues facilitating protein folding and conformational changes affecting the function of the targeted proteins. (lu.se)
  • The peptidyl-prolyl cis / trans isomerase (PPIase) class of proteins is traditionally comprised of three distinct protein families, the cyclophilins (cyclosporin A binding proteins), FKBPs (FK506 binding proteins) and parvulins, that are linked by their shared ability to catalyse the bond preceding a proline residue between its cis and trans forms. (biomedcentral.com)
  • Launch Cyclophilins and FK506 binding protein (FKBPs) are mobile goals TKI-258 for the immunosuppressive medications cyclosporin A and FK506 respectively and screen a peptidyl- prolyl isomerase (PPIase) function that's thought to catalyze proteins folding (Galat and Metcalfe 1995). (techuniq.com)
  • Cyclophilin inhibitors, such as cyclosporin, are being developed to treat neurodegenerative diseases. (wikipedia.org)
  • Current inhibitors of peptidylprolyl isomerases show no selectivity between the tightly conserved cyclophilin paralogs and exhibit significant off-target effects, immunosuppression, and toxicity. (rcsb.org)
  • Ongar, UK, 10th February 2017 / Sciad Newswire / Selcia , with colleagues from Cypralis and Gilead Sciences Inc., have published in the Journal of Medicinal Chemistry a novel strategy of structural simplification of a natural product to generate synthetically tractable cyclophilin inhibitors for the treatment of HCV. (sciad.com)
  • Selcia's collaboration with Cypralis and Gilead delivered a set of synthetic macrocyclic cyclophilin inhibitors inspired by the core structure of the natural product sanglifehrin A. (sciad.com)
  • The paper describes how novel macrocyclic non-immunosuppressive cyclophilin inhibitors, with high potency in both biochemical and antiviral assays were generated by employing structure based drug design, modern synthetic methods and deep understanding of the property profile required of a successful drug. (sciad.com)
  • Mike Peel, CSO of Cypralis, said: 'The discovery of completely synthetic and very potent cyclophilin inhibitors that fully reproduce the biology of a semi-synthetic natural product lead is a major breakthrough in this field. (sciad.com)
  • Cyclophilin inhibitors restrict Middle East respiratory syndrome coronavirus via interferon-λ in vitro and in mice. (bvsalud.org)
  • Liqian Ren, Wei Liu, Wenbo Li, Wenjun Liu, Lei Sun. Peptidylprolyl cis/trans isomerase activity and molecular evolution of vertebrate Cyclophilin A[J]. Hereditas(Beijing), 2016, 38(8): 736-745. (chinagene.cn)
  • Host cyclophilins (Cyps) have been implicated in viral evasion of host antiviral responses, although the mechanisms are still unclear. (nih.gov)
  • Cyclophilin A is a cytosolic and highly abundant protein. (wikipedia.org)
  • The protein belongs to a family of isozymes, including cyclophilins B and C, and natural killer cell cyclophilin-related protein. (wikipedia.org)
  • Scholars@Duke publication: The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis. (duke.edu)
  • The cyclophilin-like domain (CLD) of Ran-binding protein-2 (RanBP2/Nup358) associates specifically with at least one subunit, S1, of the base subcomplex of the 19S RP, but the functional implications of this interaction on the UPS activity are elusive. (duke.edu)
  • A comparison of their known functions has identified, besides a common role within protein folding, multiple roles for the cyclophilins within pre-mRNA splicing and cellular signalling, and within transcription and cell cycle regulation for the parvulins. (biomedcentral.com)
  • Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/calmodulin-dependent phosphatase, calcineurin, the inhibition of which is thought to suppress organ rejection by halting the production of the pro-inflammatory molecules TNF alpha and interleukin 2. (wikipedia.org)
  • Cyclophilin D is thought to regulate the opening of the pore because cyclosporin A, which binds to CyP-D, inhibits the pore opening. (wikipedia.org)
  • This review also discusses the emerging roles of cyclophilins, which are peptidyl-prolyl isomerases with chaperone functions, in replication of selected (+)RNA viruses. (uky.edu)
  • In the Quarter Horse, HERDA is associated with a mutation in cyclophilin B (PPIB), an enzyme involved in triple helix formation of collagen. (gstsvs.ch)
  • Beim Quarter Horse ist HERDA mit einer Mutation im Cyclophilin B Gen (PPIB) assoziiert. (gstsvs.ch)
  • Positive Control #1 targets PPIB (aka Cyclophilin B). (horizondiscovery.com)
  • Some patients have mutations in the TACI (transmembrane activator and calcium-modulator and cyclophilin ligand interactor) gene. (msdmanuals.com)
  • Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. (usf.edu)
  • However, mitochondria obtained from the cysts of Artemia franciscana, do not exhibit the mitochondrial permeability transition pore Overexpression of Cyclophilin A has been linked to poor response to inflammatory diseases, the progression or metastasis of cancer, and aging. (wikipedia.org)
  • Cyclophilin overexpression is a common event in fibrotic tissues playing a key role in different stages of the fibrotic process, including inflammation, hepatocyte death, and activation of the hepatic stellate cells leading to increased collagen production. (lu.se)
  • Overexpression of cyclophilins has been observed in HCC increasing proliferation, metastasis and promoting chemoresistance. (lu.se)
  • Given this data, we would hypothesize that: (i) the evolution of the fungal PPIases is driven, at least in part, by the size of the proteome, (ii) evolutionary pressures differ both between the different PPIase families and the different fungi, and (iii) whilst the cyclophilins and parvulins have evolved to perform conserved functions, the FKBPs have evolved to perform more variable roles. (biomedcentral.com)
  • Cyclophilin inhibition may also be a therapy for liver diseases. (wikipedia.org)
  • In summary, cyclophilin inhibition in liver fibrosis and HCC could be used as a potential therapeutic strategy, individually or in combination. (lu.se)
  • 6] Colgan J, Yuan HE, Franke EK, Luban J. Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization. (chinagene.cn)
  • Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner. (ox.ac.uk)
  • Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. (ox.ac.uk)
  • Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is located in the matrix of mitochondria, is only a modulatory, but may or may not be a structural component of the mitochondrial permeability transition pore. (wikipedia.org)
  • Calcineurin is a common target of cyclophilin-cyclosporine A and Fkbp-Fk506 complexes. (chinagene.cn)
  • unpublished data), may indicate a shared early evolutionary history for the cyclophilin and FKBP families. (biomedcentral.com)
  • We investigated the antifibrotic effect of NV556, a novel potent sanglifehrin-based cyclophilin inhibitor in vitro and in vivo. (lu.se)
  • Treatment with the novel cyclophilin inhibitor NV651, presented a potent antiproliferative effect in HCC cell lines via cell cycle perturbations arresting cells in the mitotic phase. (lu.se)
  • and Blair, Laura J., "Human Cyclophilin 40 Unravels Neurotoxic Amyloids" (2017). (usf.edu)
  • Mitochondrial permeability transition pore component cyclophilin D distinguishes nigrostriatal dopaminergic death paradigms in the MPTP mouse model of Parkinson's disease. (musc.edu)
  • 5A0E: Crystal structure of cyclophilin D in complex with CsA analogue, JW47. (rcsb.org)
  • Cyclophilins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (musc.edu)
  • Human Cyclophilin 40 Unravels Neurotoxic Amyloids" by Jeremy D. Baker, Lindsey B. Shelton et al. (usf.edu)
  • Twelve of the 17 human cyclophilins and both human parvulins, but only one of the 13 human FKBPs, identified orthologues within these fungi. (biomedcentral.com)
  • Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury. (musc.edu)
  • Phylogenetic analysis showed the single-domain FKBPs to evolve prior to the multi-domain FKBPs, whereas the multi-domain cyclophilins appear to evolve throughout cyclophilin evolution. (biomedcentral.com)
  • This graph shows the total number of publications written about "Cyclophilins" by people in this website by year, and whether "Cyclophilins" was a major or minor topic of these publications. (musc.edu)
  • Below are the most recent publications written about "Cyclophilins" by people in Profiles. (musc.edu)