A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
Inorganic and organic derivatives of sulfuric acid (H2SO4). The salts and esters of sulfuric acid are known as SULFATES and SULFURIC ACID ESTERS respectively.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.
A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.
Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the MITOCHONDRIA; the GOLGI APPARATUS; ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
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.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies.
Interacting DNA-encoded regulatory subsystems in the GENOME that coordinate input from activator and repressor TRANSCRIPTION FACTORS during development, cell differentiation, or in response to environmental cues. The networks function to ultimately specify expression of particular sets of GENES for specific conditions, times, or locations.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
UNSATURATED FATTY ACIDS that contain at least one double bond in the trans configuration, which results in a greater bond angle than the cis configuration. This results in a more extended fatty acid chain similar to SATURATED FATTY ACIDS, with closer packing and reduced fluidity. HYDROGENATION of unsaturated fatty acids increases the trans content.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
Established cell cultures that have the potential to propagate indefinitely.
A computer architecture, implementable in either hardware or software, modeled after biological neural networks. Like the biological system in which the processing capability is a result of the interconnection strengths between arrays of nonlinear processing nodes, computerized neural networks, often called perceptrons or multilayer connectionist models, consist of neuron-like units. A homogeneous group of units makes up a layer. These networks are good at pattern recognition. They are adaptive, performing tasks by example, and thus are better for decision-making than are linear learning machines or cluster analysis. They do not require explicit programming.
A group of alicyclic hydrocarbons with the general formula R-C5H9.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
Glycoproteins found on the membrane or surface of cells.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Complex sets of enzymatic reactions connected to each other via their product and substrate metabolites.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A meshlike structure composed of interconnecting nerve cells that are separated at the synaptic junction or joined to one another by cytoplasmic processes. In invertebrates, for example, the nerve net allows nerve impulses to spread over a wide area of the net because synapses can pass information in any direction.
The rate dynamics in chemical or physical systems.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
A system containing any combination of computers, computer terminals, printers, audio or visual display devices, or telephones interconnected by telecommunications equipment or cables: used to transmit or receive information. (Random House Unabridged Dictionary, 2d ed)
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
Computer-based representation of physical systems and phenomena such as chemical processes.
Organizations and individuals cooperating together toward a common goal at the local or grassroots level.
Methods for determining interaction between PROTEINS.
A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
An enzyme that hydrolyzes thiamine pyrophosphate to thiamine monophosphate plus inorganic phosphate. EC 3.6.1.-.
Comprehensive, methodical analysis of complex biological systems by monitoring responses to perturbations of biological processes. Large scale, computerized collection and analysis of the data are used to develop and test models of biological systems.
A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories for solving biological problems including manipulation of models and datasets.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
TRANSPORT VESICLES formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum (ENDOPLASMIC RETICULUM, ROUGH), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to the Golgi apparatus.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Graphs representing sets of measurable, non-covalent physical contacts with specific PROTEINS in living organisms or in cells.
Addition of hydrogen to a compound, especially to an unsaturated fat or fatty acid. (From Stedman, 26th ed)
Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.
Techniques using energy such as radio frequency, infrared light, laser light, visible light, or acoustic energy to transfer information without the use of wires, over both short and long distances.
Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
Theoretical representations that simulate the behavior or activity of the neurological system, processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47
Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.
Neural tracts connecting one part of the nervous system with another.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.
Nocodazole is an antineoplastic agent which exerts its effect by depolymerizing microtubules.
Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)

Processing, stability, and receptor binding properties of oligomeric envelope glycoprotein from a primary HIV-1 isolate. (1/690)

The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is thought to exist on the virion surface as a trimer of non-covalently associated gp120/gp41 molecules. We expressed trimeric envelope glycoprotein from three primary, macrophage tropic HIV-1 isolates in baby hamster kidney cells and analyzed the furin-mediated cleavage, stability, and receptor binding properties of the oligomers. The envelope glycoprotein was secreted in a soluble form deleted of its transmembrane anchor and the intracytoplasmic domain (gp140). A mixture of trimers, dimers, and monomers of gp140 as well as monomeric gp120 was detected on polyacrylamide gels. Analysis by sucrose gradient centrifugation revealed that trimers and dimers were essentially composed of uncleaved gp140, whereas most of the gp120 was found in the monomeric fraction. To analyze the effect of the cleavage of gp140 to gp120/Delta41 on trimerization, we co-expressed the furin protease along with gp140. Surprisingly, furin expression changed the subcellular localization of the envelope glycoprotein, which became in majority sequestered in the major furin compartment, the trans-Golgi network, as judged by confocal laser microscopy. The envelope glycoprotein secreted from furin-co-expressing cells was almost completely cleaved to gp120 and Deltagp41, but gp120 was found exclusively in the monomeric fraction, with a few residual oligomers being composed of uncleaved gp140. Secreted uncleaved gp140 trimers were purified to homogeneity and analyzed for their capacity to interact with cellular receptors CD4 and CC chemokine receptor 5 (CCR5). Receptor binding was analyzed on CD4- and CCR5-expressing cells as well as on peripheral blood mononuclear cells. Trimers showed greatly reduced binding to CD4 as compared with monomers. Neither monomers nor trimers bound directly to CCR5. In conclusion, our results show that the cleaved form of the envelope glycoprotein does not form stable trimers, suggesting that gp120/gp41 oligomers on the virion surface might be stabilized by a yet to be identified mechanism and that the virion might attach to CD4 via a monomeric form of gp120. These results are relevant to the development of an envelope-based vaccine against AIDS.  (+info)

Implication of sphingolipid metabolism in the stability of the Golgi apparatus. (2/690)

We examined the effects of short chain and long chain ceramides on the stability of the Golgi apparatus. Short chain ceramides, C(2)- and C(6)-ceramides, blocked brefeldin A-induced Golgi disassembly without affecting the rapid release of Golgi coat proteins, whereas they did not inhibit brefeldin A-induced tubulation of endosomes. Both short chain ceramides also retarded Golgi disassembly induced by nordihydroguaiaretic acid and nocodazole, suggesting that they stabilize the Golgi apparatus. In contrast to short chain ceramides, natural long chain ceramides, when incorporated into cells or formed within cells upon treatment with sphingomyelinase or metabolic inhibitors, enhanced brefeldin A-induced Golgi disassembly. These results suggest that sphingolipid metabolism is implicated in the stability of the Golgi apparatus.  (+info)

Syntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and Is required for late endosome-lysosome fusion. (3/690)

Protein traffic from the cell surface or the trans-Golgi network reaches the lysosome via a series of endosomal compartments. One of the last steps in the endocytic pathway is the fusion of late endosomes with lysosomes. This process has been reconstituted in vitro and has been shown to require NSF, alpha and gamma SNAP, and a Rab GTPase based on inhibition by Rab GDI. In Saccharomyces cerevisiae, fusion events to the lysosome-like vacuole are mediated by the syntaxin protein Vam3p, which is localized to the vacuolar membrane. In an effort to identify the molecular machinery that controls fusion events to the lysosome, we searched for mammalian homologues of Vam3p. One such candidate is syntaxin 7. Here we show that syntaxin 7 is concentrated in late endosomes and lysosomes. Coimmunoprecipitation experiments show that syntaxin 7 is associated with the endosomal v-SNARE Vamp 8, which partially colocalizes with syntaxin 7. Importantly, we show that syntaxin 7 is specifically required for the fusion of late endosomes with lysosomes in vitro, resulting in a hybrid organelle. Together, these data identify a SNARE complex that functions in the late endocytic system of animal cells.  (+info)

Effects of insulin on intracellular GLUT4 vesicles in adipocytes: evidence for a secretory mode of regulation. (4/690)

The facilitative glucose transporter, GLUT4 undergoes insulin-dependent movement to the cell surface in adipocytes. The magnitude of the insulin effect is much greater for GLUT4 than other recycling proteins such as the CD-MPR. In the present study we have studied the colocalisation of these proteins in adipocytes in an effort to explain this selective insulin-dependent recruitment of GLUT4. Using immunofluorescence microscopy or immuno-EM on 3T3-L1 adipocytes we find that there is considerable colocalisation between these proteins particularly within the area of the TGN. However, the distribution of CD-MPR was not significantly effected by insulin. The insulin-dependent recruitment of GLUT4 was concomitant with a selective decrease in GLUT4 labelling of cytoplasmic vesicles whereas the amount of GLUT4 in the TGN region (approx. 50% of total GLUT4) was relatively unaffected. To explore the possibility that the cytoplasmic GLUT4(+) vesicles represent an intracellular insulin-responsive storage compartment we performed quantitative immuno-EM on whole mounts of intracellular vesicles isolated from basal and insulin-stimulated adipocytes. These studies revealed that: (1) GLUT4 and CD-MPR were concentrated in small (30-200 nm) vesicles at a labelling density of 1-20+ gold particles/vesicle; (2) there was significant overlap between both proteins in that 70% of the total GLUT4 pool colocalised with CD-MPR; (3) a significant amount of GLUT4 (approx. 50% of total) was found in a subpopulation of vesicles that contained as little as 5% of the total CD-MPR pool; (4) the GLUT4(+)/CD-MPR(-) vesicles were highly insulin-responsive, and (5) the total number of GLUT4(+) vesicles, but not CD-MPR(+) vesicles, decreased by approx. 30% in response to insulin treatment. These data are consistent with a model in which GLUT4 is selectively sorted into a vesicular compartment in adipocytes that is recruited to the plasma membrane by insulin stimulation.  (+info)

Rapid transport of internalized P-selectin to late endosomes and the TGN: roles in regulating cell surface expression and recycling to secretory granules. (5/690)

Prior studies on receptor recycling through late endosomes and the TGN have suggested that such traffic may be largely limited to specialized proteins that reside in these organelles. We present evidence that efficient recycling along this pathway is functionally important for nonresident proteins. P-selectin, a transmembrane cell adhesion protein involved in inflammation, is sorted from recycling cell surface receptors (e.g., low density lipoprotein [LDL] receptor) in endosomes, and is transported from the cell surface to the TGN with a half-time of 20-25 min, six to seven times faster than LDL receptor. Native P-selectin colocalizes with LDL, which is efficiently transported to lysosomes, for 20 min after internalization, but a deletion mutant deficient in endosomal sorting activity rapidly separates from the LDL pathway. Thus, P-selectin is sorted from LDL receptor in early endosomes, driving P-selectin rapidly into late endosomes. P-selectin then recycles to the TGN as efficiently as other receptors. Thus, the primary effect of early endosomal sorting of P-selectin is its rapid delivery to the TGN, with rapid turnover in lysosomes a secondary effect of frequent passage through late endosomes. This endosomal sorting event provides a mechanism for efficiently recycling secretory granule membrane proteins and, more generally, for downregulating cell surface receptors.  (+info)

The R-SNARE endobrevin/VAMP-8 mediates homotypic fusion of early endosomes and late endosomes. (6/690)

Endobrevin/VAMP-8 is an R-SNARE localized to endosomes, but it is unknown in which intracellular fusion step it operates. Using subcellular fractionation and quantitative immunogold electron microscopy, we found that endobrevin/VAMP-8 is present on all membranes known to communicate with early endosomes, including the plasma membrane, clathrin-coated pits, late endosomes, and membranes of the trans-Golgi network. Affinity-purified antibodies that block the ability of endobrevin/VAMP-8 to form SNARE core complexes potently inhibit homotypic fusion of both early and late endosomes in vitro. Fab fragments were as active as intact immunoglobulin Gs. Recombinant endobrevin/VAMP-8 inhibited both fusion reactions with similar potency. We conclude that endobrevin/VAMP-8 operates as an R-SNARE in the homotypic fusion of early and late endosomes.  (+info)

Evidence supporting a late Golgi location for lactosylceramide to ganglioside GM3 conversion. (7/690)

Ganglioside GM2 synthase and other enzymes required for complex ganglioside synthesis were localized recently to the trans Golgi network (TGN). However, there are conflicting reports as to the location of GM3 synthase; originally this enzyme was detected in the early Golgi of rat liver but a recent report localized it to the late Golgi. We have used chimeric forms of ganglioside GM2 synthase to determine if the location of lactosylceramide (LacCer) to GM3 conversion in Chinese hamster ovary (CHO) cells was the early or late Golgi. Our approach tested whether GM3 could be utilized as a substrate by GM2 synthase chimeras which were targeted to compartments earlier than the trans Golgi, i.e., GM3 produced in the cis Golgi should be utilized by GM2 synthase located anywhere in the Golgi whereas GM3 produced in the trans Golgi should only be used by GM2 synthase located in the trans Golgi or TGN. Comparison of cell lines stably expressing these chimeras revealed that the in vivo functional activity of GM2 synthase decreased progressively as the enzyme was targeted to earlier compartments; specifically, the percentage of GM3 converted to GM2 was 83-86% for wild type enzyme, 70% for the medial Golgi targeted enzyme, 13% for the ER and cis Golgi targeted enzyme, and only 1.7% for the ER targeted enzyme. Thus, these data are consistent with a late Golgi location for LacCer to GM3 conversion in these cells.  (+info)

Binding of AP2 to sorting signals is modulated by AP2 phosphorylation. (8/690)

The two clathrin-associated adaptor complexes AP1 and AP2 are known to participate in the formation of clathrin-coated vesicles at the trans-Golgi network and at the plasma membrane. During this process adaptors are involved in the sequestration of vesicle cargo by binding to the sorting signals within the cytoplasmic domains of the cargo proteins and in the recruitment of the clathrin coat. After budding of the clathrin-coated vesicles, the clathrin and adaptors dissociate from the vesicles. Here we show that in vitro binding of AP2 to sorting signals, which is one of the initial steps in receptor-mediated endocytosis, is modulated by adaptor phosphorylation. AP2 was phosphorylated by incubating purified AP2 in the presence of ATP and dephosphorylated by incubation with alkaline phosphatase. Affinity for tyrosine-, leucine-based and noncanonical sorting motifs was 15-33 times higher for phosphorylated than for dephosphorylated AP2. Also the binding of AP2 to membranes was regulated by adaptor phosphorylation/dephosphorylation and was about 8-fold higher for phosphorylated than for dephosphorylated AP2. Moreover, AP2 isolated from cytosol is higher phosphorylated than membrane-extracted and exhibits a 5-fold higher binding affinity than AP2 extracted from membranes. Taken together these data point to a cycle of phosphorylation/dephosphorylation as a mechanism for regulating the reversible association of AP2 with membranes and sorting signals during the process of receptor-mediated endocytosis.  (+info)

The Golgi apparatus, also known as the Golgi complex or simply the Golgi, is a membrane-bound organelle found in the cytoplasm of most eukaryotic cells. It plays a crucial role in the processing, sorting, and packaging of proteins and lipids for transport to their final destinations within the cell or for secretion outside the cell.

The Golgi apparatus consists of a series of flattened, disc-shaped sacs called cisternae, which are stacked together in a parallel arrangement. These stacks are often interconnected by tubular structures called tubules or vesicles. The Golgi apparatus has two main faces: the cis face, which is closest to the endoplasmic reticulum (ER) and receives proteins and lipids directly from the ER; and the trans face, which is responsible for sorting and dispatching these molecules to their final destinations.

The Golgi apparatus performs several essential functions in the cell:

1. Protein processing: After proteins are synthesized in the ER, they are transported to the cis face of the Golgi apparatus, where they undergo various post-translational modifications, such as glycosylation (the addition of sugar molecules) and sulfation. These modifications help determine the protein's final structure, function, and targeting.
2. Lipid modification: The Golgi apparatus also modifies lipids by adding or removing different functional groups, which can influence their properties and localization within the cell.
3. Protein sorting and packaging: Once proteins and lipids have been processed, they are sorted and packaged into vesicles at the trans face of the Golgi apparatus. These vesicles then transport their cargo to various destinations, such as lysosomes, plasma membrane, or extracellular space.
4. Intracellular transport: The Golgi apparatus serves as a central hub for intracellular trafficking, coordinating the movement of vesicles and other transport carriers between different organelles and cellular compartments.
5. Cell-cell communication: Some proteins that are processed and packaged in the Golgi apparatus are destined for secretion, playing crucial roles in cell-cell communication and maintaining tissue homeostasis.

In summary, the Golgi apparatus is a vital organelle involved in various cellular processes, including post-translational modification, sorting, packaging, and intracellular transport of proteins and lipids. Its proper functioning is essential for maintaining cellular homeostasis and overall organismal health.

The trans-Golgi network (TGN) is a structure in the cell's endomembrane system that is involved in the sorting and distribution of proteins and lipids to their final destinations within the cell or for secretion. It is a part of the Golgi apparatus, which consists of a series of flattened, membrane-bound sacs called cisternae. The TGN is located at the trans face (or "exit" side) of the Golgi complex and is the final stop for proteins that have been modified as they pass through the Golgi stacks.

At the TGN, proteins are sorted into different transport vesicles based on their specific targeting signals. These vesicles then bud off from the TGN and move to their respective destinations, such as endosomes, lysosomes, the plasma membrane, or secretory vesicles for exocytosis. The TGN also plays a role in the modification of lipids and the formation of primary lysosomes.

In summary, the trans-Golgi network is a crucial sorting and distribution center within the cell that ensures proteins and lipids reach their correct destinations to maintain proper cellular function.

Brefeldin A is a fungal metabolite that inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus. It disrupts the organization of the Golgi complex and causes the redistribution of its proteins to the endoplasmic reticulum. Brefeldin A is used in research to study various cellular processes, including vesicular transport, protein trafficking, and signal transduction pathways. In medicine, it has been studied as a potential anticancer agent due to its ability to induce apoptosis (programmed cell death) in certain types of cancer cells. However, its clinical use is not yet approved.

I believe there might be a slight confusion in your question. Sulfuric acid is not a medical term, but instead a chemical compound with the formula H2SO4. It's one of the most important industrial chemicals, being a strong mineral acid with numerous applications.

If you are asking for a definition related to human health or medicine, I can tell you that sulfuric acid has no physiological role in humans. Exposure to sulfuric acid can cause irritation and burns to the skin, eyes, and respiratory tract. Prolonged exposure may lead to more severe health issues. However, it is not a term typically used in medical diagnoses or treatments.

Endosomes are membrane-bound compartments within eukaryotic cells that play a critical role in intracellular trafficking and sorting of various cargoes, including proteins and lipids. They are formed by the invagination of the plasma membrane during endocytosis, resulting in the internalization of extracellular material and cell surface receptors.

Endosomes can be classified into early endosomes, late endosomes, and recycling endosomes based on their morphology, molecular markers, and functional properties. Early endosomes are the initial sorting stations for internalized cargoes, where they undergo sorting and processing before being directed to their final destinations. Late endosomes are more acidic compartments that mature from early endosomes and are responsible for the transport of cargoes to lysosomes for degradation.

Recycling endosomes, on the other hand, are involved in the recycling of internalized cargoes back to the plasma membrane or to other cellular compartments. Endosomal sorting and trafficking are regulated by a complex network of molecular interactions involving various proteins, lipids, and intracellular signaling pathways.

Defects in endosomal function have been implicated in various human diseases, including neurodegenerative disorders, developmental abnormalities, and cancer. Therefore, understanding the mechanisms underlying endosomal trafficking and sorting is of great importance for developing therapeutic strategies to treat these conditions.

IGF-2 (Insulin-like Growth Factor 2) receptor is a type of transmembrane protein that plays a role in cell growth, differentiation, and survival. Unlike other receptors in the insulin and IGF family, IGF-2 receptor does not mediate the activation of intracellular signaling pathways upon binding to its ligand (IGF-2). Instead, it acts as a clearance receptor that facilitates the removal of IGF-2 from circulation by transporting it to lysosomes for degradation.

The IGF-2 receptor is also known as cation-independent mannose-6-phosphate receptor (CI-M6PR) because it can also bind and transport mannose-6-phosphate-containing enzymes to lysosomes for degradation.

Mutations in the IGF-2 receptor gene have been associated with certain types of cancer, as well as developmental disorders such as Beckwith-Wiedemann syndrome.

Rab GTP-binding proteins, also known as Rab GTPases or simply Rabs, are a large family of small GTP-binding proteins that play a crucial role in regulating intracellular vesicle trafficking. They function as molecular switches that cycle between an active GTP-bound state and an inactive GDP-bound state.

In the active state, Rab proteins interact with various effector molecules to mediate specific membrane trafficking events such as vesicle budding, transport, tethering, and fusion. Each Rab protein is thought to have a unique function and localize to specific intracellular compartments or membranes, where they regulate the transport of vesicles and organelles within the cell.

Rab proteins are involved in several important cellular processes, including endocytosis, exocytosis, Golgi apparatus function, autophagy, and intracellular signaling. Dysregulation of Rab GTP-binding proteins has been implicated in various human diseases, such as cancer, neurodegenerative disorders, and infectious diseases.

Organelles are specialized structures within cells that perform specific functions essential for the cell's survival and proper functioning. They can be thought of as the "organs" of the cell, and they are typically membrane-bound to separate them from the rest of the cellular cytoplasm. Examples of organelles include the nucleus (which contains the genetic material), mitochondria (which generate energy for the cell), ribosomes (which synthesize proteins), endoplasmic reticulum (which is involved in protein and lipid synthesis), Golgi apparatus (which modifies, sorts, and packages proteins and lipids for transport), lysosomes (which break down waste materials and cellular debris), peroxisomes (which detoxify harmful substances and produce certain organic compounds), and vacuoles (which store nutrients and waste products). The specific organelles present in a cell can vary depending on the type of cell and its function.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

CHO cells, or Chinese Hamster Ovary cells, are a type of immortalized cell line that are commonly used in scientific research and biotechnology. They were originally derived from the ovaries of a female Chinese hamster (Cricetulus griseus) in the 1950s.

CHO cells have several characteristics that make them useful for laboratory experiments. They can grow and divide indefinitely under appropriate conditions, which allows researchers to culture large quantities of them for study. Additionally, CHO cells are capable of expressing high levels of recombinant proteins, making them a popular choice for the production of therapeutic drugs, vaccines, and other biologics.

In particular, CHO cells have become a workhorse in the field of biotherapeutics, with many approved monoclonal antibody-based therapies being produced using these cells. The ability to genetically modify CHO cells through various methods has further expanded their utility in research and industrial applications.

It is important to note that while CHO cells are widely used in scientific research, they may not always accurately represent human cell behavior or respond to drugs and other compounds in the same way as human cells do. Therefore, results obtained using CHO cells should be validated in more relevant systems when possible.

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.

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.

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

The endoplasmic reticulum (ER) is a network of interconnected tubules and sacs that are present in the cytoplasm of eukaryotic cells. It is a continuous membranous organelle that plays a crucial role in the synthesis, folding, modification, and transport of proteins and lipids.

The ER has two main types: rough endoplasmic reticulum (RER) and smooth endoplasmic reticulum (SER). RER is covered with ribosomes, which give it a rough appearance, and is responsible for protein synthesis. On the other hand, SER lacks ribosomes and is involved in lipid synthesis, drug detoxification, calcium homeostasis, and steroid hormone production.

In summary, the endoplasmic reticulum is a vital organelle that functions in various cellular processes, including protein and lipid metabolism, calcium regulation, and detoxification.

Cell compartmentation, also known as intracellular compartmentalization, refers to the organization of cells into distinct functional and spatial domains. This is achieved through the separation of cellular components and biochemical reactions into membrane-bound organelles or compartments. Each compartment has its unique chemical composition and environment, allowing for specific biochemical reactions to occur efficiently and effectively without interfering with other processes in the cell.

Some examples of membrane-bound organelles include the nucleus, mitochondria, chloroplasts, endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes, and vacuoles. These organelles have specific functions, such as energy production (mitochondria), protein synthesis and folding (endoplasmic reticulum and Golgi apparatus), waste management (lysosomes), and lipid metabolism (peroxisomes).

Cell compartmentation is essential for maintaining cellular homeostasis, regulating metabolic pathways, protecting the cell from potentially harmful substances, and enabling complex biochemical reactions to occur in a controlled manner. Dysfunction of cell compartmentation can lead to various diseases, including neurodegenerative disorders, cancer, and metabolic disorders.

Intracellular membranes refer to the membrane structures that exist within a eukaryotic cell (excluding bacteria and archaea, which are prokaryotic and do not have intracellular membranes). These membranes compartmentalize the cell, creating distinct organelles or functional regions with specific roles in various cellular processes.

Major types of intracellular membranes include:

1. Nuclear membrane (nuclear envelope): A double-membraned structure that surrounds and protects the genetic material within the nucleus. It consists of an outer and inner membrane, perforated by nuclear pores that regulate the transport of molecules between the nucleus and cytoplasm.
2. Endoplasmic reticulum (ER): An extensive network of interconnected tubules and sacs that serve as a major site for protein folding, modification, and lipid synthesis. The ER has two types: rough ER (with ribosomes on its surface) and smooth ER (without ribosomes).
3. Golgi apparatus/Golgi complex: A series of stacked membrane-bound compartments that process, sort, and modify proteins and lipids before they are transported to their final destinations within the cell or secreted out of the cell.
4. Lysosomes: Membrane-bound organelles containing hydrolytic enzymes for breaking down various biomolecules (proteins, carbohydrates, lipids, and nucleic acids) in the process called autophagy or from outside the cell via endocytosis.
5. Peroxisomes: Single-membrane organelles involved in various metabolic processes, such as fatty acid oxidation and detoxification of harmful substances like hydrogen peroxide.
6. Vacuoles: Membrane-bound compartments that store and transport various molecules, including nutrients, waste products, and enzymes. Plant cells have a large central vacuole for maintaining turgor pressure and storing metabolites.
7. Mitochondria: Double-membraned organelles responsible for generating energy (ATP) through oxidative phosphorylation and other metabolic processes, such as the citric acid cycle and fatty acid synthesis.
8. Chloroplasts: Double-membraned organelles found in plant cells that convert light energy into chemical energy during photosynthesis, producing oxygen and organic compounds (glucose) from carbon dioxide and water.
9. Endoplasmic reticulum (ER): A network of interconnected membrane-bound tubules involved in protein folding, modification, and transport; it is divided into two types: rough ER (with ribosomes on the surface) and smooth ER (without ribosomes).
10. Nucleus: Double-membraned organelle containing genetic material (DNA) and associated proteins involved in replication, transcription, RNA processing, and DNA repair. The nuclear membrane separates the nucleoplasm from the cytoplasm and contains nuclear pores for transporting molecules between the two compartments.

Clathrin is a type of protein that plays a crucial role in the formation of coated vesicles within cells. These vesicles are responsible for transporting materials between different cellular compartments, such as from the plasma membrane to the endoplasmic reticulum or Golgi apparatus. Clathrin molecules form a lattice-like structure that curves around the vesicle, providing stability and shape to the coated vesicle. This process is known as clathrin-mediated endocytosis.

The formation of clathrin-coated vesicles begins with the recruitment of clathrin proteins to specific sites on the membrane, where they assemble into a polygonal lattice structure. As more clathrin molecules join the assembly, the lattice curves and eventually pinches off from the membrane, forming a closed vesicle. The clathrin coat then disassembles, releasing the vesicle to continue with its intracellular transport mission.

Disruptions in clathrin-mediated endocytosis can lead to various cellular dysfunctions and diseases, including neurodegenerative disorders and certain types of cancer.

Monensin is a type of antibiotic known as a polyether ionophore, which is used primarily in the veterinary field for the prevention and treatment of coccidiosis, a parasitic disease caused by protozoa in animals. It works by selectively increasing the permeability of cell membranes to sodium ions, leading to disruption of the ion balance within the cells of the parasite and ultimately causing its death.

In addition to its use as an animal antibiotic, monensin has also been studied for its potential effects on human health, including its ability to lower cholesterol levels and improve insulin sensitivity in type 2 diabetes. However, it is not currently approved for use in humans due to concerns about toxicity and potential side effects.

Gene Regulatory Networks (GRNs) are complex systems of molecular interactions that regulate the expression of genes within an organism. These networks consist of various types of regulatory elements, including transcription factors, enhancers, promoters, and silencers, which work together to control when, where, and to what extent a gene is expressed.

In GRNs, transcription factors bind to specific DNA sequences in the regulatory regions of target genes, either activating or repressing their transcription into messenger RNA (mRNA). This process is influenced by various intracellular and extracellular signals that modulate the activity of transcription factors, allowing for precise regulation of gene expression in response to changing environmental conditions.

The structure and behavior of GRNs can be represented as a network of nodes (genes) and edges (regulatory interactions), with the strength and directionality of these interactions determined by the specific molecular mechanisms involved. Understanding the organization and dynamics of GRNs is crucial for elucidating the underlying causes of various biological processes, including development, differentiation, homeostasis, and disease.

Cricetinae is a subfamily of rodents that includes hamsters, gerbils, and relatives. These small mammals are characterized by having short limbs, compact bodies, and cheek pouches for storing food. They are native to various parts of the world, particularly in Europe, Asia, and Africa. Some species are popular pets due to their small size, easy care, and friendly nature. In a medical context, understanding the biology and behavior of Cricetinae species can be important for individuals who keep them as pets or for researchers studying their physiology.

Trans fatty acids, also known as trans fats, are a type of unsaturated fat that occur in small amounts in nature, primarily in some animal-derived foods. However, most trans fats in the diet come from artificially produced trans fats, created through an industrial process called hydrogenation. This process converts liquid vegetable oils into solid or semi-solid fats, which are then used in a variety of food products for their functional properties and extended shelf life.

Artificial trans fats are formed when hydrogen is added to vegetable oil to make it more solid, a process called hydrogenation. Trans fats can raise levels of harmful LDL cholesterol and lower the level of beneficial HDL cholesterol. This can increase the risk of heart disease, stroke, and type 2 diabetes. Therefore, it is recommended to limit the intake of trans fats as much as possible. Many countries have implemented regulations to limit or ban the use of artificial trans fats in food products.

Vesicular transport proteins are specialized proteins that play a crucial role in the intracellular trafficking and transportation of various biomolecules, such as proteins and lipids, within eukaryotic cells. These proteins facilitate the formation, movement, and fusion of membrane-bound vesicles, which are small, spherical structures that carry cargo between different cellular compartments or organelles.

There are several types of vesicular transport proteins involved in this process:

1. Coat Proteins (COPs): These proteins form a coat around the vesicle membrane and help shape it into its spherical form during the budding process. They also participate in selecting and sorting cargo for transportation. Two main types of COPs exist: COPI, which is involved in transport between the Golgi apparatus and the endoplasmic reticulum (ER), and COPII, which mediates transport from the ER to the Golgi apparatus.

2. SNARE Proteins: These proteins are responsible for the specific recognition and docking of vesicles with their target membranes. They form complexes that bring the vesicle and target membranes close together, allowing for fusion and the release of cargo into the target organelle. There are two types of SNARE proteins: v-SNAREs (vesicle SNAREs) and t-SNAREs (target SNAREs), which interact to form a stable complex during membrane fusion.

3. Rab GTPases: These proteins act as molecular switches that regulate the recruitment of coat proteins, motor proteins, and SNAREs during vesicle transport. They cycle between an active GTP-bound state and an inactive GDP-bound state, controlling the various stages of vesicular trafficking, such as budding, transport, tethering, and fusion.

4. Tethering Proteins: These proteins help to bridge the gap between vesicles and their target membranes before SNARE-mediated fusion occurs. They play a role in ensuring specificity during vesicle docking and may also contribute to regulating the timing of membrane fusion events.

5. Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptors (SNAREs): These proteins are involved in intracellular transport, particularly in the trafficking of vesicles between organelles. They consist of a family of coiled-coil domain-containing proteins that form complexes to mediate membrane fusion events.

Overall, these various classes of proteins work together to ensure the specificity and efficiency of vesicular transport in eukaryotic cells. Dysregulation or mutation of these proteins can lead to various diseases, including neurodegenerative disorders and cancer.

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.

Cyclopentanes are a class of hydrocarbons that contain a cycloalkane ring of five carbon atoms. The chemical formula for cyclopentane is C5H10. It is a volatile, flammable liquid that is used as a solvent and in the production of polymers. Cyclopentanes are also found naturally in petroleum and coal tar.

Cyclopentanes have a unique structure in which the carbon atoms are arranged in a pentagonal shape, with each carbon atom bonded to two other carbon atoms and one or two hydrogen atoms. This structure gives cyclopentane its characteristic "bowl-shaped" geometry, which allows it to undergo various chemical reactions, such as ring-opening reactions, that can lead to the formation of other chemicals.

Cyclopentanes have a variety of industrial and commercial applications. For example, they are used in the production of plastics, resins, and synthetic rubbers. They also have potential uses in the development of new drugs and medical technologies, as their unique structure and reactivity make them useful building blocks for the synthesis of complex molecules.

Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.

Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.

There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.

Membrane glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. They are integral components of biological membranes, spanning the lipid bilayer and playing crucial roles in various cellular processes.

The glycosylation of these proteins occurs in the endoplasmic reticulum (ER) and Golgi apparatus during protein folding and trafficking. The attached glycans can vary in structure, length, and composition, which contributes to the diversity of membrane glycoproteins.

Membrane glycoproteins can be classified into two main types based on their orientation within the lipid bilayer:

1. Type I (N-linked): These glycoproteins have a single transmembrane domain and an extracellular N-terminus, where the oligosaccharides are predominantly attached via asparagine residues (Asn-X-Ser/Thr sequon).
2. Type II (C-linked): These glycoproteins possess two transmembrane domains and an intracellular C-terminus, with the oligosaccharides linked to tryptophan residues via a mannose moiety.

Membrane glycoproteins are involved in various cellular functions, such as:

* Cell adhesion and recognition
* Receptor-mediated signal transduction
* Enzymatic catalysis
* Transport of molecules across membranes
* Cell-cell communication
* Immunological responses

Some examples of membrane glycoproteins include cell surface receptors (e.g., growth factor receptors, cytokine receptors), adhesion molecules (e.g., integrins, cadherins), and transporters (e.g., ion channels, ABC transporters).

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.

HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.

It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Metabolic networks and pathways refer to the complex interconnected series of biochemical reactions that occur within cells to maintain life. These reactions are catalyzed by enzymes and are responsible for the conversion of nutrients into energy, as well as the synthesis and breakdown of various molecules required for cellular function.

A metabolic pathway is a series of chemical reactions that occur in a specific order, with each reaction being catalyzed by a different enzyme. These pathways are often interconnected, forming a larger network of interactions known as a metabolic network.

Metabolic networks can be represented as complex diagrams or models, which show the relationships between different pathways and the flow of matter and energy through the system. These networks can help researchers to understand how cells regulate their metabolism in response to changes in their environment, and how disruptions to these networks can lead to disease.

Some common examples of metabolic pathways include glycolysis, the citric acid cycle (also known as the Krebs cycle), and the pentose phosphate pathway. Each of these pathways plays a critical role in maintaining cellular homeostasis and providing energy for cellular functions.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.

The Fluorescent Antibody Technique (FAT) is a type of immunofluorescence assay used in laboratory medicine and pathology for the detection and localization of specific antigens or antibodies in tissues, cells, or microorganisms. In this technique, a fluorescein-labeled antibody is used to selectively bind to the target antigen or antibody, forming an immune complex. When excited by light of a specific wavelength, the fluorescein label emits light at a longer wavelength, typically visualized as green fluorescence under a fluorescence microscope.

The FAT is widely used in diagnostic microbiology for the identification and characterization of various bacteria, viruses, fungi, and parasites. It has also been applied in the diagnosis of autoimmune diseases and certain cancers by detecting specific antibodies or antigens in patient samples. The main advantage of FAT is its high sensitivity and specificity, allowing for accurate detection and differentiation of various pathogens and disease markers. However, it requires specialized equipment and trained personnel to perform and interpret the results.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

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

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

A nerve net, also known as a neural net or neuronal network, is not a medical term per se, but rather a concept in neuroscience and artificial intelligence (AI). It refers to a complex network of interconnected neurons that process and transmit information. In the context of the human body, the nervous system can be thought of as a type of nerve net, with the brain and spinal cord serving as the central processing unit and peripheral nerves carrying signals to and from various parts of the body.

In the field of AI, artificial neural networks are computational models inspired by the structure and function of biological nerve nets. These models consist of interconnected nodes or "neurons" that process information and learn patterns through a process of training and adaptation. They have been used in a variety of applications, including image recognition, natural language processing, and machine learning.

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

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

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

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

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

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

Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.

Examples of biological models include:

1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.

Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.

Coatomer is a protein complex that plays a role in the formation of transport vesicles within cells. These vesicles are responsible for carrying proteins and other cargo between different cellular compartments. Coatomer gets its name from the coat-like structure it forms on the surface of budding vesicles. It is composed of several individual protein subunits, known as α-COP, β-COP, γ-COP, δ-COP, ε-COP, ζ-COP, and η-COP. These subunits work together to help recognize and bind to specific proteins, curvature the membrane, and ultimately pinch off the vesicle from the donor compartment.

Coatomer protein is primarily involved in transport between the endoplasmic reticulum (ER) and the Golgi apparatus, but it also plays a role in other intracellular transport processes. Mutations or dysfunction in coatomer proteins have been linked to various diseases, including neurological disorders and cancer.

Computer communication networks (CCN) refer to the interconnected systems or groups of computers that are able to communicate and share resources and information with each other. These networks may be composed of multiple interconnected devices, including computers, servers, switches, routers, and other hardware components. The connections between these devices can be established through various types of media, such as wired Ethernet cables or wireless Wi-Fi signals.

CCNs enable the sharing of data, applications, and services among users and devices, and they are essential for supporting modern digital communication and collaboration. Some common examples of CCNs include local area networks (LANs), wide area networks (WANs), and the Internet. These networks can be designed and implemented in various topologies, such as star, ring, bus, mesh, and tree configurations, to meet the specific needs and requirements of different organizations and applications.

An algorithm is not a medical term, but rather a concept from computer science and mathematics. In the context of medicine, algorithms are often used to describe step-by-step procedures for diagnosing or managing medical conditions. These procedures typically involve a series of rules or decision points that help healthcare professionals make informed decisions about patient care.

For example, an algorithm for diagnosing a particular type of heart disease might involve taking a patient's medical history, performing a physical exam, ordering certain diagnostic tests, and interpreting the results in a specific way. By following this algorithm, healthcare professionals can ensure that they are using a consistent and evidence-based approach to making a diagnosis.

Algorithms can also be used to guide treatment decisions. For instance, an algorithm for managing diabetes might involve setting target blood sugar levels, recommending certain medications or lifestyle changes based on the patient's individual needs, and monitoring the patient's response to treatment over time.

Overall, algorithms are valuable tools in medicine because they help standardize clinical decision-making and ensure that patients receive high-quality care based on the latest scientific evidence.

A computer simulation is a process that involves creating a model of a real-world system or phenomenon on a computer and then using that model to run experiments and make predictions about how the system will behave under different conditions. In the medical field, computer simulations are used for a variety of purposes, including:

1. Training and education: Computer simulations can be used to create realistic virtual environments where medical students and professionals can practice their skills and learn new procedures without risk to actual patients. For example, surgeons may use simulation software to practice complex surgical techniques before performing them on real patients.
2. Research and development: Computer simulations can help medical researchers study the behavior of biological systems at a level of detail that would be difficult or impossible to achieve through experimental methods alone. By creating detailed models of cells, tissues, organs, or even entire organisms, researchers can use simulation software to explore how these systems function and how they respond to different stimuli.
3. Drug discovery and development: Computer simulations are an essential tool in modern drug discovery and development. By modeling the behavior of drugs at a molecular level, researchers can predict how they will interact with their targets in the body and identify potential side effects or toxicities. This information can help guide the design of new drugs and reduce the need for expensive and time-consuming clinical trials.
4. Personalized medicine: Computer simulations can be used to create personalized models of individual patients based on their unique genetic, physiological, and environmental characteristics. These models can then be used to predict how a patient will respond to different treatments and identify the most effective therapy for their specific condition.

Overall, computer simulations are a powerful tool in modern medicine, enabling researchers and clinicians to study complex systems and make predictions about how they will behave under a wide range of conditions. By providing insights into the behavior of biological systems at a level of detail that would be difficult or impossible to achieve through experimental methods alone, computer simulations are helping to advance our understanding of human health and disease.

Community networks, in the context of public health and medical care, typically refer to local or regional networks of healthcare providers, organizations, and resources that work together to provide integrated and coordinated care to a defined population. These networks can include hospitals, clinics, primary care providers, specialists, mental health services, home health agencies, and other community-based organizations.

The goal of community networks is to improve the overall health outcomes of the population they serve by ensuring that individuals have access to high-quality, coordinated care that meets their unique needs. Community networks can also help to reduce healthcare costs by preventing unnecessary hospitalizations and emergency department visits through better management of chronic conditions and prevention efforts.

Effective community networks require strong partnerships, clear communication, and a shared commitment to improving the health of the community. They may be organized around geographic boundaries, such as a city or county, or around specific populations, such as individuals with chronic illnesses or low-income communities.

Protein interaction mapping is a research approach used to identify and characterize the physical interactions between different proteins within a cell or organism. This process often involves the use of high-throughput experimental techniques, such as yeast two-hybrid screening, mass spectrometry-based approaches, or protein fragment complementation assays, to detect and quantify the binding affinities of protein pairs. The resulting data is then used to construct a protein interaction network, which can provide insights into functional relationships between proteins, help elucidate cellular pathways, and inform our understanding of biological processes in health and disease.

Coat Protein Complex I (CPCI or COPI) is a protein complex involved in the intracellular transport of proteins within eukaryotic cells. It functions primarily in the retrograde transport of proteins from the Golgi apparatus to the endoplasmic reticulum (ER). The complex is composed of seven subunits, known as alpha, beta, gamma, delta, epsilon, zeta, and eta COPs (coat proteins), which form a cage-like structure around transport vesicles. This coat assists in the selection of cargo proteins, vesicle budding, and subsequent fusion with target membranes during the recycling of ER-derived proteins.

Thiamine pyrophosphatase (TPP) is an enzyme that catalyzes the hydrolysis of thiamine pyrophosphate (TPP), which is a cofactor involved in several important metabolic pathways, including carbohydrate metabolism and neurotransmitter synthesis.

The reaction catalyzed by TPP is:

thiamine pyrophosphate + H2O → thiamine + phosphate

TPP is also known as thiamine diphosphatase or vitamin B1 diphosphatase. Deficiency of this enzyme can lead to thiamine deficiency disorders such as beriberi and Wernicke-Korsakoff syndrome, which are characterized by neurological and cardiovascular symptoms.

Systems Biology is a multidisciplinary approach to studying biological systems that involves the integration of various scientific disciplines such as biology, mathematics, physics, computer science, and engineering. It aims to understand how biological components, including genes, proteins, metabolites, cells, and organs, interact with each other within the context of the whole system. This approach emphasizes the emergent properties of biological systems that cannot be explained by studying individual components alone. Systems biology often involves the use of computational models to simulate and predict the behavior of complex biological systems and to design experiments for testing hypotheses about their functioning. The ultimate goal of systems biology is to develop a more comprehensive understanding of how biological systems function, with applications in fields such as medicine, agriculture, and bioengineering.

Computational biology is a branch of biology that uses mathematical and computational methods to study biological data, models, and processes. It involves the development and application of algorithms, statistical models, and computational approaches to analyze and interpret large-scale molecular and phenotypic data from genomics, transcriptomics, proteomics, metabolomics, and other high-throughput technologies. The goal is to gain insights into biological systems and processes, develop predictive models, and inform experimental design and hypothesis testing in the life sciences. Computational biology encompasses a wide range of disciplines, including bioinformatics, systems biology, computational genomics, network biology, and mathematical modeling of biological systems.

Mannosidases are a group of enzymes that catalyze the hydrolysis of mannose residues from glycoproteins, oligosaccharides, and glycolipids. These enzymes play a crucial role in the processing and degradation of N-linked glycans, which are carbohydrate structures attached to proteins in eukaryotic cells.

There are several types of mannosidases, including alpha-mannosidase and beta-mannosidase, which differ in their specificity for the type of linkage they cleave. Alpha-mannosidases hydrolyze alpha-1,2-, alpha-1,3-, alpha-1,6-mannosidic bonds, while beta-mannosidases hydrolyze beta-1,4-mannosidic bonds.

Deficiencies in mannosidase activity can lead to various genetic disorders, such as alpha-mannosidosis and beta-mannosidosis, which are characterized by the accumulation of unprocessed glycoproteins and subsequent cellular dysfunction.

COP-coated vesicles refer to transport vesicles that are coated with coat proteins (COPs) during their formation and play a crucial role in intracellular trafficking. These vesicles are involved in the transport of proteins and lipids between different cellular compartments, such as the endoplasmic reticulum, Golgi apparatus, and plasma membrane.

There are two main types of COP-coated vesicles: COPI (coat protein I) and COPII (coat protein II) coated vesicles.

COPI-coated vesicles are involved in the retrograde transport of proteins from the Golgi apparatus to the endoplasmic reticulum, as well as intra-Golgi trafficking. They are formed by the assembly of coatomer proteins (COPs) around a budding membrane, which then pinches off to form a vesicle. The COPI coat is disassembled upon arrival at the target membrane, releasing the cargo and allowing for fusion with the target membrane.

On the other hand, COPII-coated vesicles are involved in the anterograde transport of proteins from the endoplasmic reticulum to the Golgi apparatus. They are formed by the assembly of Sar1, Sec23/24, and Sec13/31 coat proteins around a budding membrane, which then pinches off to form a vesicle. The COPII coat is disassembled upon arrival at the target membrane, releasing the cargo and allowing for fusion with the target membrane.

Overall, COP-coated vesicles are essential components of the intracellular transport machinery that enables cells to regulate their protein and lipid composition in a precise and coordinated manner.

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.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Protein interaction maps are graphical representations that illustrate the physical interactions and functional relationships between different proteins in a cell or organism. These maps can be generated through various experimental techniques such as yeast two-hybrid screens, affinity purification mass spectrometry (AP-MS), and co-immunoprecipitation (Co-IP) followed by mass spectrometry. The resulting data is then visualized as a network where nodes represent proteins and edges represent the interactions between them. Protein interaction maps can provide valuable insights into cellular processes, signal transduction pathways, and disease mechanisms, and are widely used in systems biology and network medicine research.

Hydrogenation, in the context of food science and biochemistry, refers to the process of adding hydrogen atoms to certain unsaturated fats or oils, converting them into saturated fats. This is typically done through a chemical reaction using hydrogen gas in the presence of a catalyst, often a metal such as nickel or palladium.

The process of hydrogenation increases the stability and shelf life of fats and oils, but it can also lead to the formation of trans fats, which have been linked to various health issues, including heart disease. Therefore, the use of partially hydrogenated oils has been largely phased out in many countries.

Galactosyltransferases are a group of enzymes that play a crucial role in the biosynthesis of glycoconjugates, which are complex carbohydrate structures found on the surface of many cell types. These enzymes catalyze the transfer of galactose, a type of sugar, to another molecule, such as another sugar or a lipid, to form a glycosidic bond.

Galactosyltransferases are classified based on the type of donor substrate they use and the type of acceptor substrate they act upon. For example, some galactosyltransferases use UDP-galactose as a donor substrate and transfer galactose to an N-acetylglucosamine (GlcNAc) residue on a protein or lipid, forming a lactosamine unit. Others may use different donor and acceptor substrates to form different types of glycosidic linkages.

These enzymes are involved in various biological processes, including cell recognition, signaling, and adhesion. Abnormalities in the activity of galactosyltransferases have been implicated in several diseases, such as congenital disorders of glycosylation, cancer, and inflammatory conditions. Therefore, understanding the function and regulation of these enzymes is important for developing potential therapeutic strategies for these diseases.

ADP-Ribosylation Factor 1 (ARF1) is a small GTP-binding protein that belongs to the ADP-ribosylation factor family. It plays a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction pathways. ARF1 functions as a molecular switch by cycling between an active GTP-bound state and an inactive GDP-bound state.

In the active state, ARF1 regulates the recruitment of coat proteins to membranes, which facilitates vesicle formation and transport. It also activates phospholipase D, which generates second messengers that regulate various cellular processes. In contrast, in the inactive state, ARF1 is bound to GDP and cannot participate in these functions.

Mutations or dysregulation of ARF1 have been implicated in several human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the structure, function, and regulation of ARF1 is essential for developing new therapeutic strategies to treat these conditions.

I'm sorry for any confusion, but "Wireless Technology" is not a term that has a specific medical definition. Wireless technology generally refers to the transmission of information over a distance without the use of electrical conductors or "wires." It encompasses a wide range of technologies, including cellular networks, Wi-Fi, Bluetooth, and various forms of telecommunication.

However, in a medical context, wireless technology can be used to refer to devices or systems that transmit patient data without the need for physical connections. For example, wireless pulse oximeters, blood glucose monitors, or cardiac event monitors. These devices use wireless technologies to send patient data to a remote monitoring station or to a healthcare provider's electronic health record system. This can provide more flexibility and mobility for patients, and can also improve the efficiency of healthcare delivery.

Genetic models are theoretical frameworks used in genetics to describe and explain the inheritance patterns and genetic architecture of traits, diseases, or phenomena. These models are based on mathematical equations and statistical methods that incorporate information about gene frequencies, modes of inheritance, and the effects of environmental factors. They can be used to predict the probability of certain genetic outcomes, to understand the genetic basis of complex traits, and to inform medical management and treatment decisions.

There are several types of genetic models, including:

1. Mendelian models: These models describe the inheritance patterns of simple genetic traits that follow Mendel's laws of segregation and independent assortment. Examples include autosomal dominant, autosomal recessive, and X-linked inheritance.
2. Complex trait models: These models describe the inheritance patterns of complex traits that are influenced by multiple genes and environmental factors. Examples include heart disease, diabetes, and cancer.
3. Population genetics models: These models describe the distribution and frequency of genetic variants within populations over time. They can be used to study evolutionary processes, such as natural selection and genetic drift.
4. Quantitative genetics models: These models describe the relationship between genetic variation and phenotypic variation in continuous traits, such as height or IQ. They can be used to estimate heritability and to identify quantitative trait loci (QTLs) that contribute to trait variation.
5. Statistical genetics models: These models use statistical methods to analyze genetic data and infer the presence of genetic associations or linkage. They can be used to identify genetic risk factors for diseases or traits.

Overall, genetic models are essential tools in genetics research and medical genetics, as they allow researchers to make predictions about genetic outcomes, test hypotheses about the genetic basis of traits and diseases, and develop strategies for prevention, diagnosis, and treatment.

Gene expression profiling is a laboratory technique used to measure the activity (expression) of thousands of genes at once. This technique allows researchers and clinicians to identify which genes are turned on or off in a particular cell, tissue, or organism under specific conditions, such as during health, disease, development, or in response to various treatments.

The process typically involves isolating RNA from the cells or tissues of interest, converting it into complementary DNA (cDNA), and then using microarray or high-throughput sequencing technologies to determine which genes are expressed and at what levels. The resulting data can be used to identify patterns of gene expression that are associated with specific biological states or processes, providing valuable insights into the underlying molecular mechanisms of diseases and potential targets for therapeutic intervention.

In recent years, gene expression profiling has become an essential tool in various fields, including cancer research, drug discovery, and personalized medicine, where it is used to identify biomarkers of disease, predict patient outcomes, and guide treatment decisions.

Neurological models are simplified representations or simulations of various aspects of the nervous system, including its structure, function, and processes. These models can be theoretical, computational, or physical and are used to understand, explain, and predict neurological phenomena. They may focus on specific neurological diseases, disorders, or functions, such as memory, learning, or movement. The goal of these models is to provide insights into the complex workings of the nervous system that cannot be easily observed or understood through direct examination alone.

ADP-ribosylation factors (ARFs) are a family of small GTP-binding proteins that play a crucial role in intracellular membrane traffic, actin dynamics, and signal transduction. They function as molecular switches, cycling between an active GTP-bound state and an inactive GDP-bound state.

ARFs are involved in the regulation of vesicle formation, budding, and transport, primarily through their ability to activate phospholipase D and recruit coat proteins to membranes. There are six isoforms of ARFs (ARF1-6) that share a high degree of sequence similarity but have distinct cellular functions and subcellular localizations.

ADP-ribosylation factors get their name from the fact that they were originally identified as proteins that become ADP-ribosylated by cholera toxin, an enzyme produced by Vibrio cholerae bacteria. However, this post-translational modification is not required for their cellular functions.

Defects in ARF function have been implicated in various human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the regulation and function of ARFs is an important area of research in biology and medicine.

Immunoelectron microscopy (IEM) is a specialized type of electron microscopy that combines the principles of immunochemistry and electron microscopy to detect and localize specific antigens within cells or tissues at the ultrastructural level. This technique allows for the visualization and identification of specific proteins, viruses, or other antigenic structures with a high degree of resolution and specificity.

In IEM, samples are first fixed, embedded, and sectioned to prepare them for electron microscopy. The sections are then treated with specific antibodies that have been labeled with electron-dense markers, such as gold particles or ferritin. These labeled antibodies bind to the target antigens in the sample, allowing for their visualization under an electron microscope.

There are several different methods of IEM, including pre-embedding and post-embedding techniques. Pre-embedding involves labeling the antigens before embedding the sample in resin, while post-embedding involves labeling the antigens after embedding. Post-embedding techniques are generally more commonly used because they allow for better preservation of ultrastructure and higher resolution.

IEM is a valuable tool in many areas of research, including virology, bacteriology, immunology, and cell biology. It can be used to study the structure and function of viruses, bacteria, and other microorganisms, as well as the distribution and localization of specific proteins and antigens within cells and tissues.

Neural pathways, also known as nerve tracts or fasciculi, refer to the highly organized and specialized routes through which nerve impulses travel within the nervous system. These pathways are formed by groups of neurons (nerve cells) that are connected in a series, creating a continuous communication network for electrical signals to transmit information between different regions of the brain, spinal cord, and peripheral nerves.

Neural pathways can be classified into two main types: sensory (afferent) and motor (efferent). Sensory neural pathways carry sensory information from various receptors in the body (such as those for touch, temperature, pain, and vision) to the brain for processing. Motor neural pathways, on the other hand, transmit signals from the brain to the muscles and glands, controlling movements and other effector functions.

The formation of these neural pathways is crucial for normal nervous system function, as it enables efficient communication between different parts of the body and allows for complex behaviors, cognitive processes, and adaptive responses to internal and external stimuli.

Green Fluorescent Protein (GFP) is not a medical term per se, but a scientific term used in the field of molecular biology. GFP is a protein that exhibits bright green fluorescence when exposed to light, particularly blue or ultraviolet light. It was originally discovered in the jellyfish Aequorea victoria.

In medical and biological research, scientists often use recombinant DNA technology to introduce the gene for GFP into other organisms, including bacteria, plants, and animals, including humans. This allows them to track the expression and localization of specific genes or proteins of interest in living cells, tissues, or even whole organisms.

The ability to visualize specific cellular structures or processes in real-time has proven invaluable for a wide range of research areas, from studying the development and function of organs and organ systems to understanding the mechanisms of diseases and the effects of therapeutic interventions.

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.

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.

Cell fractionation is a laboratory technique used to separate different cellular components or organelles based on their size, density, and other physical properties. This process involves breaking open the cell (usually through homogenization), and then separating the various components using various methods such as centrifugation, filtration, and ultracentrifugation.

The resulting fractions can include the cytoplasm, mitochondria, nuclei, endoplasmic reticulum, Golgi apparatus, lysosomes, peroxisomes, and other organelles. Each fraction can then be analyzed separately to study the biochemical and functional properties of the individual components.

Cell fractionation is a valuable tool in cell biology research, allowing scientists to study the structure, function, and interactions of various cellular components in a more detailed and precise manner.

Nocodazole is not a medical condition or disease, but rather a pharmacological agent used in medical research and clinical settings. It's a synthetic chemical compound that belongs to the class of drugs known as microtubule inhibitors. Nocodazole works by binding to and disrupting the dynamic assembly and disassembly of microtubules, which are important components of the cell's cytoskeleton and play a critical role in cell division.

Nocodazole is primarily used in research settings as a tool for studying cell biology and mitosis, the process by which cells divide. It can be used to synchronize cells in the cell cycle or to induce mitotic arrest, making it useful for investigating various aspects of cell division and chromosome behavior.

In clinical settings, nocodazole has been used off-label as a component of some cancer treatment regimens, particularly in combination with other chemotherapeutic agents. Its ability to disrupt microtubules can interfere with the proliferation of cancer cells and enhance the effectiveness of certain anti-cancer drugs. However, its use is not widespread due to potential side effects and the availability of alternative treatments.

Subcellular fractions refer to the separation and collection of specific parts or components of a cell, including organelles, membranes, and other structures, through various laboratory techniques such as centrifugation and ultracentrifugation. These fractions can be used in further biochemical and molecular analyses to study the structure, function, and interactions of individual cellular components. Examples of subcellular fractions include nuclear extracts, mitochondrial fractions, microsomal fractions (membrane vesicles), and cytosolic fractions (cytoplasmic extracts).

Trans-Golgi network vesicle protein 23 A (TVP23A) is a protein coded for the TVP23A gene, formerly known as FAM18A. TVP23A is ... TVP23A stands for Trans-Golgi network Vesicle Protein 23A TVP23A, is the current name for the protein. Aliases of TVP23A ... The general consensus on the TVP23A protein indicate that it has some function in the late Golgi apparatus and is involved in ... Two of these proteins, YIPF1 and YIPF2, are believed to be Golgi transport proteins. TVP23A is a DUF846 containing protein, ...
... "trans-Golgi Network" by people in this website by year, and whether "trans-Golgi Network" was a major or minor topic of these ... "trans-Golgi Network" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... trans-Golgi Network*trans-Golgi Network. *Network, trans-Golgi. *trans Golgi Network ... Below are the most recent publications written about "trans-Golgi Network" by people in Profiles. ...
RHOBTB3:ADP [trans-Golgi network membrane] (Dictyostelium discoideum) RHOBTB3:ADP [trans-Golgi network membrane] (Gallus gallus ... Intra-Golgi and retrograde Golgi-to-ER traffic (Homo sapiens) * Retrograde transport at the Trans-Golgi-Network (Homo sapiens) ... RHOBTB3:ADP [trans-Golgi network membrane] (Danio rerio) ... trans-Golgi network membrane] (Bos taurus) RHOBTB3:ADP [trans- ... RHOBTB3:ADP [trans-Golgi network membrane] (Mus musculus) RHOBTB3:ADP [trans-Golgi network membrane] (Rattus norvegicus) ...
Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network Sebastien Carreno, Sebastien Carreno ... We hypothesized that Hip1R might also coordinate actin assembly with clathrin budding at the trans-Golgi network (TGN). Using ... Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science. ... Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science. ...
... trans-Golgi network membrane] (Homo sapiens) * AP1S1,2,3 [trans-Golgi network membrane] (Homo sapiens) * AP1S2 [trans-Golgi ... trans-Golgi network membrane] (Homo sapiens) * AP1S1,2,3 [trans-Golgi network membrane] (Homo sapiens) * AP1S2 [trans-Golgi ... trans-Golgi network membrane] (Homo sapiens) * AP1S1,2,3 [trans-Golgi network membrane] (Homo sapiens) * AP1S2 [trans-Golgi ... trans-Golgi network membrane] (Homo sapiens) * AP1S1,2,3 [trans-Golgi network membrane] (Homo sapiens) * AP1S2 [trans-Golgi ...
Sorting and export of transmembrane cargoes and lysosomal hydrolases at the trans-Golgi network (TGN) are well understood. ... Secretory cargo sorting by Ca2+-dependent Cab45 oligomerization at the trans-Golgi network ...
located_in trans-Golgi network IDA Inferred from Direct Assay. more info ... Located in several cellular components, including late endosome; lysosome; and trans-Golgi network. [provided by Alliance of ...
... rather it specifically perturbs endosome-to-trans Golgi network (TGN) transport of the cation-independent mannose-6-phosphate ...
is_active_in trans-Golgi network membrane IBA Inferred from Biological aspect of Ancestor. more info ... located_in trans-Golgi network IDA Inferred from Direct Assay. more info ... involved_in post-Golgi vesicle-mediated transport TAS Traceable Author Statement. more info ... They function as carriers to the cell surface in post-golgi recycling pathways. Different family members are highly related ...
Taken together, these experiments revealed that Vapyrin-bodies have an endosomal identity with trans-Golgi features, and that ... Taken together, these experiments revealed that Vapyrin-bodies have an endosomal identity with trans-Golgi features, and that ... Hence, these observations are compatible with an identity of Vapyrin-bodies as elements of the trans-Golgi network (TGN). An ... Co-expression of VAPYRIN-GFP with the post-Golgi marker mCherry-SYP61 (a), with the trans-Golgi/endosomal marker mCherry-RabA5d ...
... trans-Golgi network) from the PVC and the PM. However, trafficking of newly synthesized proteins to the PM is unaffected. The ... trans-Golgi network) [11]. This demonstrates the use of chemical genomics as a powerful tool to isolate small molecules to ... A GFP-based assay reveals a role for RHD3 in transport between the endoplasmic reticulum and Golgi apparatus ... targeted to Golgi), GFP-ARA7 (for the PVC) and VHAa1-GFP (for the TGN population). Immunolabelling revealed that native PIN2 ...
... a fine and elegant network within the cell body … completely internal in the nerve cells (Golgi 1898a; Golgi 1898b). This ... The mammalian Golgi apparatus was first described by Camillo Golgi in 1998 as apparato reticolare interno, ... 2008). In ALS, structural Golgi alterations have been revealed by the pioneering work of Gonatas and colleagues (Mourelatos et ... 2002). They manifest as fragmentation - transformation of the Golgi ribbon into disconnected stacks, c... ...
RABH1b and further GTPases shown by STRING points to an active protein sorting in the trans-Golgi or at the trans-Golgi network ... Multivesicular bodies mature from the trans-Golgi network/early endosome in Arabidopsis. Plant. Cell 23, 3463-3481, https://doi ... Among the 39 proteins identified in the development phase I, proteins related to the secretory pathway (ER, Golgi, Golgi - ER ... Samaj, J., Read, N. D., Volkmann, D., Menzel, D. & Baluska, F. The endocytic network in plants. Trends Cell Biol. 15, 425-433, ...
ST6Gal1 is processed by BACE1 in the trans-Golgi network. PS1, Presenilin-1 component of γ-secretase; N and C, N terminus and C ... 2005) GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network. Mol Cell Neurosci 29:453- ... trans-Golgi) with its active site in the lumen of the vesicles. The highest expression levels of BACE are found in neurons of ... Golgi-localized γ-ear-containing ARF-binding (GGA) proteins interact with the BACE1 C-terminal DXXLL motif via a VHL domain and ...
This study assessed whether serum Golgi phosphoprotein 3 (GOLPH3) could be used as a biomarker for detecting bladder cancer. ... Keywords: Diagnosis, trans-Golgi Network, Urinary Bladder Neoplasms, Membrane Proteins, Middle Aged, Neoplasm Invasiveness, ROC ... Diagnostic Utility of Serum Golgi Phosphoprotein 3 in Bladder Cancer Patients Jianlei Lu1ABCDEFG, Feng Zhong2ABCDEFG*, Beibei ... BACKGROUND: This study assessed whether serum Golgi phosphoprotein 3 (GOLPH3) could be used as a biomarker for detecting ...
Chen, J. & Chen, Z. J. PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation. Nature 564, 71-76 ( ...
Co-transport of gN and gM to the trans Golgi network also occurs upon replacement of conserved cysteines in gM and gN, ... gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN ... gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN ... Co-transport of gN and gM to the trans Golgi network also occurs upon replacement of conserved cysteines in gM and gN, ...
VPS13A may be involved in the control of protein cycling through the trans-Golgi network. It is broadly expressed and found in ... cytoskeleton network, erythropoiesis, and neurogenesis. The authors maintain that this network may represent a shared ... De Franceschi L, Corrocher R. Erythrocyte membrane anion exchange abnormalities in chorea-acanthocytosis: The band 3 network. ... Computational identification of phospho-tyrosine sub-networks related to acanthocyte generation in neuroacanthocytosis. PLoS ...
Next articleNEWS: Study Uncovers Mechanism of GPCR Signaling at the Trans-Golgi Network ...
The CuATPase7b transporter is a P-type ATPase associated with the trans Golgi network. These observations were the basis to ...
Conserved Arabidopsis ECHIDNA protein mediates trans-Golgi-network trafficking and cell elongation ... Exploring the trans-local nature of cultural scene * Facilitating forest restoration sustainability of tropical swidden ... Vulnerability of low-lying coastal transportation networks to natural hazards * Wideband fibre optical parametric amplifiers ... Understanding the structure and engagement of personal networks that support older people with complex care needs in ...
Trans-Golgi network. 55. Protein function. Name. # of Products. Androgen receptor binding. 134. ...
The clathrin protein is associated with vesicle formation and transport at the plasma membrane and trans-Golgi network. ... Coatomer proteins mediate transport within the Golgi complex and between the Golgi complex and ER (42). Although the sizes of ... and the Golgi complex is known as the budding compartment. Virions then accumulate in the intracisternal space that forms a ... and eventually move to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (37,41). Complete virions are produced ...
Most plasma membrane proteins are sorted by the trans-Golgi network (TGN) in the conventional secretory pathway. As ... Cilium trafficking of P/rds was sustained even when the Golgi functions, including trans-Golgi-mediated conventional secretion ... the cis-Golgi marker GM130, and the mid- and trans-Golgi marker GMII (Fig. 6A-C, bP/rds-HA-FLAG [high]). This partial ... and trans-Golgi marker GMII. The confinement of bP/rds1-312 to the late Golgi compartments suggests that the majority of bP/rds ...
Major processing enzyme of the secretory pathway and is localized in the trans-golgi network ... NEBNext ARTIC kits are based on the original work of the ARTIC Network. The kits include balanced ARTIC primer pools for ...
Newly made proteins can travel directly from the trans-Golgi network (TGN) to either the apical or basolateral surface. ... Newly made proteins can travel directly from the trans-Golgi network (TGN) to either the apical or basolateral surface. ... Newly made proteins can travel directly from the trans-Golgi network (TGN) to either the apical or basolateral surface. ... DN Rac1 causes a defect in the assembly of laminin into its normal basement membrane network, and addition of a high ...
trans-Golgi network membrane organization vesicle budding from membrane + engulfment of target by autophagosome ...
... at the trans-Golgi network, or TGN. Within the immature secretory granule, p roinsulin is converted to insulin through the ... Pre-Application Process for NICHD Network Multisite Clinical Research * Concept Proposal Info ...
During maturation, transport from the trans-Golgi network to endosomes occurs, providing newly synthesized lysosomal enzymes ... The Golgi network is marked with antibodies against γ subunit or adaptor complex 1 [49]. For colocalization with the ... and networks and biomarkers may well be observed from these studies in relation to GPCRs or factors associated with them. ...
Hyperacidification of trans-golgi network and endo/lysosomes in melanocytes by gucosylceramide-dpendent V-ATPase activity. van ... Absence of influenza A(H1N1) during seasonal and pandemic seasons in a sentinel nursing home surveillance network in the ... Mutations in the regulatory network underlie the recent clonal expansion of a dominant subclone of the Mycobacterium ... Usefulness of primary care electronic networks to assess the incidence of chlamydia, diagnosed by general practitioners. ...

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