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GRP78
Binding immunoglobulin protein (BiPS) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a protein that in humans is encoded by the ''HSPA5'' gene. BiP is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly synthesized proteins as they are translocated into the ER, and maintains them in a state competent for subsequent folding and oligomerization. BiP is also an essential component of the translocation machinery and plays a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. BiP is an abundant protein under all growth conditions, but its synthesis is markedly induced under conditions that lead to the accumulation of unfolded polypeptides in the ER. Structure BiP contains two functional domains: a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The NBD binds and hydrolyzes ATP, and the SBD bind ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chaperone (protein)
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding intermedi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Unfolded Protein Response
The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. It has been found to be conserved between mammalian species, as well as yeast and worm organisms. The UPR is activated in response to an accumulation of unfolded or misfolded proteins in the lumen of the endoplasmic reticulum. In this scenario, the UPR has three aims: initially to restore normal function of the cell by halting protein translation, degrading misfolded proteins, and activating the signaling pathways that lead to increasing the production of molecular chaperones involved in protein folding. If these objectives are not achieved within a certain time span or the disruption is prolonged, the UPR aims towards apoptosis. Sustained overactivation of the UPR has been implicated in prion diseases as well as several other neurodegenerative diseases, and inhibiting the UPR could become a treatment for those diseases. Diseases amenable to UPR inhibition include Cr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EIF2AK3
Eukaryotic translation initiation factor 2-alpha kinase 3, also known as protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK), is an enzyme that in humans is encoded by the ''EIF2AK3'' gene. Function The protein encoded by this gene phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation, and thus to a rapid reduction of translational initiation and repression of global protein synthesis. It is a type I membrane protein located in the endoplasmic reticulum (ER), where it is induced by ER stress caused by malfolded proteins. Clinical significance Patients with mutations in this gene develop Wolcott-Rallison syndrome. Interactions EIF2AK3 has been shown to interact with DNAJC3, NFE2L2, and endoplasmic reticulum chaperone BiP (Hsp70 The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ERN1
The serine/threonine-protein kinase/endoribonuclease inositol-requiring enzyme 1 α (IRE1α) is an enzyme that in humans is encoded by the ''ERN1'' gene. Function The protein encoded by this gene is the ER to nucleus signalling 1 protein, a human homologue of the yeast Ire1 gene product. This protein possesses intrinsic kinase activity and an endoribonuclease activity and it is important in altering gene expression as a response to endoplasmic reticulum-based stress signals (mainly the unfolded protein response). Two alternatively spliced transcript variants encoding different isoforms have been found for this gene. Signaling IRE1α possesses two functional enzymatic domains, an endonuclease and a trans-autophosphorylation kinase domain. Upon activation, IRE1α oligomerizes and carries out an unconventional RNA splicing activity, removing an intron from the X-box binding protein 1 (XBP1) mRNA, and allowing it to become translated into a functional transcription factor, XBP ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycosylation
Glycosylation is the reaction in which a carbohydrate (or ' glycan'), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation (also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction. Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the ''O''-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced: * ''N''-linked glycans attached to a nitrogen of asparagi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ERAD
Endoplasmic-reticulum-associated protein degradation (ERAD) designates a cellular pathway which targets misfolded proteins of the endoplasmic reticulum for ubiquitination and subsequent degradation by a protein-degrading complex, called the proteasome. Mechanism The process of ERAD can be divided into three steps: Recognition of misfolded or mutated proteins in the endoplasmic reticulum The recognition of misfolded or mutated proteins depends on the detection of substructures within proteins such as exposed hydrophobic regions, unpaired cysteine residues and immature glycans. In mammalian cells for example, there exists a mechanism called glycan processing. In this mechanism, the lectin-type chaperones calnexin/calreticulin (CNX/CRT) provide immature glycoproteins the opportunity to reach their native conformation. They can do this by way of reglucosylating these glycoproteins by an enzyme called UDP-glucose-glycoprotein glucosyltransferase also known as UGGT. Terminal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lumen (anatomy)
In biology, a lumen (: lumina) is the inside space of a tubular structure, such as an artery or intestine. It comes . It can refer to: *the interior of a vessel, such as the central space in an artery, vein or capillary through which blood flows *the interior of the gastrointestinal tract *the pathways of the bronchi in the lungs *the interior of renal tubules and urinary collecting ducts *the pathways of the female genital tract, starting with a single pathway of the vagina, splitting up in two lumina in the uterus, both of which continue through the fallopian tubes *the fluid-filled cavity forming in the blastocyst during pre-implantation development called the blastocoel In cell biology, lumen is a membrane-defined space that is found inside several organelles, cellular components, or structures, including thylakoid, endoplasmic reticulum, Golgi apparatus, lysosome, mitochondrion, and microtubule. Transluminal procedures ''Transluminal procedures'' are procedures occur ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha Factor
The ''α''-factor is a dimensionless quantity used to predict the solid–liquid interface type of a material during solidification. It was introduced by physicist Kenneth A. Jackson in 1958. In his model, crystal growth with larger values of ''α'' is smooth, whereas crystals growing at smaller ''α'' (below the threshold value of 2) have rough surfaces. Method According to John E. Gruzleski in his book ''Microstructure Development During Metalcasting'' (1996): : \alpha = \frac\cdot\frac where L is the latent heat of fusion; k is the Boltzmann constant; T_\mathrm is the freezing temperature at equilibrium; \eta is the number of nearest neighbours an atom has in the interface plane; and v is the number of nearest neighbours in the bulk solid. As \frac = \Delta S_f, where \Delta S_f is the molar entropy of fusion of the material, : \alpha = \frac \cdot \frac According to Martin Glicksman in his book ''Principles of Solidification: An Introduction to Modern Casting and Cryst ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Invertase
β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. Sucrose is a fructoside. Alternative names for β-fructofuranosidase include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase. The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertase is a glycoprotein that hydrolyses (cleaves) the non-reducing terminal β-fructofuranoside residues. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. Invertase cleaves the α-1,2-glycosidic bond of sucrose. For industrial use, invertase is usually derived from yeast. It is also synthesized by bees, which use it to make honey from nectar. The temperature optimum is 60 °C and a pH optimum i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Permissive Temperature
Temperature-sensitive mutations are variants of genes that allow the organism to function normally at low temperatures but alter its function at higher temperatures. Cold-sensitive mutants are variants of genes that allow normal function of the organism at higher temperatures but altered function at low temperatures. Mechanism Most temperature-sensitive mutations affect proteins, and cause loss of protein function at the non-permissive temperature. The permissive temperature is one at which the protein typically can fold properly or remain properly folded. At higher temperatures, the protein is unstable and ceases to function properly. These mutations are usually recessive in diploid organisms. Temperature -sensitive mutations arrange a reversible mechanism and can reduce particular gene products at varying stages of growth, which is easily done by changing the temperature of growth. Permissive temperature ditThe permissive temperature is the temperature at which a temperature-se ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
