molecular chaperone वाक्य
उदाहरण वाक्य
मोबाइल
- Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures.
- "' Hsp33 protein "'is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation.
- As a molecular chaperone, this protein may affect the folding or stability of other ciliary or basal body proteins.
- In the case of CASA, dysfunctional, nonnative proteins are recognized by molecular chaperones and become ubiquitinated by chaperone-associated ubiquitin ligases.
- It assists in the folding of other proteins, acting as a kind of molecular chaperone ( thus the name ).
- Other pro-survival factors interacting with class III ?-tubulin enabling cellular adaptation to oxidative stress include the molecular chaperone HSP70 / GRP75.
- Zinc finger and BTB domain-containing protein 16 and BAG family molecular chaperone regulator function as co-chaperone proteins in processes involving HB-EGF.
- Normally when a protein does not fold correctly, molecular chaperones in the cell can encourage refolding back into its active form.
- DNAJC6 belongs to the evolutionarily conserved DNAJ / HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity.
- It also shows homology to prefoldins which are small molecular weight proteins that assemble into molecular chaperone complexes to affect protein folding.
- HB-EGF biological activities with these genes influence cell cycle progression, molecular chaperone regulation, cell survival, cellular functions, adhesion, and mediation of cell migration.
- This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones.
- As an ER molecular chaperone, BiP is also required to import polypeptide into the ER lumen or ER membrane in an ATP-dependent manner.
- In muscle cells, BAG3 cooperates with the molecular chaperones Hsc70 and HspB8 to induce the degradation of mechanically damaged cytoskeleton components in lysosomes.
- Unlike many other molecular chaperones, prefoldin does not use chemical energy, in the form of adenosine triphosphate ( ATP ), to promote protein folding.
- From 1990 until 2009, he organised annual meetings of the UK Molecular Chaperone Club at the Universities of Oxford, Cambridge, London, Bristol, Birmingham and Warwick.
- The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules.
- The encoded protein is one of six subunits of prefoldin, a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thereby allowing them to fold correctly.
- This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex ( CCT ), also known as the TCP1 ring complex ( TRiC ).
- This gene encodes a molecular chaperone that is a member of the chaperonin containing TCP1 complex ( CCT ), also known as the TCP1 ring complex ( TRiC ).
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