chaperones in protein folding - Search
  1. Chaperone machines for protein folding, unfolding and ... - Nature

    • •Molecular chaperones have key roles in protein quality control and recovery from stress conditions. They assist folding and unfolding and prevent or reverse aggregation of a wide range of substrates, but th… See more

    Abstract

    Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascent proteins to reach their native fold, protect subunits from heat shock durin… See more

    Nature
    Main

    Protein quality control, also known as proteostasis, constitutes the regulation of protein synthesis, folding, unfolding and turnover. It is mediated by chaperone and protease sy… See more

    Nature
    Chaperone families

    Members of the HSP60 (known as GroEL in Escherichia coli), HSP70 (known as DnaK in E. coli), HSP90 (known as HptG in E. coli) and HSP100 (known as ClpA and ClpB in E. … See more

    Nature
    HSP70 — a tuneable chaperone system

    HSP70 is the most abundant chaperone and exists as many orthologues in different cellular compartments. In association with various cofactors it carries out diverse functions, i… See more

    Nature
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  2. Chaperones are a functionally related group of proteins assisting protein folding in the cell under physiological and stress conditions. They share the ability to recognize and bind nonnative proteins thus preventing unspecific aggregation.
    Author: M Beissinger, J Buchner
    Publish Year: 1998
    pubmed.ncbi.nlm.nih.gov/9563819/
    pubmed.ncbi.nlm.nih.gov/9563819/
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  3. People also ask
    What role do molecular chaperones play in protein folding?
    The role of molecular chaperones in protein folding Folding of newly synthesized polypeptides in the crowded cellular environment requires the assistance of so-called molecular chaperone proteins.
    Which molecular chaperones fold nascent client proteins?
    The folding of nascent client proteins by their chaperone and co-chaperones. Exemplifying the folding of the muscle myosin II globular head domain by Hsp90α1 and Unc45b as an example of molecular chaperones folding their client proteins.
    Does a protein fold without a chaperone?
    Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same. Other chaperones work as holdases: they bind folding intermediates to prevent their aggregation, for example DnaJ or Hsp33. [ 6]
    Do chaperone systems work as foldases?
    Some chaperone systems work as foldases: they support the folding of proteins in an ATP-dependent manner (for example, the GroEL / GroES or the DnaK / DnaJ / GrpE system). Although most newly synthesized proteins can fold in absence of chaperones, a minority strictly requires them for the same.
     
  4. Molecular chaperones in protein folding and proteostasis | Nature

     
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  13. How chaperones fold proteins - PubMed

  14. Chaperone machines for protein folding, unfolding and …

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  16. Chaperone (protein) - Wikipedia

  17. Chaperone-Mediated Protein Folding | Physiological Reviews

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  19. The Hsp70 chaperone network | Nature Reviews Molecular Cell …

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  21. What are Chaperone Proteins? - News-Medical.net

  22. The role of molecular chaperones in protein folding - PubMed

  23. A Master Regulator of Protein Production - www.caltech.edu

  24. Pathways of chaperone-mediated protein folding in the cytosol

  25. How do chaperonins fold protein? - PMC - National Center for ...

  26. Comprehensive Analysis of Age- and Sex-Related Expression of …