Molecular Chaperones

January 2004
Encyclopedic Reference of Molecular Pharmacology;2004, p602
Reference Entry
The article presents an encyclopedia entry for "molecular chaperones." They refer to the protein family that mediates the correct folding of other proteins, and, in some cases, their assembly into oligomeric structures. Molecular chaperones assist the folding of protein by inhibiting the alternative folding pathways that lead to nonfunctional structures.


Related Articles

  • Biological activities of HAP46/BAG-1. Gehring, Ulrich // EMBO Reports;Feb2004, Vol. 5 Issue 2, p148 

    HAP46/BAG-1M and its isoforms affect the protein-folding activities of mammalian HSP70 chaperones. They interact with the ATP-binding domain of HSP70 or HSC70, leaving the substratebinding site available for further interactions. Trimeric complexes can therefore form with, for example,...

  • Kinetic model of lysozyme renaturation with the molecular chaperone GroEL. Xiao-Yan Dong; Yu-Bing Wang; Xiao-Guang Liu; Yan Sun // Biotechnology Letters;Jul2001, Vol. 23 Issue 14, p1165 

    From the renaturation kinetics of denatured/reduced lysozyme assisted by the molecular chaperone GroEL, a simplified kinetic model was established based on the competition between protein folding and aggregation. In the presence of GroEL and ATP, the aggregate formation was a second order...

  • Protein folding: Chaperone embrace. Cesari, Francesca // Nature Reviews Molecular Cell Biology;Jul2008, Vol. 9 Issue 7, p497 

    This article reports on heat-shock protein-70 proteins, the molecular chaperones that are involved in many cellular processes, such as protein folding, transport across membranes, prevention of protein aggregation and degradation. The activity of heat-shock protein-70 is regulated by...

  • Protein quality control: knowing when to fold. Swaminathan, Sowmya // Nature Cell Biology;Jul2005, Vol. 7 Issue 7, p647 

    The article cites a study conducted by researcher Judith Frydman published in the June 3, 2005 issue of "Cell" which shows that distinct chaperone pathways control the decision between either folding or degrading cytoplasmic proteins. Misfolded proteins can be refolded or they can be degraded by...

  • Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. Dubaquié, Yves; Looser, Renate; Fünfschilling, Ursula; Jenö, Paul; Rospert, Sabine // EMBO Journal;10/15/98, Vol. 17 Issue 20, p5868 

    The mechanism of chaperonin-assisted protein folding has been mostly analyzed in vitro using non-homologous substrate proteins. In order to understand the relative importance of hsp60 and hsp10 in the living cell, homologous substrate proteins need to be identified and analyzed. We have devised...

  • A New Understanding of Protein Mutation Unfolds. Conn, P. Michael; Janovick, Jo Ann // American Scientist;Jul/Aug2005, Vol. 93 Issue 4, p314 

    This article focuses on an experiment on pharmacological chaperones or pharmacoperones. Pharmacoperones correct the intracellular routing of a misfolded yet potentially functional protein, thereby reversing in cultured cells one cause of a hormonal disease called hypogonadolropic hypogonadism....

  • Protein folding: Sticky N17 speeds huntingtin pile-up. Liebman, Susan W.; Meredith, Stephen C. // Nature Chemical Biology;Jan2010, Vol. 6 Issue 1, p7 

    The article discusses the role of the 17-residue N-terminal domain in the aggregation of huntingtin (Htt) protein. Research also found that deletion of N17 stops Htt aggregation. The authors also discuss that the research indicates that chaperonin TRiC binding to N17 can explain the inhibition...

  • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. Dragovic, Zdravko; Broadley, Sarah A; Shomura, Yasuhito; Bracher, Andreas; Hartl, F Ulrich // EMBO Journal;6/7/2006, Vol. 25 Issue 11, p2519 

    Hsp70 molecular chaperones function in protein folding in a manner dependent on regulation by co-chaperones. Hsp40s increase the low intrinsic ATPase activity of Hsp70, and nucleotide exchange factors (NEFs) remove ADP after ATP hydrolysis, enabling a new Hsp70 interaction cycle with non-native...

  • Role of the ?-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. Chaudhry, Charu; Farr, George W.; Todd, Matthew J.; Rye, Hays S.; Brunger, Axel T.; Adams, Paul D.; Horwich, Arthur L.; Sigler, Paul B. // EMBO Journal;10/1/2003, Vol. 22 Issue 19, p4877 

    Productive cis folding by the chaperonin GroEL is triggered by the binding of ATP but not ADP, along with cochaperonin GroES, to the same ring as nonnative polypeptide, ejecting polypeptide into an encapsulated hydrophilic chamber. We examined the specific contribution of the γ-phosphate of...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics