We are analyzing https://link.springer.com/article/10.1007/s00018-004-4464-6.

Title:
Hsp70 chaperones: Cellular functions and molecular mechanism | Cellular and Molecular Life Sciences
Description:
Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.
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Keywords {🔍}

google, scholar, article, pubmed, cas, hsp, biol, chaperone, protein, molecular, cell, proteins, chem, chaperones, bukau, dnak, function, heat, mol, shock, binding, sci, mayer, bag, embo, cellular, substrate, domain, structure, dnaj, folding, natl, usa, mechanism, nat, proc, acad, hsc, activity, atpase, nucleotide, regulation, peptide, cycle, exchange, hartl, escherichia, coli, factor, action,

Topics {✒️}

month download article/chapter hsp90/hsp70-based chaperone machinery anti-apoptotic protein bag-1 heat shock/stress proteins anti-apoptotic function downstream gly/phe-rich region hsp90-based chaperone system hsp90-based chaperone machinery chaperone/ubiquitin ligase chip 60-kilodalton stress-related protein tumor-derived mutant forms heat-shock protein 70 hsp70/hsp90 chaperone system heat shock proteins heat-shock proteins protein import motor hsp70/atp-dependent process molecular chaperone hsp70/hsc70 converts t-cell tolerance atp-induced conformational change tumor-specific death program low affinity state hsp70–hsp90 multichaperone machine molecular chaperones hsc70/hsp70 heat shock response tpr domain-peptide complexes dnaj-mediated activation full article pdf heat-inactivated proteins peres ben zvi peres ben-zvi bag4/sodd protein escherichia coli dnaj molecular chaperone hsca chaperone-protein interaction privacy choices/manage cookies polyglutamine protein aggregation nucleotide exchange factor dnak chaperone machinery dna-binding protein molecular chaperone hsc70 ubiquitinating hsp/hsc70 substrate binding domain short bag domain ubiquitin-related bag-1 hsp70-protein complexes signaling protein function nucleotide exchange factors protein folding processes hsp70 chaperone dnak

Questions {❓}

(2002) The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?
(2002) What's in the ‘BAG'?

Schema {🗺️}

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