We are analyzing https://link.springer.com/article/10.1007/s12192-017-0776-y.

Title:
The remarkable multivalency of the Hsp70 chaperones | Cell Stress and Chaperones
Description:
Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases.
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Keywords {🔍}

pubmed, article, google, scholar, cas, hsp, central, protein, biol, chaperone, cell, chaperones, chem, proteins, molecular, mol, zuiderweg, sci, dnak, heat, shock, binding, gestwicki, domain, structure, stress, structural, hsc, doijbcm, interaction, interactions, proc, natl, acad, hartl, hightower, biochem, folding, chaperonemediated, complex, kda, cochaperone, substrate, zhang, dnaj, science, york, privacy, cookies, content,

Topics {✒️}

month download article/chapter multivalent protein–protein interactions hsp70-bag3 protein-protein interaction heat-shock cognate protein o'leary jc 3rd chaperone-mediated protein folding protein-protein interface regulates post-translational protein import nih grant 5-r01-ns-059690-01-08 chaperone-mediated autophagy atp-bound open conformation c-terminal allosteric pocket related subjects tumor-specific death program hsc70-binding peptides selected biological nanopore-based sensors leung sm full article pdf 16-kda protein functions optimize adenosine-derived inhibitors isoform-selective genetic inhibition nmr structure determination article cell stress hsp70 nucleotide exchange hsp70 chaperone proteins hsp70 chaperone cycle protein quality control hsc70-interacting protein hsp70 chaperone machinery chaperoned client proteins privacy choices/manage cookies hsc70 molecular chaperone hsp70 molecular chaperone carboxy-terminal domain bag/hsc70 complex cation channel formed reconstituted multiprotein complex jinwal uk human hsp70 family protein folding handbook cell-penetrating activity target cytosolic proteins unusual dynamic interface antitumor compound mkt-077 dnaj-promoted binding hip-hop connection newly translated proteins allosteric mechanism mediated molecular chaperone dnak ligand discrimination

Questions {❓}

Radons J (2016) The human HSP70 family of chaperones: where do we stand?

Schema {🗺️}

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