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, proc, natl, acad, hartl, hightower, interactions, biochem, folding, chaperonemediated, complex, kda, cochaperone, substrate, zhang, dnaj, science, york, privacy, cookies, journal,

Topics {✒️}

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

Questions {❓}

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

Schema {🗺️}

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