Copilot
Your everyday AI companion
  1. SymbolHSP70
    Pfam clanCL0108
    InterProIPR013126
  1. Heat shock protein - Wikipedia

  2. People also ask
    "Chaperone-Based Therapeutic Target Innovation: Heat Shock Protein 70 (HSP70) for Type 2 Diabetes Mellitus".
    en.wikipedia.org
    Proteins with similar structure exist in virtually all living organisms. Intracellularly localized Hsp70s are an important part of the cell's machinery for protein folding, performing chaperoning functions, and helping to protect cells from the adverse effects of physiological stresses.
    en.wikipedia.org
    The Hsp70 chaperones function in a wide range of cellular housekeeping activities, including the folding of newly synthesized proteins, the translocation of polypeptides into mitochondria, chloroplasts and the endoplasmic reticulum (ER), the disassembly of protein complexes and the regulation of protein activity (Fig. 1 ).
    Canonical model: J protein delivery and NEF-driven release. Much of the early biochemical work on HSP70 function focused on the ability of the core machinery to facilitate the folding of denatured proteins (such as luciferase) in vitro.
  3. The Hsp70 chaperone network | Nature Reviews โ€ฆ

    WEBJun 28, 2019 · This knowledge showcases how the Hsp70 chaperone system controls diverse cellular functions, and offers new opportunities โ€ฆ

    • Author: Rina Rosenzweig, Nadinath B. Nillegoda, Matthias P. Mayer, Bernd Bukau, Bernd Bukau
    • Publish Year: 2019
  4. Hsp70 - Wikiwand

  5. Hsp70 - an overview | ScienceDirect Topics

  6. The human HSP70 family of chaperones: where do we stand?

  7. The HSP70 chaperone machinery: J proteins as drivers โ€ฆ

    WEBSep 23, 2010 · Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across...

  8. Hsp70 chaperones: Cellular functions and molecular mechanism

  9. The complex evolution of the metazoan HSP70 gene family

  10. The nucleotide exchange factors of Hsp70 molecular โ€ฆ

    WEBHsp70 proteins comprise an N-terminal nucleotide binding domain (NBD) and a substrate binding domain (SBD), which communicate by allosteric signals (reviewed in Mayer, 2013 ). The nucleotide is bound โ€ฆ

  11. Some results have been removed