Study of Protein Expresion in Peri-Infarct Tissue after Cerebral Ischemia.
Santiago de Compostela, Spain. In Sci Rep, Dec 2014
Further studies by 1D and 2D western blotting and immunohistochemistry revealed that only one member of this family (the inducible form, HSP72 or HSP70i) is specifically expressed by the peri-infarct tissue, while the majority of this family (the constitutive form, HSC70 or HSP70c) is expressed in the whole brain.
Matrine modulates HSC70 levels and rescues ΔF508-CFTR.
Salerno, Italy. In J Cell Physiol, 2012
downregulation of HSC70 resulted in increased levels of DeltaF508-CFTR complexes with the co-chaperone BAG3 that in addition appeared to co-localize with the mutated protein on the cell surface.
Molecular mechanism and physiological functions of clathrin-mediated endocytosis.
Cambridge, United Kingdom. In Nat Rev Mol Cell Biol, 2011
The process involves the formation of a putative FCH domain only (FCHO) initiation complex, which matures through adaptor protein 2 (AP2)-dependent cargo selection, and subsequent coat building, dynamin-mediated scission and finally auxilin- and heat shock cognate 70 (HSC70)-dependent uncoating.
Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein.
Wako, Japan. In Nat Biotechnol, 2010
As the polyglutamine binding peptide 1 (QBP1) is known to bind an expanded polyQ tract but not the polyQ motif found in normal HTT, we selectively targeted mutant HTT for degradation by expressing a fusion molecule comprising two copies of QBP1 and copies of two different heat shock cognate protein 70 (HSC70)-binding motifs in cellular and mouse models of HD.