Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70)
نویسندگان
چکیده
منابع مشابه
Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody.
Immunization of mice with a 14-mer peptide TKDNNLLGRFELSG, termed "TKD," comprising amino acids 450-461 (aa(450-461)) in the C terminus of inducible Hsp70, resulted in the generation of an IgG1 mouse mAb cmHsp70.1. The epitope recognized by cmHsp70.1 mAb, which has been confirmed to be located in the TKD sequence by SPOT analysis, is frequently detectable on the cell surface of human and mouse ...
متن کاملmolecular, evolution and stratification study of the heat shock protein 70 (hsp70) genes family in cattle
heat shock proteins (hsps), are highly important due to their association with such economically important traits in animals as resistance to temperature shock and mastitis. in the current study, to get a comprehensive information on molecular structure and evolution of the hsp70s, and the available hsp70 sequences of the cattle and other animals taken from ncbi and aligned together. then, nucl...
متن کاملmolecular characterization of a 70 kda heat shock protein (hsp70) gene in entamoeba dispar
amebiasis caused by entamoeba histolytica is still mentioned as one of the major health problems in tropical and subtropical areas. e. histolytica has recently been redescribed as two distinct species; e. histolytica and e. dispar. in the present study, we characterized the 70 kda heat shock protein (hsp70) of e. dispar at molecular level and compared it with that of e. histolytica. with these ...
متن کاملAllosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.
The 70-kDa heat shock protein (Hsp70) chaperones perform a wide array of cellular functions that all derive from the ability of their N-terminal nucleotide-binding domains (NBDs) to allosterically regulate the substrate affinity of their C-terminal substrate-binding domains in a nucleotide-dependent mechanism. To explore the structural origins of Hsp70 allostery, we performed NMR analysis on th...
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ژورنال
عنوان ژورنال: Current Topics in Medicinal Chemistry
سال: 2016
ISSN: 1568-0266
DOI: 10.2174/1568026616666160413140911