Topic
HSPA4
About: HSPA4 is a research topic. Over the lifetime, 1234 publications have been published within this topic receiving 75561 citations. The topic is also known as: APG-2 & HEL-S-5a.
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TL;DR: A cDNA clone is characterized that encodes a protein related to the 70 kd heat shock protein, but is expressed in normal rat liver, and it is identical with two previously described proteins: GRP78, whose synthesis is induced by glucose starvation, and BiP, which is found bound to immunoglobulin heavy chains in pre-B cells.
1,401 citations
TL;DR: It is concluded that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1, which can be activated by nonnative protein, heat, and geldanamycin.
1,181 citations
TL;DR: Many specific sites in Drosophila chromatin are hypersensitive to DNase I and the positions of such sites were mapped along the regions of the genome coding for two heat shock proteins.
Abstract: Many specific sites in Drosophila chromatin are hypersensitive to DNase I. The positions of such sites were mapped along the regions of the genome coding for two heat shock proteins. Such sites lie at the 5' ends of heat shock genes and may function as elements for recognition by molecules which regulate gene activity.
968 citations
TL;DR: A 73-kilodalton protein was found to bind to peptide regions that target intracellular proteins for lysosomal degradation in response to serum withdrawal, and sequences of two internal peptides of the 73-kD protein confirm that it is a member of this family.
Abstract: A 73-kilodalton (kD) intracellular protein was found to bind to peptide regions that target intracellular proteins for lysosomal degradation in response to serum withdrawal. This protein cross-reacted with a monoclonal antibody raised to a member of the 70-kD heat shock protein (hsp70) family, and sequences of two internal peptides of the 73-kD protein confirm that it is a member of this family. In response to serum withdrawal, the intracellular concentration of the 73-kD protein increased severalfold. In the presence of adenosine 5'-triphosphate (ATP) and MgCl2, the 73-kD protein enhanced protein degradation in two different cell-free assays for lysosomal proteolysis.
882 citations
TL;DR: It is shown here that the widely conserved heat shock protein DegP (HtrA) has both general molecular chaperone and proteolytic activities, which mean that a single cellular factor can switch between two key pathways, controlling protein stability and turnover.
777 citations