ArticleThe Biochemical journal1995
Chemical modifications of a recombinant bovine stress-inducible 70 kDa heat-shock protein (Hsp70) mimics Hsp70 isoforms from tissues.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 43 citations in OpenAlex.
- Association of heat-shock protein 70.1 gene with physiological and physical performance of Bali cattle.Veterinary world · 2024Article
- Identification of abnormal gene expression in bovine transgenic somatic cell nuclear transfer embryos.Journal of veterinary science · 2014Article
- Molecular cloning and characterization of cDNA encoding a putative stress-induced heat-shock protein from Camelus dromedarius.International journal of molecular sciences · 2011Article
- Proteomic and phosphoproteomic analyses of the soluble fraction following acute spinal cord contusion in rats.Journal of neurotrauma · 2010Article
- Molecular Characterization of Heat Shock Protein 70-1 Gene of Goat (Capra hircus).Molecular biology international · 2010Article
- Hsp70B' regulation and function.Cell stress & chaperones · 2007Article
- Hsp70B' regulation and function.Cell stress & chaperones · 2007Article
- cDNA of canine heat shock protein 70 (HSP70).Veterinary research communications · 2004Article
- Identification of sequence similarity between 60 kDa and 70 kDa molecular chaperones: evidence for a common evolutionary background?The Biochemical journal · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A cDNA clone for the stress-inducible 70 kDa heat-shock protein (Hsp70) has been isolated from a bovine skeletal-muscle cDNA library. This mRNA encodes a protein with a calculated molecular mass of 70250 Da. The cDNA has one continuous open reading frame capable of encoding a 641-amino-acid protein. Expression of this cDNA in a bacterial expression system produced a protein with a mobility identical with that of the inducible Hsp70 protein from bovine skeletal muscle as determined by SDS/PAGE. Two-dimensional gel electrophoresis demonstrated this protein to have focusing properties identical with that of a minor isoform from bovine skeletal muscle. Upon carbamylation of this bacterially expressed protein, a train of charged proteins with charge differences of -1 were produced. These carbamylated proteins were shown to have similar focusing mobilities to the Hsp70 isoforms isolated from bovine skeletal muscle. These results demonstrate the identification of a skeletal-muscle inducible Hsp70 gene and suggest that the presence of multiple Hsp70 isoforms may be the product of post-translational modifications to the Hsp70 proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.