ArticleBiophysical chemistry2010
Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP.
Article in Biophysical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Maize heat shock proteins-prospection, validation, categorization and in silico analysis of the different ZmHSP families.Stress biology · 2023Article
- Real-time single-molecule observation of chaperone-assisted protein folding.Science advances · 2022Article
- Vesicle-based cell-free synthesis of short and long unspecific peroxygenases.Frontiers in bioengineering and biotechnology · 2022Article
- Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational Modification.ACS central science · 2019Article
- Endoplasmic reticulum stress, autophagic and apoptotic cell death, and immune activation by a natural triterpenoid in human prostate cancer cells.Journal of cellular biochemistry · 2019Article
- The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.The Journal of biological chemistry · 2019Review
- Constructive approach for synthesis of a functional IgG using a reconstituted cell-free protein synthesis system.Scientific reports · 2019Article
- High-throughput screen for inhibitors of protein-protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex.The Journal of biological chemistry · 2018Article
- Article
- A peptidic unconjugated GRP78/BiP ligand modulates the unfolded protein response and induces prostate cancer cell death.PloS one · 2012Article
- Localization of BiP to translating ribosomes increases soluble accumulation of secreted eukaryotic proteins in an Escherichia coli cell-free system.Biotechnology and bioengineering · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Hsp70 family of molecular chaperones is an essential class of chaperones that is present in many different cell types and cellular compartments. We have compared the bioactivities of the prokaryotic cytosolic Hsp70, DnaK, to that of the eukaryotic Hsp70, BiP, located in the endoplasmic reticulum (ER). Both chaperones helped to prevent protein aggregation. However, only DnaK provided enhanced refolding of denatured proteins. We also tested chaperone folding assistance during translation in the context of cell-free protein synthesis reactions for several protein targets and show that both DnaK and BiP can provide folding assistance under these conditions. Our results support previous reports suggesting that DnaK provides both post-translational and co-translational folding assistance while BiP predominantly provides folding assistance that is contemporaneous with translation.
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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.