ReviewFASEB journal : official publication of the Federation of American Societies for Experimental Biology1996
Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.
Review in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 149 citations in OpenAlex.
- How does protein aggregate structure affect mechanisms of disaggregation?Biochemical Society transactions · 2025Review
- The Right-Handed Parallel β-Helix Topology ofBiomolecules · 2021Article
- Article
- Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis.Nature structural & molecular biology · 2016Article
- Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.Biochemistry · 2014Article
- The βγ-crystallins: native state stability and pathways to aggregation.Progress in biophysics and molecular biology · 2014Review
- Protein quantity on the air-solid interface determines degradation rates of human growth hormone in lyophilized samples.Journal of pharmaceutical sciences · 2014Article
- Folding the proteome.Trends in biochemical sciences · 2013Review
- Article
- The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.Bacteriophage · 2012Article
- Life in the cold: a proteomic study of cold-repressed proteins in the antarctic bacterium pseudoalteromonas haloplanktis TAC125.Applied and environmental microbiology · 2011Article
- Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability.Biomacromolecules · 2010Article
- Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- A simple and efficient expression and purification system using two newly constructed vectors.Protein expression and purification · 2009Article
- Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo.Journal of molecular biology · 2008Article
- Bacterial inclusion bodies contain amyloid-like structure.PLoS biology · 2008Article
- Contrasting disease and nondisease protein aggregation by molecular simulation.Accounts of chemical research · 2008Review
- Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure.Protein science : a publication of the Protein Society · 2006Article
- Influence of denatured and intermediate states of folding on protein aggregation.Protein science : a publication of the Protein Society · 2005Article
- Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli.Protein science : a publication of the Protein Society · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
An unexpected aspect of the expression of cloned genes is the frequent failure of newly synthesized polypeptide chains to reach their native state, accumulating instead as insoluble inclusion bodies. Amyloid deposits represent a related state associated with a variety of human diseases. The critical folding intermediates at the juncture of productive folding and the off-pathway aggregation reaction have been identified for the phage P22 tailspike and coat proteins. Though the parallel beta coil tailspike is thermostable, an early intracellular folding intermediate is thermolabile. As the temperature of intracellular folding is increased, this species partitions to inclusion bodies, a kinetic trap within the cell. The earliest intermediates along the in vitro aggregation pathway, sequential multimers of the thermolabile folding intermediates, have been directly identified by native gel electrophoresis. Temperature-sensitive folding (tsf) mutations identify sites in the beta coil domain, which direct the junctional intermediate down the productive pathway. Global suppressors of tsf mutants inhibit the pathway to inclusion bodies, rescuing the mutant chains. These mutants identify sites important for avoiding aggregation. Coat folding intermediates also partition to inclusion bodies as temperature is increased. Coat tsf mutants are suppressed by overexpression of the GroE chaperonin, indicating that the thermolabile intermediate is a physiological substrate for GroE. We suggest that many proteins are likely to have thermolabile intermediates in their intracellular folding pathways, which will be precursors to inclusion body formation at elevated temperatures and therefore substrates for heat shock chaperonins.
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What OpenQuestion holds
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.