ArticleNature medicine2011
Protein folding in the cell: an inside story.
Article in Nature medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
16 citing papers in PubMed.
- Human Aha1's N-terminal extension confers it holdase activity in vitro.Protein science : a publication of the Protein Society · 2023Article
- Clearance of variant Creutzfeldt-Jakob disease prions in vivo by the Hsp70 disaggregase system.Brain : a journal of neurology · 2022Article
- The Possible Role of the Type I Chaperonins in Human Insulin Self-Association.Life (Basel, Switzerland) · 2022Article
- Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.Molecules (Basel, Switzerland) · 2021Article
- Function and Fiber-Type Specific Distribution of Hsp60 and αB-Crystallin in Skeletal Muscles: Role of Physical Exercise.Biology · 2021Review
- HSP60 Regulates Lipid Metabolism in Human Ovarian Cancer.Oxidative medicine and cellular longevity · 2021Article
- Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes.The Journal of biological chemistry · 2019Article
- Review
- Chaperonin of Group I: Oligomeric Spectrum and Biochemical and Biological Implications.Frontiers in molecular biosciences · 2017Review
- Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle.Frontiers in molecular biosciences · 2016Review
- Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity.Frontiers in molecular biosciences · 2016Review
- Identification of microRNAs and their targets in tomato infected with Cucumber mosaic virus based on deep sequencing.Planta · 2014Article
- Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural basis for protein antiaggregation activity of the trigger factor chaperone.Science (New York, N.Y.) · 2014Article
- Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
PubMed holds no abstract for this paper.
Indexed as
Identifiers
21989012What 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.