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Structural basis for protein antiaggregation activity of the trigger factor chaperone.
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Nuclear magnetic resonance data show how molecular chaperones recognize and prevent aggregation and misfolding of unfolded proteins. [Also see Perspective by Gamerdinger and Deuerling ]
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“Translocation competence is furthermore supported by chaperones like Trigger factor (TF) (Saio et al., 2014, 2018; Can et al., 2017; De Geyter et al., 2020) or SecB (Bechtluft et al., 2010; Huang et al., 2016; Figure 2).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Saio et al., 2014
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Metadata
- Authors
- Saio, T., Guan, X., Rossi, P., Economou, A., & Kalodimos, C. G.
- Affiliations
- Rutgers, The State University of New Jersey (US)
- University of Crete (GR)
- Corresponding author
- Saio, Tomohide
- Guan, Xiao
- Kalodimos, Charalampos G.
- Venue
- Science
- Published
- 2014-05-09
- Volume
- 344
- Issue
- 6184
- Pages
- 1250494-1250494
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4070327
- OpenAlex
- W2086628547
- Cited by
- 289
- References
- 93
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 21 · 2023: 17 · 2022: 24 · 2021: 37 · 2020: 21 · 2019: 29 · 2018: 32 · 2017: 29 · 2016: 31 · 2015: 19 · 2014: 8
- FWCI
- 11.90
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Lirias (KU Leuven) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM073854, GM073854)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- precipitating factors, molecular chaperones, alkaline phosphatase, phoA, hydrophobic interactions, multivalent binding, protein dynamics, protein folding
- MeSH terms
- Alkaline Phosphatase, Binding Sites, Peptides, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Molecular Chaperones, Peptidylprolyl Isomerase, Nuclear Magnetic Resonance, Biomolecular, Escherichia coli Proteins, Hydrophobic and Hydrophilic Interactions, Intrinsically Disordered Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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