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 supported by chaperones like Trigger factor (TF) and SecB.
“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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The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins
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Szekely, O., Olsen, G. L., Novakovic, M., Rosenzweig, R., & Frydman, L. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c00807 · Cited by 32 · see citing works
- 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
- Physical Sciences › Materials Science › Materials Chemistry › 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
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