Cited by 289Heat shock proteins researchProtein Structure and DynamicsEnzyme Structure and Function

Structural basis for protein antiaggregation activity of the trigger factor chaperone.

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Saio, Tomohide, Guan, Xiao, Rossi, Paolo, Economou, Anastassios, Kalodimos, Charalampos G.·2014·Science

Abstract

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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Crossref · 10.1126/science.1250494

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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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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
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
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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