The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Open accessAbstract
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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Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
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In vivo aspects of protein folding and quality control
Balchin, D., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Science · doi:10.1126/science.aac4354 · Cited by 1,477
Protein export through the bacterial Sec pathway
Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447
Self-citationRegulation of α-synuclein by chaperones in mammalian cells
Burmann, B. M., Gerez, J. A., Matečko-Burmann, I., Campioni, S., Kumari, P., Ghosh, D., Mazur, A., Aspholm, E. E., Šulskis, D., Wawrzyniuk, M., et al. (2020) · Nature · doi:10.1038/s41586-019-1808-9 · Cited by 255
NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function
Alderson, T. R., & Kay, L. E. (2021) · Cell · doi:10.1016/j.cell.2020.12.034 · Cited by 233
Single-Molecule Studies of Protein Folding with Optical Tweezers
Bustamante, C., Alexander, L., Maciuba, K., & Kaiser, C. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111442 · Cited by 200
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
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