Cited by 54Heat shock proteins researchProtein Structure and DynamicsEnzyme Structure and Function

Chaperone-Bound Clients: The Importance of Being Dynamic

Open access
Hiller, Sebastian·2019·Trends in Biochemical Sciences

Abstract

Several recent atomic-resolution studies have resolved how chaperones interact with their client proteins. In some cases, molecular chaperones recognize and bind their clients in conformational ensembles that are locally highly dynamic and interconvert, while in other cases clients bind in unique conformations. The presence of a locally dynamic client ensemble state has important consequences, both for the interpretation of experimental data and for the functionality of chaperones, as local dynamics facilitate rapid client release, folding on and from the chaperone surface, and client recognition without shape complementarity. Facilitated by the local dynamics, at least some chaperones appear to specifically recognize energetically frustrated sites of partially folded client proteins, such that the release of frustration contributes to the interaction affinity.

Integrity signals

Registry

Crossref · 10.1016/j.tibs.2018.12.005

Cites

84 of 84 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Hiller, S.
Affiliations
University of Basel (CH)
Corresponding author
Hiller, Sebastian
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2019-06
Volume
44
Issue
6
Pages
517-527
ISSN
0968-0004 (ISSN-L)
OpenAlex
W2906694226
Cited by
54
References
84
Citations by year
2026: 1 · 2025: 5 · 2024: 5 · 2023: 10 · 2022: 20 · 2021: 3 · 2020: 5 · 2019: 5
FWCI
0.73
Type
journal article
Language
en
Open access
Locations
  • Trends in Biochemical Sciences (publishedVersion)
  • PubMed (publishedVersion)
  • edoc (University of Basel) (acceptedVersion, other-oa)
Funders
Swiss National Science Foundation
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
molecular chaperones, chaperone-client interactions, conformational ensembles, local dynamics, protein folding
MeSH terms
Humans, Protein Conformation, Thermodynamics, Protein Folding, Molecular Chaperones, Nuclear Magnetic Resonance, Biomolecular, Periplasmic 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 ›

Are you an author, or do you see a problem with this page? Request a review