The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers
Open accessAbstract
The small heat shock protein αB-crystallin (αB) contributes to cellular protection against stress. For decades, high-resolution structural studies on oligomeric αB have been confounded by its polydisperse nature. Here, we present a structural basis of oligomer assembly and activation of the chaperone using solid-state NMR and small-angle X-ray scattering (SAXS). The basic building block is a curved dimer, with an angle of ∼121° between the planes of the β-sandwich formed by α-crystallin domains. The highly conserved IXI motif covers a substrate binding site at pH 7.5. We observe a pH-dependent modulation of the interaction of the IXI motif with β4 and β8, consistent with a pH-dependent regulation of the chaperone function. N-terminal region residues Ser59-Trp60-Phe61 are involved in intermolecular interaction with β3. Intermolecular restraints from NMR and volumetric restraints from SAXS were combined to calculate a model of a 24-subunit αB oligomer with tetrahedral symmetry.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Rajasekaran, N. S., Connell, P., Christians, E. S., Yan, L.-J., Taylor, R. P., Orosz, A., Zhang, X. Q., Stevenson, T. J., Peshock, R. M., Leopold, J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.044 · Cited by 437
Cited by
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
Basha, E., O’Neill, H., & Vierling, E. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.11.005 · Cited by 538
One size does not fit all: The oligomeric states of αB crystallin
Delbecq, S. P., & Klevit, R. E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.021 · Cited by 263
Self-citationCapturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution
Berkeley, R. F., Plonski, A. P., Phan, T. M., Grohe, K., Becker, L., Wegner, S., Herzik, M. A., Mittal, J., & Debelouchina, G. T. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c18668 · Cited by 12
Metadata
- Authors
- Jehle, S., Rajagopal, P., Bardiaux, B., Markovic, S., Kühne, R., Stout, J. R., Higman, V. A., Klevit, R. E., van Rossum, B.-J., & Oschkinat, H.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-08-29
- Volume
- 17
- Issue
- 9
- Pages
- 1037-1042
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2138456893
- Cited by
- 276
- References
- 2
- FWCI
- 12.29
- Type
- journal article
- Language
- en
- Open access
- green
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers. https://app.cochat.ai/papers/10.1038/nsmb.1891
- The paper
- Jehle, S., Rajagopal, P., Bardiaux, B., Markovic, S., Kühne, R., Stout, J. R., Higman, V. A., Klevit, R. E., van Rossum, B.-J., & Oschkinat, H. (2010). Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1891
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
