The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
Open accessOverview
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
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,715
Satisfying Hydrogen Bonding Potential in Proteins
McDonald, I. K., & Thornton, J. M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1334 · Cited by 2,130
Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters
Yamashita, A., Singh, S. K., Kawate, T., Jin, Y., & Gouaux, E. (2005) · Nature · doi:10.1038/nature03978 · Cited by 1,661
Structure of bacteriorhodopsin at 1.55 Å resolution
Luecke, H., Schobert, B., Richter, H.-T., Cartailler, J.-P., & Lanyi, J. K. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3027 · Cited by 1,450
GPCR Engineering Yields High-Resolution Structural Insights into β 2 -Adrenergic Receptor Function
Rosenbaum, D. M., Cherezov, V., Hanson, M. A., Rasmussen, S. G. F., Thian, F. S., Kobilka, T. S., Choi, H.-J., Yao, X.-J., Weis, W. I., Stevens, R. C., et al. (2007) · Science · doi:10.1126/science.1150609 · Cited by 1,336
Fersht, A. R., Matouschek, A., & Serrano, L. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90561-w · Cited by 932
Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å
Khademi, S., O'Connell, J., Remis, J., Robles-Colmenares, Y., Miercke, L. J. W., & Stroud, R. M. (2004) · Science · doi:10.1126/science.1101952 · Cited by 667
Helical Membrane Protein Folding, Stability, and Evolution
Popot, J.-L., & Engelman, D. M. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.881 · Cited by 589
Zhang, Z., & Marshall, A. G. (1998) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(97)00284-5 · Cited by 509
Cited by
Contribution of hydrogen bonds to protein stability
Pace, C. N., Fu, H., Lee Fryar, K., Landua, J., Trevino, S. R., Schell, D., Thurlkill, R. L., Imura, S., Scholtz, J. M., Gajiwala, K., et al. (2014) · Protein Science · doi:10.1002/pro.2449 · Cited by 599
Experimental Binding Energies in Supramolecular Complexes
Biedermann, F., & Schneider, H.-J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00583 · Cited by 554
Nick Pace, C., Scholtz, J. M., & Grimsley, G. R. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.05.006 · Cited by 386
Carbon-Oxygen Hydrogen Bonding in Biological Structure and Function
Horowitz, S., & Trievel, R. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.418574 · Cited by 338
Protein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 312
Metadata
- Authors
- Joh, N. H., Min, A., Faham, S., Whitelegge, J. P., Yang, D., Woods, V. L., & Bowie, J. U.
- Venue
- Nature
- Published
- 2008-05-25
- Volume
- 453
- Issue
- 7199
- Pages
- 1266-1270
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2041256732
- Cited by
- 254
- References
- 33
- FWCI
- 10.05
- 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: Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins. https://app.cochat.ai/papers/10.1038/nature06977
- The paper
- Joh, N. H., Min, A., Faham, S., Whitelegge, J. P., Yang, D., Woods, V. L., & Bowie, J. U. (2008). Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins. Nature. https://doi.org/10.1038/nature06977
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.