The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Interior and surface of monomeric proteins
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
The relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
Self-citationThe three‐dimensional structure of retinol‐binding protein.
Newcomer, M. E., Jones, T. A., Aqvist, J., Sundelin, J., Eriksson, U., Rask, L., & Peterson, P. A. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01995.x · Cited by 405
Cited by
COLLINS, K. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.021 · Cited by 1,091
A Highly Conserved Program of Neuronal Microexons Is Misregulated in Autistic Brains
Irimia, M., Weatheritt, R. J., Ellis, J. D., Parikshak, N. N., Gonatopoulos-Pournatzis, T., Babor, M., Quesnel-Vallières, M., Tapial, J., Raj, B., O’Hanlon, D., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.035 · Cited by 693
Interactome3D: adding structural details to protein networks
Mosca, R., Céol, A., & Aloy, P. (2013) · Nature Methods · doi:10.1038/nmeth.2289 · Cited by 479
Using AlphaFold to predict the impact of single mutations on protein stability and function
Pak, M. A., Markhieva, K. A., Novikova, M. S., Petrov, D. S., Vorobyev, I. S., Maksimova, E. S., Kondrashov, F. A., & Ivankov, D. N. (2023) · PLOS One · doi:10.1371/journal.pone.0282689 · Cited by 322
“where ASA is the solvent accessible surface area and maxASA is the maximum possible solvent accessible surface area of an amino acid [20].”
BackgroundA simple definition of structural regions in proteins and its use in analyzing interface evolution
Levy, E. D. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.09.028 · Cited by 254
Record, M. T., Courtenay, E. S., Cayley, S., & Guttman, H. J. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01207-9 · Cited by 226
Wang, M., Cang, Z., & Wei, G.-W. (2020) · Nature Machine Intelligence · doi:10.1038/s42256-020-0149-6 · Cited by 202
Higgs, P. G. (2009) · Biology Direct · doi:10.1186/1745-6150-4-16 · Cited by 137
Engineering the Dynamic Properties of Protein Networks through Sequence Variation
Dooling, L. J., & Tirrell, D. A. (2016) · ACS Central Science · doi:10.1021/acscentsci.6b00205 · Cited by 63
Yamasaki, Y., Sumimoto, K., Nishikawa, M., Yamashita, F., Yamaoka, K., Hashida, M., & Takakura, Y. (2002) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.301.2.467 · Cited by 58
Epistasis between promoter activity and coding mutations shapes gene evolvability
Cisneros, A. F., Gagnon-Arsenault, I., Dubé, A. K., Després, P. C., Kumar, P., Lafontaine, K., Pelletier, J. N., & Landry, C. R. (2023) · Science Advances · doi:10.1126/sciadv.add9109 · Cited by 33
A model for hydrophobic protrusions on peripheral membrane proteins
Fuglebakk, E., & Reuter, N. (2018) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1006325 · Cited by 29
Best templates outperform homology models in predicting the impact of mutations on protein stability
Pak, M. A., & Ivankov, D. N. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac515 · Cited by 26
Poso, D., Sessions, R. B., Lorch, M., & Clarke, A. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001747200 · Cited by 23
Proteome-scale prediction of molecular mechanisms underlying dominant genetic diseases
Badonyi, M., & Marsh, J. A. (2023) · doi:10.1101/2023.09.08.556798 · Cited by 6
AFFIPred : AlphaFold2 structure‐based Functional Impact Prediction of missense variations
Pir, M. S., & Timucin, E. (2025) · Protein Science · doi:10.1002/pro.70030
Metadata
- Authors
- Miller, S., Janin, J., Lesk, A. M., & Chothia, C.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1987-08
- Volume
- 196
- Issue
- 3
- Pages
- 641-656
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2068265376
- Cited by
- 949
- References
- 2
- FWCI
- 4.62
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.
