The DOI matches its Crossref record.
A new force field for molecular mechanical simulation of nucleic acids and proteins
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTA new force field for molecular mechanical simulation of nucleic acids and proteinsScott J. Weiner, Peter A. Kollman, David A. Case, U. Chandra Singh, Caterina Ghio, Guliano Alagona, Salvatore Profeta, and Paul WeinerCite this: J. Am. Chem. Soc. 1984, 106, 3, 765–784Publication Date (Print):February 1, 1984Publication History Published online1 May 2002Published inissue 1 February 1984https://pubs.acs.org/doi/10.1021/ja00315a051https://doi.org/10.1021/ja00315a051research-articleACS PublicationsRequest reuse permissionsArticle Views10306Altmetric-Citations3968LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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
Cited by
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
Self-citationMolecular Docking: A Powerful Approach for Structure-Based Drug Discovery
Meng, X.-Y., Zhang, H.-X., Mezei, M., & Cui, M. (2011) · Current Computer Aided-Drug Design · doi:10.2174/157340911795677602 · Cited by 3,771
Solving the multiple instance problem with axis-parallel rectangles
Dietterich, T. G., Lathrop, R. H., & Lozano-Pérez, T. (1997) · Artificial Intelligence · doi:10.1016/s0004-3702(96)00034-3 · Cited by 2,866
A semiempirical free energy force field with charge‐based desolvation
Huey, R., Morris, G. M., Olson, A. J., & Goodsell, D. S. (2007) · Journal of Computational Chemistry · doi:10.1002/jcc.20634 · Cited by 2,246
Structural basis of water-specific transport through the AQP1 water channel
Sui, H., Han, B.-G., Lee, J. K., Walian, P., & Jap, B. K. (2001) · Nature · doi:10.1038/414872a · Cited by 1,166
Comparative evaluation of 11 scoring functions for molecular docking.
Wang, R., Lu, Y., & Wang, S. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0203783 · Cited by 849
Huang, S.-Y., Grinter, S. Z., & Zou, X. (2010) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp00151a · Cited by 508
Österberg, F., Morris, G. M., Sanner, M. F., Olson, A. J., & Goodsell, D. S. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10028 · Cited by 474
Faster superoxide dismutase mutants designed by enhancing electrostatic guidance
Getzoff, E. D., Cabelli, D. E., Fisher, C. L., Parge, H. E., Viezzoli, M. S., Banci, L., & Hallewell, R. A. (1992) · Nature · doi:10.1038/358347a0 · Cited by 399
Helix Distortion and Crystal Structure of the α-Form of Poly(l-lactide)
Sasaki, S., & Asakura, T. (2003) · Macromolecules · doi:10.1021/ma0348674 · Cited by 296
Pereira de Jésus‐Tran, K., Côté, P., Cantin, L., Blanchet, J., Labrie, F., & Breton, R. (2006) · Protein Science · doi:10.1110/ps.051905906 · Cited by 278
Kollman, P., Dixon, R., Cornell, W., Fox, T., Chipot, C., & Pohorille, A. (1997) · Computer Simulation of Biomolecular Systems · doi:10.1007/978-94-017-1120-3_2 · Cited by 242
Self-citationConsensus scoring criteria for improving enrichment in virtual screening.
Yang, J.-M., Chen, Y.-F., Shen, T.-W., Kristal, B. S., & Hsu, D. F. (2005) · Journal of Chemical Information and Modeling · doi:10.1021/ci050034w · Cited by 241
Deep Learning in Protein Structural Modeling and Design
Gao, W., Mahajan, S. P., Sulam, J., & Gray, J. J. (2020) · Patterns · doi:10.1016/j.patter.2020.100142 · Cited by 227
Structures of the σ2 receptor enable docking for bioactive ligand discovery
Alon, A., Lyu, J., Braz, J. M., Tummino, T. A., Craik, V., O’Meara, M. J., Webb, C. M., Radchenko, D. S., Moroz, Y. S., Huang, X.-P., et al. (2021) · Nature · doi:10.1038/s41586-021-04175-x · Cited by 211
Molecular Models for DNA Damaged by Photoreaction
Pearlman, D. A., Holbrook, S. R., Pirkle, D. H., & Kim, S.-H. (1985) · Science · doi:10.1126/science.3975615 · Cited by 183
Fisher, C. L., Cabelli, D. E., Tainer, J. A., Hallewell, R. A., & Getzoff, E. D. (1994) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340190105 · Cited by 125
Hu, X., & Shelver, W. H. (2003) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(03)00153-0 · Cited by 112
Biomolecular simulation and modelling: status, progress and prospects
van der Kamp, M. W., Shaw, K. E., Woods, C. J., & Mulholland, A. J. (2008) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0105.focus · Cited by 90
Antibody H3 structure prediction
Marks, C., & Deane, C. M. (2017) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2017.01.010 · Cited by 56
Challenges in the computational design of proteins
Suárez, M., & Jaramillo, A. (2009) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0508.focus · Cited by 59
Robust scoring functions for protein-ligand interactions with quantum chemical charge models.
Wang, J.-C., Lin, J.-H., Chen, C.-M., Perryman, A. L., & Olson, A. J. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci200220v · Cited by 54
l-Arginine Binding to Nitric-oxide Synthase
Babu, B. R., Frey, C., & Griffith, O. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25218 · Cited by 48
Progestins as inhibitors of the human 20-ketosteroid reductases, AKR1C1 and AKR1C3
Beranič, N., Gobec, S., & Rižner, T. L. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.12.012 · Cited by 39
State-of-the-RNArt: benchmarking current methods for RNA 3D structure prediction
Bernard, C., Postic, G., Ghannay, S., & Tahi, F. (2024) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqae048 · Cited by 40
Recruiting Zn2+to Mediate Potent, Specific Inhibition of Serine Proteases
Katz, B. A., & Luong, C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3071 · Cited by 34
DU, L., ZHAO, Y.-X., YANG, L.-M., ZHENG, Y.-T., TANG, Y., SHEN, X., & JIANG, H.-L. (2008) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2008.00863.x · Cited by 22
Performance-Based Screening of Porous Materials for Carbon Capture
Farmahini, A. H., Krishnamurthy, S., Friedrich, D., Brandani, S., & Sarkisov, L. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01266 · Cited by 7
4D structural biology–quantitative dynamics in the eukaryotic RNA exosome complex
Liebau, J., Lazzaretti, D., Fürtges, T., Bichler, A., Pilsl, M., Rudack, T., & Sprangers, R. (2025) · Nature Communications · doi:10.1038/s41467-025-62982-6 · Cited by 7
Computational Approaches to Zeolite-Based Adsorption Processes
Gutiérrez-Sevillano, J. J., & Calero, S. (2020) · Structure and Bonding · doi:10.1007/430_2020_66 · Cited by 4
Metadata
- Authors
- Weiner, S. J., Kollman, P. A., Case, D. A., Singh, U. C., Ghio, C., Alagona, G., Profeta, S., & Weiner, P.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 1984-02
- Volume
- 106
- Issue
- 3
- Pages
- 765-784
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1979046104
- Cited by
- 4,639
- References
- 0
- FWCI
- 17.07
- 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.