The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Macromolecular TLS Refinement in REFMAC at Moderate Resolutions
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
Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Research works printed but not linked: 41
- Trueblood, 1996, Acta Crystallogr. A, 52, 770, 10.1107/S0108767396005697 · DOI
- Schomaker, 1968, Acta Crystallogr. B, 24, 63, 10.1107/S0567740868001718 · DOI
- Diamond, 1990, Acta Crystallogr. A, 46, 425, 10.1107/S0108767390002082 · DOI
- Kidera, 1990, Proc. Natl. Acad. Sci. USA, 87, 3718, 10.1073/pnas.87.10.3718 · DOI
- Kidera, 1992, J. Mol. Biol., 225, 457, 10.1016/0022-2836(92)90932-A · DOI
- Haliloglu, 1997, Phys. Rev. Lett., 79, 3090, 10.1103/PhysRevLett.79.3090 · DOI · Paper page
- Atilgan, 2001, Biophys. J., 80, 505, 10.1016/S0006-3495(01)76033-X · DOI · Paper page
- Tirion, 1996, Phys. Rev. Lett., 77, 1905, 10.1103/PhysRevLett.77.1905 · DOI · Paper page
- Holbrook, 1984, J. Mol. Biol., 173, 361, 10.1016/0022-2836(84)90126-8 · DOI
- Holbrook, 1985, Acta Crystallogr. B, 41, 255, 10.1107/S0108768185002087 · DOI
- Driessen, 1989, J. Appl. Crystallogr., 22, 510, 10.1107/S0021889889004097 · DOI
- 4, 1994, Acta Crystallogr. D Biol. Crystallogr., 50, 760, 10.1107/S0907444994003112 · DOI · Paper page
- Howlin, 1989, Acta Crystallogr. A, 45, 851, 10.1107/S0108767389009177 · DOI
- Harris, 1992, Acta Crystallogr. B, 48, 67, 10.1107/S0108768191006663 · DOI
- Šali, 1992, Proteins Struct. Funct. Genet., 12, 158, 10.1002/prot.340120209 · DOI
- Stec, 1995, Acta Crystallogr. D Biol. Crystallogr., 51, 663, 10.1107/S0907444994014484 · DOI
- Wilson, 2000, J. Mol. Biol., 301, 1237, 10.1006/jmbi.2000.4029 · DOI · Paper page
- Murshudov, 1997, Acta Crystallogr. D Biol. Crystallogr., 53, 240, 10.1107/S0907444996012255 · DOI · Paper page
- Winn, 2001, Acta Crystallogr. D Biol. Crystallogr., 57, 122, 10.1107/S0907444900014736 · DOI
- Howlin, 1993, J. Appl. Crystallogr., 26, 622, 10.1107/S0021889893002729 · DOI
- Schomaker, 1998, Acta Crystallogr. B, 54, 507, 10.1107/S0108768198003243 · DOI
- Murshudov, 1999, Acta Crystallogr. D Biol. Crystallogr., 55, 247, 10.1107/S090744499801405X · DOI · Paper page
- Kuriyan, 1991, Proc. Natl. Acad. Sci. USA, 88, 2773, 10.1073/pnas.88.7.2773 · DOI
- Winn, 2001, CCP4 Newsletter
- Papiz, 2003, J. Mol. Biol., 326, 1523, 10.1016/S0022-2836(03)00024-X · DOI · Paper page
- Hayward, 1998, Proteins Struct. Funct. Genet., 30, 144, 10.1002/(SICI)1097-0134(19980201)30:2<144::AID-PROT4>3.0.CO;2-N · DOI
- Schneider, 2000, Acta Crystallogr. D Biol. Crystallogr., 56, 714, 10.1107/S0907444900003723 · DOI
- Rosenfield, 1978, Acta Crystallogr. A, 34, 828, 10.1107/S0567739478001692 · DOI
- Brock, 1985, J. Am. Chem. Soc., 107, 6964, 10.1021/ja00310a036 · DOI
- Hörer, 2001, J. Biol. Chem., 276, 27555, 10.1074/jbc.M102850200 · DOI
- Kraulis, 1991, J. Appl. Crystallogr., 24, 946, 10.1107/S0021889891004399 · DOI · Paper page
- Isupov, 1999, J. Mol. Biol., 291, 651, 10.1006/jmbi.1999.3003 · DOI
- Ducros, 2001, J. Mol. Biol., 306, 759, 10.1006/jmbi.2001.4443 · DOI
- Merritt, 1997, Methods Enzymol., 277, 505, 10.1016/S0076-6879(97)77028-9 · DOI
- McDermott, 1995, Nature, 374, 517, 10.1038/374517a0 · DOI · Paper page
- Rudolph, 2001, Immunity, 14, 231, 10.1016/S1074-7613(01)00105-4 · DOI
- Moroz, 2001, Acta Crystallogr. D Biol. Crystallogr., 57, 20, 10.1107/S090744490001458X · DOI
- Karlsson, 2002, Journal of Molecular Biology, 318, 261, 10.1016/S0022-2836(02)00039-6 · DOI
- Keep, 2002, Biochemistry, 41, 6303, 10.1021/bi025651h · DOI
- Schwartz, 2001, Nat. Struct. Biol., 8, 761, 10.1038/nsb0901-761 · DOI
- Sandalova, 2001, Proc. Natl. Acad. Sci., 98, 9533, 10.1073/pnas.171178698 · DOI · Paper page
Cited by
Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
Self-citationPutnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184
Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements
Korostelev, A., Trakhanov, S., Laurberg, M., & Noller, H. F. (2006) · Cell · doi:10.1016/j.cell.2006.08.032 · Cited by 498
Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75
Cherepanov, P., Ambrosio, A. L. B., Rahman, S., Ellenberger, T., & Engelman, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506924102 · Cited by 408
Structural mechanism of demethylation and inactivation of protein phosphatase 2A
Xing, Y., Li, Z., Chen, Y., Stock, J. B., Jeffrey, P. D., & Shi, Y. (2008) · Cell · doi:10.1016/j.cell.2008.02.041 · Cited by 206
Gaieb, Z., Liu, S., Gathiaka, S., Chiu, M., Yang, H., Shao, C., Feher, V. A., Walters, W. P., Kuhn, B., Rudolph, M. G., et al. (2018) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-017-0088-4 · Cited by 193
The structural basis for tight control of PP2A methylation and function by LCMT-1
Stanevich, V., Jiang, L., Satyshur, K. A., Li, Y., Jeffrey, P. D., Li, Z., Menden, P., Semmelhack, M. F., & Xing, Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.030 · Cited by 142
Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone
Guo, F., Stanevich, V., Wlodarchak, N., Sengupta, R., Jiang, L., Satyshur, K. A., & Xing, Y. (2014) · Cell Research · doi:10.1038/cr.2013.138 · Cited by 100
Wang, J., Wang, Z., Yu, T., Yang, H., Virshup, D. M., Kops, G. J. P. L., Lee, S. H., Zhou, W., Li, X., Xu, W., et al. (2016) · Protein & Cell · doi:10.1007/s13238-016-0283-4 · Cited by 80
Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation
Wlodarchak, N., Guo, F., Satyshur, K. A., Jiang, L., Jeffrey, P. D., Sun, T., Stanevich, V., Mumby, M. C., & Xing, Y. (2013) · Cell Research · doi:10.1038/cr.2013.77 · Cited by 72
Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins
Golczak, M., Kiser, P. D., Sears, A. E., Lodowski, D. T., Blaner, W. S., & Palczewski, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361550 · Cited by 77
Shimon, L. J. W., Rabinkov, A., Shin, I., Miron, T., Mirelman, D., Wilchek, M., & Frolow, F. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.041 · Cited by 69
Structural basis of protein phosphatase 2A stable latency
Jiang, L., Stanevich, V., Satyshur, K. A., Kong, M., Watkins, G. R., Wadzinski, B. E., Sengupta, R., & Xing, Y. (2013) · Nature Communications · doi:10.1038/ncomms2663 · Cited by 68
Docquier, J.-D., Benvenuti, M., Calderone, V., Stoczko, M., Menciassi, N., Rossolini, G. M., & Mangani, S. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00409-10 · Cited by 51
Epsin and Sla2 form assemblies through phospholipid interfaces
Garcia-Alai, M. M., Heidemann, J., Skruzny, M., Gieras, A., Mertens, H. D. T., Svergun, D. I., Kaksonen, M., Uetrecht, C., & Meijers, R. (2018) · Nature Communications · doi:10.1038/s41467-017-02443-x · Cited by 52
Methylation-regulated decommissioning of multimeric PP2A complexes
Wu, C.-G., Zheng, A., Jiang, L., Rowse, M., Stanevich, V., Chen, H., Li, Y., Satyshur, K. A., Johnson, B., Gu, T.-J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02405-3 · Cited by 45
A CLC-type F-/H+ antiporter in ion-swapped conformations
Last, N. B., Stockbridge, R. B., Wilson, A. E., Shane, T., Kolmakova-Partensky, L., Koide, A., Koide, S., & Miller, C. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0082-0 · Cited by 45
Design of high-affinity binders to immune modulating receptors for cancer immunotherapy
Yang, W., Hicks, D. R., Ghosh, A., Schwartze, T. A., Conventry, B., Goreshnik, I., Allen, A., Halabiya, S. F., Kim, C. J., Hinck, C. S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57192-z · Cited by 40
Zhang, W., Zeng, F., Liu, Y., Zhao, Y., Lv, H., Niu, L., Teng, M., & Li, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463901 · Cited by 40
Mechanistic signs of double-barreled structure in a fluoride ion channel
Last, N. B., Kolmakova-Partensky, L., Shane, T., & Miller, C. (2016) · eLife · doi:10.7554/elife.18767 · Cited by 34
Malmirchegini, G. R., Sjodt, M., Shnitkind, S., Sawaya, M. R., Rosinski, J., Newton, S. M., Klebba, P. E., & Clubb, R. T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.583013 · Cited by 33
A Structural Model for the Generation of Continuous Curvature on the Surface of a Retroviral Capsid
Bailey, G. D., Hyun, J.-K., Mitra, A. K., & Kingston, R. L. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.014 · Cited by 33
Molecular determinants of permeation in a fluoride-specific ion channel
Last, N. B., Sun, S., Pham, M. C., & Miller, C. (2017) · eLife · doi:10.7554/elife.31259 · Cited by 25
Sun, Y., Florio, T. J., Gupta, S., Young, M. C., Marshall, Q. F., Garfinkle, S. E., Papadaki, G. F., Truong, H. V., Mycek, E., Li, P., et al. (2023) · Science Immunology · doi:10.1126/sciimmunol.adj5792 · Cited by 19
Pfoh, R., Subramanian, A. S., Huang, J., Little, D. J., Forman, A., DiFrancesco, B. R., Balouchestani-Asli, N., Kitova, E. N., Klassen, J. S., Pomès, R., et al. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010750 · Cited by 17
Structural insights into regulation of CNNM-TRPM7 divalent cation uptake by the small GTPase ARL15
Mahbub, L., Kozlov, G., Zong, P., Lee, E. L., Tetteh, S., Nethramangalath, T., Knorn, C., Jiang, J., Shahsavan, A., Yue, L., et al. (2023) · eLife · doi:10.7554/elife.86129 · Cited by 14
Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers
Turman, D. L., Cheloff, A. Z., Corrado, A. D., Nathanson, J. T., & Miller, C. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01272 · Cited by 10
Dixon, T., MacPherson, D., Mostofian, B., Dauzhenka, T., Lotz, S., McGee, D., Shechter, S., Shrestha, U. R., Wiewiora, R., McDargh, Z. A., et al. (2021) · doi:10.1101/2021.09.26.461830 · Cited by 7
Das, D., Kozbial, P., Han, G. W., Carlton, D., Jaroszewski, L., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Chen, C., et al. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109018168 · Cited by 2
Metadata
- Authors
- Winn, M. D., Murshudov, G. N., & Papiz, M. Z.
- Venue
- Methods in Enzymology
- Publisher
- Elsevier
- Published
- 2003
- Volume
- 374
- Pages
- 300-321
- ISSN
- 0076-6879 (ISSN-L)
- OpenAlex
- W1506664007
- Cited by
- 802
- References
- 1
- FWCI
- 44.62
- Type
- book chapter
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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.