The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Abstract
The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR. The outputs include a detailed breakdown of the restraint violations, a number of plots in PostScript format and summary statistics. These various analyses indicate both the degree of agreement of the model structures with the experimental dat, and the quality of their geometrical properties. They are intended to be of use both to support ongoing NMR structure determination and in the validation of the final results.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Furthermore, the quality of Cn-AMP1 structures was evaluated by analyzing the Ramachandran diagram that is part of the PROCHECK-NMR software [18,25].”
From Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water (2015) · cites this paper as [18]
In the citing paper
“On the basis of Procheck82 analysis of secondary structure elements, the Ramachandran statistics among the top 20 lowest-energy structures are 98% for most favoured regions, 2% for additional allowed regions and 0% for disallowed regions.”
From Predicting multiple conformations via sequence clustering and AlphaFold2 (2024) · cites this paper as [82]
Citations
Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Self-citationKabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
The protein data bank: A computer-based archival file for macromolecular structures
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80200-3 · Cited by 8,574
MOLMOL: A program for display and analysis of macromolecular structures
Koradi, R., Billeter, M., & Wüthrich, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,156
Stereochemistry of polypeptide chain configurations
Ramachandran, G. N., Ramakrishnan, C., & Sasisekharan, V. (1963) · Journal of Molecular Biology · doi:10.1016/s0022-2836(63)80023-6 · Cited by 3,651
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424
Stereochemical quality of protein structure coordinates
Morris, A. L., MacArthur, M. W., Hutchinson, E. G., & Thornton, J. M. (1992) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340120407 · Cited by 1,568
Self-citationGüntert, P., Braun, W. A., & Kurt Wüthrich, A. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90754-t · Cited by 784
Havel, T. F. (1991) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(91)90007-f · Cited by 425
PostScript Language Reference Manual
Press, A. (1985) · Addison-Wesley Longman Publishing Co., Inc. eBooks · Cited by 317
Cited by
Sorted by citations
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Comparative Protein Structure Modeling Using Modeller
Eswar, N., Webb, B., Martı́-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Šali, A. (2006) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s15 · Cited by 4,618
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
Davis, I., Leaver‐Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J. S., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,918
Comparative Protein Structure Modeling of Genes and Genomes
Martí-Renom, M. A., Stuart, A. C., Fiser, A., Sánchez, R., Melo, F., & Šali, A. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.291 · Cited by 3,169
Comparative Protein Structure Modeling Using MODELLER
Eswar, N., Webb, B., Martı́-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Šali, A. (2007) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps0209s50 · Cited by 2,874
Structure and ligand of a histone acetyltransferase bromodomain
Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M. (1999) · Nature · doi:10.1038/20974 · Cited by 1,732
Yap, K. L., Li, S., Muñoz-Cabello, A. M., Raguz, S., Zeng, L., Mujtaba, S., Gil, J., Walsh, M. J., & Zhou, M.-M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.021 · Cited by 1,391
The Process of Structure-Based Drug Design
Anderson, A. C. (2003) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.09.002 · Cited by 965
Elfiky, A. A. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117592 · Cited by 929
Structural mechanism of plant aquaporin gating
Törnroth‐Horsefield, S., Wang, Y., Hedfalk, K., Johanson, U., Karlsson, M. E., Tajkhorshid, E., Neutze, R., & Kjellbom, P. O. (2005) · Nature · doi:10.1038/nature04316 · Cited by 863
Consistent blind protein structure generation from NMR chemical shift data
Shen, Y., Lange, O., Delaglio, F., Rossi, P., Aramini, J. M., Liu, G., Eletsky, A., Wu, Y., Singarapu, K. K., Lemak, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800256105 · Cited by 855
Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M. M., Nussinov, R., & Ishii, Y. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2991 · Cited by 826
Craik, D. J., Daly, N. L., Bond, T., & Waine, C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3383 · Cited by 810
Autoinhibition and activation mechanisms of the Wiskott–Aldrich syndrome protein
Kim, A. S., Kakalis, L. T., Abdul-Manan, N., Liu, G. A., & Rosen, M. K. (2000) · Nature · doi:10.1038/35004513 · Cited by 765
Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751
Evaluating protein structures determined by structural genomics consortia
Bhattacharya, A., Tejero, R., & Montelione, G. T. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21165 · Cited by 735
Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., & Wright, P. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80463-8 · Cited by 728
Anti-HCV, nucleotide inhibitors, repurposing against COVID-19
Elfiky, A. A. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117477 · Cited by 719
SHIFTX2: significantly improved protein chemical shift prediction
Han, B., Liu, Y., Ginzinger, S., & Wishart, D. S. (2011) · Journal of Biomolecular NMR · doi:10.1007/s10858-011-9478-4 · Cited by 685
Structural Basis of Integrin Activation by Talin
Wegener, K. L., Partridge, A. W., Han, J., Pickford, A. R., Liddington, R., Ginsberg, M. H., & Campbell, I. D. (2007) · Cell · doi:10.1016/j.cell.2006.10.048 · Cited by 677
Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus
Mygind, P. H., Fischer, R. L., Schnorr, K. M., Hansen, M. T., Sönksen, C. P., Ludvigsen, S., Raventós, D., Buskov, S., Christensen, B. B., Maria, L. D., et al. (2005) · Nature · doi:10.1038/nature04051 · Cited by 655
Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
Liu, Z., Sun, C. C., Olejniczak, E. T., Meadows, R. P., Betz, S. F., Oost, T. K., Herrmann, J. E., Wu, J. C., & Fesik, S. W. (2000) · Nature · doi:10.1038/35050006 · Cited by 647
Open channel structure of MscL and the gating mechanism of mechanosensitive channels
Perozo, E., Cortés, D. M., Sompornpisut, P., Kloda, A., & Martinac, B. (2002) · Nature · doi:10.1038/nature00992 · Cited by 616
Predicting multiple conformations via sequence clustering and AlphaFold2
Wayment-Steele, H. K., Ojoawo, A., Otten, R., Apitz, J. M., Pitsawong, W., Hömberger, M., Ovchinnikov, S., Colwell, L., & Kern, D. (2024) · Nature · doi:10.1038/s41586-023-06832-9 · Cited by 545
Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts
Neal, S., Nip, A. M., Zhang, H., & Wishart, D. S. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1023812930288 · Cited by 546
Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination
Tang, J., Cho, N. W., Cui, G., Manion, E. M., Shanbhag, N. M., Botuyan, M. V., Mer, G., & Greenberg, R. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2499 · Cited by 521
Kortemme, T., Morozov, A. V., & Baker, D. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00021-4 · Cited by 516
Hagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310901f · Cited by 499
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.
Brzović, P. S., Rajagopal, P., Hoyt, D. W., King, M., & Klevit, R. E. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-833 · Cited by 511
Allen, M. D., Yamasaki, K., Ohme‐Takagi, M., Tateno, M., & Suzuki, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.18.5484 · Cited by 490
Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor
Endres, N., Das, R., Smith, A. W., Arkhipov, A. S., Kovács, E., Huang, Y., Pelton, J. G., Shan, Y., Shaw, D. E., Wemmer, D. E., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.032 · Cited by 509
Shi, J., Wang, Y., Zeng, L., Wu, Y., Deng, J., Zhang, Q., Lin, Y., Li, J., Kang, T., Tao, M., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.01.028 · Cited by 483
Wang, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805533200 · Cited by 483
Intestinal serotonin and fluoxetine exposure modulate bacterial colonization in the gut
Fung, T. C., Vuong, H. E., Luna, C. G. G., Pronovost, G. N., Aleksandrova, A. A., Riley, N. G., Vavilina, A., McGinn, J., Rendon, T. K., Forrest, L. R., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0540-4 · Cited by 492
Nonself RNA-Sensing Mechanism of RIG-I Helicase and Activation of Antiviral Immune Responses
Takahasi, K., Yoneyama, M., Nishihori, T., Hirai, R., Kumeta, H., Narita, R., Gale, M., Inagaki, F., & Fujita, T. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.11.028 · Cited by 474
Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., & Kurt Wüthrich, A. (1998) · Journal of Biomolecular NMR · doi:10.1023/a:1008290618449 · Cited by 467
Self-citationStructural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1α
Freedman, S. J., Sun, Z., Poy, F., Kung, A. L., Livingston, D. M., Wagner, G., & Eck, M. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082117899 · Cited by 457
Structure of the chemokine receptor CXCR1 in phospholipid bilayers
Park, S. H., Das, B. B., Casagrande, F., Tian, Y., Nothnagel, H. J., Chu, M., Kiefer, H., Maier, K., Angelis, A. A. D., Marassi, F. M., et al. (2012) · Nature · doi:10.1038/nature11580 · Cited by 459
Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
Demarest, S. J., Martinez‐Yamout, M. A., Chung, J., Chen, H.-W., Xu, W., Dyson, H. J., Evans, R. M., & Wright, P. E. (2002) · Nature · doi:10.1038/415549a · Cited by 466
Transglutaminase 2 Undergoes a Large Conformational Change upon Activation
Pinkas, D. M., Strop, P., Brünger, A. T., & Khosla, C. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050327 · Cited by 460
Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain
Lingel, A., Simon, B., Izaurralde, E., & Sattler, M. (2003) · Nature · doi:10.1038/nature02123 · Cited by 451
Han, X., Bushweller, J. H., Cafiso, D. S., & Tamm, L. K. (2001) · Nature Structural Biology · doi:10.1038/90434 · Cited by 450
Structural insights into the degradation of Mcl-1 induced by BH3 domains
Czabotar, P. E., Lee, E. F., van Delft, M. F., Day, C. L., Smith, B. J., Huang, D. C. S., Fairlie, W. D., Hinds, M. G., & Colman, P. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701297104 · Cited by 459
Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J.-L., Patel, D. J., & Allis, C. D. (2009) · Nature · doi:10.1038/nature08036 · Cited by 446
Evolutionary information for specifying a protein fold
Socolich, M., Lockless, S. W., Russ, W. P., Lee, H. J., Gardner, K. H., & Ranganathan, R. (2005) · Nature · doi:10.1038/nature03991 · Cited by 437
Bateman, A., & Bycroft, M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3778 · Cited by 432
Structural Basis for Tumor Pyruvate Kinase M2 Allosteric Regulation and Catalysis ,
Dombrauckas, J. D., Santarsiero, B. D., & Mesecar, A. D. (2005) · Biochemistry · doi:10.1021/bi0474923 · Cited by 414
Petros, A. M., Nettesheim, D. G., Wang, Y., Olejniczak, E. T., Meadows, R. P., Mack, J. C., Swift, K. M., Matayoshi, E. D., Zhang, H., Thompson, C. B., et al. (2000) · Protein Science · doi:10.1110/ps.9.12.2528 · Cited by 413
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
Lukavsky, P. J., Daujotyte, D., Tollervey, J. R., Ule, J., Stuani, C., Buratti, E., Baralle, F. E., Damberger, F. F., & Allain, F. H. ‐. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2698 · Cited by 408
Structural basis for Hif-1α/CBP recognition in the cellular hypoxic response
Dames, S. A., Martinez‐Yamout, M. A., Guzman, R. N. D., Dyson, H. J., & Wright, P. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082121399 · Cited by 404
Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., & Kurt Wüthrich, A. (1998) · Pure and Applied Chemistry · doi:10.1351/pac199870010117 · Cited by 402
Self-citationStructure of an Intermediate State in Protein Folding and Aggregation
Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine‐Afsar, A., Sharpe, S. J., Vendruscolo, M., & Kay, L. E. (2012) · Science · doi:10.1126/science.1214203 · Cited by 397
Solution Structure of the Proapoptotic Molecule BID
McDonnell, J. M., Fushman, D., Milliman, C. L., Korsmeyer, S. J., & Cowburn, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80573-5 · Cited by 401
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.
Arora, A., Abildgaard, F., Bushweller, J. H., & Tamm, L. K. (2001) · Nature Structural Biology · doi:10.1038/86214 · Cited by 389
Aghazadeh, B., Lowry, W. E., Huang, X.-Y., & Rosen, M. K. (2000) · Cell · doi:10.1016/s0092-8674(00)00085-4 · Cited by 383
Optimized ratiometric calcium sensors for functional in vivo imaging of neurons and T lymphocytes
Thestrup, T., Litzlbauer, J., Bartholomäus, I., Mues, M., Russo, L., Dana, H., Kovalchuk, Y., Liang, Y., Kalamakis, G., Laukat, Y., et al. (2014) · Nature Methods · doi:10.1038/nmeth.2773 · Cited by 366
Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d
Hudson, B. P., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb738 · Cited by 336
Shen, Y., & Bax, A. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9166-6 · Cited by 367
Mutations in a newly identified GTPase gene cause autosomal dominant hereditary spastic paraplegia
Zhao, X., Alvarado, D., Rainier, S., Lemons, R., Hedera, P., Weber, C. H., Tukel, T., Apak, M., Heiman-Patterson, T., Ming, L., et al. (2001) · Nature Genetics · doi:10.1038/ng758 · Cited by 357
Dormitzer, P. R., Sun, Z. J., Wagner, G., & Harrison, S. C. (2002) · The EMBO Journal · doi:10.1093/emboj/21.5.885 · Cited by 353
Four New Members Expand the Interleukin-1 Superfamily
Smith, D. E., Renshaw, B. R., Ketchem, R. R., Kubin, M. Z., Garka, K. E., & Sims, J. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1169 · Cited by 342
Hsu, C. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki725 · Cited by 337
Structure and function of the complex formed by the tuberculosis virulence factors CFP‐10 and ESAT‐6
Renshaw, P. S., Lightbody, K. L., Veverka, V., Muskett, F. W., Kelly, G. P., Frenkiel, T. A., Gordon, S. V., Hewinson, R. G., Burke, B., Norman, J. C., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600732 · Cited by 329
Solution structure and dynamics of the outer membrane enzyme PagP by NMR
Hwang, P. M., Choy, W., Lo, E. I., Chen, L., Forman-Kay, J. D., Raetz, C. R. H., Privé, G. G., Bishop, R. E., & Kay, L. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212344499 · Cited by 324
SMN tudor domain structure and its interaction with the Sm proteins.
Sattler, M., Selenko, P., Sprangers, R., Stier, G., Bühler, D., & Fischer, U. (2001) · Nature Structural Biology · doi:10.1038/83014 · Cited by 324
10 Residue Folded Peptide Designed by Segment Statistics
Honda, S., Yamasaki, K., Sawada, Y., & Morii, H. (2004) · Structure · doi:10.1016/j.str.2004.05.022 · Cited by 323
Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
Zeng, L., Zhang, Q., Li, S., Plotnikov, A. N., Walsh, M. J., & Zhou, M. (2010) · Nature · doi:10.1038/nature09139 · Cited by 321
Entropic switch regulates myristate exposure in the HIV-1 matrix protein
Tang, C., Loeliger, E., Luncsford, P. J., Kinde, I., Beckett, D., & Summers, M. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305665101 · Cited by 320
Structural Mechanism of the Bromodomain of the Coactivator CBP in p53 Transcriptional Activation
Mujtaba, S., He, Y., Zeng, L., Yan, S. X., Plotnikova, O. V., Sachchidanand, Sánchez, R., Zeleznik‐Le, N. J., Ronai, Z. A., & Zhou, M. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00528-8 · Cited by 318
Abdul-Manan, N., Aghazadeh, B., Liu, G. A., Majumdar, A. K., Ouerfelli, O., Siminovitch, K., & Rosen, M. K. (1999) · Nature · doi:10.1038/20726 · Cited by 315
Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
Beglova, N., Blacklow, S. C., Takagi, J., & Springer, T. A. (2002) · Nature Structural Biology · doi:10.1038/nsb779 · Cited by 314
Solution Structure of the Methyl-CpG Binding Domain of Human MBD1 in Complex with Methylated DNA
Ohki, I., Shimotake, N., Fujita, N., Jee, J.-G., Ikegami, T., Nakao, M., & Shirakawa, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00324-5 · Cited by 317
Yamasaki, K., Kigawa, T., Inoue, M., Tateno, M., Yamasaki, T., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Nunokawa, E., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.015 · Cited by 310
Hosoda, K., Imamura, A., Katoh, E., Hatta, T., Tachiki, M., Yamada, H., Mizuno, T., & Yamazaki, T. (2002) · The Plant Cell · doi:10.1105/tpc.002733 · Cited by 310
The Protein Data Bank: unifying the archive
Westbrook, J. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.245 · Cited by 309
Ilangovan, U., Ton-That, H., Iwahara, J., Schneewind, O., & Clubb, R. T. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101064198 · Cited by 304
Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302
Structure and Function of the Membrane Anchor Domain of Hepatitis C Virus Nonstructural Protein 5A
Pénin, F., Brass, V., Appel, N., Ramboarina, S., Montserret, R., Ficheux, D., Blum, H. E., Bartenschlager, R. F. W., & Moradpour, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404761200 · Cited by 301
Structure and functional interactions of the Tsg101 UEV domain
Pornillos, O., Alam, S. L., Rich, R. L., Myszka, D. G., Davis, D. R., & Sundquist, W. I. (2002) · The EMBO Journal · doi:10.1093/emboj/21.10.2397 · Cited by 295
Recommendations for the presentation of NMR structures of proteins and nucleic acids
Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., & Kurt Wüthrich, A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1852 · Cited by 301
Self-citationA new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS
Wang, X., Lord, D. M., Cheng, H.-Y., Osbourne, D. O., Hong, S. H., Sánchez-Torres, V., Quiroga, C., Zheng, K., Herrmann, T., Peti, W., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1062 · Cited by 299
Structural insights into the U-box, a domain associated with multi-ubiquitination
Ohi, M. D., Kooi, C. W. V., Rosenberg, J. A., Chazin, W., & Gould, K. L. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb906 · Cited by 308
SARS-CoV-2 RNA dependent RNA polymerase (RdRp) targeting: an in silico perspective
Elfiky, A. A. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1761882 · Cited by 284
Melckebeke, H. V., Wasmer, C., Lange, A., Eiso, A. B., Loquet, A., Böckmann, A., & Meier, B. H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja104213j · Cited by 283
A Small Molecule RAS-Mimetic Disrupts RAS Association with Effector Proteins to Block Signaling
Divakar, S. K. A., Carpio, R. V., Dutta, K., Baker, S. J., Cosenza, S. C., Basu, I., Gupta, Y. K., Reddy, M. V. R., Ueno, L. A., Hart, J. R., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.045 · Cited by 278
Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP Synthase
Girvin, M. E., Rastogi, V. K., Abildgaard, F., Markley, J. L., & Fillingame, R. H. (1998) · Biochemistry · doi:10.1021/bi980511m · Cited by 278
Pell, L. G., Kanelis, V., Donaldson, L. W., Howell, P. L., & Davidson, A. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900044106 · Cited by 276
Jehle, S., Rajagopal, P., Bardiaux, B., Marković, S., Kühne, R., Stout, J. R., Higman, V. A., Klevit, R. E., van Rossum, B., & Oschkinat, H. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1891 · Cited by 276
Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain
Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300629200 · Cited by 274
Das, K., Xiong, X., Yang, H., Westland, C. E., Gibbs, C. S., Sarafianos, S. G., & Arnold, E. (2001) · Journal of Virology · doi:10.1128/jvi.75.10.4771-4779.2001 · Cited by 274
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1
Guettler, T., Madl, T., Neumann, P., Deichsel, D., Corsini, L., Monecke, T., Ficner, R., Sattler, M., & Görlich, D. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1931 · Cited by 280
A minimal sequence code for switching protein structure and function
Alexander, P., He, Y., Chen, Y., Orban, J. P., & Bryan, P. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906408106 · Cited by 270
Small Ubiquitin-like Modifier (SUMO) Recognition of a SUMO Binding Motif
Song, J., Zhang, Z., Hu, W., & Chen, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507059200 · Cited by 264
Molecular basis of RNA recognition by the human alternative splicing factor Fox-1
Auweter, S. D., Fasan, R., Reymond, L., Underwood, J. G., Black, D. L., Pitsch, S., & Allain, F. H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600918 · Cited by 264
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria
Banci, L., Bertini, I., Cefaro, C., Ciofi‐Baffoni, S., Gallo, A., Martinelli, M., Sideris, D. P., Katrakili, N., & Tokatlidis, K. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1553 · Cited by 260
Structure of Adeno-Associated Virus Serotype 8, a Gene Therapy Vector
Nam, H.-J., Lane, M. D., Padron, E., Gurda, B. L., McKENNA, R. V., Kohlbrenner, E., Aslanidi, G., Byrne, B. J., Muzyczka, N., Zolotukhin, S., et al. (2007) · Journal of Virology · doi:10.1128/jvi.01304-07 · Cited by 257
Byeon, I.-J. L., Meng, X., Jung, J., Zhao, G., Yang, R., Ahn, J., Shi, J., Concel, J., Aiken, C., Zhang, P., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.010 · Cited by 253
Huang, Y. J., Powers, R., & Montelione, G. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja047109h · Cited by 253
Camenisch, G., Pisabarro, M. T., Sherman, D. A., Kowalski, J., Nagel, M., Hass, P., Xie, M.-H., Gurney, A. L., Bodary, S. C., Liang, X. H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109768200 · Cited by 253
Linge, J. P., & Nilges, M. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008365802830 · Cited by 253
Metadata
- Authors
- Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J.
- Affiliations
- Utrecht University (NL)
- ORCID
- Kaptein, Robert
- Venue
- Journal of Biomolecular NMR
- Published
- 1996-12
- Volume
- 8
- Issue
- 4
- Pages
- 477-86
- ISSN
- 0925-2738 (ISSN-L)
- 1573-5001
- OpenAlex
- W1975459052
- Cited by
- 5,502
- References
- 21
- Citations by year
- 2026: 142 · 2025: 203 · 2024: 205 · 2023: 219 · 2022: 238 · 2021: 204 · 2020: 198 · 2019: 153 · 2018: 130 · 2017: 173 · 2016: 191 · 2015: 194 · 2014: 248 · 2013: 248 · 2012: 233
- FWCI
- 21.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Biomolecular NMR (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Aqua, protein conformational ensembles
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, DNA-Binding Proteins, Evaluation Studies as Topic, Models, Molecular, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Proteins, Quality Control, Software, Solutions, Reproducibility of Results, Molecular Structure, Protein Structure, Secondary
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