The DOI matches its Crossref record.
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Open accessAbstract
The MOLSCRIPT program produces plots of protein structures using several different kinds of representations. Schematic drawings, simple wire models, ball-and-stick models, CPK models and text labels can be mixed freely. The schematic drawings are shaded to improve the illusion of three dimensionality. A number of parameters affecting various aspects of the objects drawn can be changed by the user. The output from the program is in PostScript format.
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
Items 101–200 of 225
Messerschmidt, A., Prade, L., & Wever, R. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.3-4.309 · Cited by 275
LINUS: a hierarchic procedure to predict the fold of a protein
Srinivasan, R., & Rose, G. D. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340220202 · Cited by 266
Lactoferrin and iron: Structural and dynamic aspects of binding and release
Baker, H. M., & Baker, E. N. (2004) · Biometals · doi:10.1023/b:biom.0000027694.40260.70 · Cited by 265
Targeting of Ikaros to pericentromeric heterochromatin by direct DNA binding
Cobb, B. S., Morales-Alcelay, S., Kleiger, G., Brown, K. E., Fisher, A. G., & Smale, S. T. (2000) · Genes & Development · doi:10.1101/gad.816400 · Cited by 252
Sinars, C. R., Cheung-Flynn, J., Rimerman, R. A., Scammell, J. G., Smith, D. F., & Clardy, J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0231020100 · Cited by 254
Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein
Jiang, J., Zhang, Y., Krainer, A. R., & Xu, R.-M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3572 · Cited by 253
Recombining the structures of HIV integrase, RuvC and RNase H
Yang, W., & Steitz, T. A. (1995) · Structure · doi:10.1016/s0969-2126(01)00142-3 · Cited by 246
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
Prodromou, C., Roe, S. M., Piper, P. W., & Pearl, L. H. (1997) · Nature Structural Biology · doi:10.1038/nsb0697-477 · Cited by 239
Xing, Y., Clements, W. K., Kimelman, D., & Xu, W. (2003) · Genes & Development · doi:10.1101/gad.1142603 · Cited by 237
Hewitson, K. S., Liénard, B. M. R., McDonough, M. A., Clifton, I. J., Butler, D., Soares, A. S., Oldham, N. J., McNeill, L. A., & Schofield, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608337200 · Cited by 235
Structural basis for recognition of AU-rich element RNA by the HuD protein.
(2001) · Nature Structural Biology · doi:10.1038/84131 · Cited by 234
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
(2001) · Nature Structural Biology · doi:10.1038/84152 · Cited by 227
Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
Rittinger, K., Walker, P. A., Eccleston, J. F., Nurmahomed, K., Owen, D., Laue, E., Gamblin, S. J., & Smerdon, S. J. (1997) · Nature · doi:10.1038/41805 · Cited by 227
Evolution of the Thyroid Hormone-Binding Protein, Transthyretin
Power, D. M., Elias, N. P., Richardson, S. J., Mendes, J., Soares, C. M., & Santos, C. R. A. (2000) · General and Comparative Endocrinology · doi:10.1006/gcen.2000.7520 · Cited by 226
Optimization of the Tet-On system for regulated gene expression through viral evolution
Zhou, X., Vink, M., Klaver, B., Berkhout, B., & Das, A. T. (2006) · Gene Therapy · doi:10.1038/sj.gt.3302780 · Cited by 224
Fujii, Y., Shimizu, T., Kusumoto, M., Kyogoku, Y., Taniguchi, T., & Hakoshima, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5028 · Cited by 223
Rossman, K. L., Worthylake, D. K., Snyder, J. T., Siderovski, D. P., Campbell, S. L., & Sondek, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.6.1315 · Cited by 222
Great Metalloclusters in Enzymology
Rees, D. C. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135406 · Cited by 220
Functional implications of the structure of the murine parvovirus, minute virus of mice
Agbandje-McKenna, M., Llamas-Saiz, A. L., Wang, F., Tattersall, P., & Rossmann, M. G. (1998) · Structure · doi:10.1016/s0969-2126(98)00137-3 · Cited by 218
Crystal Structure and Thermodynamic Analysis of Human Brain Fatty Acid-binding Protein
Balendiran, G. K., Schnütgen, F., Scapin, G., Börchers, T., Xhong, N., Lim, K., Godbout, R., Spener, F., & Sacchettini, J. C. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61478-x · Cited by 217
Predicting oligomerization states of coiled coils
Woolfson, D. N., & Alber, T. (1995) · Protein Science · doi:10.1002/pro.5560040818 · Cited by 214
Brotherton, D. H., Dhanaraj, V., Wick, S., Brizuela, L., Domaille, P. J., Volyanik, E., Xu, X., Parisini, E., Smith, B. O., Archer, S. J., et al. (1998) · Nature · doi:10.1038/26164 · Cited by 210
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.
Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997) · Nature · doi:10.1038/385365a0 · Cited by 210
Structural basis for the selective activation of Rho GTPases by Dbl exchange factors
Snyder, J. T., Worthylake, D. K., Rossman, K. L., Betts, L., Pruitt, W. M., Siderovski, D. P., Der, C. J., & Sondek, J. (2002) · Nature Structural Biology · doi:10.1038/nsb796 · Cited by 209
Crennell, S., Garman, E., Laver, G., Vimr, E., & Taylor, G. (1994) · Structure · doi:10.1016/s0969-2126(00)00053-8 · Cited by 205
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
Tang, C., Ndassa, Y., & Summers, M. F. (2002) · Nature Structural Biology · doi:10.1038/nsb806 · Cited by 205
Crystal structure of SIV matrix antigen and implications for virus assembly
Rao, Z., Belyaev, A. S., Fry, E., Roy, P., Jones, I. M., & Stuart, D. I. (1995) · Nature · doi:10.1038/378743a0 · Cited by 183
Amyloid P component. A critical review
Pepys, M. B., Booth, D. R., Hutchinson, W. L., Gallimore, J. R., Collins, I. M., & Hohenester, E. (1997) · Amyloid · doi:10.3109/13506129709003838 · Cited by 181
Structure of the metal-ion-activated diphtheria toxin repressor/ tox operator complex
White, A., Ding, X., vanderSpek, J. C., Murphy, J. R., & Ringe, D. (1998) · Nature · doi:10.1038/28893 · Cited by 180
The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
de Kok, A., Hengeveld, A. F., Martin, A., & Westphal, A. H. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00079-x · Cited by 174
Crystal Structure of the Human Cytosolic Sialidase Neu2
Chavas, L. M. G., Tringali, C., Fusi, P., Venerando, B., Tettamanti, G., Kato, R., Monti, E., & Wakatsuki, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411506200 · Cited by 176
Structure of the BRCT Repeats of BRCA1 Bound to a BACH1 Phosphopeptide
Shiozaki, E. N., Gu, L., Yan, N., & Shi, Y. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00238-2 · Cited by 174
Domain Architectures and Characterization of an RNA-binding Protein, TLS
Iko, Y., Kodama, T. S., Kasai, N., Oyama, T., Morita, E. H., Muto, T., Okumura, M., Fujii, R., Takumi, T., Tate, S.-I., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408552200 · Cited by 168
RosettaAntibody: antibody variable region homology modeling server
Sircar, A., Kim, E. T., & Gray, J. J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp387 · Cited by 161
Aravind, L., Anantharaman, V., & Koonin, E. V. (2002) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10064 · Cited by 153
Hyman, J., Chen, H., Di Fiore, P. P., De Camilli, P., & Brunger, A. T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.537 · Cited by 158
Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., Tsukita, S., & Hakoshima, T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg039 · Cited by 155
Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases
Vallée, F., Karaveg, K., Herscovics, A., Moremen, K. W., & Howell, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006927200 · Cited by 152
Soares, C. M., Teixeira, V. H., & Baptista, A. M. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74972-8 · Cited by 149
Carrodeguas, J. A., Theis, K., Bogenhagen, D. F., & Kisker, C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00153-8 · Cited by 150
Tomarev, S. I., & Piatigorsky, J. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00449.x · Cited by 146
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA
Ikegami, T., Kuraoka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K., & Shirakawa, M. (1998) · Nature Structural & Molecular Biology · doi:10.1038/1400 · Cited by 139
Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase
Jin, R., Junutula, J. R., Matern, H. T., Ervin, K. E., Scheller, R. H., & Brunger, A. T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600699 · Cited by 145
Tandem binding in crystals of a trp represser/operator half-site complex
Lawson, C. L., & Carey, J. (1993) · Nature · doi:10.1038/366178a0 · Cited by 145
Müller, A., Müller, J. J., Muller, Y. A., Uhlmann, H., Bernhardt, R., & Heinemann, U. (1998) · Structure · doi:10.1016/s0969-2126(98)00031-8 · Cited by 142
Zhang, Z., Lee, C., Mandiyan, V., Borg, J., Margolis, B., Schlessinger, J., & Kuriyan, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.20.6141 · Cited by 140
Krahn, J. M., Beard, W. A., Miller, H., Grollman, A. P., & Wilson, S. H. (2003) · Structure · doi:10.1016/s0969-2126(02)00930-9 · Cited by 138
CUDA, G., FANANAPAZIR, L., EPSTEIN, N. D., & SELLERS, J. R. (1997) · Journal of Muscle Research & Cell Motility · doi:10.1023/a:1018613907574 · Cited by 137
Esser, L., Elberry, M., Zhou, F., Yu, C.-A., Yu, L., & Xia, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708608200 · Cited by 137
Zhang, X., Kurnasov, O. V., Karthikeyan, S., Grishin, N. V., Osterman, A. L., & Zhang, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300073200 · Cited by 136
The interaction of Ras with GTPase‐activating proteins
Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00321-9 · Cited by 135
Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
Buchwald, G., Friebel, A., Galán, J. E., Hardt, W., Wittinghofer, A., & Scheffzek, K. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf329 · Cited by 135
Stenkamp, R. E., Filipek, S., Driessen, C. A. G. G., Teller, D. C., & Palczewski, K. (2002) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(02)00567-9 · Cited by 128
Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis
Smith, K. R., Dahl, H.-H. M., Canafoglia, L., Andermann, E., Damiano, J., Morbin, M., Bruni, A. C., Giaccone, G., Cossette, P., Saftig, P., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/dds558 · Cited by 130
Saul, F. A., Arié, J.-P., Vulliez-le Normand, B., Kahn, R., Betton, J.-M., & Bentley, G. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.056 · Cited by 130
Efficiency of Correct Nucleotide Insertion Governs DNA Polymerase Fidelity
Beard, W. A., Shock, D. D., Vande Berg, B. J., & Wilson, S. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m210036200 · Cited by 129
Viral Evolution as a Tool to Improve the Tetracycline-regulated Gene Expression System
Das, A. T., Zhou, X., Vink, M., Klaver, B., Verhoef, K., Marzio, G., & Berkhout, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313895200 · Cited by 129
KORTT, A. A., MALBY, R. L., CALDWELL, J. B., GRUEN, L. C., IVANCIC, N., LAWRENCE, M. C., HOWLETT, G. J., WEBSTER, R. G., HUDSON, P. J., & COLMAN, P. M. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18724.x · Cited by 128
A Structural Solution for the DNA Polymerase λ-Dependent Repair of DNA Gaps with Minimal Homology
Garcia-Diaz, M., Bebenek, K., Krahn, J. M., Blanco, L., Kunkel, T. A., & Pedersen, L. C. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00061-9 · Cited by 126
Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex
Fukai, S., Matern, H. T., Jagath, J. R., Scheller, R. H., & Brunger, A. T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg329 · Cited by 126
Coll, M., Seidman, J. G., & Müller, C. W. (2002) · Structure · doi:10.1016/s0969-2126(02)00722-0 · Cited by 121
Campos-Olivas, R., Newman, J. L., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3475 · Cited by 119
Mechanism for Multiple Ligand Recognition by the Human Transferrin Receptor
Giannetti, A. M., Snow, P. M., Zak, O., & Björkman, P. J. (2003) · PLoS Biology · doi:10.1371/journal.pbio.0000051 · Cited by 122
The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus
Das, D., & Georgiadis, M. M. (2004) · Structure · doi:10.1016/j.str.2004.02.032 · Cited by 117
Ceccarelli, C., Grodsky, N. B., Ariyaratne, N., Colman, R. F., & Bahnson, B. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207306200 · Cited by 116
Banerjee, S., Wei, B., Bhattacharyya-Pakrasi, M., Pakrasi, H. B., & Smith, T. J. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.008 · Cited by 113
New Insights into the Heparan Sulfate Proteoglycan-binding Activity of Apolipoprotein E
Libeu, C. P., Lund-Katz, S., Phillips, M. C., Wehrli, S., Hernáiz, M. J., Capila, I., Linhardt, R. J., Raffaı̈, R. L., Newhouse, Y. M., Zhou, F., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104746200 · Cited by 113
Structure and self-association of the Rous sarcoma virus capsid protein
Kingston, R. L., Fitzon-Ostendorp, T., Eisenmesser, E. Z., Schatz, G. W., Vogt, V. M., Post, C. B., & Rossmann, M. G. (2000) · Structure · doi:10.1016/s0969-2126(00)00148-9 · Cited by 112
Budayova‐Spano, M., Lacroix, M., Thielens, N. M., Arlaud, G. J., Fontecilla‐Camps, J. C., & Gaboriaud, C. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.231 · Cited by 111
Rath, V. L., Ammirati, M., LeMotte, P. K., Fennell, K. F., Mansour, M. N., Danley, D. E., Hynes, T. R., Schulte, G. K., Wasilko, D. J., & Pandit, J. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00006-7 · Cited by 107
Structures of SAP-1 Bound to DNA Targets from the E74 and c-fos Promoters
Mo, Y., Vaessen, B., Johnston, K., & Marmorstein, R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80130-6 · Cited by 103
“MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures.”
MethodExtended knobs-into-holes packing in classical and complex coiled-coil assemblies☆
Walshaw, J., & Woolfson, D. N. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.014 · Cited by 104
The Frameshift Infidelity of Human DNA Polymerase λ
Bebenek, K., Garcia-Diaz, M., Blanco, L., & Kunkel, T. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305705200 · Cited by 104
Wang, J., Yu, P., Lin, T. C., Konigsberg, W. H., & Steitz, T. A. (1996) · Biochemistry · doi:10.1021/bi960178r · Cited by 99
Structure and distribution of pentapeptide repeats in bacteria
Bateman, A., Murzin, A. G., & Teichmann, S. A. (1998) · Protein Science · doi:10.1002/pro.5560070625 · Cited by 99
Rudenko, G., Bonten, E., d'Azzo, A., & GJ Hol, W. (1995) · Structure · doi:10.1016/s0969-2126(01)00260-x · Cited by 97
Fluoride Inhibition of Enolase: Crystal Structure and Thermodynamics ,
Qin, J., Chai, G., Brewer, J. M., Lovelace, L. L., & Lebioda, L. (2006) · Biochemistry · doi:10.1021/bi051558s · Cited by 97
Kurzbauer, R., Teis, D., de Araujo, M. E. G., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403435101 · Cited by 95
Structure of 3α-Hydroxysteroid/Dihydrodiol Dehydrogenase Complexed with NADP+
Bennett, M. J., Schlegel, B. P., Jez, J. M., Penning, T. M., & Lewis, M. (1996) · Biochemistry · doi:10.1021/bi9604688 · Cited by 92
Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase
Durbecq, V., Sainz, G., Oudjama, Y., Clantin, B., Bompard‐Gilles, C., Tricot, C., Caillet, J., Stalon, V., Droogmans, L., & Villeret, V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1530 · Cited by 90
Crystal Structure of the Catalytic Domain of Human ADAM33
Orth, P., Reichert, P., Wang, W., Prosise, W. W., Yarosh-Tomaine, T., Hammond, G., Ingram, R. N., Xiao, L., Mirza, U. A., Zou, J., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.037 · Cited by 90
Oh, K. J., Singh, P., Lee, K., Foss, K., Lee, S., Park, M., Lee, S., Aluvila, S., Park, M., Singh, P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135293 · Cited by 87
Structure-function studies of the human immunodeficiency virus type 1 matrix protein, p17
Cannon, P. M., Matthews, S., Clark, N., Byles, E. D., Iourin, O., Hockley, D. J., Kingsman, S. M., & Kingsman, A. J. (1997) · Journal of Virology · doi:10.1128/jvi.71.5.3474-3483.1997 · Cited by 86
Artymiuk, P. J., Rice, D. W., Poirrette, A. R., & Willet, P. (1994) · Nature Structural Biology · doi:10.1038/nsb1194-758 · Cited by 83
Thalidomide mimics uridine binding to an aromatic cage in cereblon
Hartmann, M. D., Boichenko, I., Coles, M., Zanini, F., Lupas, A. N., & Hernandez Alvarez, B. (2014) · Journal of Structural Biology · doi:10.1016/j.jsb.2014.10.010 · Cited by 83
Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae
Unno, M., Matsui, T., Chu, G. C., Couture, M., Yoshida, T., Rousseau, D. L., Olson, J. S., & Ikeda-Saito, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400491200 · Cited by 83
Structural analysis of neprilysin with various specific and potent inhibitors
Oefner, C., Roques, B. P., Fournie-Zaluski, M.-C., & Dale, G. E. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444903027410 · Cited by 81
AHVAZI, B., COULOMBE, R., DELARGE, M., VEDADI, M., ZHANG, L., MEIGHEN, E., & VRIELINK, A. (2000) · Biochemical Journal · doi:10.1042/bj3490853 · Cited by 82
Reisch, N., Högler, W., Parajes, S., Rose, I. T., Dhir, V., Götzinger, J., Arlt, W., & Krone, N. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-1306 · Cited by 73
Crystal structure of archaeal RNase HII: a homologue of human major RNase H
Lai, L., Yokota, H., Hung, L.-W., Kim, R., & Kim, S.-H. (2000) · Structure · doi:10.1016/s0969-2126(00)00179-9 · Cited by 71
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
Diversity in Structure and Function of the Ets Family PNT Domains
Mackereth, C. D., Schärpf, M., Gentile, L. N., MacIntosh, S. E., Slupsky, C. M., & McIntosh, L. P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.094 · Cited by 67
Sequence Variations within Protein Families are Linearly Related to Structural Variations
Koehl, P., & Levitt, M. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00971-3 · Cited by 67
Kobayashi, K., Masuda, T., Tajima, N., Wada, H., & Sato, N. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu170 · Cited by 65
YodA from Escherichia coli is a metal-binding, lipocalin-like protein
David, G., Blondeau, K., Schiltz, M., Penel, S., & Lewit-Bentley, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304484200 · Cited by 63
Wong, G. W., Yasuda, S., Madhusudhan, M. S., Li, L., Yang, Y., Krilis, S. A., Šali, A., & Stevens, R. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108677200 · Cited by 61
Structure and Backbone Dynamics of Apo- and Holo-cellular Retinol-binding Protein in Solution
Franzoni, L., Lücke, C., Pérez, C., Cavazzini, D., Rademacher, M., Ludwig, C., Spisni, A., Rossi, G. L., & Rüterjans, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201994200 · Cited by 59
Structure-based Analysis of High Pressure Adaptation of α-Actin
Morita, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302328200 · Cited by 58
Mechanism of metal ion activation of the diphtheria toxin repressor DtxR
D'Aquino, J. A., Tetenbaum-Novatt, J., White, A., Berkovitch, F., & Ringe, D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500908102 · Cited by 57
Insights into the Phosphoregulation of β‐Secretase Sorting Signal by the VHS Domain of GGA1
Shiba, T., Kametaka, S., Kawasaki, M., Shibata, M., Waguri, S., Uchiyama, Y., & Wakatsuki, S. (2004) · Traffic · doi:10.1111/j.1600-0854.2004.00188.x · Cited by 56
Metadata
- Authors
- Kraulis, P. J.
- Venue
- Journal of Applied Crystallography
- Published
- 1991-10-01
- Volume
- 24
- Issue
- 5
- Pages
- 946-950
- ISSN
- 0021-8898 (ISSN-L)
- OpenAlex
- W2028231353
- Cited by
- 14,085
- References
- 0
- FWCI
- 248.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
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.