AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR

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

Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

Kabsch, 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

Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA

Güntert, P., Braun, W. A., & Kurt Wüthrich, A. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90754-t · Cited by 784

An evaluation of computational strategies for use in the determination of protein structure from distance constraints obtained by nuclear magnetic resonance

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

Solution NMR structure of a human FGF‐1 monomer, activated by a hexasaccharide heparin‐analogue

Canales, Á., Lozano, R. M., Mendez, B. L., Angulo, J., Ojeda, R., Nieto, P. M., Martín‐Lomas, M., Giménez‐Gallego, G., & Jiménez‐Barbero, J. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05474.x · Cited by 66

Nuclear Magnetic Resonance Structure-Based Epitope Mapping and Modulation of Dust Mite Group 13 Allergen as a Hypoallergen

Chan, S. L., Ong, S. T., Ong, S. Y., Chew, F. T., & Mok, Y. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4852 · Cited by 66

Solution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei

Zhang, L., Wang, Y., Picking, W. L., Picking, W. D., & Guzman, R. N. D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.03.028 · Cited by 66

NMR Solution Structure of Rat Aβ(1–16): Toward Understanding the Mechanism of Rats' Resistance to Alzheimer's Disease

Istrate, A., Tsvetkov, P. O., Mantsyzov, A. B., Kulikova, A. A., Kozin, S. A., Makarov, A. А., & Polshakov, V. I. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.4006 · Cited by 66

A structural and functional perspective into the mechanism of Ca2+-sensitizers that target the cardiac troponin complex

Robertson, I. M., Sun, Y., Li, M. X., & Sykes, B. D. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.08.019 · Cited by 66

Recognition of Unmodified Histone H3 by the First PHD Finger of Bromodomain-PHD Finger Protein 2 Provides Insights into the Regulation of Histone Acetyltransferases Monocytic Leukemic Zinc-finger Protein (MOZ) and MOZ-related factor (MORF)

Su, Q., Jin, L., Zhang, J., Liu, L., Ji, P., Wu, J., Wu, J., & Shi, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.244400 · Cited by 66

Analysis of the Structure and Conformational States of DewA Gives Insight into the Assembly of the Fungal Hydrophobins

Morris, V. K., Kwan, A. H., & Sunde, M. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.10.021 · Cited by 66

Structural and biophysical characterization of an antimicrobial peptide chimera comprised of lactoferricin and lactoferrampin

Haney, E. F., Nazmi, K., Bolscher, J. G. M., & Vogel, H. J. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.023 · Cited by 67

Structure of the Male Determinant Factor for Brassica Self-incompatibility

Mishima, M., Takayama, S., Sasaki, K., Jee, J., Kojima, C., Isogai, A., & Shirakawa, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305305200 · Cited by 66

Engineering a Protein Scaffold from a PHD Finger

Kwan, A. H., Gell, D. A., Verger, A., Crossley, M., Matthews, J. M., & Mackay, J. P. (2003) · Structure · doi:10.1016/s0969-2126(03)00122-9 · Cited by 66

Structure of an Atypical Orphan Response Regulator Protein Supports a New Phosphorylation-independent Regulatory Mechanism

Hong, E., Lee, H. M., Ko, H., Kim, D.-U., Jeon, B., Jung, J., Shin, J. S., Lee, S.-A., Kim, Y., Jeon, Y. H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609104200 · Cited by 66

Structure of the split PH domain and distinct lipid‐binding properties of the PH–PDZ supramodule of α‐syntrophin

Yan, J., Wen, W., Xu, W., Long, J., Adams, M. E., Froehner, S. C., & Zhang, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600858 · Cited by 66

Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: The role of charges and hydrogen bonding interactions in stabilizing helix conformations

Resende, J. M., de Moraes, C. M., Prates, M. V., César, A., Almeida, F. C. L., Mundim, N. C. C. R., Valente, A. P., Bemquerer, M. P., Piló‐Veloso, D., & Bechinger, B. (2008) · Peptides · doi:10.1016/j.peptides.2008.06.022 · Cited by 66

Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization

Saravanan, R., Mohanram, H., Joshi, M., Domadia, P. N., Torres, J., Ruedl, C., & Bhattacharjya, S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.03.015 · Cited by 66

High resolution structure of the HDGF PWWP domain: A potential DNA binding domain

Lukasik, S. M., Cierpicki, T., Borloz, M. P., Grembecka, J. E., Everett, A. D., & Bushweller, J. H. (2005) · Protein Science · doi:10.1110/ps.051751706 · Cited by 66

Structure-Activity Relationships of Hainantoxin-IV and Structure Determination of Active and Inactive Sodium Channel Blockers

Li, D., Xiao, Y., Xu, X., Xiong, X., Lu, S., Liu, Z., Zhu, Q., Wang, M., Gu, X., & Liang, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405765200 · Cited by 66

Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton‐gated channels

Chagot, B., Escoubas, P., Diochot, S., Bernard, C., Lazdunski, M., & Darbon, H. (2005) · Protein Science · doi:10.1110/ps.051378905 · Cited by 66

Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study

Ramelot, T. A., Raman, S., Kuzin, A. P., Xiao, R., Ma, L., Acton, T., Hunt, J. F., Montelione, G. T., Baker, D. A., & Kennedy, M. A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22229 · Cited by 66

Actions of water extract from Cordyceps militaris in hyperuricemic mice induced by potassium oxonate combined with hypoxanthine

Yong, T., Zhang, M., Chen, D., Shuai, O., Chen, S., Su, J., Jiao, C., Feng, D., & Xie, Y. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.10.001 · Cited by 68

Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit

Tatebe, H., Murayama, S., Yonekura, T., Hatano, T., Richter, D., Furuya, T., Kataoka, S., Furuita, K., Kojima, C., & Shiozaki, K. (2017) · eLife · doi:10.7554/elife.19594 · Cited by 66

Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48

Moreno‐Beltrán, B., Guerra‐Castellano, A., Dı́az-Quintana, A., Conte, R. D., García‐Mauriño, S. M., Díaz‐Moreno, S., González‐Arzola, K., Santos‐Ocaña, C., Velázquez‐Campoy, A., la Rosa, M. Á. D., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1618008114 · Cited by 65

Structural Analysis of the Complement Control Protein (CCP) Modules of GABAB Receptor 1a

Blein, S., Ginham, R., Uhrı́n, D., Smith, B. O., Soares, D. C., Veltel, S., McIlhinney, R. A. J., White, J. H. M., & Barlow, P. N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406540200 · Cited by 65

Accuracy of structure-derived properties in simple comparative models of protein structures

Chakravarty, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki162 · Cited by 66

Structural and functional insights into PINCH LIM4 domain–mediated integrin signaling

Vėlyvis, A., Vaynberg, J., Yang, Y., Vinogradova, O., Zhang, Y., Wu, C., & Qin, J. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb938 · Cited by 66

Solution structure of human GAIP (Gα interacting protein): a regulator of G protein signaling

de Alba, E., Vries, L. D., Farquhar, M. G., & Tjandra, N. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2989 · Cited by 66

NMR solution structure of the N-terminal domain of hERG and its interaction with the S4–S5 linker

Li, Q., Gayen, S., Chen, A. S., Huang, Q., Raida, M., & Kang, C. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.10.132 · Cited by 65

Single-Nucleotide Polymorphisms (SNP) Mining and Their Effect on the Tridimensional Protein Structure Prediction in a Set of Immunity-Related Expressed Sequence Tags (EST) in Atlantic Salmon (Salmo salar)

Vallejos‐Vidal, E., Reyes-Cerpa, S., Rivas‐Pardo, J. A., Maisey, K. R., Yañez, J. M., Valenzuela, H., Cea, P. A., Castro‐Fernández, V., Tort, L., Sandino, A. M., et al. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2019.01406 · Cited by 73

An Integrated Platform for Automated Analysis of Protein NMR Structures

Huang, Y. J., Moseley, H., Baran, M., Arrowsmith, C. H., Powers, R., Tejero, R., Szyperski, T., & Montelione, G. T. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)94005-6 · Cited by 65

A Novel AT-Rich DNA Recognition Mechanism for Bacterial Xenogeneic Silencer MvaT

Ding, P., McFarland, K. A., Jin, S., Tong, G., Duan, B., Yang, A. W. H., Hughes, T. R., Liu, J., Dove, S. L., Navarre, W. W., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004967 · Cited by 65

C-Terminal Half of Human Centrin 2 Behaves like a Regulatory EF-Hand Domain

Matei, E., Miron, S. M., Blouquit, Y., Duchambon, P., Durussel, I., Cox, J. A., & Craescu, C. T. (2003) · Biochemistry · doi:10.1021/bi0269714 · Cited by 65

Toward the Molecular Basis of Inherited Prion Diseases: NMR Structure of the Human Prion Protein with V210I Mutation

Biljan, I., Ilc, G., Giachin, G., Raspadori, A., Zhukov, I., Plavec, J., & Legname, G. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.07.067 · Cited by 65

NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP248−286

Nanga, R. P. R., Brender, J., Vivekanandan, S., Popovych, N., & Ramamoorthy, A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja908170s · Cited by 65

The Par‐3 NTD adopts a PB1‐like structure required for Par‐3 oligomerization and membrane localization

Feng, W., Wu, H., Chan, L.-N., & Zhang, M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601702 · Cited by 66

Characterization of the RNA recognition mode of hnRNP G extends its role in SMN2 splicing regulation

Moursy, A., Allain, F. H. ‐., & Cléry, A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku244 · Cited by 65

Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism

Biljan, I., Giachin, G., Ilc, G., Zhukov, I., Plavec, J., & Legname, G. (2012) · Biochemical Journal · doi:10.1042/bj20111940 · Cited by 65

Cyclic AMP Analog Blocks Kinase Activation by Stabilizing Inactive Conformation: Conformational Selection Highlights a New Concept in Allosteric Inhibitor Design

Badireddy, S., Yunfeng, G., Ritchie, M. A., Akamine, P., Wu, J., Kim, C., Taylor, S. S., Lin, Q., Swaminathan, K., & Anand, G. S. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.004390 · Cited by 65

Solution Structure of the Recombinant Penaeidin-3, a Shrimp Antimicrobial Peptide

Yang, Y., Poncet, J., Garnier, J., Zatylny‐Gaudin, C., Evelyne Bachère, B., & Aumelas, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305450200 · Cited by 65

Dicarba Analogues of α-Conotoxin RgIA. Structure, Stability, and Activity at Potential Pain Targets

Chhabra, S., Belgi, A., Bartels, P., van Lierop, B. J., Robinson, S. D., Kompella, S. N., Hung, A., Callaghan, B. P., Adams, D. J., Robinson, A. J., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501126u · Cited by 65

Structural insights into a high fidelity variant of SpCas9

Guo, M., Ren, K., Zhu, Y., Tang, Z., Wang, Y., Zhang, B., & Huang, Z. (2019) · Cell Research · doi:10.1038/s41422-018-0131-6 · Cited by 65

Structure of the heterodimeric complex between CAD domains of CAD and ICAD.

Otomo, T., Sakahira, H., Uegaki, K., Nagata, S., & Yamazaki, T. (2000) · Nature Structural Biology · doi:10.1038/77957 · Cited by 65

Solution structure of the DNA binding domain from Dead ringer, a sequence‐specific AT‐rich interaction domain (ARID)

Iwahara, J., & Clubb, R. T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6084 · Cited by 65

A domain-based vaccine construct against SARS-CoV-2, the causative agent of COVID-19 pandemic: development of self-amplifying mRNA and peptide vaccines

Pourseif, M. M., Parvizpour, S., Jafari, B., Dehghani, J., Naghili, B., & Omidi, Y. (2020) · Bioimpacts · doi:10.34172/bi.2021.11 · Cited by 63

Structure and Dynamics of a β-Helical Antifreeze Protein,

Daley, M. E., Spyracopoulos, L., Jia, Z., Davies, P. L., & Sykes, B. D. (2002) · Biochemistry · doi:10.1021/bi0121252 · Cited by 64

Recognition of Mitochondrial Targeting Sequences by the Import Receptors Tom20 and Tom22

Rimmer, K. A., Foo, J. H., Ng, A., Petrie, E. J., Shilling, P. J., Perry, A., Mertens, H. D. T., Lithgow, T. J., Mulhern, T. D., & Gooley, P. R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.11.017 · Cited by 64

NMR Structure of a Heterodimeric SAM:SAM Complex: Characterization and Manipulation of EphA2 Binding Reveal New Cellular Functions of SHIP2

Lee, H. J., Hota, P. K., Chugha, P., Guo, H., Miao, H., Zhang, L., Kim, S.-J., Stetzik, L., Wang, B.-C., & Buck, M. (2012) · Structure · doi:10.1016/j.str.2011.11.013 · Cited by 64

Identification and Solution Structure of a Highly Conserved C-terminal Domain within ORF1p Required for Retrotransposition of Long Interspersed Nuclear Element-1

Januszyk, K., Li, P. W.-L., Villareal, V. A., Branciforte, D., Wu, H., Xie, Y., Feigon, J. F., Loo, J. A., Martin, S. L., & Clubb, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702023200 · Cited by 64

RBM7 subunit of the NEXT complex binds U-rich sequences and targets 3′-end extended forms of snRNAs

Hroššová, D., Šikorský, T., Potěšil, D., Bartošovič, M., Pasulka, J., Zdráhal, Z., Štefl, R., & Vaňáčová, Š. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv240 · Cited by 68

Solution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidis

Cantini, F., Veggi, D., Dragonetti, S., Savino, S., Scarselli, M., Romagnoli, G., Pizza, M., Banci, L., & Rappuoli, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c800214200 · Cited by 64

Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein

Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C., & Tjandra, N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4395 · Cited by 64

Solution Structure of Human Saposin C in a Detergent Environment

Hawkins, C. A., de Alba, E., & Tjandra, N. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.045 · Cited by 64

Structure of the fMet‐tRNAfMet‐binding domain of B.stearothermophilus initiation factor IF2

Meunier, S., Spurio, R., Czisch, M., Wechselberger, R. W., Guenneugues, M., Gualerzi, C. O., & Boelens, R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1918 · Cited by 64

NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding

Tugarinov, V., Zvi, A., Levy, R., Hayek, Y., Matsushita, S., & Anglister, J. (2000) · Structure · doi:10.1016/s0969-2126(00)00119-2 · Cited by 64

Structural basis for the network of functional cooperativities in cytochrome c3 from Desulfovibrio gigas: solution structures of the oxidised and reduced states

Brennan, L., Turner, D. L., Messias, A. C., Teodoro, M. L., LeGall, J., Santos, H., & Xavier, A. V. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3652 · Cited by 64

Characterization of Phospholipase Cγ Enzymes with Gain-of-Function Mutations

Everett, K. L., Bunney, T. D., Yoon, Y., Rodrigues-Lima, F., Harris, R., Driscoll, P. C., Abe, K., Fuchs, H., Hrabé de Angelis, M., Yu, P., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019265 · Cited by 63

Solution Structure of Human Cardiac Troponin C in Complex with the Green Tea Polyphenol, (−)-Epigallocatechin 3-Gallate

Robertson, I. M., Li, M. X., & Sykes, B. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021352 · Cited by 63

Structure of the central core domain of TFIIEβ with a novel double‐stranded DNA‐binding surface

Okuda, M., Watanabe, Y., Okamura, H., Hanaoka, F., Ohkuma, Y., & Nishimura, Y. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1346 · Cited by 63

NMR Structures of the Histidine-Rich Peptide LAH4 in Micellar Environments: Membrane Insertion, pH-Dependent Mode of Antimicrobial Action, and DNA Transfection

Georgescu, J., Munhoz, V. H. O., & Bechinger, B. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.05.038 · Cited by 63

Three-dimensional Solution Structure of an Archaeal FKBP with a Dual Function of Peptidyl Prolyl cis–trans Isomerase and Chaperone-like Activities

Suzuki, R., Nagata, K., Yumoto, F., Kawakami, M., Nemoto, N., Furutani, M., Adachi, K., Maruyama, T., & Tanokura, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00379-6 · Cited by 63

Viewing Human DNA Polymerase β Faithfully and Unfaithfully Bypass an Oxidative Lesion by Time-Dependent Crystallography

Vyas, R., Reed, A. J., Tokarsky, E. J., & Suo, Z. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b02109 · Cited by 60

Structure of a Zinc-binding Domain in the Junín Virus Envelope Glycoprotein

Briknarová, K., Thomas, C. J., York, J., & Nunberg, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166025 · Cited by 63

High Precision NMR Structure and Function of the RING-H2 Finger Domain of EL5, a Rice Protein Whose Expression Is Increased upon Exposure to Pathogen-derived Oligosaccharides

Katoh, S., Hong, C., Tsunoda, Y., Murata, K., Takai, R., Minami, E., Yamazaki, T., & Katoh, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210531200 · Cited by 63

UBIAD1 Mutation Alters a Mitochondrial Prenyltransferase to Cause Schnyder Corneal Dystrophy

Nickerson, M. L., Kostiha, B. N., Brandt, W., Fredericks, W. J., Xu, K.-P., Yu, F.-S., Gold, B., Chodosh, J., Goldberg, M., Lu, D., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010760 · Cited by 63

NMR and Crystal Structures of the Pyrococcus horikoshii RadA Intein Guide a Strategy for Engineering a Highly Efficient and Promiscuous Intein

Oeemig, J. S., Zhou, D., Kajander, T., Wlodawer, A., & Iwaï, H. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.04.029 · Cited by 63

Novel DNA binding domain and genetic regulation model of Bacillus subtilis transition state regulator abrB.

Cavanagh, J., Vaughn, J. L., Feher, V. A., Naylor, S., & Strauch, M. A. (2000) · Nature Structural Biology · doi:10.1038/81999 · Cited by 63

Association of a Model Class A (Apolipoprotein) Amphipathic α Helical Peptide with Lipid

Mishra, V., Anantharamaiah, G. M., Segrest, J. P., Palgunachari, M. N., Chaddha, M., Sham, S. W. S., & Krishna, N. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511475200 · Cited by 63

Topology Scanning and Putative Three-Dimensional Structure of the Extracellular Binding Domains of the Apical Sodium-Dependent Bile Acid Transporter (SLC10A2)

Zhang, E. Y., Phelps, M. A., Banerjee, A., Khantwal, C. M., Chang, C. K., Helsper, F., & Swaan, P. W. (2004) · Biochemistry · doi:10.1021/bi049270a · Cited by 63

Structural Consequences of Carboxyamidation of Dermaseptin S3

Shalev, D. E., Mor, A., & Kustanovich, I. M. (2002) · Biochemistry · doi:10.1021/bi016013m · Cited by 63

Structure of a Construct of a Human Poly(C)-binding Protein Containing the First and Second KH Domains Reveals Insights into Its Regulatory Mechanisms

Du, Z., Fenn, S., Tjhen, R., & James, T. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803046200 · Cited by 63

Solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state

Falzone, C. J., Vu, B. C., Scott, N. L., & Lecomte, J. T. J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01093-8 · Cited by 63

High-Resolution Solution Structure of the Beryllofluoride-Activated NtrC Receiver Domain

Hastings, C. A., Lee, S., Cho, H. S., Yan, D., Kustu, S. G., & Wemmer, D. E. (2003) · Biochemistry · doi:10.1021/bi0273866 · Cited by 63

PALSSE: A program to delineate linear secondary structural elements from protein structures

Majumdar, I., Krishna, S., & Grishin, N. V. (2005) · BMC Bioinformatics · doi:10.1186/1471-2105-6-202 · Cited by 63

A Structural Characterization of Human SCO2

Banci, L., Bertini, I., Ciofi‐Baffoni, S., Gerothanassis, I. P., Leontari, I., Martinelli, M., & Wang, S. (2007) · Structure · doi:10.1016/j.str.2007.07.011 · Cited by 63

Conformational preferences of the amylin nucleation site in SDS micelles: An NMR study

Mascioni, A., Porcelli, F., Ilangovan, U., Ramamoorthy, A., & Veglia, G. (2003) · Biopolymers · doi:10.1002/bip.10305 · Cited by 63

Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity

Byeon, I. L., Byeon, C., Wu, T., Mitra, M., Singer, D., Levin, J. G., & Gronenborn, A. M. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00382 · Cited by 61

Molecular dynamics simulation of docking structures of SARS-CoV-2 main protease and HIV protease inhibitors

Cardoso, W. B., & Mendanha, S. A. (2020) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2020.129143 · Cited by 62

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Bae, B., Ohene-Adjei, S., Kocherginskaya, S. A., Mackie, R. I., Spies, M., Cann, I., & Nair, S. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706513200 · Cited by 62

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Hudáky, P., Stráner, P., Farkas, V., Váradi, G., Tóth, G. J., & Perczel, A. (2007) · Biochemistry · doi:10.1021/bi701371x · Cited by 62

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Tossavainen, H., Pihlajamaa, T., Huttunen, T. K., Raulo, E., Rauvala, H., Permi, P., & Kilpeläinen, I. (2006) · Protein Science · doi:10.1110/ps.052068506 · Cited by 62

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Hopkins, E. J., Layfield, S. L., Ferraro, T., Bathgate, R. A. D., & Gooley, P. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609526200 · Cited by 62

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Hamada, T., Asanuma, M., Ueki, T., Hayashi, F., Kobayashi, N., Yokoyama, S., Michibata, H., & Hirota, H. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042687j · Cited by 62

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Pell, L. G., Gasmi-Seabrook, G. M. C., Morais, M. C., Neudecker, P., Kanelis, V., Bona, D., Donaldson, L. W., Edwards, A. M., Howell, P. L., Davidson, A. R., et al. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.044 · Cited by 62

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Heikkinen, O., Ruskamo, S., Konarev, P. V., Svergun, D. I., Iivanainen, T., Heikkinen, S. M., Permi, P., Koskela, H. T., Kilpeläinen, I., & Ylänne, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019661 · Cited by 62

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Wen, W., Liu, W., Yan, J., & Zhang, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803417200 · Cited by 62

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Mao, B., Tejero, R., Baker, D. A., & Montelione, G. T. (2014) · Journal of the American Chemical Society · doi:10.1021/ja409845w · Cited by 65

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Chen, C., Hsu, C., Su, N., Lin, Y., Chiou, S., & Wu, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106182200 · Cited by 62

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Banci, L., Bertini, I., Ciofi‐Baffoni, S., Su, X., Miras, R., Bal, N., Mintz, E., Catty, P., Shokes, J. E., & Scott, R. A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.055 · Cited by 62

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Jee, J.-G., Ikegami, T., Hashimoto, M., Kawabata, T., Ikeguchi, M., Watanabe, T., & Shirakawa, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109726200 · Cited by 62

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Rodrigues‐Lima, F., Deloménie, C., GOODFELLOW, G. H., Grant, D. M., & Dupret, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560327 · Cited by 62

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Jouvensal, L., Quillien, L., Ferrasson, E., Rahbé, Y., Guéguen, J., & Vovelle, F. (2003) · Biochemistry · doi:10.1021/bi034803l · Cited by 61

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Singer, J., Fazekas, J., Wang, W., Weichselbaumer, M., Matz, M., Mäder, A., Steinfellner, W., Meitz, S., Mechtcheriakova, D., Sobanov, Y., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0288 · Cited by 61

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Bertini, I., Case, D. A., Ferella, L., Giachetti, A., & Rosato, A. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr415 · Cited by 61

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Vuister, G. W., Fogh, R. H., Hendrickx, P. M. S., Doreleijers, J. F., & Gutmanas, A. (2013) · Journal of Biomolecular NMR · doi:10.1007/s10858-013-9750-x · Cited by 35

Quality assessment of NMR structures: a statistical survey

Doreleijers, J. F., Rullmann, J. A. C., & Kaptein, R. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1808 · Cited by 105

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MacArthur, M. W., Laskowski, R. A., & Thornton, J. M. (1994) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(94)90172-4 · Cited by 114

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Nabuurs, S. B., Spronk, C. A. E. M., Vriend, G., & Vuister, G. W. (2004) · Concepts in Magnetic Resonance Part A · doi:10.1002/cmr.a.20016 · Cited by 22

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Spronk, C. A. E. M., Nabuurs, S. B., Krieger, E., Vriend, G., & Vuister, G. W. (2004) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2004.08.003 · Cited by 74