Cited by 2,957Advanced NMR Techniques and ApplicationsProtein Structure and DynamicsMolecular spectroscopy and chirality

The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Cornilescu, Gabriel, Delaglio, Frank, Bax, Ad·1999·Journal of Biomolecular NMR

DOI 10.1023/a:1008392405740

Open this paper in CoChat — free account

Abstract

Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error.

Integrity signals

Registry

Crossref · 10.1023/a:1008392405740

Cites

75 of 75 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961
1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D. S., Bigam, C. G., Yao, J. S., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211777 · Cited by 2,361
The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
Wishart, D. S., & Sykes, B. D. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175245 · Cited by 2,174
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90214-q · Cited by 1,908
Structure of ubiquitin refined at 1.8 A resolution.
Vijay-Kumar, S., Bugg, C., & Cook, W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,636
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00227471 · Cited by 1,635
Tcl and the Tk Toolkit
Ousterhout, J. K. (1994) · Cited by 1,627
Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts
Spera, S., & Bax, A. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00014a071 · Cited by 1,101
Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,032
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., & Sykes, B. D. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00211764 · Cited by 1,012

Flagged first, then by citations

Show all 75 references

Research works printed but not linked: 5

Brünger, A.T. (1993) XPLOR Manual, Version 3.1, Yale University, New Haven, CT.
Pastore, A. and Saudek, V. (1990) J. Magn. Reson., 90, 165–176.
Redfield, C. and Robertson, J. (1991) Proceedings of a NATO Advanced Research Workshop on Computational Aspects of the Study of Biological Macromolecules by NMR, Plenum Press, New York, NY.
Vuister, G.W., Delaglio, F. and Bax, A. (1993) J. Biomol. NMR, 3, 67–80.
Wang, A.C., Grzesiek, S., Tschudin, R., Lodi, P.J. and Bax, A. (1995) J. Biomol. NMR, 5, 376–382.

Sorted by citations

Items 701–800 of 1,004

The PHD3 Domain of MLL Acts as a CYP33-Regulated Switch between MLL-Mediated Activation and Repression,
Park, S., Osmers, U., Raman, G., Schwantes, R. H., Dı́az, M. O., & Bushweller, J. H. (2010) · Biochemistry · doi:10.1021/bi1009387 · Cited by 70
“φ and ψ dihedral angle restraints were generated by TALOS prediction based onCR, Cβ, C0, andN chemical shifts (30).”
Method
A Surface Groove Essential for Viral Bcl-2 Function During Chronic Infection In Vivo
Loh, J., Huang, Q., Petros, A. M., Nettesheim, D. G., van Dyk, L. F., Labrada, L., Speck, S. H., Levine, B., Olejniczak, E. T., & Virgin, H. W. (2005) · PLoS Pathogens · doi:10.1371/journal.ppat.0010010 · Cited by 71
Structure and topology of the non‐amyloid‐β component fragment of human α‐synuclein bound to micelles: Implications for the aggregation process
Bisaglia, M., Trolio, A., Bellanda, M., Bergantino, E., Bubacco, L., & Mammi, S. (2006) · Protein Science · doi:10.1110/ps.052048706 · Cited by 68
Solution structure of a viral DNA polymerase X and evidence for a mutagenic function.
Showalter, A. K., Byeon, I. L., Su, M., & Tsai, M. (2001) · Nature Structural Biology · doi:10.1038/nsb1101-942 · Cited by 70
HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations
Swanson, K. A., Knoepfler, P. S., Huang, K., Kang, R. S.-O., Cowley, S. M., Laherty, C. D., Eisenman, R. N., & Radhakrishnan, I. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb798 · Cited by 70
NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: Implications for KaiA–KaiC interaction
Vakonakis, I., Sun, J., Wu, T., Holzenburg, A., Golden, S. S., & LiWang, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305516101 · Cited by 70
Tertiary Structure and Carbohydrate Recognition by the Chitin-Binding Domain of a Hyperthermophilic Chitinase from Pyrococcus furiosus
Nakamura, T., Mine, S., Hagihara, Y., Ishikawa, K., Ikegami, T., & Uegaki, K. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.006 · Cited by 69
Solution Structure and Sugar-Binding Mechanism of Mouse Latrophilin-1 RBL: a 7TM Receptor-Attached Lectin-Like Domain
Vakonakis, I., Langenhan, T., Prömel, S., Russ, A., & Campbell, I. D. (2008) · Structure · doi:10.1016/j.str.2008.02.020 · Cited by 69
Solution Structure and Phylogenetics of Prod1, a Member of the Three-Finger Protein Superfamily Implicated in Salamander Limb Regeneration
Garza-Garcı́a, A., Harris, R., Esposito, D., Gates, P. B., & Driscoll, P. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007123 · Cited by 70
Solution structure of a paradigm ArsR family zinc sensor in the DNA-bound state
Arunkumar, A. I., Campanello, G. C., & Giedroc, D. P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905558106 · Cited by 69
The Carboxyl-terminal Nucleoplasmic Region of MAN1 Exhibits a DNA Binding Winged Helix Domain
Caputo, S. M., Couprie, J., Duband‐Goulet, I., Kondé, E., Lin, F., Braud, S., Gondry, M., Gilquin, B., Worman, H. J., & Zinn‐Justin, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601980200 · Cited by 69
Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity
Lee, J., Nyenhuis, D. A., Nelson, E. A., Cafiso, D. S., White, J. M., & Tamm, L. K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708052114 · Cited by 69
“Dihedral angle restraints were calculated using TALOS+, and CYANA was used to obtain initial structures (58, 59).”
Method
Solution Structure of the Phosphoryl Transfer Complex between the Signal-transducing Protein IIAGlucose and the Cytoplasmic Domain of the Glucose Transporter IICBGlucose of the Escherichia coli Glucose Phosphotransferase System
Cai, M., Williams, D. C., Wang, G., Lee, B. R., Peterkofsky, A., & Clore, G. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302677200 · Cited by 69
Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor
Pan, B., Li, B., Russell, S. J., Tom, J., Cochran, A. G., & Fairbrother, W. J. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5370 · Cited by 69
RAP Uses a Histidine Switch to Regulate Its Interaction with LRP in the ER and Golgi
Lee, D., Walsh, J. D., MIKHAILENKO, I. A., Yu, P., Migliorini, M., Wu, Y., Krueger, S., Curtis, J. E., Harris, B., Lockett, S., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.04.011 · Cited by 72
Measurement of Homonuclear Proton Couplings from Regular 2D COSY Spectra
Delaglio, F., Wu, Z., & Bax, A. (2001) · Journal of Magnetic Resonance · doi:10.1006/jmre.2001.2297 · Cited by 69
Hybrid methods for combined experimental and computational determination of protein structure
Seffernick, J. T., & Lindert, S. (2020) · The Journal of Chemical Physics · doi:10.1063/5.0026025 · Cited by 70
The Metastasis-Associated Extracellular Matrix Protein Osteopontin Forms Transient Structure in Ligand Interaction Sites
Platzer, G., Schedlbauer, A., Chemelli, A., Ozdowy, P., Coudevylle, N., Auer, R., Kontaxis, G., Hartl, M., Miles, A. J., Wallace, B. A., et al. (2011) · Biochemistry · doi:10.1021/bi200291e · Cited by 68
Structure, Dynamics, and Selectivity of the Sodium Channel Blocker μ-Conotoxin SIIIA
Yao, S., Zhang, M., Yoshikami, D., Azam, L., Olivera, B. M., Bulaj, G. W., & Norton, R. S. (2008) · Biochemistry · doi:10.1021/bi801010u · Cited by 68
Progress in correlation spectroscopy at ultra-fast magic-angle spinning: Basic building blocks and complex experiments for the study of protein structure and dynamics
Demers, J., Chevelkov, V., & Lange, A. (2011) · Solid State Nuclear Magnetic Resonance · doi:10.1016/j.ssnmr.2011.07.002 · Cited by 68
Solid-state NMR as a method to reveal structure and membrane-interaction of amyloidogenic proteins and peptides
Naito, A., & Kawamura, I. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.03.025 · Cited by 68
The IsdC Protein from Staphylococcus aureus Uses a Flexible Binding Pocket to Capture Heme
Villareal, V. A., Pilpa, R. M., Robson, S. A., Fadeev, E. A., & Clubb, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801126200 · Cited by 69
Solution Structure of the SWIRM Domain of Human Histone Demethylase LSD1
Tochio, N., Umehara, T., Koshiba, S., Inoue, M., Yabuki, T., Aoki, M., Seki, E., Watanabe, S., Tomo, Y., Hanada, M., et al. (2006) · Structure · doi:10.1016/j.str.2005.12.004 · Cited by 70
Assignment Strategies for Large Proteins by Magic-Angle Spinning NMR: The 21-kDa Disulfide-Bond-Forming Enzyme DsbA
Sperling, L. J., Berthold, D. A., Sasser, T., Jeisy-Scott, V., & Rienstra, C. M. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.04.012 · Cited by 68
Determination of Protein Backbone Structures from Residual Dipolar Couplings
Prestegard, J. H., Mayer, K. L., Valafar, H., & Benison, G. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)94007-x · Cited by 68
Sequence-Specific Deoxyribonucleic Acid (DNA) Recognition by Steroidogenic Factor 1: A Helix at the Carboxy Terminus of the DNA Binding Domain Is Necessary for Complex Stability
Little, T. H., Zhang, Y., Matulis, C. K., Weck, J., Zhang, Z., Ramachandran, A., Mayo, K. E., & Radhakrishnan, I. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0384 · Cited by 68
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
BioMagResBank (BMRB) as a Resource for Structural Biology
Romero, P. R., Kobayashi, N., Wedell, J. R., Baskaran, K., Iwata, T., Yokochi, M., Maziuk, D., Yao, H., Fujiwara, T., Kurisu, G., et al. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0270-6_14 · Cited by 67
α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones
Sprague‐Piercy, M. A., Rocha, M. A., Kwok, A. O., & Martin, R. W. (2020) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-090419-121428 · Cited by 67
Solution structure of the envelope protein domain III of dengue-4 virus
Volk, D. E., Lee, Y.-C., Li, X., Thiviyanathan, V., Gromowski, G. D., Li, L., Lamb, A. R., Beasley, D. W. C., Barrett, A. D. T., & Gorenstein, D. G. (2007) · Virology · doi:10.1016/j.virol.2007.02.023 · Cited by 67
Structural Characterization of the Cyclic Cystine Ladder Motif of θ-Defensins
Conibear, A. C., Rosengren, K. J., Harvey, P. J., & Craik, D. J. (2012) · Biochemistry · doi:10.1021/bi301363a · Cited by 68
Structural and thermodynamic insight into the process of “weak” dimerization of the ErbB4 transmembrane domain by solution NMR
Bocharov, E. V., Mineev, K. S., Goncharuk, M. V., & Arseniev, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.05.001 · Cited by 67
“The backbone dihedral angle restraints for φ and ψwere estimated basing on the assigned chemical shifts with the program PREDITOR [32].”
Method
The solution structure of ParD, the antidote of the ParDE toxin–antitoxin module, provides the structural basis for DNA and toxin binding
Oberer, M., Zangger, K., Gruber, K. F., & Keller, W. (2007) · Protein Science · doi:10.1110/ps.062680707 · Cited by 67
Structure of the Cadherin-related Neuronal Receptor/Protocadherin-α First Extracellular Cadherin Domain Reveals Diversity across Cadherin Families
Morishita, H., Umitsu, M., Murata, Y., Shibata, N., Udaka, K., Higuchi, Y., Akutsu, H., Yamaguchi, T. F., Yagi, T., & Ikegami, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603298200 · Cited by 69
Conformational stability and activity of p73 require a second helix in the tetramerization domain
Coutandin, D., Löhr, F., Niesen, F., Ikeya, T., Weber, T. A., Schäfer, B., Zielonka, E. M., Bullock, A. N., Yang, A. E., Güntert, P., et al. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.139 · Cited by 67
Solid-State NMR Studies of Biomineralization Peptides and Proteins
Roehrich, A. M., & Drobny, G. P. (2013) · Accounts of Chemical Research · doi:10.1021/ar300321e · Cited by 67
NOE Assignment With ARIA 2.0: The Nuts and Bolts
Habeck, M., Rieping, W., Linge, J. P., & Nilges, M. (2004) · Humana Press eBooks · doi:10.1385/1-59259-809-9:379 · Cited by 67
Cooperation between Fixed and Low pH-Inducible Interfaces Controls Lipoprotein Release by the LDL Receptor
Beglova, N., Jeon, H., Fisher, C. A., & Blacklow, S. C. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.038 · Cited by 67
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
NMR analysis of the αIIbβ3 cytoplasmic interaction suggests a mechanism for integrin regulation
Metcalf, D. G., Moore, D. T., Wu, Y., Kielec, J. M., Molnar, K. S., Valentine, K. G., Wand, A. J., BENNETT, J. S., & DeGrado, W. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015545107 · Cited by 66
“chemical shifts using the TALOS+ algorithm (43).”
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
“The ψ and φ dihedral angle restraints predicted by TALOS [33] were used for both cNTnC and cTnI144–163.”
Method
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
Phosphorylation Controls the Interaction of the Connexin43 C-Terminal Domain with Tubulin and Microtubules
Brikci-Nigassa, A. S., Clément, M., Ha‐Duong, T., Adjadj, É., Ziani, L., Pastré, D., Curmi, P. A., & Savarin, P. (2012) · Biochemistry · doi:10.1021/bi201806j · 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
The INAD Scaffold Is a Dynamic, Redox-Regulated Modulator of Signaling in the Drosophila Eye
Liu, W., Wen, W., Wei, Z., Yu, J., Ye, F., Liu, C.-H., Hardie, R., & Zhang, M. (2011) · Cell · doi:10.1016/j.cell.2011.05.015 · 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
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
T7 phage protein Gp2 inhibits the Escherichia coli RNA polymerase by antagonizing stable DNA strand separation near the transcription start site
Cámara, B., Liu, M., Reynolds, J., Shadrin, A. M., Liu, B., Kwok, K. Y. R., Simpson, P. J., Weinzierl, R. O. J., Severinov, K., Cota, E., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907908107 · Cited by 66
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Xue, Y., Ward, J. M., Yuwen, T., Podkorytov, I. S., & Skrynnikov, N. R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206442c · Cited by 67
Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca2+-calmodulin
Liu, Z., & Vogel, H. J. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00038 · Cited by 66
“The dihedral angles along the sequence of each protein were calculated by TALOS (Cornilescu et al., 1999).”
MethodInfluential
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
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
“The 71 ϕ and 71 ψ dihedral-angle constraints were derived from 15N, 13C′, 13Cα, 13Cβ, and Hα chemical shifts, using TALOS+ (34).”
Method
The structure of the Dead ringer–DNA complex reveals how AT‐rich interaction domains (ARIDs) recognize DNA
Iwahara, J., Iwahara, M., Daughdrill, G. W., Ford, J., & Clubb, R. T. (2002) · The EMBO Journal · doi:10.1093/emboj/21.5.1197 · Cited by 66
Solution Structure of the Phosphoryl Transfer Complex between the Cytoplasmic A Domain of the Mannitol Transporter IIMannitol and HPr of the Escherichia coliPhosphotransferase System
Cornilescu, G., Lee, B. R., Cornilescu, C. C., Wang, G., Peterkofsky, A., & Clore, G. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207314200 · Cited by 66
Induced Fit in HIV-Neutralizing Antibody Complexes: Evidence for Alternative Conformations of the gp120 V3 Loop and the Molecular Basis for Broad Neutralization,
Rosen, O., Chill, J. H., Sharon, M., Kessler, N., Mester, B., Zolla‐Pazner, S., & Anglister, J. (2005) · Biochemistry · doi:10.1021/bi047387t · Cited by 66
Structural Properties of the Promiscuous VP16 Activation Domain
Jonker, H. R. A., Wechselberger, R. W., Boelens, R., Folkers, G. E., & Kaptein, R. (2004) · Biochemistry · doi:10.1021/bi0482912 · Cited by 66
Structure of a Conserved Domain Common to the Transcription Factors TFIIS, Elongin A, and CRSP70
Booth, V. K., Koth, C. M., Edwards, A. M., & Arrowsmith, C. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002595200 · 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
The Native Conformation of the Human VDAC1 N Terminus
Schneider, R. C., Etzkorn, M., Giller, K., Daebel, V., Eisfeld, J., Zweckstetter, M., Griesinger, C., Becker, S., & Lange, A. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906241 · Cited by 65
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
ARIA for Solution and Solid-State NMR
Bardiaux, B., Malliavin, T. E., & Nilges, M. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-480-3_23 · Cited by 65
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Krishnarjuna, B., Jaipuria, G., Thakur, A., D’Silva, P., & Atreya, H. S. (2010) · Journal of Biomolecular NMR · doi:10.1007/s10858-010-9459-z · Cited by 65
Conformational Change of H+-ATPase β Monomer Revealed on Segmental Isotope Labeling NMR Spectroscopy
Yagi, H., Tsujimoto, T., Yamazaki, T., Yoshida, M., & Akutsu, H. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045279o · Cited by 65
The Intrinsic Affinity between E2 and the Cys Domain of E1 in Ubiquitin-like Modifications
Wang, J., Hu, W., Cai, S., Lee, B., Song, J., & Chen, Y. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.023 · 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
“Protein dihedral angle constraints were generated by TALOS (45).”
Method
Molecular Dynamics Studies of the Process of Amyloid Aggregation of Peptide Fragments of Transthyretin
Paci, E., Gsponer, J. A., Salvatella, X., & Vendruscolo, M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.009 · Cited by 65
Rapid Identification of Small Binding Motifs with High-Throughput Phage Display
Deshayes, K., Schaffer, M. L., Skelton, N. J., Nakamura, G. R., Kadkhodayan, S., & Sidhu, S. S. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00129-1 · Cited by 65
Resonance Assignments and Secondary Structure Analysis of E. coli Thioredoxin by Magic Angle Spinning Solid-State NMR Spectroscopy
Marulanda, D., Tasayco, M. L., Cataldi, M., Arriaran, V., & Polenova, T. E. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp052774d · Cited by 65
Structure of the Bundle-forming Pilus from Enteropathogenic Escherichia coli*
Ramboarina, S., Fernandes, P. J., Daniell, S., Islam, S., Simpson, P., Frankel, G., Booy, F. P., Donnenberg, M., & Matthews, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508099200 · Cited by 70
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
BAG4/SODD Protein Contains a Short BAG Domain
Briknarová, K., Takayama, S.-I. J., Homma, S. T., Baker, K. K., Cabezas, E., Hoyt, D. W., Li, Z., Satterthwait, A. C., & Ely, K. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202792200 · Cited by 64
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
The 3D Solution Structure of the C-terminal Region of Ku86 (Ku86CTR)
Harris, R., Esposito, D., Sankar, A., Maman, J. D., Hinks, J. A., Pearl, L. H., & Driscoll, P. C. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.047 · Cited by 64
Disruption of FAT10–MAD2 binding inhibits tumor progression
Theng, S. S., Wang, W., Mah, W.-C., Chan, C. S. C., Zhuo, J., Gao, Y., Qin, H., Lim, L., Chong, S. S., Song, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403383111 · Cited by 64
“Briefly, NOE-derived distance and TALOS-based dihedral angle restraints (19) were used in the CYANA software package (20) to calculate 50 NMR structures.”
Method
Structural Characterization of the Type-III Pilot-Secretin Complex from Shigella flexneri
Okon, M., Moraes, T. F., Lario, P. I., Creagh, A. L., Haynes, C. A., Strynadka, N. C. J., & McIntosh, L. P. (2008) · Structure · doi:10.1016/j.str.2008.08.006 · 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 and Dynamics of the HIV-1 Vpu Transmembrane Domain Revealed by Solid-State NMR with Magic-Angle Spinning
Sharpe, S. J., Yau, W., & Tycko, R. (2005) · Biochemistry · doi:10.1021/bi051766k · Cited by 64
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
Correlation of Amyloid Fibril β‐Structure with the Unfolded State of α‐Synuclein
Kim, H., Heise, H., Fernández, C. O., Baldus, M., & Zweckstetter, M. (2007) · ChemBioChem · doi:10.1002/cbic.200700366 · Cited by 61
Solid‐State NMR Spectroscopy of Amyloid Proteins
Heise, H. (2007) · ChemBioChem · doi:10.1002/cbic.200700630 · 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
Monomeric Solution Structure of the Prototypical ‘C' Chemokine Lymphotactin,
Elgin, E. S., McCaslin, D. R., Kitabwalla, M., Pauza, C. D., Markley, J. L., & Volkman, B. F. (2001) · Biochemistry · doi:10.1021/bi011106p · Cited by 65
Structural Analysis of Cassiicolin, a Host-selective Protein Toxin from Corynespora cassiicola
Barthe, P., Pujade‐Renaud, V., Breton, F., Gargani, D., Thaï, R., Roumestand, C., & de Lamotte, F. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.086 · 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
Structural determinants of specific DNA-recognition by the THAP zinc finger
Campagne, S., Saurel, O., Gervais, V., & Milon, A. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq053 · 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
Unmasking the Annexin I Interaction from the Structure of Apo-S100A11
Rintala‐Dempsey, A. C., Walsh, M. P., & Shaw, G. S. (2003) · Structure · doi:10.1016/s0969-2126(03)00126-6 · Cited by 63
Identification of a Novel Co-regulator Interaction Surface on the Ligand Binding Domain of Nurr1 Using NMR Footprinting
Codina, A., Benoit, G., Gooch, J. T., Neuhaus, D., Perlmann, T., & Schwabe, J. W. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409096200 · Cited by 63
Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR
Huster, D. (2005) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2005.01.001 · 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
Towards an Understanding of the Poliovirus Replication Complex: The Solution Structure of the Soluble Domain of the Poliovirus 3A Protein
Strauss, D., Glustrom, L. W., & Wuttke, D. S. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00577-1 · Cited by 63
An approach for high-throughput structure determination of proteins by NMR spectroscopy
Medek, A., Olejniczak, E. T., Meadows, R. P., & Fesik, S. W. (2000) · Journal of Biomolecular NMR · doi:10.1023/a:1026544801001 · Cited by 63
Disordered proteins studied by chemical shifts
Kjærgaard, M., & Poulsen, F. M. (2011) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2011.10.001 · Cited by 68
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
Building native protein conformation from highly approximate backbone torsion angles
Gong, H., Fleming, P. J., & Rose, G. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508415102 · Cited by 62

Authors: Cornilescu, G., Delaglio, F., & Bax, A.
Affiliations: National Institutes of Health (US)
ORCID: Cornilescu, Gabriel
Delaglio, Frank
Bax, Ad
Venue: Journal of Biomolecular NMR
Publisher: Springer Science and Business Media LLC
Published: 1999-03
Volume: 13
Issue: 3
Pages: 289-302
ISSN: 0925-2738 (ISSN-L)
1573-5001
DOI: 10.1023/a:1008392405740
OpenAlex: W1589295940
Cited by: 2,957
References: 75
Citations by year: 2026: 6 · 2025: 7 · 2024: 15 · 2023: 9 · 2022: 19 · 2021: 21 · 2020: 37 · 2019: 27 · 2018: 35 · 2017: 42 · 2016: 53 · 2015: 67 · 2014: 87 · 2013: 112 · 2012: 141
FWCI: 52.55
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Journal of Biomolecular NMR (publishedVersion)
PubMed (publishedVersion)
Topics: Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Chemistry › Spectroscopy › Molecular spectroscopy and chirality
Keywords: Talos, sequence homology, 13C NMR chemical shifts, 15N chemical shifts, protein structure prediction, X-ray structure comparison, database searching
MeSH terms: Amino Acid Sequence, Animals, Computer Graphics, Enzymes, Humans, Molecular Sequence Data, Protein Conformation, Proteins, Software, HIV Protease, Sequence Homology, Amino Acid, Nuclear Magnetic Resonance, Biomolecular, Databases as Topic

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

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks