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Protein structure validation by generalized linear model root‐mean‐square deviation prediction
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/1097-0134(20010215)42:3<378::aid-prot70>3.0.co;2-3openalex-snapshot
Protein structural alignments and functional genomics
inferredcites →https://doi.org/10.1002/pro.5560010606openalex-snapshot
The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures
inferredcites →https://doi.org/10.1002/prot.10286openalex-snapshot
Structure validation by Cα geometry: ϕ,ψ and Cβ deviation
inferredcites →https://doi.org/10.1002/prot.20491openalex-snapshot
Comparison of X‐ray and NMR structures: Is there a systematic difference in residue contacts between X‐ray‐ and NMR‐resolved protein structures?
inferredcites →https://doi.org/10.1002/prot.20499openalex-snapshot
Assessing precision and accuracy of protein structures derived from NMR data
inferredcites →https://doi.org/10.1002/prot.21165openalex-snapshot
Evaluating protein structures determined by structural genomics consortia
inferredcites →https://doi.org/10.1002/prot.21466openalex-snapshot
Assessing model accuracy using the homology modeling automatically software
inferredcites →https://doi.org/10.1002/prot.21767openalex-snapshot
Critical assessment of methods of protein structure prediction—Round VII
inferredcites →https://doi.org/10.1002/prot.22589openalex-snapshot
Critical assessment of methods of protein structure prediction—Round VIII
inferredcites →https://doi.org/10.1002/prot.24452openalex-snapshot
Critical assessment of methods of protein structure prediction (CASP) — round x
inferredcites →https://doi.org/10.1002/prot.340170404openalex-snapshot
Recognition of errors in three‐dimensional structures of proteins
inferredcites →https://doi.org/10.1006/jmbi.1997.1284openalex-snapshot
Torsion angle dynamics for NMR structure calculation with the new program Dyana
inferredcites →https://doi.org/10.1006/jmbi.1998.1808openalex-snapshot
Quality assessment of NMR structures: a statistical survey
inferredcites →https://doi.org/10.1007/s10858-008-9288-5openalex-snapshot
De novo protein structure generation from incomplete chemical shift assignments
inferredcites →https://doi.org/10.1007/s10858-009-9339-6openalex-snapshot
Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system
inferredcites →https://doi.org/10.1016/0263-7855(90)80070-vopenalex-snapshot
WHAT IF: A molecular modeling and drug design program
inferredcites →https://doi.org/10.1016/s0076-6879(97)77022-8openalex-snapshot
[20] VERIFY3D: Assessment of protein models with three-dimensional profiles
inferredcites →https://doi.org/10.1021/ci049924mopenalex-snapshot
Prediction of Homology Model Quality with Multivariate Regression
inferredcites →https://doi.org/10.1021/ja047109hopenalex-snapshot
Protein NMR Recall, Precision, and F -measure Scores (RPF Scores): Structure Quality Assessment Measures Based on Information Retrieval Statistics
inferredcites →https://doi.org/10.1021/ja905934copenalex-snapshot
Accurate Automated Protein NMR Structure Determination Using Unassigned NOESY Data
inferredcites →https://doi.org/10.1023/a:1008365802830openalex-snapshot
Influence of non-bonded parameters on the quality of NMR structures: A new force field for NMR structure calculation
inferredcites →https://doi.org/10.1038/356083a0openalex-snapshot
Assessment of protein models with three-dimensional profiles
inferredcites →https://doi.org/10.1038/nmeth0909-625openalex-snapshot
CASD-NMR: critical assessment of automated structure determination by NMR
inferredcites →https://doi.org/10.1073/pnas.0610313104openalex-snapshot
Protein structure determination from NMR chemical shifts
inferredcites →https://doi.org/10.1073/pnas.0800256105openalex-snapshot
Consistent blind protein structure generation from NMR chemical shift data
inferredcites →https://doi.org/10.1093/protein/gzq030openalex-snapshot
Sub-AQUA: real-value quality assessment of protein structure models
inferredcites →https://doi.org/10.1103/physrevlett.80.2733openalex-snapshot
Vibrational Dynamics of Folded Proteins: Significance of Slow and Fast Motions in Relation to Function and Stability
inferredcites →https://doi.org/10.1107/s0021889892009944openalex-snapshot
PROCHECK: a program to check the stereochemical quality of protein structures
inferredcites →https://doi.org/10.1107/s0907444909042073openalex-snapshot
MolProbity : all-atom structure validation for macromolecular crystallography
inferredcites →https://doi.org/10.1110/ps.036061.108openalex-snapshot
How well can the accuracy of comparative protein structure models be predicted?
inferredcites →https://doi.org/10.1110/ps.9.2.290openalex-snapshot
Microscopic stability of cold shock protein a examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N‐oxide
inferredcites →https://doi.org/10.1110/ps.9.9.1753openalex-snapshot
Modeling of loops in protein structures
inferredcites →https://doi.org/10.1186/1471-2105-12-170openalex-snapshot
Objective identification of residue ranges for the superposition of protein structures
inferredcites →https://doi.org/10.1186/1471-2105-8-345openalex-snapshot
Benchmarking consensus model quality assessment for protein fold recognition
inferredcites →https://doi.org/10.1201/9781420035001.ch4openalex-snapshot
Protein Structure Prediction
inferredcites →https://doi.org/10.1371/journal.pcbi.0020009openalex-snapshot
Traditional Biomolecular Structure Determination by NMR Spectroscopy Allows for Major Errors
inferredcites →https://doi.org/10.2174/138920309788452173openalex-snapshot
Quality Assessment of Protein Structure Models
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