Abstract
Contact and support
Need help, have a question, or want to contact the ResearchHub team?
© 2026 ResearchHub. Built for responsible scholarly connection.
Wataru Nemoto, Hayato Oikawa
Abstract
Authors
Institutions
Provenance
crossref
Confidence 100%
ror
Confidence 99%
pubmed
Confidence 98%
europepmc
Confidence 96%
unpaywall
Confidence 95%
openalex
Confidence 95%
doaj
Confidence 92%
No local reference links have been materialized yet.
No local citing links have been materialized yet.
Predicting protein function from sequence and structural data
10.1016/j.sbi.2005.04.003 · 2005
10.1006/jmbi.1996.0167
10.1006/jmbi.1996.0167
Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
10.1006/jmbi.2001.4540 · 2001
10.1006/jmbi.2001.5327
10.1006/jmbi.2001.5327
10.1093/bioinformatics/19.1.163
10.1093/bioinformatics/19.1.163
10.1016/j.jmb.2004.08.022
10.1016/j.jmb.2004.08.022
Automatic methods for predicting functionally important residues
10.1016/s0022-2836(02)01451-1 · 2003
10.1006/jmbi.2001.4870
10.1006/jmbi.2001.4870
Prediction of functional sites in proteins using conserved functional group analysis
10.1016/j.jmb.2004.01.053 · 2004
Evolutionary trace report_maker: a new type of service for comparative analysis of proteins
10.1093/bioinformatics/btl157 · 2006
datacite
Confidence 0%
JEvTrace: refinement and variations of the evolutionary trace in JAVA
10.1186/gb-2002-3-12-research0077 · 2002
Evolutionary trace analysis of TGF-beta and related growth factors: implications for site-directed mutagenesis
10.1093/protein/13.12.839 · 2000
10.1093/nar/gkq399
10.1093/nar/gkq399
10.1002/prot.10146
10.1002/prot.10146
10.1002/pro.5560010203
10.1002/pro.5560010203
Improvement in protein functional site prediction by distinguishing structural and functional constraints on protein family evolution using computational design
10.1093/nar/gki894 · 2005
10.1073/pnas.97.19.10383
10.1073/pnas.97.19.10383
10.1093/nar/gkr1129
10.1093/nar/gkr1129
Heterotachy, an important process of protein evolution
10.1093/oxfordjournals.molbev.a003973 · 2002
Unresolved referenced work
Kept as external metadata until matched
10.1110/ps.03323604
10.1110/ps.03323604
10.1371/journal.pcbi.1000267
10.1371/journal.pcbi.1000267
Disentangling evolutionary signals: conservation, specificity determining positions and coevolution. Implication for catalytic residue prediction
10.1186/1471-2105-13-235 · 2012
10.1016/s0022-2836(03)00663-6
10.1016/s0022-2836(03)00663-6
10.1371/journal.pcbi.1000978
10.1371/journal.pcbi.1000978
An automated stochastic approach to the identification of the protein specificity determinants and functional subfamilies
10.1186/1748-7188-5-29 · 2010
SitesIdentify: a protein functional site prediction tool
10.1186/1471-2105-10-379 · 2009
Correlated mutations and residue contacts in proteins
10.1002/prot.340180402 · 1994
Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations?
10.1093/protein/7.3.349 · 1994
Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions
10.1021/bi050293e · 2005
10.1093/bioinformatics/bti671
10.1093/bioinformatics/bti671
Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments
10.1093/bioinformatics/btg072 · 2003
10.1093/bioinformatics/btm584
10.1093/bioinformatics/btm584
InterMap3D: predicting and visualizing co-evolving protein residues
10.1093/bioinformatics/btp335 · 2009
CAPS: coevolution analysis using protein sequences
10.1093/bioinformatics/btl493 · 2006
10.1093/nar/gks488
10.1093/nar/gks488
Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions
10.1006/jmbi.2000.4146 · 2000
10.1023/b:jopc.0000039556.95629.cf
10.1023/b:jopc.0000039556.95629.cf
Prediction of heterodimerization interfaces of G-protein coupled receptors with a new subtractive correlated mutation method
10.1093/protein/15.11.881 · 2002
10.1371/journal.pone.0041430
10.1371/journal.pone.0041430
10.1016/j.jmb.2011.02.017
10.1016/j.jmb.2011.02.017 · doi-reference
GeMMA: functional subfamily classification within superfamilies of predicted protein structural domains
10.1093/nar/gkp1049 · doi-reference
10.1101/gr.772403
10.1101/gr.772403 · doi-reference
10.1093/nar/gkr1065
10.1093/nar/gkr1065 · doi-reference
FunShift: a database of function shift analysis on protein subfamilies
10.1093/nar/gki067 · doi-reference
10.1016/j.jmb.2003.12.078
10.1016/j.jmb.2003.12.078 · doi-reference
A structure and evolution-guided Monte Carlo sequence selection strategy for multiple alignment-based analysis of proteins
10.1093/bioinformatics/bti791 · doi-reference
Evolutionary and structural feedback on selection of sequences for comparative analysis of proteins
10.1002/prot.20866 · doi-reference
Functional region prediction with a set of appropriate homologous sequences-an index for sequence selection by integrating structure and sequence information with spatial statistics
10.1186/1472-6807-12-11 · doi-reference
10.1371/journal.pone.0014286
10.1371/journal.pone.0014286 · doi-reference
Prediction of enzyme function based on 3D templates of evolutionarily important amino acids
10.1186/1471-2105-9-17 · doi-reference
Protein function prediction using local 3D templates
10.1016/j.jmb.2005.05.067 · doi-reference
Automated discovery of 3D motifs for protein function annotation
10.1093/bioinformatics/btk038 · doi-reference
A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structures
10.1006/jmbi.1994.1657 · doi-reference
10.1016/s0022-2836(03)00045-7
10.1016/s0022-2836(03)00045-7 · doi-reference
Recognition of spatial motifs in protein structures
10.1006/jmbi.1998.2393 · doi-reference
10.1002/pro.5560061104
10.1002/pro.5560061104 · doi-reference
ProFunc: a server for predicting protein function from 3D structure
10.1093/nar/gki414 · doi-reference
PDBSite: a database of the 3D structure of protein functional sites
10.1093/nar/gki105 · doi-reference
PDBSiteScan: a program for searching for active, binding and posttranslational modification sites in the 3D structures of proteins
10.1093/nar/gkh439 · doi-reference
10.1016/s0022-2836(02)00811-2
10.1016/s0022-2836(02)00811-2 · doi-reference
10.1023/a:1011318527094
10.1023/a:1011318527094 · doi-reference
A method for localizing ligand binding pockets in protein structures
10.1002/prot.20769 · doi-reference
pvSOAR: detecting similar surface patterns of pocket and void surfaces of amino acid residues on proteins
10.1093/nar/gkh390 · doi-reference
10.1016/j.jmb.2004.04.012
10.1016/j.jmb.2004.04.012 · doi-reference
Detection, delineation, measurement and display of cavities in macromolecular structures
10.1107/s0907444993011333 · doi-reference
An algorithm for constraint-based structural template matching: application to 3D templates with statistical analysis
10.1093/bioinformatics/btg226 · doi-reference
Highly specific protein sequence motifs for genome analysis
10.1073/pnas.95.11.5865 · doi-reference
PROSITE: A documented database using patterns and profiles as motif descriptors
10.1093/bib/3.3.265 · doi-reference
10.1093/nar/gkl788
10.1093/nar/gkl788 · doi-reference
The SuMo server: 3D search for protein functional sites
10.1093/bioinformatics/bti645 · doi-reference
A new bioinformatic approach to detect common 3D sites in protein structures
10.1002/prot.10339 · doi-reference
Motif-based searching in TOPS protein topology databases
10.1093/bioinformatics/15.4.317 · doi-reference
pdbFun: mass selection and fast comparison of annotated PDB residues
10.1093/nar/gki499 · doi-reference
Recognizing the fold of a protein structure
10.1093/bioinformatics/btg240 · doi-reference
Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
10.1107/s0907444904026460 · doi-reference
10.1002/prot.340230309
10.1002/prot.340230309 · doi-reference
10.1006/jmbi.1993.1489
10.1006/jmbi.1993.1489 · doi-reference
10.1016/s0022-2836(05)80360-2
10.1016/s0022-2836(05)80360-2 · doi-reference
MISTIC: mutual information server to infer coevolution
10.1093/nar/gkt427 · doi-reference