Published in PLoS Comput Biol on March 27, 2017
The Protein Data Bank. Nucleic Acids Res (2000) 187.10
Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol (1993) 64.61
MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics (2004) 50.89
Pfam: the protein families database. Nucleic Acids Res (2013) 22.48
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell (2006) 20.92
ROCR: visualizing classifier performance in R. Bioinformatics (2005) 19.60
Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science (1996) 19.48
UniRef: comprehensive and non-redundant UniProt reference clusters. Bioinformatics (2007) 17.43
UniProt: a hub for protein information. Nucleic Acids Res (2014) 16.72
Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J Mol Biol (2002) 9.74
PEST sequences and regulation by proteolysis. Trends Biochem Sci (1996) 8.90
The regulation of transcription by phosphorylation. Cell (1992) 7.99
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res (2011) 7.84
Systematic discovery of in vivo phosphorylation networks. Cell (2007) 6.94
The PDBbind database: collection of binding affinities for protein-ligand complexes with known three-dimensional structures. J Med Chem (2004) 6.50
Serine/threonine phosphatases: mechanism through structure. Cell (2009) 6.19
Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science (2009) 5.37
An experimentally derived confidence score for binary protein-protein interactions. Nat Methods (2008) 5.27
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol (2005) 5.05
ERK1/2 MAP kinases: structure, function, and regulation. Pharmacol Res (2012) 3.48
Phospho.ELM: a database of phosphorylation sites--update 2011. Nucleic Acids Res (2010) 3.38
The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer development. Trends Cell Biol (2008) 3.30
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Mol Cell Proteomics (2008) 3.13
Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors. Nature (2004) 2.86
ELM--the database of eukaryotic linear motifs. Nucleic Acids Res (2011) 2.84
Systematic functional prioritization of protein posttranslational modifications. Cell (2012) 2.78
PhosphoSitePlus, 2014: mutations, PTMs and recalibrations. Nucleic Acids Res (2014) 2.66
SIFTS: Structure Integration with Function, Taxonomy and Sequences resource. Nucleic Acids Res (2012) 2.61
Global and site-specific quantitative phosphoproteomics: principles and applications. Annu Rev Pharmacol Toxicol (2009) 2.53
Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics (2009) 2.49
Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis. Science (2013) 2.44
Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation. Cell (2001) 2.31
Ten thousand interactions for the molecular biologist. Nat Biotechnol (2004) 2.30
Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell (1996) 2.17
Weak functional constraints on phosphoproteomes. Trends Genet (2009) 2.10
A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange. EMBO J (2002) 2.07
Phosphorylation in protein-protein binding: effect on stability and function. Structure (2011) 1.96
Functional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins. J Proteome Res (2007) 1.92
Interactome3D: adding structural details to protein networks. Nat Methods (2012) 1.89
Deciphering a global network of functionally associated post-translational modifications. Mol Syst Biol (2012) 1.86
eggNOG 4.5: a hierarchical orthology framework with improved functional annotations for eukaryotic, prokaryotic and viral sequences. Nucleic Acids Res (2015) 1.63
Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nat Struct Biol (1998) 1.63
Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J Mol Biol (1998) 1.60
ATM activates p53 by regulating MDM2 oligomerization and E3 processivity. EMBO J (2009) 1.56
A mechanism for the evolution of phosphorylation sites. Cell (2011) 1.47
SH2 domains: modulators of nonreceptor tyrosine kinase activity. Curr Opin Struct Biol (2009) 1.45
Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium. Mol Syst Biol (2012) 1.44
PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins. Nucleic Acids Res (2012) 1.39
Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors. J Biol Chem (2001) 1.37
Lessons from structural genomics. Annu Rev Biophys (2009) 1.33
Evolution and functional cross-talk of protein post-translational modifications. Mol Syst Biol (2013) 1.30
Identification of a molecular target for the Yersinia protein kinase A. Mol Cell (2007) 1.29
Phosphoproteomics strategies for the functional analysis of signal transduction. Proteomics (2006) 1.26
Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. J Mol Biol (2001) 1.23
The impact of structural genomics on the protein data bank. Am J Pharmacogenomics (2004) 1.21
Why nature chose phosphate to modify proteins. Philos Trans R Soc Lond B Biol Sci (2012) 1.18
Structure of the heterodimeric complex between CAD domains of CAD and ICAD. Nat Struct Biol (2000) 1.16
Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase. Proc Natl Acad Sci U S A (2012) 1.15
Regulation of yeast central metabolism by enzyme phosphorylation. Mol Syst Biol (2012) 1.15
A post-translational modification code for transcription factors: sorting through a sea of signals. Trends Cell Biol (2009) 1.14
Promoting a structural view of biology for varied audiences: an overview of RCSB PDB resources and experiences. J Appl Crystallogr (2010) 1.09
Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation. Nat Struct Biol (2003) 1.05
Modular evolution of phosphorylation-based signalling systems. Philos Trans R Soc Lond B Biol Sci (2012) 1.02
Correlation between posttranslational modification and intrinsic disorder in protein. Pac Symp Biocomput (2012) 1.02
PTMcode v2: a resource for functional associations of post-translational modifications within and between proteins. Nucleic Acids Res (2014) 1.01
Structural analysis of adenine phosphoribosyltransferase from Saccharomyces cerevisiae. Biochemistry (2001) 1.01
Mechismo: predicting the mechanistic impact of mutations and modifications on molecular interactions. Nucleic Acids Res (2014) 1.01
Design of an encodable tyrosine kinase-inducible domain: detection of tyrosine kinase activity by terbium luminescence. J Am Chem Soc (2010) 0.98
Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions. J Biol Chem (2007) 0.97
Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target. Proc Natl Acad Sci U S A (2006) 0.95
dbPTM 2016: 10-year anniversary of a resource for post-translational modification of proteins. Nucleic Acids Res (2015) 0.90
Regulation of cytosolic enzymes in primary metabolism by reversible protein phosphorylation. Curr Opin Plant Biol (1998) 0.87
Protein structure as a means to triage proposed PTM sites. Proteomics (2013) 0.83