Published in Protein Sci on October 07, 2015
Selection on protein structure, interaction, and sequence. Protein Sci (2016) 0.78
Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr (2004) 227.01
PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr (2010) 108.52
Phaser crystallographic software. J Appl Crystallogr (2007) 108.34
NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR (1995) 93.94
Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr (2005) 61.38
Oncogenes and signal transduction. Cell (1991) 14.84
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry (1994) 13.94
The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins (2005) 13.03
Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng (1993) 5.47
Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell (1993) 5.47
Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell (1999) 5.09
3D domain swapping: a mechanism for oligomer assembly. Protein Sci (1995) 4.96
3D domain swapping: as domains continue to swap. Protein Sci (2002) 4.35
Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell (2000) 4.21
Domain swapping: entangling alliances between proteins. Proc Natl Acad Sci U S A (1994) 4.20
Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci (1999) 3.41
Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences. Chem Rev (2006) 3.00
Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nat Methods (2010) 2.74
The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol Cell (2006) 2.51
Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1. Mol Cell (2002) 2.00
The unfolding story of three-dimensional domain swapping. Structure (2003) 1.89
Deposition diseases and 3D domain swapping. Structure (2006) 1.88
The MORPHEUS protein crystallization screen. J Appl Crystallogr (2009) 1.87
High-throughput phosphotyrosine profiling using SH2 domains. Mol Cell (2007) 1.72
Structure and dynamic regulation of Src-family kinases. Cell Mol Life Sci (2008) 1.69
Conformational switch and role of phosphorylation in PAK activation. Mol Cell Biol (2001) 1.37
Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry (1996) 1.27
The phosphotyrosine peptide binding specificity of Nck1 and Nck2 Src homology 2 domains. J Biol Chem (2006) 1.20
P21 activated kinases: structure, regulation, and functions. Small GTPases (2014) 1.06
Loops govern SH2 domain specificity by controlling access to binding pockets. Sci Signal (2010) 1.06
Probing the "two-pronged plug two-holed socket" model for the mechanism of binding of the Src SH2 domain to phosphotyrosyl peptides: a thermodynamic study. Biochemistry (1998) 1.05
The evolving role of 3D domain swapping in proteins. Structure (2004) 1.05
The SH2 domain-containing proteins in 21 species establish the provenance and scope of phosphotyrosine signaling in eukaryotes. Sci Signal (2011) 1.03
Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex. Biochemistry (2000) 1.02
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. Structure (1997) 1.00
The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction. FEBS Lett (2012) 0.97
Structural and energetic aspects of Grb2-SH2 domain-swapping. Arch Biochem Biophys (2007) 0.96
Solution structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase. J Mol Biol (1998) 0.93
Superbinder SH2 domains act as antagonists of cell signaling. Sci Signal (2012) 0.92
Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity. J Mol Biol (2002) 0.92
Solution studies of the SH2 domain from the fyn tyrosine kinase: secondary structure, backbone dynamics and protein association. Eur Biophys J (1996) 0.87
Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: implications for drug design. Proteins (2008) 0.87
Phosphotyrosine recognition domains: the typical, the atypical and the versatile. Cell Commun Signal (2012) 0.86
Self-association and backbone dynamics of the hck SH2 domain in the free and phosphopeptide-complexed forms. Biochemistry (1998) 0.86
Intertwined associations in structures of homooligomeric proteins. Structure (2013) 0.84
Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide. Acta Crystallogr Sect F Struct Biol Cryst Commun (2012) 0.79
Structure of the interleukin-2 tyrosine kinase Src homology 2 domain; comparison between X-ray and NMR-derived structures. Acta Crystallogr Sect F Struct Biol Cryst Commun (2012) 0.79
1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide. Biomol NMR Assign (2011) 0.76