PDF) SH2 Domains Recognize Contextual Peptide Sequence Information to Determine Selectivity
IJMS | Free Full-Text | SH2 Domains: Folding, Binding and Therapeutical Approaches
Studying Cellular Signal Transduction with OMIC Technologies. - Abstract - Europe PMC
PDF) Selectivity and promiscuity in the interaction network mediated by protein recognition modules | Luisa Castagnoli and Serena Paoluzi - Academia.edu
Hierarchical Organization Endows the Kinase Domain with Regulatory Plasticity
Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1. - Abstract - Europe PMC
Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response | Nature Reviews Molecular Cell Biology
Effective Disruption of Phosphoprotein−Protein Surface Interaction Using Zn(II) Dipicolylamine-Based Artificial Receptors via Two-Point Interaction | Journal of the American Chemical Society
STK38 promotes ATM activation by acting as a reader of histone H4 ufmylation | Science Advances
PDF) Targeting Protein Kinase Substrate Docking in Cancers | Achuth Padmanabhan - Academia.edu
Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response | Nature Reviews Molecular Cell Biology
IJMS | Free Full-Text | SH2 Domains: Folding, Binding and Therapeutical Approaches
PDF) Phosphotyrosine-Binding Domains in Signal Transduction
Approaches to Study Phosphatases | ACS Chemical Biology
A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes | Scientific Reports
Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response | Nature Reviews Molecular Cell Biology
Dissecting the role of protein phosphorylation: a chemical biology toolbox - Chemical Society Reviews (RSC Publishing) DOI:10.1039/D1CS00991E
Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck | PNAS
Kinase inhibition profiles as a tool to identify kinases for specific phosphorylation sites | Nature Communications
KINATEST-ID: A Pipeline To Develop Phosphorylation-Dependent Terbium Sensitizing Kinase Assays | Journal of the American Chemical Society
IJMS | Free Full-Text | SH2 Domains: Folding, Binding and Therapeutical Approaches
RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template | Chemical Reviews
