KinoPlex, a computational framework that integrates predicted protein structures and kinase recognition motifs to assign phosphorylation potential and kinase specificity to all serine/threonine/tyrosine residues, is presented.
An integrated energetic and structural classification of the activation segment across the human and murine kinome is provided, complementing existing conformational catalogues and offering a quantitative comparative basis for understanding kinase activation mechanisms relevant to drug design.
A. Ahiri, A. Aboulmouhajir· The European Chemistry and B...· 0 citations
A pipeline reformulating kinase-substrate modeling as a Bayesian inference problem is presented and it is revealed that the interaction types and distances to the catalytic pocket significantly influence pathogenicity scores.
Jinyuan Hu, Shimian Li, Yue Xue et al.· Journal of Chemical Informat...· 0 citations
Mass-spectrometry-based phosphoproteomics now profiles phosphorylation at proteome scale, yet converting site-level measurements into coherent, kinase-centered biology — and into actionable drug discovery decisions — remains a persistent barrier to target nomination, mechanism-of-action confirmation, and resistance m...
Tomer M. Yaron-Barir, Jared L. Johnson, Lewis C. Cantley· Clinical Cancer Research· 0 citations
KinConfBench is introduced, a curated benchmark of 2225 high-quality human kinase chains to evaluate the ability of four state-of-the-art cofolding models—Boltz-2, Chai-1, Protenix, and RoseTTAFold-All-Atom—to recover both canonical and rare conformational states.
Kun-Yang Sun, T. Head-Gordon· npj Drug Discovery· 0 citations
The regulation of protein stability is essential for cellular homeostasis and is determined by a combination of intrinsic sequence motifs and extrinsic recognition enzymes. Despite growing knowledge of the protein degradation machinery, the ability to predict a protein’s stability from its amino acid sequence remains c...
Océane Marescal, Iain M. Cheeseman· bioRxiv· 0 citations
A structure-based method using SE(3)-transformers to learn residue compatibility with the local structural environment from experimentally resolved kinase 3D structures that captures biologically meaningful relationships between residue identity and 3D structural context is presented.
Shakiba Fadaei, F. Krebs, V. Zoete· Bioinformatics· 0 citations
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