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Design of a Split Intein with Exceptional Protein Splicing ActivityStructural and dynamical features of inteins and implications on protein splicing.Naturally split inteins assemble through a "capture and collapse" mechanismModification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding.Streamlined expressed protein ligation using split inteins.Extein residues play an intimate role in the rate-limiting step of protein trans-splicing.Split Inteins: Nature's Protein Ligases.An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor.Inteins: Nature's Gift to Protein Chemists.A promiscuous split intein with expanded protein engineering applications.Deconstruction of the Ras switching cycle through saturation mutagenesis.Oligo(N-aryl glycines): a new twist on structured peptoids.Fine-tuning of substrate preferences of the Src-family kinase Lck revealed through a high-throughput specificity screen.The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinasesLck promotes Zap70-dependent LAT phosphorylation by bridging Zap70 to LATLearning from ancestorsPeptoid atropisomersDeep mutational analysis reveals functional trade-offs in the sequences of EGFR autophosphorylation sitesSlow phosphorylation of a tyrosine residue in LAT optimizes T cell ligand discriminationUnderstanding molecular mechanisms in cell signaling through natural and artificial sequence variationVariation in assembly stoichiometry in non-metazoan homologs of the hub domain of Ca2+ /calmodulin-dependent protein kinase II
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P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Neel H Shah
@ast
Neel H Shah
@en
Neel H Shah
@es
Neel H Shah
@nl
type
label
Neel H Shah
@ast
Neel H Shah
@en
Neel H Shah
@es
Neel H Shah
@nl
prefLabel
Neel H Shah
@ast
Neel H Shah
@en
Neel H Shah
@es
Neel H Shah
@nl
P106
P31
P496
0000-0002-1186-0626