Associated Papers
Accurate affinity models for SH2 domains from peptide binding assays and free-energy regression.
Gagoski D et al.
Protein Science : a Publication of the Protein Society, 2025
41088778 (PubMed )
Supplement: PRO-34-e70317-s008.xlsx › _S6_-_PTMVar_-_Lyn
Unraveling a novel missense mutation (c.A248C) in Wiskott-Aldrich syndrome gene by whole exome sequencing: Insights from dynamic simulation, molecular docking and in-silico studies.
Mohammad-Rezaei F et al.
International Immunopharmacology, 2025
Accurate sequence-to-affinity models for SH2 domains from multi-round peptide binding assays coupled with free-energy regression.
Gagoski D et al.
Biorxiv : the Preprint Server for Biology, 2025
39764007 (PubMed )
Supplement: media-1.xlsx › _S6_-_PTMVar_-_Lyn
Characterization of Wiskott-Aldrich syndrome (WAS) mutants using Saccharomyces cerevisiae.
Rajmohan R et al.
Fems Yeast Research, 2009
Two novel mutations identified in the Wiskott-Aldrich syndrome protein gene cause Wiskott-Aldrich syndrome and thrombocytopenia.
Andreu N et al.
International Journal of Molecular Medicine, 2007
Missense C168T in the Wiskott--Aldrich Syndrome protein gene is a common mutation in X-linked thrombocytopenia.
Ho LL et al.
British Journal of Haematology, 2001
Novel mutations in the Wiskott-Aldrich syndrome protein gene and their effects on transcriptional, translational, and clinical phenotypes.
Lemahieu V et al.
Human Mutation, 1999
Select a paper to view details