Associated Papers
Identification of pathogenic missense mutations using protein stability predictors.
Gerasimavicius L et al.
Scientific Reports, 2020
32958805 (PubMed )
Supplement: 41598_2020_72404_MOESM2_ESM.xlsx › ClinVar
Lipid and Protein Co-Regulation of PI3K Effectors Akt and Itk in Lymphocytes.
Wang X et al.
Frontiers in Immunology, 2015
Unimpaired activation of c-Jun NH2-terminal kinase (JNK) 1 upon CD40 stimulation in B cells of patients with X-linked agammaglobulinemia.
Brunner C et al.
Journal of Clinical Immunology, 2002
Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate.
Baraldi E et al.
Structure (london, England : 1993), 1999
Molecular and structural characterization of five novel mutations in the Bruton's tyrosine kinase gene from patients with X-linked agammaglobulinemia.
Saha BK et al.
Molecular Medicine (cambridge, Mass.), 1997
Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia.
Hyvönen M et al.
The Embo Journal, 1997
Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity.
Fukuda M et al.
The Journal of Biological Chemistry, 1996
Mutation analysis in Bruton's tyrosine kinase, the X-linked agammaglobulinaemia gene, including identification of an insertional hotspot.
Gaspar HB et al.
Human Molecular Genetics, 1995
Structural basis for pleckstrin homology domain mutations in X-linked agammaglobulinemia.
Vihinen M et al.
Biochemistry, 1995
Unique mutations of Bruton's tyrosine kinase in fourteen unrelated X-linked agammaglobulinemia families.
Zhu Q et al.
Human Molecular Genetics, 1994
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