Cutting Edge: FcγRII-B1 Regulates the Presentation of B Cell Receptor-Bound Antigens (original) (raw)

Receptor-Bound Antigens Regulates the Presentation of B Cell Cutting Edge: Fc{gamma}RII-B1

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Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif

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Cutting Edge: FcgRII-B1 Regulates the Presentation of B Cell Receptor-Bound Antigens 1

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SHP1 upon Tyrosine Phosphorylation CD72 Recruits the Tyrosine Phosphatase Cutting Edge: The B Cell Surface Protein

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The SH2 domain containing inositol 5-phosphatase SHIP2 associates to the immunoreceptor tyrosine-based inhibition motif of FcγRIIB in B cells under negative signaling

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Fcγ receptor type IIb induced recruitment of inositol and protein phosphatases to the signal transductory complex of human B-cell

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Fcγ receptor induced recruitment of inositol and protein phosphatases to the signal transductory complex of human B cell

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Interference with Immunoglobulin (Ig) Immunoreceptor Tyrosine-Based Activation Motif (Itam) Phosphorylation Modulates or Blocks B Cell Development, Depending on the Availability of an Ig Cytoplasmic Tail

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p120 Is a Major Substrate of Tyrosine Phosphorylation upon B Cell Antigen Receptor Stimulation and Interacts in Vivo with Fyn and Syk Tyrosine Kinases, Grb2 and Shc Adaptors, and the p85 Subunit of Phosphatidylinositol 3-Kinase

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The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited to the intracytoplasmic domain of human FcγRIIB and is mandatory for negative regulation of B cell activation

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