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Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions

Autor: S Tridandapani, G W Chacko, J R Van Brocklyn, K M Coggeshall

Publikováno v: The Journal of Immunology. 158:1125-1132

To elucidate the molecular basis for inhibition of B cell proliferation and differentiation by the Fc receptor for IgG (Fc(gamma)RII), we compared the signaling events in B cells stimulated by cross-linking surface Ig alone (positive signaling), or b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::187bbdcf0db4aface1c3ef89da52e094
https://doi.org/10.4049/jimmunol.158.3.1125

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Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP

Autor: G W Chacko, S Tridandapani, J E Damen, L Liu, G Krystal, K M Coggeshall

Publikováno v: The Journal of Immunology. 157:2234-2238

Stimulation of the B cell Ag receptor (BCR) has been reported to induce tyrosine phosphorylation of a 145-kDa protein and its association with the adapter protein Shc. We have identified this protein as the novel inositol polyphosphate 5-phosphatase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::18225c202c56dc351fa6a67b196d1aae
https://doi.org/10.4049/jimmunol.157.6.2234

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Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions

Autor: S, Tridandapani, G W, Chacko, J R, Van Brocklyn, K M, Coggeshall

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 158(3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::25de74c3ed4106ae75805a81cb27ce5a
https://pubmed.ncbi.nlm.nih.gov/9013951

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Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP

Autor: G W, Chacko, S, Tridandapani, J E, Damen, L, Liu, G, Krystal, K M, Coggeshall

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 157(6)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::753baf21a5e80442d4b492c2e9df4d9a
https://pubmed.ncbi.nlm.nih.gov/8805618

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Phosphoinositide 3-kinase and p72syk noncovalently associate with the low affinity Fc gamma receptor on human platelets through an immunoreceptor tyrosine-based activation motif. Reconstitution with synthetic phosphopeptides

Autor: G W, Chacko, J T, Brandt, K M, Coggeshall, C L, Anderson

Publikováno v: The Journal of biological chemistry. 271(18)

Previously, we have demonstrated that the cytoplasmic tyrosine kinase p72syk is coupled to the platelet Fc receptor for IgG (Fc gamma RIIA) (Chacko, G. W., Duchemin, A. M., Coggeshall, K. M., Osborne, J. M., Brandt, J. T., and Anderson, C. L. (1994)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f6708ff5d54220e109c4f7f2c028a4aa
https://pubmed.ncbi.nlm.nih.gov/8631888

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Clustering of the platelet Fc gamma receptor induces noncovalent association with the tyrosine kinase p72syk

Autor: G W, Chacko, A M, Duchemin, K M, Coggeshall, J M, Osborne, J T, Brandt, C L, Anderson

Publikováno v: The Journal of biological chemistry. 269(51)

The Fc receptor for IgG in platelets was identified as the integral membrane isoform encoded by the Fc gamma RIIA gene. Functional analysis of this molecule determined that activated Fc gamma RIIA is tyrosine phosphorylated and that activation induce

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5dfaaf0241da409baee64242478acbd4
https://pubmed.ncbi.nlm.nih.gov/7798242

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