Zobrazeno 1 - 10
of 12
pro vyhledávání: '"J E Damen"'
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
https://doi.org/10.4049/jimmunol.157.6.2234
Publikováno v:
Blood. 82:2296-2303
Although the erythropoietin receptor (EpR) lacks a tyrosine kinase consensus sequence within its proline-rich intracellular domain, addition of its ligand to Ep-responsive cells stimulates the rapid and transient tyrosine phosphorylation of a number
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac48136e0a364c5e3a8c0e73647ccb16
https://doi.org/10.1182/blood.v82.8.2296.bloodjournal8282296
https://doi.org/10.1182/blood.v82.8.2296.bloodjournal8282296
The role of the SRC homology 2-containing inositol 5'-phosphatase in Fc epsilon R1-induced signaling
Autor:
M, Huber, C D, Helgason, J E, Damen, M P, Scheid, V, Duronio, V, Lam, R K, Humphries, G, Krystal
Publikováno v:
Current topics in microbiology and immunology. 244
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8965fb1502a393fdba5bc7dd9dd57e36
https://pubmed.ncbi.nlm.nih.gov/10453647
https://pubmed.ncbi.nlm.nih.gov/10453647
Publikováno v:
Blood. 92(4)
The SH2-containing inositol phosphatase, SHIP, often appears as multiple bands in anti-SHIP immunoblots. To characterize these bands, antisera were generated against the N-terminal (anti-N), mid-region (anti-M), and C-terminal (anti-C) portions of SH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c9da0cd4aa82e534f630eb43590729a1
https://pubmed.ncbi.nlm.nih.gov/9694708
https://pubmed.ncbi.nlm.nih.gov/9694708
The role of erythropoietin receptor tyrosine phosphorylation in erythropoietin-induced proliferation
Autor:
J E, Damen, L, Liu, H, Wakao, A, Miyajima, P, Rosten, A B, Jefferson, P W, Majerus, J, Krosl, R K, Humphries, G, Krystal
Publikováno v:
Leukemia. 11
Although studies with truncated erythropoietin receptors (EpoRs) have suggested the tyrosine phosphorylation (Yphos) of the EpoR may not play a significant role in Epo-induced proliferation, we found, using a full length EpoR mutant designed Null, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8ceae7e23d1066a5bfec73d2341f24bd
https://pubmed.ncbi.nlm.nih.gov/9209412
https://pubmed.ncbi.nlm.nih.gov/9209412
Autor:
J E, Damen, G, Krystal
Publikováno v:
Experimental hematology. 24(13)
The cloning of the erythropoietin receptor (EpoR) in 1989 has allowed very rapid progress in our understanding of the early intracellular events that may be triggered by erythropoietin (Epo) in erythroid progenitor cells. From studies carried out pri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b76faab00cd1d6fb67d8375b9e488788
https://pubmed.ncbi.nlm.nih.gov/8950227
https://pubmed.ncbi.nlm.nih.gov/8950227
Publikováno v:
Blood. 88(8)
We recently cloned and sequenced a cDNA encoding a 145-kD protein from the murine hematopoietic cell line B6SUtA, that becomes tyrosine phosphorylated and associated with Shc after cytokine stimulation. Based on its domains and enzymatic activity, we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5cef12fbed17d54f9f0550c500e92128
https://pubmed.ncbi.nlm.nih.gov/8874179
https://pubmed.ncbi.nlm.nih.gov/8874179
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 157(6)
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=pmid________::753baf21a5e80442d4b492c2e9df4d9a
https://pubmed.ncbi.nlm.nih.gov/8805618
https://pubmed.ncbi.nlm.nih.gov/8805618
Publikováno v:
Blood. 87(11)
Erythropoietin (Epo), the primary in vivo stimulator of erythroid proliferation and differentiation, acts, in part, by altering the tyrosine phosphorylation levels of various intracellular signaling molecules. These phosphorylation levels are tightly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fad1d50098486f7d28e730d533d77bb0
https://pubmed.ncbi.nlm.nih.gov/8639815
https://pubmed.ncbi.nlm.nih.gov/8639815
Publikováno v:
Blood. 85(1)
To compare the signal transduction pathways used by erythropoietin (Ep) and interleukin-3 (IL-3), the cDNA for the murine erythropoietin receptor (EpR) was introduced into the IL-3-responsive cell lines Ba/F3 and DA-3 using retrovirally mediated gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::55c24de2d0ad3b61463e136db41ca535
https://pubmed.ncbi.nlm.nih.gov/7803809
https://pubmed.ncbi.nlm.nih.gov/7803809