Zobrazeno 1 - 10
of 26
pro vyhledávání: '"H. Kabra"'
Autor:
S. Saha, Nathan Bachtell, T. Skurnac, John E. Paderi, Andrew J. Woolley, Alyssa Panitch, J. Chen, H. Kabra, Kate Stuart
Publikováno v:
European Heart Journal. 38
Akademický článek
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Autor:
Morten A. Karsdal, H. Kabra, T. Skurnac, K. Stuart, S. Jalgaonkar, Nathan Bachtell, N. Snead, Diana Julie Leeming, J. Paderi, Andrew J. Woolley
Publikováno v:
Journal of Hepatology. 68:S91
Autor:
H. Kabra, J. Chen, A. Chan, M.G. Chambers, John E. Paderi, S. Saha, K. Egodoge, Kate Stuart, Morten A. Karsdal, C. Lin, J.L. Oskins
Publikováno v:
Osteoarthritis and Cartilage. 25:S415
Publikováno v:
The Journal of Immunology. 163:1888-1893
The Dad1 protein has been shown to play a role in prevention of apoptosis in certain cell types. Dad1 is also a subunit of the oligosaccharyltransferase enzyme complex that initiates N-linked glycosylation. It is encoded by a gene located adjacent to
Publikováno v:
The Journal of Immunology. 162:2766-2774
The Fas receptor delivers signals crucial for lymphocyte apoptosis through its cytoplasmic death domain. Several Fas cytoplasmic-associated proteins have been reported and studied in cell lines. So far, only Fas-associated death domain protein (FADD)
Autor:
Gretchen E. Diehl, A. Deyoung, H.G. Kasler, S.J. Sohn, Jianke Zhang, Nisha H. Kabra, Astar Winoto, Christopher Bishop, A.A. Kuang
Publikováno v:
Scopus-Elsevier
Publikováno v:
The Journal of Immunology. 155:811-817
The lymphocyte cell-surface Ag CD38 catabolizes NAD to adenosine 5' diphosphoribose (ADPR) and cyclic ADPR (cADPR). We show here that the soluble extracellular domain of CD38 (sCD38) mediates ADP ribosylation of several proteins. This was demonstrate
Publikováno v:
The Journal of biological chemistry. 276(32)
FADD is an adapter protein that was originally isolated as a transducer of apoptotic signals for death domain-containing receptors. However, FADD-deficient mice are embryonic lethal and FADD(-/-) T cells developed from FADD(-/-) embryonic stem cells
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 98(11)
FADD/Mort1, initially identified as a Fas-associated death-domain containing protein, functions as an adapter molecule in apoptosis initiated by Fas, tumor necrosis factor receptor-I, DR3, and TRAIL-receptors. However, FADD likely participates in add