Zobrazeno 1 - 10
of 97
pro vyhledávání: '"Norman J. Oppenheimer"'
Autor:
Pascal F Egea, Hélène Muller-Steffner, Isabelle Kuhn, Céline Cakir-Kiefer, Norman J Oppenheimer, Robert M Stroud, Esther Kellenberger, Francis Schuber
Publikováno v:
PLoS ONE, Vol 7, Iss 4, p e34918 (2012)
Bovine CD38/NAD(+)glycohydrolase (bCD38) catalyses the hydrolysis of NAD(+) into nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose (cADPR). We solved the crystal structures of the mono N-glycosylated forms of the ecto-domain of bCD38
Externí odkaz:
https://doaj.org/article/c292c8f9ebde4e57b19de2aa4ca4f8f3
Publikováno v:
DNA Repair. 23:95-100
A new, acyclic NAD-analog, acycloNAD + has been synthesized where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety. The chemical properties of this analog are comparable to those of β-NAD + with a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79e4687265db677053a2920b4cbdc546
https://doi.org/10.1016/j.dnarep.2014.09.005
https://doi.org/10.1016/j.dnarep.2014.09.005
Autor:
Irina A. Kriksunov, Hong Jiang, Richard M. Graeff, Hon Cheung Lee, Hening Lin, Norman J. Oppenheimer, Quan Hao, Bo Zhang, Barry V. L. Potter, Qun Liu
Publikováno v:
The Journal of Biological Chemistry
Cyclic ADP-ribose (cADPR) is a universal calcium messenger molecule that regulatesmanyphysiological processes.Theproduction and degradation of cADPR are catalyzed by a family of related enzymes, including the ADP-ribosyl cyclase from Aplysia californ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e74408a379ef274ec8cd40fcb2a9942c
https://doi.org/10.1074/jbc.m109.031005
https://doi.org/10.1074/jbc.m109.031005
Autor:
Santiago Partida-Sanchez, Francis Schuber, Leopoldo Santos-Argumedo, Miguel E. Moreno-García, Héctor Romero-Ramírez, Hélène Muller-Steffner, Melissa Makris, Frances E. Lund, Norman J. Oppenheimer
Publikováno v:
International Immunology. 18:1029-1042
Cross-linking of CD38 on hematopoietic cells induces activation, proliferation and differentiation of mature T and B cells and mediates apoptosis of myeloid and lymphoid progenitor cells. In addition to acting as a signaling receptor, CD38 is also an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88519f53d256f92813c6b2347026c989
https://doi.org/10.1093/intimm/dxl037
https://doi.org/10.1093/intimm/dxl037
Publikováno v:
Biochemical Journal. 382:849-856
Ca(2+) ions play a critical role in the biochemical cascade of signal transduction pathways, leading to the activation of immune cells. In the present study, we show that the exposure of freshly isolated human monocytes to NAD(+) results in a rapid c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8b50630dd223f7415f23ab5dfb4880c
https://doi.org/10.1042/bj20040979
https://doi.org/10.1042/bj20040979
Autor:
Hélène Muller-Steffner, Frances E. Lund, Leopoldo Santos-Argumedo, Norman J. Oppenheimer, Santiago Partida-Sanchez, Francis Schuber, Adriana Sumoza-Toledo, Julie Primack, Miguel E. Moreno-García
Publikováno v:
European Journal of Biochemistry. 271:1025-1034
CD38 is a transmembrane glycoprotein that functions as an ectoenzyme and as a receptor. Based on the structural similarity between CD38 and ADP-ribosyl cyclase from Aplysia californica, it was hypothesized that CD38 is expressed as a homodimer on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a139ee84445e60b3d73e58d29a4b4c4c
https://doi.org/10.1111/j.1432-1033.2004.04006.x
https://doi.org/10.1111/j.1432-1033.2004.04006.x
Autor:
Ji-Liang Gao, Norman J. Oppenheimer, Philip M. Murphy, Pablo Iribarren, Frances E. Lund, Ji Ming Wang, Santiago Partida-Sanchez, Miguel E. Moreno-García
Publikováno v:
The Journal of Immunology. 172:1896-1906
Cyclic ADP ribose (cADPR) is a calcium-mobilizing metabolite that regulates intracellular calcium release and extracellular calcium influx. Although the role of cADPR in modulating calcium mobilization has been extensively examined, its potential rol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a5de092d601c1d6ec6d6421e888ce8f
https://doi.org/10.4049/jimmunol.172.3.1896
https://doi.org/10.4049/jimmunol.172.3.1896
Publikováno v:
Journal of Biological Chemistry. 278:50985-50998
Silent information regulator 2 (Sir2) enzymes catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, producing nicotinamide and the novel meta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78fe12b72a261328fae32f4c3647c9a1
https://doi.org/10.1074/jbc.m306552200
https://doi.org/10.1074/jbc.m306552200
Autor:
Jean-Jacques Lacapère, Geneviève Boulla, Norman J. Oppenheimer, Francis Schuber, Frances E. Lund, Philippe Deterre, Julie Primack
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1652:17-26
The lymphoid surface antigen CD38 is a NAD + -glycohydrolase that also catalyzes the transformation of NAD + into cyclic ADP-ribose, a calcium mobilizing second messenger. In addition, ligation of CD38 by antibodies triggers signaling in lymphoid cel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11b3e1197844dd397a63e9de54277f28
https://doi.org/10.1016/j.bbapap.2003.07.002
https://doi.org/10.1016/j.bbapap.2003.07.002
Autor:
Norman J. Oppenheimer, Francis Schuber, Satoshi Shuto, Barry V. L. Potter, Masayoshi Fukuoka, Victoria C. Bailey, Céline Cakir-Kiefer, Andreas H. Guse, Georg W. Mayr, Akira Matsuda, Karin Weber
Publikováno v:
Biochemistry. 41:6744-6751
Three novel analogues modified in the "northern" ribose (ribose linked to N1 of adenine) of the Ca(2+) mobilizing second messenger cyclic adenosine diphosphoribose, termed 2"-NH(2)-cyclic adenosine diphosphoribose, cyclic adenosine diphospho-carbocyc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3583d9d74e2945e95c5cdd29f5d0a0ff
https://doi.org/10.1021/bi020171b
https://doi.org/10.1021/bi020171b