Zobrazeno 1 - 10
of 18
pro vyhledávání: '"J C Grimaldi"'
Autor:
A.D. Goddard, Xing Xian Yu, P Dowd, S L Schilbach, David A. Lewin, J C Grimaldi, Clarissa J. Chui, James Lee, S Colman, Sean H. Adams
Publikováno v:
Biochemical Journal. 360:135-142
We hypothesized that certain proteins encoded by temperature-responsive genes in brown adipose tissue (BAT) contribute to the remarkable metabolic shifts observed in this tissue, thus prompting a differential mRNA expression analysis to identify cand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5ca29f0b5ff47f26ea8fe5c4fa77624
https://doi.org/10.1042/bj3600135
https://doi.org/10.1042/bj3600135
Autor:
J C Grimaldi, Hélène Muller-Steffner, Francis Schuber, Debra A. Cockayne, Frances E. Lund, Tony Muchamuel, Troy D. Randall, Maureen Howard, Robin M. Murray
Publikováno v:
Blood. 92:1324-1333
CD38 is a membrane-associated ecto-nicotinamide adenine dinucleotide (NAD+) glycohydrolase that is expressed on multiple hematopoietic cells. The extracellular domain of CD38 can mediate the catalysis of NAD+ to cyclic adenosine diphosphoribose (cADP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bc51d11063077620465ff1b9760d096
https://doi.org/10.1182/blood.v92.4.1324
https://doi.org/10.1182/blood.v92.4.1324
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a316413bd743b0bf580401f24d63a987
https://doi.org/10.4049/jimmunol.155.2.811
https://doi.org/10.4049/jimmunol.155.2.811
Autor:
Leopoldo Santos-Argumedo, Solvason N, Maureen Howard, Wu Ww, R. M. E. Parkhouse, A W Heath, J C Grimaldi, Frances E. Lund
Publikováno v:
International Immunology. 7:163-170
CD38 is a 42 kDa membrane-associated ectoenzyme expressed by a large proportion of human and mouse lymphocytes. Agonistic antibodies to CD38 induce a strong proliferative response in lymphocytes additionally co-stimulated with other growth co-factors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f9164dd764032f07e1798fa64739fd7
https://doi.org/10.1093/intimm/7.2.163
https://doi.org/10.1093/intimm/7.2.163
Autor:
N Harada, L Santos-Argumedo, R Chang, J C Grimaldi, F E Lund, C I Brannan, N G Copeland, N A Jenkins, A W Heath, R M Parkhouse
Publikováno v:
The Journal of Immunology. 151:3111-3118
A rat mAb (NIM-R5) has recently been prepared against a novel murine B cell activation marker. We report here isolation of a cDNA (1-19) encoding the B cell-derived protein recognized by NIM-R5 antibody. This cDNA contains an open reading frame that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c3b53ca10c3997e922a917ba825b615
https://doi.org/10.4049/jimmunol.151.6.3111
https://doi.org/10.4049/jimmunol.151.6.3111
Autor:
Xiaoyan Wu, N.-X. Yu, J C Grimaldi, Nancy Ann Hosken, Douglas S. Robinson, R L Coffman, Anne O'Garra, B. W. P. Seymour, G. Grunig, Walter Ferlin, Maureen Howard, Françoise Cottrez, H. Soto
Publikováno v:
Scopus-Elsevier
We have generated rat monoclonal antibodies specific for the mouse eotaxin receptor, C-C chemokine receptor 3 (CCR3). Several anti-CCR3 mAbs proved to be useful for in vivo depletion of CCR3-expressing cells and immunofluorescent staining. In vivo CC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aed9cd05376bba31ca6ebeb2028b01f3
https://pubmed.ncbi.nlm.nih.gov/10380909
https://pubmed.ncbi.nlm.nih.gov/10380909
Autor:
D A, Cockayne, T, Muchamuel, J C, Grimaldi, H, Muller-Steffner, T D, Randall, F E, Lund, R, Murray, F, Schuber, M C, Howard
Publikováno v:
Blood. 92(4)
CD38 is a membrane-associated ecto-nicotinamide adenine dinucleotide (NAD+) glycohydrolase that is expressed on multiple hematopoietic cells. The extracellular domain of CD38 can mediate the catalysis of NAD+ to cyclic adenosine diphosphoribose (cADP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3d38ad91d9b242bc792fd4399edeec45
https://pubmed.ncbi.nlm.nih.gov/9694721
https://pubmed.ncbi.nlm.nih.gov/9694721
Autor:
J C, Grimaldi, S, Balasubramanian, N H, Kabra, A, Shanafelt, J F, Bazan, G, Zurawski, M C, Howard
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 155(2)
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::51f1f6837573f41282d8cea05a3bbc6a
https://pubmed.ncbi.nlm.nih.gov/7608558
https://pubmed.ncbi.nlm.nih.gov/7608558
Autor:
N, Harada, L, Santos-Argumedo, R, Chang, J C, Grimaldi, F E, Lund, C I, Brannan, N G, Copeland, N A, Jenkins, A W, Heath, R M, Parkhouse
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 151(6)
A rat mAb (NIM-R5) has recently been prepared against a novel murine B cell activation marker. We report here isolation of a cDNA (1-19) encoding the B cell-derived protein recognized by NIM-R5 antibody. This cDNA contains an open reading frame that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::25dab6149016d4a7296ca3c1a3824643
https://pubmed.ncbi.nlm.nih.gov/8376770
https://pubmed.ncbi.nlm.nih.gov/8376770
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 149(12)
The B cell-associated surface molecule, CD40, is likely to play a central role in the expansion of Ag-stimulated B cells, and their interaction with activated Th cells. In our study we have isolated genomic clones of murine CD40 from a mouse liver ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e55e8525b971abf3935a13c7e3a346ed
https://pubmed.ncbi.nlm.nih.gov/1281194
https://pubmed.ncbi.nlm.nih.gov/1281194