Zobrazeno 1 - 8
of 8
pro vyhledávání: '"James P. Mulrooney"'
Autor:
Jason J. Bisaillon, Legairre A. Radden II, Eric T. Szabo, Samantha R. Hughes, Aaron M. Feliciano, Alex V. Nesta, Belinda Petrovic, Kenneth M. Palanza, Dainius Lancinskas, Theodore A. Szmurlo, David C. Artus, Martin A. Kapper, James P. Mulrooney, Thomas R. King
Publikováno v:
Molecular Genetics and Metabolism Reports, Vol 1, Iss C, Pp 378-390 (2014)
Because of the similar phenotypes they generate and their proximate reported locations on Chromosome 7, we tested the recessive retarded hair growth (rhg) and frizzy (fr) mouse mutations for allelism, but found instead that these defects complement.
Externí odkaz:
https://doaj.org/article/9efcf5e7a54343e2a3afd8cd858106f1
Autor:
Belinda Petrovic, David C. Artus, Dainius Lancinskas, Samantha R. Hughes, Legairre A. Radden, Eric T. Szabo, Martin A. Kapper, Jason J. Bisaillon, James P. Mulrooney, Aaron M Feliciano, Alex V. Nesta, Kenneth M. Palanza, Theodore A. Szmurlo, Thomas R. King
Publikováno v:
Molecular Genetics and Metabolism Reports
Molecular Genetics and Metabolism Reports, Vol 1, Iss C, Pp 378-390 (2014)
Molecular Genetics and Metabolism Reports, Vol 1, Iss C, Pp 378-390 (2014)
Because of the similar phenotypes they generate and their proximate reported locations on Chromosome 7, we tested the recessive retarded hair growth (rhg) and frizzy (fr) mouse mutations for allelism, but found instead that these defects complement.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f334028ffb8f2ea62c01d6201ca5398
Publikováno v:
Cell Communication & Adhesion. 9:249-258
Tetraspanins modulate the function of a variety of membrane proteins, including integrin receptors. We show here that the tetraspanin CD9 preferentially coimmunoprecipitates with the alpha6beta1 integrin heterodimer in F9-derived parietal endoderm ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c7afaf510c82173e8ce771163ef4946
https://doi.org/10.1080/15419060216304
https://doi.org/10.1080/15419060216304
Publikováno v:
Experimental Cell Research. 258:332-341
As F9 stem cells differentiate into parietal endoderm they form focal adhesion sites. There is a concomitant decrease in the level of phosphorylation of S785 in the cytoplasmic domain of the beta1 integrin subunit. Previous transfection studies demon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66759568200944b1041746500d4a83cc
https://doi.org/10.1006/excr.2000.4964
https://doi.org/10.1006/excr.2000.4964
Publikováno v:
The FASEB Journal. 21
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b755f94c9acb12bde1a2a2ebad50e575
https://doi.org/10.1096/fasebj.21.6.a1429-b
https://doi.org/10.1096/fasebj.21.6.a1429-b
Publikováno v:
Cell communicationadhesion. 12(1-2)
The first cell migration event in the mouse embryo is the movement of parietal endoderm cells from the surface of the inner cell mass facing the blastocoel cavity to line the inner surface of the trophectoderm. F9 embryoid bodies provide an in vitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bcbab97b7f249ba8feb25d2ce8085c9
https://pubmed.ncbi.nlm.nih.gov/16371343
https://pubmed.ncbi.nlm.nih.gov/16371343
Publikováno v:
Cell communicationadhesion. 9(5-6)
Tetraspanins modulate the function of a variety of membrane proteins, including integrin receptors. We show here that the tetraspanin CD9 preferentially coimmunoprecipitates with the alpha6beta1 integrin heterodimer in F9-derived parietal endoderm ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::51582e6ad4b9cf1b90ba6e2e43369037
https://pubmed.ncbi.nlm.nih.gov/12745436
https://pubmed.ncbi.nlm.nih.gov/12745436
Publikováno v:
Journal of cell science. 114(Pt 13)
The integrin β1 cytoplasmic domain plays a key role in a variety of integrin-mediated events including adhesion, migration and signaling. A number of studies suggest that phosphorylation may modify the functional state of the cytoplasmic domain, but
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bba7535a8f0d6fba98fdda3d2f91a21
https://pubmed.ncbi.nlm.nih.gov/11559760
https://pubmed.ncbi.nlm.nih.gov/11559760