Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Peter M, Snow"'
Publikováno v:
PLoS Biology, Vol 1, Iss 3, p E51 (2003)
Transferrin receptor 1 (TfR) plays a critical role in cellular iron import for most higher organisms. Cell surface TfR binds to circulating iron-loaded transferrin (Fe-Tf) and transports it to acidic endosomes, where low pH promotes iron to dissociat
Externí odkaz:
https://doaj.org/article/d478c513ce8e49d1967cc210ab48f9fd
Publikováno v:
Protein Science. 4:472-483
Fasciclin III is an integral membrane protein expressed on a subset of axons in the developing Drosophila nervous system. It consists of an intracellular domain, a transmembrane region, and an extracellular region composed of three domains, each pred
Autor:
Angeline Douvas, Minnie McMillan, Peter M. Snow, Bethany M DeBoer, William P. Cheevers, Katherine A. Louie, Hilary Weisbuch, Joseph M. Dadgari
Publikováno v:
Virology. 315(1):217-223
Lentiviruses display surprisingly disparate clinical manifestations in their specific hosts, share complex genetic structures, and exhibit extensive diversity, particularly in their envelope genes. The envelope protein, gp135, of caprine arthritis-en
Publikováno v:
The Journal of Immunology. 171:733-744
Autoantigen-based immunotherapy can modulate autoimmune diabetes, perhaps due to the activation of Ag-specific regulatory T cells. Studies of these regulatory T cells should help us understand their roles in diabetes and aid in designing a more effec
Publikováno v:
Journal of Biological Chemistry. 277:7889-7896
DNA polymerase epsilon (pol epsilon) is a multiple subunit complex consisting of at least four proteins, including catalytic Po12p, Dpb2p, Dpb3p, and Dpb4p. Pol epsilon has been shown to play essential roles in chromosomal DNA replication. Here, we r
Autor:
Anthony P. West, Melanie J. Bennett, Jasvinder S. Nangiana, Leslie P. Weiner, Pamela J. Bjorkman, Peter M. Snow, Andrew B. Herr, James R. Pierce, Anthony M. Giannetti
Publikováno v:
Journal of Molecular Biology. 313:385-397
The transferrin receptor (TfR) binds two proteins critical for iron metabolism: transferrin (Tf) and HFE, the protein mutated in hereditary hemochromatosis. Previous results demonstrated that Tf and HFE compete for binding to TfR, suggesting that Tf
Publikováno v:
Journal of Molecular Biology. 241:483-487
A truncated form of Drosophila fasciclin III has been engineered by site-directed mutagenesis. Secreted fasciclin III is expressed at 35 to 40 mg/l in insect cells with baculovirus carrying the recombinant gene. Single crystals of purified soluble fa
Autor:
Corey S. Goodman, Michael Hortsch, Zaida R. Traquina, E. J. Rehm, Allan J. Bieber, Gabriele Grenningloh, Nipam H. Patel, Peter M. Snow
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 55:327-340
Publikováno v:
PLoS Biology, Vol 1, Iss 3, p E51 (2003)
Transferrin receptor 1 (TfR) plays a critical role in cellular iron import for most higher organisms. Cell surface TfR binds to circulating iron-loaded transferrin (Fe-Tf) and transports it to acidic endosomes, where low pH promotes iron to dissociat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c20ea2f9b486133845960d82ebb3b09
https://resolver.caltech.edu/CaltechAUTHORS:GIApb03
https://resolver.caltech.edu/CaltechAUTHORS:GIApb03
Autor:
Katherine A, Louie, Joseph M, Dadgari, Bethany M, DeBoer, Hilary, Weisbuch, Peter M, Snow, William P, Cheevers, Angeline, Douvas, Minnie, McMillan
Publikováno v:
Virology. 315(1)
Lentiviruses display surprisingly disparate clinical manifestations in their specific hosts, share complex genetic structures, and exhibit extensive diversity, particularly in their envelope genes. The envelope protein, gp135, of caprine arthritis-en