Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Carol A. Vater"'
Publikováno v:
Molecular Biology of the Cell. 3:1389-1402
The collection of vacuolar protein sorting mutants (vps mutants) in Saccharomyces cerevisiae comprises of 41 complementation groups. The vacuoles in these mutant strains were examined using immunofluorescence microscopy. Most of the vps mutants were
Publikováno v:
The Journal of Cell Biology
The product of the VPS1 gene, Vps1p, is required for the sorting of soluble vacuolar proteins in the yeast Saccharomyces cerevisiae. We demonstrate here that Vps1p, which contains a consensus tripartite motif for guanine nucleotide binding, is capabl
Autor:
Carol A. Vater, Victor S. Goldmacher
Publikováno v:
Macromolecular Anticancer Therapeutics ISBN: 9781441905062
The original rationale underlying the development of antibody–cytotoxic compound conjugates (ACC) was to improve the selectivity of cytotoxic anti-cancer drugs by targeting them to tumors with the help of antibodies. The ACC concept has since matur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::17b905fbe14618af77c76d6db84453ef
https://doi.org/10.1007/978-1-4419-0507-9_9
https://doi.org/10.1007/978-1-4419-0507-9_9
Publikováno v:
Ciba Foundation Symposium 176-The GTPase Superfamily
VPS1 encodes a 79 kDa protein required for the proper sorting of soluble vacuolar proteins in Saccharomyces cerevisiae. The N-terminal half of Vps1p, which contains a consensus GTP-binding motif, shares extensive homology with a growing family of hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1623dca2d5c81ca52fd08b539b257350
https://doi.org/10.1002/9780470514450.ch13
https://doi.org/10.1002/9780470514450.ch13
Autor:
Carol A. Vater, Anna Skaletskaya, Laura M. Bartle, Cheryl A. Dionne, Edward S. Mocarski, Robert J. Lutz, Shinya Watanabe, Elliott Kieff, Victor S. Goldmacher, Thomas Chittenden, Jia-wen Han, Nancy Kedersha, Ellen Cahir McFarland
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 96(22)
Human cytomegalovirus (CMV), a herpesvirus that causes congenital disease and opportunistic infections in immunocompromised individuals, encodes functions that facilitate efficient viral propagation by altering host cell behavior. Here we show that C
Publikováno v:
The Journal of biological chemistry. 273(28)
The BCL-2 proto-oncogene contains unusually long untranslated 5' and 3' sequences. Deletion of the sequences flanking the BCL-2 open reading frame dramatically increases the level of protein expression. Transient high level BCL-2 protein expression m
Publikováno v:
The Journal of biological chemistry. 270(21)
Indirect immunofluorescence studies revealed that when fixed, permeabilized cultured human cells were incubated with ricin A chain, the toxin molecule localized in a staining pattern indicative of binding to the endoplasmic reticulum and to nucleoli.
Publikováno v:
Analytical biochemistry. 224(1)
A procedure has been developed for measuring antibody binding to cell surface antigens using an immobilized plasma membrane fraction. In this method, isolated plasma membranes are dried onto wells of a 96-well microtiter plate and incubated with anti
Autor:
Christopher J. Roberts, Carol A. Vater, Steven E Nothwehr, Tom H. Stevens, Christopher K. Raymond
Soluble proteins and integral membrane proteins of the yeast vacuole appear to be delivered to the organelle by distinctly different mechanisms. Unsorted soluble proteins that enter the secretory pathway are secreted from the cell in Saccharomyces ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4560de833f1b288a9411da64942c8aac
https://doi.org/10.1016/s0167-7306(08)60091-5
https://doi.org/10.1016/s0167-7306(08)60091-5