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pro vyhledávání: '"Richard S. Mitchell"'
Autor:
Richard S. Mitchell
Publikováno v:
A Flora of the White Mountains, California and Nevada ISBN: 9780520340305
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::51eb5a0fc4138befdb4abb431f531992
https://doi.org/10.2307/jj.2430514.7
https://doi.org/10.2307/jj.2430514.7
Autor:
Robert M. Lloyd, Richard S. Mitchell
This title is part of UC Press's Voices Revived program, which commemorates University of California Press's mission to seek out and cultivate the brightest minds and give them voice, reach, and impact. Drawing on a backlist dating to 1893, Voices Re
Autor:
Richard S Mitchell, Chris Katsura, Mark A Skasko, Katie Fitzpatrick, David Lau, Autumn Ruiz, Edward B Stephens, Florence Margottin-Goguet, Richard Benarous, John C Guatelli
Publikováno v:
PLoS Pathogens, Vol 5, Iss 5, p e1000450 (2009)
The interferon-induced transmembrane protein BST-2/CD317 (tetherin) restricts the release of diverse enveloped viruses from infected cells. The HIV-1 accessory protein Vpu antagonizes this restriction by an unknown mechanism that likely involves the
Externí odkaz:
https://doaj.org/article/9f2e60a5427f440ca85621752c99e315
Publikováno v:
Molecular Therapy. 8:674-687
We have examined the changes in cellular transcription resulting from infection with HIV-based vectors. Previous work suggested that the incoming viral genome may under some circumstances be detected as DNA damage, so to explore this possibility, we
Autor:
David G. Myszka, Joan K. Stuart, Zhihua Xie, Shawn M. McDonald, Lisa Joss, Richard S. Mitchell, Kathryn R. Ely, John C. Reed, Shinichi Takayama
Publikováno v:
Journal of Biological Chemistry. 273:22506-22514
The anti-cell death protein BAG-1 binds to 70-kDa heat shock proteins (Hsp70/Hsc70) and modulates their chaperone activity. Among other facilitory roles, BAG-1 may serve as a nucleotide exchange factor for Hsp70/Hsc70 family proteins and thus represe
Autor:
Richard S. Mitchell, Chao-Zhou Ni, John Wickersham, David S. Peabody, Kathryn R. Ely, Carol A. White, Ramadurgam Kodandapani
Publikováno v:
Protein Science. 5:2485-2493
There are four groups of RNA bacteriophages with distinct antigenic and physicochemical properties due to differences in surface residues of the viral coat proteins. Coat proteins also play a role as translational repressor during the viral life cycl
Autor:
Chao-Zhou Ni, Scott R. McKercher, John B. Knight, Michael J. Klemsz, Angela Lombardo, Richard S. Mitchell, Frederic Pio, Kathryn R. Ely, Richard A. Maki
Publikováno v:
Journal of Biological Chemistry. 270:24258-24263
The PU.1 transcription factor is a member of the ets gene family of regulatory proteins. These molecules play a role in normal development and also have been implicated in malignant processes such as the development of erythroid leukemia. The Ets pro
Autor:
John C. Guatelli, Autumn Ruiz, Richard S. Mitchell, David Lau, Kimberly Schmitt, Edward B. Stephens, M. Sarah Hill
Publikováno v:
Virology. 406(2)
Pathogenic simian–human immunodeficiency viruses (SHIV) contain HIV-1 Vpu and SIV Nef, both shown to counteract BST-2 (HM1.24; CD317; tetherin) inhibition of virus release in a species-specific manner. We show that human and pig-tailed BST-2 (ptBST
Autor:
Richard S. Mitchell, Richard Benarous, Edward B. Stephens, Katie L Fitzpatrick, Chris Katsura, John C. Guatelli, Autumn Ruiz, Mark Skasko, David Lau, Florence Margottin-Goguet
Publikováno v:
PLoS Pathogens
PLoS Pathogens, Vol 5, Iss 5, p e1000450 (2009)
PLoS Pathogens, Vol 5, Iss 5, p e1000450 (2009)
The interferon-induced transmembrane protein BST-2/CD317 (tetherin) restricts the release of diverse enveloped viruses from infected cells. The HIV-1 accessory protein Vpu antagonizes this restriction by an unknown mechanism that likely involves the
Autor:
Richard S. Mitchell, Juan S. Bonifacino, Rudy Murillo, John C. Guatelli, David Lau, O. Wolf Lindwasser, Rittik Chaudhuri, Kristie A. Tanaka
The human immunodeficiency virus type 1 (HIV-1) Nef protein upregulates the expression of the invariant chain (Ii)/major histocompatibility complex class II (MHC-II) complex at the cell surface. This complex appears to reach the antigen-loading endos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b59e0049f00a99f3bc5c0edbbb3c25c2
https://europepmc.org/articles/PMC2519569/
https://europepmc.org/articles/PMC2519569/