Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Sidne A. Omori"'
Autor:
Sidne A. Omori, Diego H. Castrillon, Robert C. Rickert, G. V. Baracho, Shane Bruckner, Ronald A. DePinho, Karen C. Arden, Hart S Dengler
Publikováno v:
Nature Immunology. 9:1388-1398
The transcription factors Foxo1, Foxo3 and Foxo4 modulate cell fate 'decisions' in diverse systems. Here we show that Foxo1-dependent gene expression was critical at many stages of B cell differentiation. Early deletion of Foxo1 caused a substantial
Autor:
Frank Weber, Sidne A. Omori, Alicia A. Bicknell, Leslie Friend, Ryan L. Brunsing, Maho Niwa, Robert C. Rickert
Publikováno v:
Journal of Biological Chemistry. 283:17954-17961
The unfolded protein response (UPR) signaling pathway regulates the functional capacity of the endoplasmic reticulum for protein folding. Beyond a role for UPR signaling during terminal differentiation of mature B cells to antibody-secreting plasma c
Autor:
Matthew H. Cato, Robert C. Rickert, Kathryn Calame, Miriam Shapiro-Shelef, Sidne A. Omori, Kamal D. Puri, Amy Anzelon-Mills
Publikováno v:
Immunity. 25(4):545-557
SummaryClass-switch recombination (CSR) is essential for humoral immunity. However, the regulation of CSR is not completely understood. Here we demonstrate that phosphatidylinositol 3-kinase (PI3K) actively suppressed the onset and frequency of CSR i
Autor:
Robert L. Fairchild, Xiaoxia Li, E. Charles Snow, Sidne A. Omori, Youcun Qian, Brian L. Kotzin, Carl F. Ware, Robert C. Rickert, Martin L. Scott, Grace Cui, Mayumi Naramura, Jinzhong Qin
Publikováno v:
Immunity. 21:575-587
TNF receptor (TNFR) superfamily members, CD40, and BAFFR play critical roles in B cell survival and differentiation. Genetic deficiency in a novel adaptor molecule, Act1, for CD40 and BAFF results in a dramatic increase in peripheral B cells, which c
Autor:
Michael J. Gilly, William A. May, Cindy S. Malone, Sidne A. Omori, William J. Wood, Christopher T. Denny, Erina K. Miyoshi, Jeff Gimble, Randolph Wall, Alexis A. Thompson, Melinda S. Gordon
Publikováno v:
Genomics. 32:352-357
The pp52 gene encodes an intracellular, F-actin-binding phosphoprotein (also designated LSP1 and WP34) postulated to function in cytoskeleton dynamics and cell motility. We previously reported that different mRNA isoforms are expressed from this gene
Autor:
Michael A. Damore, Michael J. Gilly, Alexis A. Thompson, William J. Wood, Randolph Wall, Sidne A. Omori
Publikováno v:
Blood. 87:666-673
The product of the B-cell-specific B29 gene (B29, Ig beta, CD79b) is essential for Ig-mediated B-cell activation via the B-cell antigen receptor complex (BCR) on human and murine B lymphocytes. To better understand the regulation of this pivotal gene
Autor:
Sidne A. Omori, Randolph Wall
Publikováno v:
Proceedings of the National Academy of Sciences. 90:11723-11727
The B-cell-specific B29 and mb1 genes code for covalently linked proteins (B29 or Ig beta and mb1 or Ig alpha, respectively) associated with membrane immunoglobulins in the antigen receptor complex on B cells. We have functionally analyzed the upstre
Publikováno v:
Current opinion in immunology. 23(2)
Phosphoinositide 3-kinase (PI3K) defines a family of lipid kinases that direct a wide range of cellular processes and cell fate decisions. Since its discovery, and that of its enzymatic antagonist PTEN, much of the focus on PI3K has been on its oncog
Publikováno v:
Molecular and cellular biology. 31(1)
The generation of robust T-cell-dependent humoral immune responses requires the formation and expansion of germinal center structures within the follicular regions of the secondary lymphoid tissues. B-cell proliferation in the germinal center drives
Autor:
David M. Mills, Amy Anzelon-Mills, Silvia Bolland, Dong-Mi Shin, Sidne A. Omori, Irene M. Pedersen, Ana V. Miletic, Herbert C. Morse, Robert C. Rickert, Jeffrey V. Ravetch
Publikováno v:
The Journal of experimental medicine, vol 207, iss 11
The Journal of Experimental Medicine
The Journal of Experimental Medicine
Mice lacking both PTEN and SHIP phosphatases develop spontaneous B cell lymphoma.
The inositol phosphatases phosphatase and tensin homologue (PTEN) and Src homology 2 domain–containing inositol phosphatase (SHIP) negatively regulate phosphatid
The inositol phosphatases phosphatase and tensin homologue (PTEN) and Src homology 2 domain–containing inositol phosphatase (SHIP) negatively regulate phosphatid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ce3aded6c50b6d1439586d737db9c26
https://escholarship.org/uc/item/0jg8p825
https://escholarship.org/uc/item/0jg8p825