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Splicing Regulator SC35 Is Essential for Genomic Stability and Cell Proliferation during Mammalian Organogenesis

Autor: Xue Li, Shengrong Lin, Ye Sun, Ran Xiao, D W Rose, Jian-Hua Ding, Michael G. Rosenfeld, Xiang-Dong Fu

Publikováno v: Molecular and Cellular Biology. 27:5393-5402

The members of the SR family of splicing regulators were initially characterized for their critical roles in constitutive and regulated splicing. They are implicated in different aspects of gene expression processes, including transcription, RNA stab

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c31c8505be08a447f389ff13a73f1fc8
https://doi.org/10.1128/mcb.00288-07

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REST Repression of Neuronal Genes Requires Components of the hSWI·SNF Complex

Autor: Gail Mandel, Josh G. Chenoweth, D W Rose, Michael G. Rosenfeld, Mary E. Anderson, Elena Battaglioli, María Estela Andrés

Publikováno v: Journal of Biological Chemistry. 277:41038-41045

A function of the transcription factor REST is to block the expression of neuronal phenotypic traits in non-neuronal cells. Previous studies have shown that REST-mediated repression requires histone deacetylase activity and that recruitment of deacet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff27a8f5a864c7e54698399947d74365
https://doi.org/10.1074/jbc.m205691200

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Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators

Autor: D W Rose, Stefan Westin, Wisely Gb, Michael V. Milburn, Eileen M. McInerney, Michael G. Rosenfeld, Robert T. Nolte, Riki Kurokawa, Christopher K. Glass

Publikováno v: Nature. 395:199-202

Retinoic-acid receptor-α (RAR-α) and peroxisome proliferator-activated receptor-γ (PPAR-γ) are members of the nuclear-receptor superfamily that bind to DNA as heterodimers with retinoid-X receptors (RXRs)1,2. PPAR–RXR heterodimers can be activa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aac904443bbbaf7a54168f8339d8eab
https://doi.org/10.1038/26040

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Microinjection of the SH2 domain of the 85-kilodalton subunit of phosphatidylinositol 3-kinase inhibits insulin-induced DNA synthesis and c-fos expression

Autor: Jerrold M. Olefsky, D W Rose, Alan R. Saltiel, Lewis C. Cantley, Lucia E. Rameh, Byung Hak Jhun, B L Seely

Publikováno v: Molecular and Cellular Biology. 14:7466-7475

We have investigated the functional role of the SH2 domain of the 85-kDa subunit (p85) of the phosphatidylinositol 3-kinase in the insulin signal transduction pathway. Microinjection of a bacterial fusion protein containing the N-terminal SH2 domain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f502ae6a2873b837b453f4902cb6c21d
https://doi.org/10.1128/mcb.14.11.7466

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Syp (SH-PTP2) is a positive mediator of growth factor-stimulated mitogenic signal transduction

Autor: Hiroshi Maegawa, D W Rose, Steven E. Shoelson, T Sasaoka, P. P. Roller, Jerrold M. Olefsky, Terrence R. Burke, Sen Xiao

Publikováno v: Scopus-Elsevier

Syp (SH-PTP2) was recently identified as a phosphotyrosine phosphatase containing two SH2 domains within its primary structure. In response to appropriate growth factor stimulation, Syp becomes phosphorylated on tyrosine residues and associates with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5edac2b8081d8e833167b5a389ba7d7d
https://doi.org/10.1016/s0021-9258(17)31955-5

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Deoxyadenosine analogs induce programmed cell death in chronic lymphocytic leukemia cells by damaging the DNA and by directly affecting the mitochondria

Autor: D, Genini, S, Adachi, Q, Chao, D W, Rose, C J, Carrera, H B, Cottam, D A, Carson, L M, Leoni

Publikováno v: Blood. 96(10)

Adenine deoxynucleosides induce apoptosis in quiescent lymphocytes and are thus useful drugs for the treatment of indolent lymphoproliferative diseases. To explain why deoxyadenosine and its analogs are toxic to a cell that is not undergoing replicat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::59d773cab6d0cde8bb23d4c99dc3d721
https://pubmed.ncbi.nlm.nih.gov/11071652

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The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells

Autor: Y. Le Marchand-Brustel, Tetsuro Haruta, Stuart S. Martin, Mireille Cormont, Aaron J. Morris, Peter Vollenweider, D W Rose, James G. Nelson, Jerrold M. Olefsky

Publikováno v: Endocrinology. 138(11)

Insulin's stimulation of glucose transport involves the translocation of vesicles containing the glucose transporter GLUT4 to the plasma membrane. Small GTP-binding proteins have been implicated in the regulation of vesicular traffic. We studied the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebd24d998b39de3fb1a3e855c0e8afaa
https://pubmed.ncbi.nlm.nih.gov/9348225

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Inhibition of Raf-1 signaling by a monoclonal antibody, which interferes with Raf-1 activation and with Mek substrate binding

Autor: W, Kolch, A, Philipp, H, Mischak, E M, Dutil, T M, Mullen, J R, Feramisco, J L, Meinkoth, D W, Rose

Publikováno v: Oncogene. 13(6)

Raf-1 is a serine/threonine specific kinase that integrates signaling by a large number of mitogens to elicit a transcriptional response in the nucleus. Activated Raf-1 phosphorylates and activates MAPK/ERK kinase Mek), thus initiating the Mek--MAP k

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::22a3021ce6551e6a77c203cad8b48496
https://pubmed.ncbi.nlm.nih.gov/8808705

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