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5 documents found
1: Title: Human gene expression microarray analysis of the HPV 6bE7-HaCaT stable cell line.
Authors: Zhang, Boya, et.al. .
Journal: Gene, 2018 .
Snippet: The most significantly enhanced genes HPV 6bE7-HaCaT cells were SIMC1, S100A8 and S100A9, whereas PXDN expression was markedly down-regulated.
Affiliation: Department of Dermatology, Sir Run Run Shaw Hospital, Zhejiang University, School of Medicine, China. Department of Dermatology, Sir Run Run Shaw Hospital, Zhejiang University, School of Medicine, China. Electronic address: chenghao1@zju.edu.cn. .
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2: Title: Compositional Control of Phase-Separated Cellular Bodies.
Authors: Banani, Salman F, et.al. .
Journal: Cell, Vol. 166 (3): 651-63, 2016 .
Snippet: Cellular bodies such as P bodies and PML nuclear bodies (PML NBs) appear to be phase-separated liquids organized by multivalent interactions among proteins and RNA molecules.
Affiliation: Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA. Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA. Department of Biophysics and Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: michael.rosen@utsouthwestern.edu. .
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3: Title: Assay methods for small ubiquitin-like modifier (SUMO)-SUMO-interacting motif (SIM) interactions in vivo and in vitro using a split-luciferase complementation system.
Authors: Hirohama, Mikako, et.al. .
Journal: Analytical biochemistry (Anal Biochem), Vol. 448, 2014 .
Snippet: SUMOylation is a posttranslational process that attaches a small ubiquitin-like modifier (SUMO) to its target proteins covalently.
Affiliation: Chemical Genetics Laboratory, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; Japan Science and Technology Corporation, CREST Research Project, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan; Department of Chemistry and Biochemistry, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan. Zhang Initiative Research Unit, RIKEN, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Department of Chemistry, School of Science, The University of Tokyo, 7-3-1 Bunkyo-ku, Hongo, Tokyo 113-0033, Japan. Department of New Frontier Sciences, Graduate School of Science and Technology, Kumamoto University, 2-39-1 Kurokami, Kumamoto 860-8555, Japan. Department of Chemistry and Biochemistry, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan. Chemical Genetics Laboratory, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; Chemical Genomics Research Group, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Electronic address: akihiro-i@riken.jp. Chemical Genetics Laboratory, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; Chemical Genomics Research Group, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; Japan Science and Technology Corporation, CREST Research Project, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan. .
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4: Title: Interplay of the fungal sumoylation network for control of multicellular development.
Authors: Harting, Rebekka, et.al. .
Journal: Molecular microbiology (Mol Microbiol), Vol. 90 (5): 1125-45, 2013 .
Snippet: This includes the SumO processing enzyme UlpB, the E1 SumO activating enzyme AosA/UbaB, the E2 conjugation enzyme UbcN and UlpA as major SumO isopeptidase.
Affiliation: Institut für Mikrobiologie und Genetik, Georg-August Universität Göttingen, Grisebachstrasse 8, D-37077, Göttingen, Germany. .
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5: Title: PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.
Authors: Ono, Yasuko, et.al. .
Journal: Journal of molecular biology (J Mol Biol), Vol. 425 (16): 2955-72, 2013 .
Snippet: Here, we report that a novel CAPN3-binding protein, PLEIAD [Platform element for inhibition of autolytic degradation; originally called SIMC1/C5orf25 (SUMO-interacting motif containing protein 1/chromosome 5open reading frame 25)], suppresses the protease activity of CAPN3.
Affiliation: Calpain Project, Department of Advanced Science for Biomolecules, Tokyo Metropolitan Institute of Medical Science (IGAKUKEN), 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo 156-8506, Japan. ono-ys@igakuken.or.jp .
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