يعرض 1 - 3 نتائج من 3 نتيجة بحث عن '"Nanaocha Sharma"', وقت الاستعلام: 0.81s تنقيح النتائج
  1. 1
  2. 2
  3. 3

    المساهمون: Department of Molecular Biotechnology and Health Sciences, Università degli studi di Torino = University of Turin (UNITO), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), University of Turin, Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

    المصدر: PLoS ONE, Vol 8, Iss 1, p e54931 (2013)
    PLoS ONE
    PLoS ONE, 2012, 8 (1), pp.e54931
    Repetto, D, Aramu, S, Boeri Erba, E, Sharma, N, Grasso, S, Russo, I, Jensen, O N, Cabodi, S, Turco, E, Di Stefano, P & Defilippi, P 2013, ' Mapping of p140Cap phosphorylation sites : the EPLYA and EGLYA motifs have a key role in tyrosine phosphorylation and Csk binding, and are substrates of the Abl kinase ', P L o S One, vol. 8, no. 1, pp. e54931 . https://doi.org/10.1371/journal.pone.0054931
    PLoS ONE, Public Library of Science, 2012, 8 (1), pp.e54931

    مصطلحات موضوعية: Proteomics, Amino Acid Motifs, lcsh:Medicine, MESH: Amino Acid Sequence, Protein tyrosine phosphatase, SH2 domain, Biochemistry, SH3 domain, Receptor tyrosine kinase, MESH: Tyrosine, Phosphorylation cascade, CSK Tyrosine-Protein Kinase, MESH: Amino Acid Motifs, chemistry.chemical_compound, 0302 clinical medicine, Molecular Cell Biology, Tyrosine Kinase Signaling Cascade, Basic Cancer Research, Signaling in Cellular Processes, Protein phosphorylation, Phosphorylation, MESH: Proto-Oncogene Proteins c-abl, Proto-Oncogene Proteins c-abl, lcsh:Science, 0303 health sciences, Multidisciplinary, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Signaling Cascades, MESH: MCF-7 Cells, MESH: Mutagenesis, Site-Directed, src-Family Kinases, Oncology, MESH: HEK293 Cells, 030220 oncology & carcinogenesis, MCF-7 Cells, Medicine, Protein Binding, Research Article, Signal Transduction, Molecular Sequence Data, Biology, Signaling Pathways, Peptide Mapping, MESH: src Homology Domains, src Homology Domains, 03 medical and health sciences, Humans, MESH: Protein Binding, Amino Acid Sequence, Protein Interactions, 030304 developmental biology, Binding Sites, MESH: Humans, MESH: Molecular Sequence Data, MESH: Phosphorylation, lcsh:R, Proteins, Tyrosine phosphorylation, MESH: Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Vesicular Transport, HEK293 Cells, MESH: src-Family Kinases, MESH: Binding Sites, chemistry, Mutagenesis, Site-Directed, biology.protein, Tyrosine, lcsh:Q