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  • Phosphorylation  (667)
  • Malaysia
  • OBIS
  • Oceanography
  • American Association for the Advancement of Science (AAAS)  (679)
  • UNESCO  (16)
  • 2020-2023  (4)
  • 2010-2014  (123)
  • 2000-2004  (282)
  • 1995-1999  (280)
  • 1975-1979  (6)
Collection
Keywords
Publisher
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Year
  • 11
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    IODE Group of Experts on Marine Information Management (GE-MIM), Eleventh Session, 25-28 May 2010 (2012)
    UNESCO | Paris
    Details
    Publication Date: 2021-01-30
    Description: Supported by IOC for UNESCO.
    Description: Document available in English.
    Description: Published
    Description: Marine information management
    Keywords: Information services ; Oceanography
    Repository Name: AquaDocs
    Type: Non-Refereed
    Format: 64
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  • 12
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    Ad hoc meeting of the IODE Steering Group for OBIS IODE Project Office, Oostende, Belgium 18-19 November 2010 (2012)
    UNESCO | Paris
    Details
    Publication Date: 2021-01-30
    Description: Supported by iOC for UNESCO.
    Description: Document available in English.
    Description: Published
    Keywords: Oceanography
    Repository Name: AquaDocs
    Type: Non-Refereed
    Format: 45
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  • 13
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    Meeting of the Inter-sessional working group for updating the IOC Strategic Plan for Oceanographic Data and Information Exchange (2012-2015) IOC Project Office for IODE Oostende, Belgium 1-2 March 2012 (2012)
    UNESCO | Paris
    Details
    Publication Date: 2021-01-30
    Description: Supported by IOC for UNESCO.
    Description: Document available in English.
    Description: Published
    Keywords: Oceanography
    Repository Name: AquaDocs
    Type: Non-Refereed
    Format: 23
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  • 14
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    Joint WMO-IOC Technical Commission for Oceanography and Marine Meteorology, fourth session, Yeosu, Republic of Korea, 28-31 May 2012 (2012)
    UNESCO | Paris
    Details
    Publication Date: 2021-01-30
    Description: The fourth session of the Joint IOC-WMO Technical Commission for Oceanography and Marine Meteorology (JCOMM-4) took place in Yeosu, from 28 to 31 May 2012, hosted by the Republic of Korea through the Korean Meteorological Administration, the Expo 2012 Yeosu Korea organizing committee, the government of Jeollanamdo province and the city of Yeosu. An opening ceremony on 23 May was followed by a Scientific and Technical Workshop on 24-25 May 2012. There were some 140 participants in the session, from 47 Members/Member States and 4 international organizations. All final approved session documents are available on the JCOMM website (www.jcomm.info/jcomm4).
    Description: Supported by IOC for UNESCO.
    Description: Document available in English.
    Description: Published
    Keywords: Marine meteorology ; UNESCO ; Marine meteorology ; Oceanography
    Repository Name: AquaDocs
    Type: Report , Non-Refereed
    Format: 53
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  • 15
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    IOC Working Committee on International Oceanographic Data Exchange (IODE), Ninth session (2012)
    UNESCO
    Details
    Publication Date: 2021-01-30
    Description: Supported by IOC/IODE
    Description: Document available in English
    Description: Unpublished
    Description: Working committee
    Keywords: Oceanography ; Oceanography
    Repository Name: AquaDocs
    Type: Report , Non-Refereed
    Format: 102
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  • 16
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    IOC Committee on International Oceanographic Data and Information Exchange, twenty-first session Palais des Congrès, Liège, Belgium, 23-26 March 2011 (2012)
    UNESCO | Paris
    Details
    Publication Date: 2021-01-30
    Description: The IOC Committee on International Oceanographic Data and Information Exchange held its Twenty-first Session (IODE-XXI) at the Palais des Congrès, Liège, Belgium between 23 and 26 March 2011. The Session was attended by 74 participants from 36 IOC Member States and 7 organizations. The Session’s outcomes included: (i) the further steps towards the adoption of OBIS by IODE, including the recommended establishment of an IOC Project Office for IODE/OBIS; (ii) the continuation of the IOC Project Office for IODE in Oostende, Belgium; (iii) a statement on the IODE role in the ICSU World Data System; (iv) the planned further expansion of OceanTeacher to include a wider range of IOC disciplines as well as the recommended development of a 5-year training plan; (v) the planned revision of the IOC Strategic Plan for Oceanographic Data and Information Exchange (2012-2015). The Committee elected Ms Sissy Iona (Greece) and Mr Ariel Troisi (Argentina) as IODE Co-Chairs.
    Description: Supported by IOC/ IODE
    Description: Report is available in English
    Description: Published
    Keywords: Oceanography ; Marine biology ; Oceanographic data
    Repository Name: AquaDocs
    Type: Non-Refereed
    Format: 109
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  • 17
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    Mitochondria. Cell cycle-dependent regulation of mitochondrial preprotein translocase (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-11-08
    Description: Mitochondria play central roles in cellular energy conversion, metabolism, and apoptosis. Mitochondria import more than 1000 different proteins from the cytosol. It is unknown if the mitochondrial protein import machinery is connected to the cell division cycle. We found that the cyclin-dependent kinase Cdk1 stimulated assembly of the main mitochondrial entry gate, the translocase of the outer membrane (TOM), in mitosis. The molecular mechanism involved phosphorylation of the cytosolic precursor of Tom6 by cyclin Clb3-activated Cdk1, leading to enhanced import of Tom6 into mitochondria. Tom6 phosphorylation promoted assembly of the protein import channel Tom40 and import of fusion proteins, thus stimulating the respiratory activity of mitochondria in mitosis. Tom6 phosphorylation provides a direct means for regulating mitochondrial biogenesis and activity in a cell cycle-specific manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harbauer, Angelika B -- Opalinska, Magdalena -- Gerbeth, Carolin -- Herman, Josip S -- Rao, Sanjana -- Schonfisch, Birgit -- Guiard, Bernard -- Schmidt, Oliver -- Pfanner, Nikolaus -- Meisinger, Chris -- New York, N.Y. -- Science. 2014 Nov 28;346(6213):1109-13. doi: 10.1126/science.1261253. Epub 2014 Nov 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany. Trinationales Graduiertenkolleg 1478, Universitat Freiburg, 79104 Freiburg, Germany. Faculty of Biology, Universitat Freiburg, 79104 Freiburg, Germany. BIOSS Centre for Biological Signalling Studies, Universitat Freiburg, 79104 Freiburg, Germany. ; Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany. ; Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany. Trinationales Graduiertenkolleg 1478, Universitat Freiburg, 79104 Freiburg, Germany. Faculty of Biology, Universitat Freiburg, 79104 Freiburg, Germany. ; Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany. Faculty of Biology, Universitat Freiburg, 79104 Freiburg, Germany. Spemann Graduate School of Biology and Medicine, Universitat Freiburg, 79104 Freiburg, Germany. ; Centre de Genetique Moleculaire, CNRS, 91190 Gif-sur-Yvette, France. ; Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany. BIOSS Centre for Biological Signalling Studies, Universitat Freiburg, 79104 Freiburg, Germany. ; Institut fur Biochemie und Molekularbiologie, ZBMZ, Universitat Freiburg, 79104 Freiburg, Germany. BIOSS Centre for Biological Signalling Studies, Universitat Freiburg, 79104 Freiburg, Germany. nikolaus.pfanner@biochemie.uni-freiburg.de chris.meisinger@biochemie.uni-freiburg.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25378463" target="_blank"〉PubMed〈/a〉
    Keywords: CDC2 Protein Kinase/metabolism ; *Cell Cycle ; Cyclin B/metabolism ; Cytosol/metabolism ; Mitochondria/*metabolism ; Mitochondrial Membrane Transport Proteins/*metabolism ; Phosphorylation ; Protein Precursors/*metabolism ; Protein Transport ; Saccharomyces cerevisiae/*cytology/*metabolism ; Saccharomyces cerevisiae Proteins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 18
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    Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-09-23
    Description: Ribonucleotide reductase (RNR) supplies the balanced pools of deoxynucleotide triphosphates (dNTPs) necessary for DNA replication and maintenance of genomic integrity. RNR is subject to allosteric regulatory mechanisms in all eukaryotes, as well as to control by small protein inhibitors Sml1p and Spd1p in budding and fission yeast, respectively. Here, we show that the metazoan protein IRBIT forms a deoxyadenosine triphosphate (dATP)-dependent complex with RNR, which stabilizes dATP in the activity site of RNR and thus inhibits the enzyme. Formation of the RNR-IRBIT complex is regulated through phosphorylation of IRBIT, and ablation of IRBIT expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression. We demonstrate a mechanism for RNR regulation in higher eukaryotes that acts by enhancing allosteric RNR inhibition by dATP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnaoutov, Alexei -- Dasso, Mary -- New York, N.Y. -- Science. 2014 Sep 19;345(6203):1512-5. doi: 10.1126/science.1251550.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. arnaouta@mail.nih.gov. ; Laboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25237103" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Catalytic Domain ; Deoxyadenine Nucleotides/*metabolism ; HeLa Cells ; Humans ; Immunoprecipitation ; Lectins, C-Type/genetics/*metabolism ; Membrane Proteins/genetics/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Ribonucleotide Reductases/*antagonists & inhibitors/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-08-02
    Description: Many RNA regulatory proteins controlling pre-messenger RNA splicing contain serine:arginine (SR) repeats. Here, we found that these SR domains bound hydrogel droplets composed of fibrous polymers of the low-complexity domain of heterogeneous ribonucleoprotein A2 (hnRNPA2). Hydrogel binding was reversed upon phosphorylation of the SR domain by CDC2-like kinases 1 and 2 (CLK1/2). Mutated variants of the SR domains changing serine to glycine (SR-to-GR variants) also bound to hnRNPA2 hydrogels but were not affected by CLK1/2. When expressed in mammalian cells, these variants bound nucleoli. The translation products of the sense and antisense transcripts of the expansion repeats associated with the C9orf72 gene altered in neurodegenerative disease encode GRn and PRn repeat polypeptides. Both peptides bound to hnRNPA2 hydrogels independent of CLK1/2 activity. When applied to cultured cells, both peptides entered cells, migrated to the nucleus, bound nucleoli, and poisoned RNA biogenesis, which caused cell death.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4459787/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4459787/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwon, Ilmin -- Xiang, Siheng -- Kato, Masato -- Wu, Leeju -- Theodoropoulos, Pano -- Wang, Tao -- Kim, Jiwoong -- Yun, Jonghyun -- Xie, Yang -- McKnight, Steven L -- U01 GM107623/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Sep 5;345(6201):1139-45. doi: 10.1126/science.1254917. Epub 2014 Jul 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9152, USA. ; Quantitative Biomedical Research Center, Department of Clinical Sciences, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9152, USA. ; Department of Biochemistry, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9152, USA. steven.mcknight@utsouthwestern.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25081482" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amyotrophic Lateral Sclerosis/genetics/*metabolism/pathology ; Astrocytes/*metabolism/pathology ; Cell Death ; Cell Nucleolus/*metabolism ; Cells, Cultured ; Dipeptides/genetics/*metabolism/pharmacology ; Frontotemporal Dementia/genetics/*metabolism/pathology ; Glutamate Plasma Membrane Transport Proteins/genetics ; Heterogeneous-Nuclear Ribonucleoprotein Group A-B/*metabolism ; Humans ; Hydrogel ; Phosphorylation ; Protein Biosynthesis ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/*genetics ; RNA, Antisense/antagonists & inhibitors/biosynthesis ; RNA, Messenger/antagonists & inhibitors/biosynthesis ; RNA, Ribosomal/antagonists & inhibitors/biosynthesis ; Repetitive Sequences, Amino Acid ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 20
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    A mutually assured destruction mechanism attenuates light signaling in Arabidopsis (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-06-07
    Description: After light-induced nuclear translocation, phytochrome photoreceptors interact with and induce rapid phosphorylation and degradation of basic helix-loop-helix transcription factors, such as PHYTOCHROME-INTERACTING FACTOR 3 (PIF3), to regulate gene expression. Concomitantly, this interaction triggers feedback reduction of phytochrome B (phyB) levels. Light-induced phosphorylation of PIF3 is necessary for the degradation of both proteins. We report that this PIF3 phosphorylation induces, and is necessary for, recruitment of LRB [Light-Response Bric-a-Brack/Tramtrack/Broad (BTB)] E3 ubiquitin ligases to the PIF3-phyB complex. The recruited LRBs promote concurrent polyubiqutination and degradation of both PIF3 and phyB in vivo. These data reveal a linked signal-transmission and attenuation mechanism involving mutually assured destruction of the receptor and its immediate signaling partner.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4414656/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4414656/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ni, Weimin -- Xu, Shou-Ling -- Tepperman, James M -- Stanley, David J -- Maltby, Dave A -- Gross, John D -- Burlingame, Alma L -- Wang, Zhi-Yong -- Quail, Peter H -- 2R01 GM-047475/GM/NIGMS NIH HHS/ -- 5R01GM066258/GM/NIGMS NIH HHS/ -- 8P41GM103481/GM/NIGMS NIH HHS/ -- P41 GM103481/GM/NIGMS NIH HHS/ -- P50 GM082250/GM/NIGMS NIH HHS/ -- R01 GM047475/GM/NIGMS NIH HHS/ -- R01 GM066258/GM/NIGMS NIH HHS/ -- T32 GM008284/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Jun 6;344(6188):1160-4. doi: 10.1126/science.1250778.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Plant Gene Expression Center, Agriculture Research Service (ARS), U.S. Department of Agriculture (USDA), Albany, CA 94710, USA. ; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA. Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA. ; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143, USA. ; Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA. ; Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA 94720, USA. Plant Gene Expression Center, Agriculture Research Service (ARS), U.S. Department of Agriculture (USDA), Albany, CA 94710, USA. quail@berkeley.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24904166" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Arabidopsis/genetics/*growth & development/metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Basic Helix-Loop-Helix Transcription Factors/genetics/*metabolism ; Cell Nucleus/metabolism ; Cullin Proteins/*metabolism ; Gene Expression Regulation, Plant ; HeLa Cells ; Humans ; *Light Signal Transduction ; Nuclear Proteins/genetics/metabolism ; Phosphorylation ; Phytochrome B/*metabolism ; Polyubiquitin/metabolism ; Proteolysis ; *Ubiquitination
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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