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  • 1
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    The 2003 Bam (SE Iran) earthquake: precise source parameters from satellite radar interferometry (2004)
    In:  Geophysical Journal International, Taipei, AGU, vol. 159, no. 3, pp. 917-922, pp. B06410, (ISSN: 1340-4202)
    Details
    Publication Date: 2004
    Keywords: Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Earthquake ; Source parameters ; Dislocation ; Modelling ; Inversion ; InSAR ; Geodesy ; GJI
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    BIBLIOGRAPHY SEISMOLOGY
  • 2
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    Seismic unloading and loading in Northern Central Chile as observed by D-INSAR and Global Positioning System (2003)
    In:  International Journal of Remote Sensing, Reykjavík, Icelandic Meteorological Office, Ministry for the Environment, University of Iceland, vol. 24, no. 22, pp. 4375-4391, pp. L01305, (ISSN: 1340-4202)
    Details
    Publication Date: 2003
    Keywords: Stress ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Strain ; Geodesy ; South ; America ; nokms
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    BIBLIOGRAPHY SEISMOLOGY
  • 3
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    The serine protease TMPRSS6 is required to sense iron deficiency (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-05-03
    Description: Hepcidin, a liver-derived protein that restricts enteric iron absorption, is the key regulator of body iron content. Several proteins induce expression of the hepcidin-encoding gene Hamp in response to infection or high levels of iron. However, mechanism(s) of Hamp suppression during iron depletion are poorly understood. We describe mask: a recessive, chemically induced mutant mouse phenotype, characterized by progressive loss of body (but not facial) hair and microcytic anemia. The mask phenotype results from reduced absorption of dietary iron caused by high levels of hepcidin and is due to a splicing defect in the transmembrane serine protease 6 gene Tmprss6. Overexpression of normal TMPRSS6 protein suppresses activation of the Hamp promoter, and the TMPRSS6 cytoplasmic domain mediates Hamp suppression via proximal promoter element(s). TMPRSS6 is an essential component of a pathway that detects iron deficiency and blocks Hamp transcription, permitting enhanced dietary iron absorption.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2430097/" 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/PMC2430097/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Du, Xin -- She, Ellen -- Gelbart, Terri -- Truksa, Jaroslav -- Lee, Pauline -- Xia, Yu -- Khovananth, Kevin -- Mudd, Suzanne -- Mann, Navjiwan -- Moresco, Eva Marie Y -- Beutler, Ernest -- Beutler, Bruce -- AI054523/AI/NIAID NIH HHS/ -- DK53505-09/DK/NIDDK NIH HHS/ -- R01 DK053505-09/DK/NIDDK NIH HHS/ -- U54 AI054523/AI/NIAID NIH HHS/ -- U54 AI054523-019005/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2008 May 23;320(5879):1088-92. doi: 10.1126/science.1157121. Epub 2008 May 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18451267" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Macrocytic/genetics/metabolism ; Animals ; Antimicrobial Cationic Peptides/*genetics/metabolism ; Cell Line, Tumor ; Gene Expression Regulation ; Hepcidins ; Humans ; Iron/blood/*deficiency/metabolism ; Membrane Proteins/chemistry/genetics/*metabolism ; Mice ; Mice, Mutant Strains ; Mice, Transgenic ; Models, Biological ; Mutation ; Phenotype ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Serine Endopeptidases/chemistry/genetics/*metabolism ; Signal Transduction ; Transfection
    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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  • 4
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    Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-14
    Description: NIH 3T3 fibroblasts stably transformed with a constitutively active isoform of p21(Ras), H-RasV12 (v-H-Ras or EJ-Ras), produced large amounts of the reactive oxygen species superoxide (.O2-). .O2- production was suppressed by the expression of dominant negative isoforms of Ras or Rac1, as well as by treatment with a farnesyltransferase inhibitor or with diphenylene iodonium, a flavoprotein inhibitor. The mitogenic activity of cells expressing H-RasV12 was inhibited by treatment with the chemical antioxidant N-acetyl-L-cysteine. Mitogen-activated protein kinase (MAPK) activity was decreased and c-Jun N-terminal kinase (JNK) was not activated in H-RasV12-transformed cells. Thus, H-RasV12-induced transformation can lead to the production of .O2- through one or more pathways involving a flavoprotein and Rac1. The implication of a reactive oxygen species, probably .O2-, as a mediator of Ras-induced cell cycle progression independent of MAPK and JNK suggests a possible mechanism for the effects of antioxidants against Ras-induced cellular transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Irani, K -- Xia, Y -- Zweier, J L -- Sollott, S J -- Der, C J -- Fearon, E R -- Sundaresan, M -- Finkel, T -- Goldschmidt-Clermont, P J -- HL52315/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1649-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054359" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Acetylcysteine/pharmacology ; Animals ; Antioxidants/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Cell Cycle ; Cell Line, Transformed ; *Cell Transformation, Neoplastic ; DNA/biosynthesis ; Electron Spin Resonance Spectroscopy ; GTP-Binding Proteins/metabolism ; *Genes, ras ; JNK Mitogen-Activated Protein Kinases ; Mice ; *Mitogen-Activated Protein Kinases ; Oxidation-Reduction ; Proto-Oncogene Proteins p21(ras)/genetics/*metabolism ; Reactive Oxygen Species/*metabolism ; Signal Transduction ; Superoxides/*metabolism ; Transfection ; rac GTP-Binding Proteins
    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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  • 5
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    Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-11
    Description: The turnover of Jun proteins, like that of other transcription factors, is regulated through ubiquitin-dependent proteolysis. Usually, such processes are regulated by extracellular stimuli through phosphorylation of the target protein, which allows recognition by F box-containing E3 ubiquitin ligases. In the case of c-Jun and JunB, we found that extracellular stimuli also modulate protein turnover by regulating the activity of an E3 ligase by means of its phosphorylation. Activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and JunB through phosphorylation-dependent activation of the E3 ligase Itch. This pathway modulates cytokine production by effector T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Min -- Labuda, Tord -- Xia, Ying -- Gallagher, Ewen -- Fang, Deyu -- Liu, Yun-Cai -- Karin, Michael -- AI43477/AI/NIAID NIH HHS/ -- ES04151/ES/NIEHS NIH HHS/ -- ES06376/ES/NIEHS NIH HHS/ -- R21AI48542/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):271-5. Epub 2004 Sep 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0723, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15358865" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD28/immunology ; CD4-Positive T-Lymphocytes/immunology/*metabolism ; Interferon-gamma/metabolism ; Interleukins/metabolism ; Lymphocyte Activation ; *MAP Kinase Kinase Kinase 1 ; MAP Kinase Kinase Kinases/genetics/metabolism ; Mice ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinase 9 ; Mitogen-Activated Protein Kinases/*metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-jun/genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Receptors, Antigen, T-Cell/immunology ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology/*metabolism ; Th2 Cells/cytology/immunology/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/*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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  • 6
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    Nuclear PKM2 regulates beta-catenin transactivation upon EGFR activation (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-11-08
    Description: The embryonic pyruvate kinase M2 (PKM2) isoform is highly expressed in human cancer. In contrast to the established role of PKM2 in aerobic glycolysis or the Warburg effect, its non-metabolic functions remain elusive. Here we demonstrate, in human cancer cells, that epidermal growth factor receptor (EGFR) activation induces translocation of PKM2, but not PKM1, into the nucleus, where K433 of PKM2 binds to c-Src-phosphorylated Y333 of beta-catenin. This interaction is required for both proteins to be recruited to the CCND1 promoter, leading to HDAC3 removal from the promoter, histone H3 acetylation and cyclin D1 expression. PKM2-dependent beta-catenin transactivation is instrumental in EGFR-promoted tumour cell proliferation and brain tumour development. In addition, positive correlations have been identified between c-Src activity, beta-catenin Y333 phosphorylation and PKM2 nuclear accumulation in human glioblastoma specimens. Furthermore, levels of beta-catenin phosphorylation and nuclear PKM2 have been correlated with grades of glioma malignancy and prognosis. These findings reveal that EGF induces beta-catenin transactivation via a mechanism distinct from that induced by Wnt/Wingless and highlight the essential non-metabolic functions of PKM2 in EGFR-promoted beta-catenin transactivation, cell proliferation and tumorigenesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3235705/" 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/PMC3235705/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Weiwei -- Xia, Yan -- Ji, Haitao -- Zheng, Yanhua -- Liang, Ji -- Huang, Wenhua -- Gao, Xiang -- Aldape, Kenneth -- Lu, Zhimin -- 5 P50 CA127001-03/CA/NCI NIH HHS/ -- 5R01CA109035/CA/NCI NIH HHS/ -- CA16672/CA/NCI NIH HHS/ -- R01 CA109035/CA/NCI NIH HHS/ -- R01 CA109035-05/CA/NCI NIH HHS/ -- England -- Nature. 2011 Dec 1;480(7375):118-22. doi: 10.1038/nature10598.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22056988" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line, Tumor ; Cyclin D1/metabolism ; *Gene Expression Regulation, Neoplastic ; HEK293 Cells ; Humans ; Mice ; NIH 3T3 Cells ; Neoplasms/physiopathology ; Nuclear Proteins/*metabolism ; Phosphorylation ; Protein Binding ; Protein Transport ; Protein-Tyrosine Kinases/metabolism ; Pyruvate Kinase/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; beta Catenin/*metabolism ; src-Family Kinases
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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