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  • 1
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    In:  Terra Nova, Hannover, Bundesanstalt für Geowissenschaften und Rohstoffe, vol. 5, no. 1, pp. 164-173, pp. 1175, (ISSN: 1340-4202)
    Publication Date: 1993
    Keywords: Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Geodesy ; Geothermics ; Seismicity ; Tectonics ; Fluids
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  • 2
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    Gen. Dir. of Disaster Affairs, Ankara and GeoForschungsZentrum, Potsdam
    In:  New York, Gen. Dir. of Disaster Affairs, Ankara and GeoForschungsZentrum, Potsdam, vol. 231, no. 3, pp. 2-203, (ISBN 1-86239-165-3, vi + 330 pp.)
    Publication Date: 1996
    Keywords: Proceedings of a conference ; Earthquake precursor: prediction research ; NAF ; Turkey ; Project report/description ; Tectonics ; Plate tectonics ; Seismology ; paleo ; Seismicity ; Geodesy ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Global Positioning System ; Earthquake precursor: chemical (Rn, water(-level,...) ; Earthquake ; Dinar ; Geol. aspects ; Turkey ; Erguenay ; Ergunay ; Isikara
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  • 3
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    In:  J. Geophys. Res., Leyden, Noordhoff International Publishing, vol. 102, no. B12, pp. 27,587-27,601, pp. B04306, (ISSN: 1340-4202)
    Publication Date: 1997
    Keywords: Geodesy ; Geol. aspects ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Plate tectonics ; Turkey ; JGR
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  • 4
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    kassel university press
    In:  New York, 164 pp., kassel university press, vol. 4, no. Publ. No. 12, pp. 267, (ISBN 3-7281-2425-7)
    Publication Date: 1999
    Keywords: Turkey ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Geodesy ; Geol. aspects ; Fluids ; Geothermics ; Seismology ; Project report/description ; NAF ; Fault zone
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  • 5
    Publication Date: 2019
    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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  • 6
    Publication Date: 2016-07-02
    Description: Recent research has shown that compassionate feelings for the suffering environment promote conservation of nature. We extend this notion and relate compassion for suffering humans to proenvironmental tendencies. The proposed relation should hold true as compassion elicits moral actions and judgments across different moral domains which should also be applicable to the environment. Therefore, we expect compassion for other humans to relate positively to proenvironmental tendencies. Two studies were conducted to test this assumption. Study 1 included three independent samples (final N = 2,096) and several measures of proenvironmental tendencies. Results revealed that compassion was indeed positively related to proenvironmental values, proenvironmental intentions, and reported donations to nature or environmental organizations. In Study 2, we experimentally tested and found a causal path between compassion for humans and proenvironmental intentions. Implications for climate change and protection of nature are discussed.
    Print ISSN: 0013-9165
    Electronic ISSN: 1552-390X
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Psychology
    Published by Sage
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  • 7
    Publication Date: 1992-12-21
    Description: Interferon-gamma (IFN-gamma) induces the transcription of the gene encoding a guanylate binding protein by activating a latent cytoplasmic factor, GAF (gamma-activated factor). GAF is translocated to the nucleus and binds a DNA element, the gamma-activated site. Through cross-linking and the use of specific antibodies GAF was found to be a 91-kilodalton DNA binding protein that was previously identified as one of four proteins in interferon-stimulated gene factor-3 (ISGF-3), a transcription complex activated by IFN-alpha. The IFN-gamma-dependent activation of the 91-kilodalton DNA binding protein required cytoplasmic phosphorylation of the protein on tyrosine. The 113-kilodalton ISGF-3 protein that is phosphorylated in response to IFN-alpha was not phosphorylated nor translocated to the nucleus in response to IFN-gamma. Thus the two different ligands result in tyrosine phosphorylation of different combinations of latent cytoplasmic transcription factors that then act at different DNA binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuai, K -- Schindler, C -- Prezioso, V R -- Darnell, J E Jr -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1808-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1281555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/isolation & purification/*metabolism ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; GTP-Binding Proteins/*genetics ; Gene Expression Regulation/drug effects ; Interferon-alpha/pharmacology ; Interferon-gamma/*pharmacology ; Models, Biological ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides ; Phosphorylation ; Phosphotyrosine ; Promoter Regions, Genetic ; STAT1 Transcription Factor ; Signal Transduction/drug effects ; *Trans-Activators ; *Transcription, Genetic/drug effects ; Tyrosine/analogs & derivatives/analysis
    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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  • 8
    Publication Date: 1995-03-31
    Description: Members of the interleukin-6 family of cytokines bind to and activate receptors that contain a common subunit, gp130. This leads to the activation of Stat3 and Stat1, two cytoplasmic signal transducers and activators of transcription (STATs), by tyrosine phosphorylation. Serine phosphorylation of Stat3 was constitutive and was enhanced by signaling through gp130. In cells of lymphoid and neuronal origins, inhibition of serine phosphorylation prevented the formation of complexes of DNA with Stat3-Stat3 but not with Stat3-Stat1 or Stat1-Stat1 dimers. In vitro serine dephosphorylation of Stat3 also inhibited DNA binding of Stat3-Stat3. The requirement of serine phosphorylation for Stat3-Stat3.DNA complex formation was inversely correlated with the affinity of Stat3-Stat3 for the binding site. Thus, serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3.DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, X -- Blenis, J -- Li, H C -- Schindler, C -- Chen-Kiang, S -- CA46595/CA/NCI NIH HHS/ -- HL 21006/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1990-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701321" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Ciliary Neurotrophic Factor ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Humans ; Interleukin-6/metabolism/*pharmacology ; Isoquinolines/pharmacology ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/pharmacology ; Phosphorylation ; Piperazines/pharmacology ; *Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Serine/*metabolism ; Signal Transduction ; Threonine/metabolism ; Trans-Activators/*metabolism ; Tumor Cells, Cultured ; Tyrosine/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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  • 9
    Publication Date: 1995-07-14
    Description: The ability of interferon gamma (IFN-gamma) to inhibit the proliferation of type 2 T helper cells (TH2), but not that of type 1 (TH1) cells, suggests that helper cell subsets might differ in their activation of the IFN-gamma signaling pathway. The IFN-gamma-inducible signal transducing factor (STF-IFN gamma) was activated in murine TH2 but not in TH1 cell clones, because in the latter the second chain of the IFN-gamma receptor (accessory factor 1 or IFN-gamma R beta) was absent. Thus, TH1 cells use receptor modification to prevent the activation of STF-IFN gamma and achieve an IFN-gamma-resistant state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pernis, A -- Gupta, S -- Gollob, K J -- Garfein, E -- Coffman, R L -- Schindler, C -- Rothman, P -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):245-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618088" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Clone Cells ; DNA-Binding Proteins/genetics/metabolism ; Down-Regulation ; Gene Expression Regulation ; Interferon Regulatory Factor-1 ; Interferon-gamma/pharmacology/*physiology ; Interleukin-4/pharmacology ; Janus Kinase 1 ; Janus Kinase 2 ; Mice ; Molecular Sequence Data ; Phosphoproteins/genetics ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; Receptors, Interferon/*physiology ; STAT1 Transcription Factor ; *Signal Transduction ; Th1 Cells/*immunology/metabolism ; Th2 Cells/*immunology/metabolism ; Trans-Activators/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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  • 10
    Publication Date: 1993-12-03
    Description: Components of a signaling pathway that couples the ciliary neurotrophic factor (CNTF) receptor to induction of transcription were identified. CNTF stimulated the tyrosine phosphorylation of p91, a protein implicated in interferon signaling pathways, and of two proteins that are distinct but related to p91. Tyrosine-phosphorylated p91 translocated to the nucleus, where p91 and p91-related proteins bound to a DNA sequence found in promoters of genes responsive to CNTF. This DNA sequence, when inserted upstream of a reporter gene, conferred a transcriptional response to CNTF. A pathway that transduces interferon signals may therefore have a more general function in the propagation of responses to certain neurotrophic factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonni, A -- Frank, D A -- Schindler, C -- Greenberg, M E -- HL21006-17/HL/NHLBI NIH HHS/ -- R01 CA43855/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1575-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Neuroscience, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7504325" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biological Transport/physiology ; Cell Nucleus/*metabolism ; Ciliary Neurotrophic Factor ; DNA-Binding Proteins/biosynthesis ; Fibroblast Growth Factor 2/physiology ; Gene Expression Regulation/physiology ; HeLa Cells ; Humans ; Interferon-alpha/physiology ; Interferon-gamma/physiology ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins/*physiology ; Phosphoproteins/biosynthesis/chemistry ; Phosphotyrosine ; Regulatory Sequences, Nucleic Acid/physiology ; Signal Transduction/*physiology ; Transcription, Genetic/*physiology ; Tumor Cells, Cultured ; Tyrosine/analogs & derivatives/analysis
    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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