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  • 1
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    Global Positioning System constraints on plate kinematics and dynamics in the eastern Mediterranean and Caucasus (2000)
    In:  J. Geophys. Res., New York, 1-2, vol. 105, no. B3, pp. 5695-5719, pp. 1610, (ISSN: 1340-4202)
    Details
    Publikationsdatum: 2000
    Schlagwort(e): Global Positioning System ; Turkey ; NAF ; Plate tectonics ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Fault plane solution, focal mechanism ; JGR ; 1206 ; Geodesy ; and ; gravity ; Crustal ; movements--interplate ; (8155) ; 1208 ; Crustal ; movements--intraplate ; (8110) ; 1243 ; Space ; geodetic ; surveys ; 8110 ; Tectonophysics ; Continental ; tectonics--general ; (0905) ; Toksoez ; Toksoz ; Sanli
    Standort Signatur Erwartet Verfügbarkeit
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    BIBLIOGRAFIE SEISMOLOGIE
  • 2
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    Interseismic strain accumulation in south central Chile from Global Positioning System measurements, 1996-1999 (2002)
    In:  Geophys. Res. Lett., Kobe, Dec. 6-11, 1993, The Local Organizing Committee for the CRCM '93, vol. 29, no. 11, pp. 12-1 to 12-4, pp. 1517, (ISSN: 1340-4202)
    Details
    Publikationsdatum: 2002
    Schlagwort(e): Strain ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Geodesy ; Subduction zone ; GRL ; 1242 ; Geodesy ; and ; Gravity: ; Seismic ; deformations ; (7205) ; 1208 ; Crustal ; movements--intraplate ; (8110) ; 7230 ; Seismology: ; Seismicity ; and ; seismotectonics ; Chabalier
    Standort Signatur Erwartet Verfügbarkeit
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    BIBLIOGRAFIE SEISMOLOGIE
  • 3
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    Geodetic data on the Earth's crustal kinematic processes within the Sofia seismo-forecasting test area (1992)
    In:  Tectonophys., Warszawa, EGS, vol. 202, no. 17, pp. 135-140, pp. 1050, (ISSN: 1340-4202)
    Details
    Publikationsdatum: 1992
    Schlagwort(e): Earthquake precursor: prediction research ; Project report/description ; Geodesy ; Crustal deformation (cf. Earthquake precursor: deformation or strain)
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    BIBLIOGRAFIE SEISMOLOGIE
  • 4
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    Insights on Continental Collisional Processes from GPS Data : Dynamics of the Peri-Adriatic Belts (2015)
    Wiley
    Details
    Publikationsdatum: 2015-11-24
    Beschreibung: We present a new GPS velocity field covering the peri-Adriatic tectonically-active belts and the entire Balkan Peninsula. From the velocities, we calculate consistent strain rate and interpolated velocity fields. Significant features of the crustal deformation include: (1) the eastward motion of the northern part of the Eastern Alps together with part the Alpine foreland and Bohemian Massif towards the Pannonian Basin, (2) shortening across the Dinarides, (3) a clock-wise rotation of the Albanides-Hellenides and (4) a southward motion South of 44 ∘ N of the inner Balkan lithosphere between the rigid Apulia and Black Sea, towards the Aegean domain. Using this new velocity-field, we derive the strain rate tensor to analyze the regional style of the deformation. Then, we devise a simple test based on the momentum balance equation, to investigate the role of horizontal gradients of gravitational potential energy in driving the deformation in the Peri-Adriatic tectonically-active mountain belts : the Eastern Alps, the Dinarides, the Albanides and the Apennines. We show that the strain rate fields observed in the Apennines and Albanides are consistent with a fluid, with viscosity η ∼ 3×10 21 Pas, deforming in response to horizontal gradients of gravitational potential energy. Conversely, both the Dinarides and Eastern Alps are probably deforming in response to the North and North-East oriented motion of the Adria-Apulia indenter respectively, and as a consequence of horizontal lithospheric heterogeneity.
    Print ISSN: 0148-0227
    Thema: Geologie und Paläontologie , Physik
    Publiziert von Wiley im Namen von American Geophysical Union (AGU).
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  • 5
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    Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2011-08-13
    Beschreibung: Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1 isolates. To understand how such broadly neutralizing antibodies develop, we used x-ray crystallography and 454 pyrosequencing to characterize additional VRC01-like antibodies from HIV-1-infected individuals. Crystal structures revealed a convergent mode of binding for diverse antibodies to the same CD4-binding-site epitope. A functional genomics analysis of expressed heavy and light chains revealed common pathways of antibody-heavy chain maturation, confined to the IGHV1-2*02 lineage, involving dozens of somatic changes, and capable of pairing with different light chains. Broadly neutralizing HIV-1 immunity associated with VRC01-like antibodies thus involves the evolution of antibodies to a highly affinity-matured state required to recognize an invariant viral structure, with lineages defined from thousands of sequences providing a genetic roadmap of their development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3516815/" 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/PMC3516815/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Xueling -- Zhou, Tongqing -- Zhu, Jiang -- Zhang, Baoshan -- Georgiev, Ivelin -- Wang, Charlene -- Chen, Xuejun -- Longo, Nancy S -- Louder, Mark -- McKee, Krisha -- O'Dell, Sijy -- Perfetto, Stephen -- Schmidt, Stephen D -- Shi, Wei -- Wu, Lan -- Yang, Yongping -- Yang, Zhi-Yong -- Yang, Zhongjia -- Zhang, Zhenhai -- Bonsignori, Mattia -- Crump, John A -- Kapiga, Saidi H -- Sam, Noel E -- Haynes, Barton F -- Simek, Melissa -- Burton, Dennis R -- Koff, Wayne C -- Doria-Rose, Nicole A -- Connors, Mark -- NISC Comparative Sequencing Program -- Mullikin, James C -- Nabel, Gary J -- Roederer, Mario -- Shapiro, Lawrence -- Kwong, Peter D -- Mascola, John R -- 5U19 AI 067854-06/AI/NIAID NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- U19 AI067854/AI/NIAID NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1593-602. doi: 10.1126/science.1207532. Epub 2011 Aug 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, 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/21835983" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): AIDS Vaccines ; Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/genetics/*immunology/isolation & purification ; Antibody Affinity ; Antibody Specificity ; Antigens, CD4/metabolism ; Base Sequence ; Binding Sites ; Binding Sites, Antibody ; Complementarity Determining Regions/genetics ; Crystallography, X-Ray ; Epitopes ; *Evolution, Molecular ; Genes, Immunoglobulin Heavy Chain ; HIV Antibodies/*chemistry/genetics/*immunology/isolation & purification ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV Infections/immunology ; HIV-1/chemistry/*immunology ; High-Throughput Nucleotide Sequencing ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology ; Immunoglobulin Heavy Chains/chemistry/immunology ; Immunoglobulin J-Chains/genetics ; Immunoglobulin Light Chains/chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 6
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    Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9 (2011)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2011-11-25
    Beschreibung: Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody neutralization, and are themselves protected by extraordinary sequence diversity and N-linked glycosylation. Human antibodies such as PG9 nonetheless engage V1/V2 and neutralize 80% of HIV-1 isolates. Here we report the structure of V1/V2 in complex with PG9. V1/V2 forms a four-stranded beta-sheet domain, in which sequence diversity and glycosylation are largely segregated to strand-connecting loops. PG9 recognition involves electrostatic, sequence-independent and glycan interactions: the latter account for over half the interactive surface but are of sufficiently weak affinity to avoid autoreactivity. The structures of V1/V2-directed antibodies CH04 and PGT145 indicate that they share a common mode of glycan penetration by extended anionic loops. In addition to structurally defining V1/V2, the results thus identify a paradigm of antibody recognition for highly glycosylated antigens, which-with PG9-involves a site of vulnerability comprising just two glycans and a strand.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3406929/" 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/PMC3406929/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McLellan, Jason S -- Pancera, Marie -- Carrico, Chris -- Gorman, Jason -- Julien, Jean-Philippe -- Khayat, Reza -- Louder, Robert -- Pejchal, Robert -- Sastry, Mallika -- Dai, Kaifan -- O'Dell, Sijy -- Patel, Nikita -- Shahzad-ul-Hussan, Syed -- Yang, Yongping -- Zhang, Baoshan -- Zhou, Tongqing -- Zhu, Jiang -- Boyington, Jeffrey C -- Chuang, Gwo-Yu -- Diwanji, Devan -- Georgiev, Ivelin -- Kwon, Young Do -- Lee, Doyung -- Louder, Mark K -- Moquin, Stephanie -- Schmidt, Stephen D -- Yang, Zhi-Yong -- Bonsignori, Mattia -- Crump, John A -- Kapiga, Saidi H -- Sam, Noel E -- Haynes, Barton F -- Burton, Dennis R -- Koff, Wayne C -- Walker, Laura M -- Phogat, Sanjay -- Wyatt, Richard -- Orwenyo, Jared -- Wang, Lai-Xi -- Arthos, James -- Bewley, Carole A -- Mascola, John R -- Nabel, Gary J -- Schief, William R -- Ward, Andrew B -- Wilson, Ian A -- Kwong, Peter D -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- RR017573/RR/NCRR NIH HHS/ -- Canadian Institutes of Health Research/Canada -- Intramural NIH HHS/ -- England -- Nature. 2011 Nov 23;480(7377):336-43. doi: 10.1038/nature10696.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22113616" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): AIDS Vaccines/chemistry/immunology ; Amino Acid Motifs ; Amino Acid Sequence ; Antibodies, Neutralizing/chemistry/*immunology ; Antibody Affinity/immunology ; Antibody Specificity/*immunology ; Antigen-Antibody Complex/chemistry/immunology ; Binding Sites, Antibody/immunology ; Conserved Sequence ; Crystallography, X-Ray ; Epitopes/chemistry/immunology ; Glycopeptides/chemistry/immunology ; Glycosylation ; HIV Antibodies/chemistry/*immunology ; HIV Envelope Protein gp120/*chemistry/*immunology ; HIV-1/*chemistry/*immunology ; Hydrogen Bonding ; Immune Evasion ; Models, Molecular ; Molecular Sequence Data ; Polysaccharides/chemistry/immunology ; Protein Structure, Quaternary ; Protein Structure, Tertiary
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
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  • 7
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    Increased HIV-1 vaccine efficacy against viruses with genetic signatures in Env V2 (2012)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2012-09-11
    Beschreibung: The RV144 trial demonstrated 31% vaccine efficacy at preventing human immunodeficiency virus (HIV)-1 infection. Antibodies against the HIV-1 envelope variable loops 1 and 2 (Env V1 and V2) correlated inversely with infection risk. We proposed that vaccine-induced immune responses against V1/V2 would have a selective effect against, or sieve, HIV-1 breakthrough viruses. A total of 936 HIV-1 genome sequences from 44 vaccine and 66 placebo recipients were examined. We show that vaccine-induced immune responses were associated with two signatures in V2 at amino acid positions 169 and 181. Vaccine efficacy against viruses matching the vaccine at position 169 was 48% (confidence interval 18% to 66%; P = 0.0036), whereas vaccine efficacy against viruses mismatching the vaccine at position 181 was 78% (confidence interval 35% to 93%; P = 0.0028). Residue 169 is in a cationic glycosylated region recognized by broadly neutralizing and RV144-derived antibodies. The predicted distance between the two signature sites (21 +/- 7 A) and their match/mismatch dichotomy indicate that multiple factors may be involved in the protection observed in RV144. Genetic signatures of RV144 vaccination in V2 complement the finding of an association between high V1/V2-binding antibodies and reduced risk of HIV-1 acquisition, and provide evidence that vaccine-induced V2 responses plausibly had a role in the partial protection conferred by the RV144 regimen.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3551291/" 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/PMC3551291/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rolland, Morgane -- Edlefsen, Paul T -- Larsen, Brendan B -- Tovanabutra, Sodsai -- Sanders-Buell, Eric -- Hertz, Tomer -- deCamp, Allan C -- Carrico, Chris -- Menis, Sergey -- Magaret, Craig A -- Ahmed, Hasan -- Juraska, Michal -- Chen, Lennie -- Konopa, Philip -- Nariya, Snehal -- Stoddard, Julia N -- Wong, Kim -- Zhao, Hong -- Deng, Wenjie -- Maust, Brandon S -- Bose, Meera -- Howell, Shana -- Bates, Adam -- Lazzaro, Michelle -- O'Sullivan, Annemarie -- Lei, Esther -- Bradfield, Andrea -- Ibitamuno, Grace -- Assawadarachai, Vatcharain -- O'Connell, Robert J -- deSouza, Mark S -- Nitayaphan, Sorachai -- Rerks-Ngarm, Supachai -- Robb, Merlin L -- McLellan, Jason S -- Georgiev, Ivelin -- Kwong, Peter D -- Carlson, Jonathan M -- Michael, Nelson L -- Schief, William R -- Gilbert, Peter B -- Mullins, James I -- Kim, Jerome H -- 2R37AI05465-10/AI/NIAID NIH HHS/ -- K25 AI087397/AI/NIAID NIH HHS/ -- R01 AI054165/AI/NIAID NIH HHS/ -- R37 AI054165/AI/NIAID NIH HHS/ -- UM1 AI068635/AI/NIAID NIH HHS/ -- Y01 AI2642-12/AI/NIAID NIH HHS/ -- Y1-AI-2642-12/AI/NIAID NIH HHS/ -- England -- Nature. 2012 Oct 18;490(7420):417-20. doi: 10.1038/nature11519. Epub 2012 Sep 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉US Military HIV Research Program, Silver Spring, Maryland 20910, USA. mrolland@hivresearch.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22960785" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): AIDS Vaccines/adverse effects/*immunology ; Genetic Predisposition to Disease ; HIV Antibodies/immunology ; HIV Infections/immunology/*prevention & control/*virology ; HIV-1/*genetics/*immunology ; Humans ; Molecular Sequence Data ; Phylogeny ; Randomized Controlled Trials as Topic ; Sequence Analysis, DNA ; env Gene Products, Human Immunodeficiency Virus/*genetics/*immunology
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
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  • 8
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    Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01 (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2010-07-10
    Beschreibung: During HIV-1 infection, antibodies are generated against the region of the viral gp120 envelope glycoprotein that binds CD4, the primary receptor for HIV-1. Among these antibodies, VRC01 achieves broad neutralization of diverse viral strains. We determined the crystal structure of VRC01 in complex with a human immunodeficiency virus HIV-1 gp120 core. VRC01 partially mimics CD4 interaction with gp120. A shift from the CD4-defined orientation, however, focuses VRC01 onto the vulnerable site of initial CD4 attachment, allowing it to overcome the glycan and conformational masking that diminishes the neutralization potency of most CD4-binding-site antibodies. To achieve this recognition, VRC01 contacts gp120 mainly through immunoglobulin V-gene regions substantially altered from their genomic precursors. Partial receptor mimicry and extensive affinity maturation thus facilitate neutralization of HIV-1 by natural human antibodies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2981354/" 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/PMC2981354/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Tongqing -- Georgiev, Ivelin -- Wu, Xueling -- Yang, Zhi-Yong -- Dai, Kaifan -- Finzi, Andres -- Kwon, Young Do -- Scheid, Johannes F -- Shi, Wei -- Xu, Ling -- Yang, Yongping -- Zhu, Jiang -- Nussenzweig, Michel C -- Sodroski, Joseph -- Shapiro, Lawrence -- Nabel, Gary J -- Mascola, John R -- Kwong, Peter D -- P30 AI060354/AI/NIAID NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2010 Aug 13;329(5993):811-7. doi: 10.1126/science.1192819. Epub 2010 Jul 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20616231" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): AIDS Vaccines ; Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/*immunology ; Antibody Affinity ; Antigenic Variation ; Antigens, CD4/chemistry/immunology/metabolism ; Base Sequence ; Binding Sites, Antibody ; Crystallography, X-Ray ; Epitopes/immunology ; HIV Antibodies/*chemistry/*immunology ; HIV Envelope Protein gp120/chemistry/genetics/*immunology ; HIV-1/*immunology ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Models, Molecular ; Molecular Mimicry ; Molecular Sequence Data ; Neutralization Tests ; Protein Conformation ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 9
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    Insights on continental collisional processes from GPS data: Dynamics of the peri-Adriatic belts (2018)
    Details
    Publikationsdatum: 2022-04-05
    Beschreibung: We present a new GPS velocity field covering the peri-Adriatic tectonically active belts and the entire Balkan Peninsula. From the velocities, we calculate consistent strain rate and interpolated velocity fields. Significant features of the crustal deformation include (1) the eastward motion of the northern part of the Eastern Alps together with part the Alpine foreland and Bohemian Massif toward the Pannonian Basin, (2) shortening across the Dinarides, (3) a clockwise rotation of the Albanides-Hellenides, and (4) a southward motion south of 44°N of the inner Balkan lithosphere between the rigid Apulia and Black Sea, toward the Aegean domain. Using this new velocity field, we derive the strain rate tensor to analyze the regional style of the deformation. Then, we devise a simple test based on the momentum balance equation, to investigate the role of horizontal gradients of gravitational potential energy in driving the deformation in the peri-Adriatic tectonically active mountain belts: the Eastern Alps, the Dinarides, the Albanides, and the Apennines. We show that the strain rate fields observed in the Apennines and Albanides are consistent with a fluid, with viscosity η ∼ 3×1021 Pa s, deforming in response to horizontal gradients of gravitational potential energy. Conversely, both the Dinarides and Eastern Alps are probably deforming in response to the North and North-East oriented motion of the Adria-Apulia indenter, respectively, and as a consequence of horizontal lithospheric heterogeneity.
    Beschreibung: Published
    Beschreibung: 8701–8719
    Beschreibung: 1T. Deformazione crostale attiva
    Beschreibung: JCR Journal
    Repository-Name: Istituto Nazionale di Geofisica e Vulcanologia (INGV)
    Materialart: article
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  • 10
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    Geodetic constraints on kinematics of southwestern Bulgaria from GPS and levelling data (2007)
    In:  Geological Society Special Publication 291: 143-157.
    Details
    Publikationsdatum: 2007-12-12
    Beschreibung: Southwestern Bulgaria belongs to the southern marginal parts of the central Balkan neotectonic region and borders the northern side of the highly seismic north Aegean region. The recent horizontal and vertical motion of the tectonic structures is controlled primarily by the collision stage, caused by continuing ENE palaeosubduction in the Ionian and Adriatic seas and extensional processes northwards of the North Aegean Trough. The present-day generation of small to moderate seismicity and crustal faulting suggests that the complex tectonic processes in the SW Bulgaria region are active. To monitor and study the tectonic deformation in SW Bulgaria, a global positioning system (GPS) network was established in early 2001. Analysis of GPS data from 1996 to 2004 resulted in a horizontal velocity field representing active surface deformations. Horizontal velocities at 38 GPS sites with respect to stable Eurasia are obtained. A new map of the recent vertical velocities is compiled, based on recomputed data from the repeated precise levelling for the period 19291991. We obtained evidence of recent active faulting. Based on the geological and geodetic data the SW Bulgaria is separated into five blocks with homogeneous kinematic behaviour. The average motion of each block varies from 1.3 to 3.4 mm a1, and the whole region velocity is c. 1.8{+/-}0.7 mm a1 in a direction N154{degrees} with respect to stable Eurasia. Geodetic data correlate well with the geological data on neotectonic motions in SW Bulgaria.
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