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  • 2020-2024  (5)
  • 1995-1999  (48)
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  • 1
    Monograph available for loan
    Monograph available for loan
    Information graphics : a comprehensive illustrated reference (1999)
    New York [u.a.] : Oxford University Press
    Details Availability
    Call number: M 08.0276
    Description / Table of Contents: This text describes the full range of charts, graphs, maps, diagrams and tables used daily to manage, analyze and communicate information. It features over 3000 illustrations, acting as a source on presenting information for anyone who writes or designs reports.
    Type of Medium: Monograph available for loan
    Pages: 448 S.
    ISBN: 9780195135329
    Location: Upper compact magazine
    Branch Library: GFZ Library
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    BOOK
    Link to Library Catalog
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  • 2
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    Heat flow and thermal regime in the Guaymas Basin, Gulf of California: Estimates of conductive and advective heat transport (2023)
    Details
    Publication Date: 2024-03-22
    Description: 〈title xmlns:mml="http://www.w3.org/1998/Math/MathML"〉Abstract〈/title〉〈p xmlns:mml="http://www.w3.org/1998/Math/MathML" xml:lang="en"〉Heat flow is estimated at eight sites drilled int the Guaymas Basin, Gulf of California, during the International Ocean Discovery Program Expedition 385. The expedition sought to understand the thermal regime of the basin and heat transfer between off‐axis sills intruding the organic‐rich sediments of the Guaymas Basin, and the basin floor. The distinct sedimentation rates, active tectonics, and magmatism make the basin interesting for scientific discoveries. Results show that sedimentation corrected heat flow values range 119–221 mW/m〈sup〉2〈/sup〉 in the basin and 257–1003 mW/m〈sup〉2〈/sup〉 at the site of a young sill intrusion, denominated Ringvent. Thermal analysis shows that heat in the Guaymas Basin is being dissipated by conduction for plate ages >0.2 Ma, whereas younger plate ages are in a state of transient cooling by both conduction and advection. Drilling sites show that Ringvent is an active sill being cooled down slowly by circulating fluids with discharge velocities of 10–200 mm/yr. Possible recharge sites are located ca. 1 km away from the sill's border. Modelling of the heat output at Ringvent indicates a sill thickness of ca. 240 m. A simple order‐of‐magnitude model predicts that relatively small amounts of magma are needed to account for the elevated heat flow in non‐volcanic, sediment‐filled rifts like the central and northern Gulf of California in which heating of the upper crust is achieved via advection by sill emplacement and hydrothermal circulation. Multiple timescales of cooling control the crustal, chemical and biological evolution of the Guaymas Basin. Here, we recognize at least four timescales: the time interval between intrusions (ca. 10〈sup〉3〈/sup〉 yr), the thermal relaxation time of sills (ca. 10〈sup〉4〈/sup〉 yr), the characteristic cooling time of the sediments (ca. 10〈sup〉5〈/sup〉 yr), and the cooling of the entire crust at geologic timescales.〈/p〉
    Description: Centro de Investigación Científica y de Educación Superior de Ensenada, Baja California http://dx.doi.org/10.13039/501100003089
    Description: German Research Center for Geosciences
    Description: https://web.iodp.tamu.edu/LORE/
    Description: https://mlp.ldeo.columbia.edu/logdb/scientific_ocean_drilling/
    Keywords: ddc:551.1 ; Guyamas Basin ; Heat Flow ; Heat Transfer ; IODP Expedition 385
    Language: English
    Type: doc-type:article
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    CITATION GEO-LEO
  • 3
    Electronic Resource
    Electronic Resource
    Chemical Modification and Site-Directed Mutagenesis Studies of Rat 3-Hydroxyisobutyrate Dehydrogenase (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 4231-4237 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00013a012
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  • 4
    Electronic Resource
    Electronic Resource
    Two-Dipole Magnetic-Field Density Functional Theory (1995)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 99 (1995), S. 2724-2726 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100009a031
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  • 5
    Electronic Resource
    Electronic Resource
    The exchange energy functional in a weak magnetic field (1998)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 109 (1998), S. 2609-2613 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: A density functional theory for the Kohn–Sham exchange energy of a bounded, closed shell system in a weak, uniform, magnetic field is presented. The form obtained vanishes when the electron density is radial and, unlike the unscreened exchange energy of a locally uniform electron gas, does not diverge due to the Coulomb interaction. The role of the exchange-correlation functional in the context of magnetic response theory is also examined. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.476874
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  • 6
    Electronic Resource
    Electronic Resource
    Implications of parity conservation for superpositions of chiral states (1998)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 109 (1998), S. 3713-3720 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: In this paper, we consider how parity conservation limits the type of superpositions of chiral states that can be created and detected. We also show how spontaneous emission can cause the left and right hands of the superposition to become coupled to different states of the radiation field. This coupling, aside from being an interesting effect in its own right, helps to enforce the restrictions that parity conservation places upon superpositions of chiral states. Finally, we outline an analogy that exists between aspects of this work and the Einstein, Podolsky, Rosen paradox. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.476972
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  • 7
    Electronic Resource
    Electronic Resource
    Hypersensitivity to nonsteroidal anti-inflammatory drugs (1995)
    [s.l.] : Nature Publishing Group
    Nature medicine 1 (1995), S. 2-4 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] To the editor — Nonsteroidal anti-inflammatory drugs (NSAIDs) are a widely used class of compounds that are prescribed as analgesic, antipyretic and anti-inflammatory agents1. NSAIDs can elicit potentially fatal hypersensitivity reactions (including anaphylaxis, bronchospasm and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0195-2b
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  • 8
    Electronic Resource
    Electronic Resource
    Murine class I major histocompatibility complex H–2Dd: expression, refolding and crystallization (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 260-262 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A truncated soluble form of the murine class I major histocompatibility antigen complex H–2Dd was cloned using an Escherichia coli based system. It was expressed, refolded in vitro and crystallized in a complex with murine β2 microglobulin and the peptide RGPGRAFVTI from the V3-loop of the gp160 HIV-1 protein. Crystals belonging to the space group P212121 with cell dimensions a = 51.3, b = 92.5, c = 108.8 Å were obtained using two different crystallization conditions. The crystals contain one complex per asymmetric unit and diffract to at least 2.4 Å resolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998005265
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  • 9
    Electronic Resource
    Electronic Resource
    Preparations of Ψ-peptide bond and peptide-aldehyde inhibitors of atrial granule serine proteinase, a candidate processing enzyme of pro-atrial natriuretic factor (1995)
    Springer
    The protein journal 14 (1995), S. 431-440 
    Details
    ISSN: 1573-4943
    Keywords: ANF ; atrial natriuretic factors ; atrial granule serine proteinase ; peptide inhibitors ; peptide aldehydes ; processing enzymes ; pseudo-bond inhibitors ; serine proteinase ; Swern oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Pseudo-peptide bond inhibitors (ψ-bond inhibitors) and peptide-aldehyde inhibitors of atrial granule serine proteinase, the candidate processing enzyme of pro-atrial natrieuretic factor, are prepared in high yield and purity by novel synthetic routes. The ψ-bond compounds retain essential residues for enzyme binding, but place the enzyme inhibition site in the midst of the peptide sequence. Thus, Bz-APR-ψ-LR and Bz-APR-ψ-SLRR can be considered “readthrough inhibitors” of atrial granule serine proteinase. The most potent ψ-peptide, Bz-APR-ψ-SLRR (IC50=250 ΜM), is about fivefold less potent than the best peptide-aldehyde inhibitor (EACA-APR-CHO), and both the ψ-bond and peptide-aldehyde compounds are competitive, reversible inhibitors of the enzyme. The ψ-bond peptides containing two C-terminal Arg residues are three-to tenfold more potent than the analogous compounds containing only one C-terminal Arg residue, confirming the importance of both Arg residues in the enzyme processing recognition site. As expected, because of their moderate potencies, the ψ-peptides are not useful affinity ligands for purification of atrial granule serine proteinase, but both peptide aldehydes are effective affinity ligands [Damodaran and Harris (1995),J. Protein Chem., this issue].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888137
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  • 10
    Electronic Resource
    Electronic Resource
    N-terminal sequence analysis of atrial granule serine proteinase purified by affinity chromatography (1995)
    Springer
    The protein journal 14 (1995), S. 441-449 
    Details
    ISSN: 1573-4943
    Keywords: Affinity chromatography ; ANF ; atrial natriuretic factors ; atrial granule serine proteinase ; N-terminal sequence determination ; peptide inhibitors ; peptide aldehydes ; processing enzymes ; protein purification ; serine proteinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Atrial granule serine proteinase is considered the leading candidate endoproteolytic processing enzyme of pro-atrial natriuretic factor. Its cleavage specificity is directed toward a monobasic amino acid processing site, and as such, the atrial enzyme is distinguished from the family of prohormone convertases which act at dibasic amino acid processing sites. To delineate the molecular mechanisms which distinguish monobasic from dibasic amino acid-directed processing enzymes, pure atrial enzyme is needed for sequence determination leading to molecular cloning, and for preparation of antisera. An affinity chromatography purification scheme seemed a logical modification of our established procedures to yield suitable amounts of enzyme for further studies. Surprisingly, pseudo-peptide bond inhibitors of the atrial enzyme [Damodaran and Harris (1995),J. Protein Chem., this issue] formed ineffective affinity ligands, even though these compounds contain essential residues on either side of what would be the scissile bond in a peptide substrate. On the other hand, tripeptide aldehydes (based on the substrate recognition sequence of the atrial enzyme) linked to Sepharose formed effective affinity matrices, permitting purification of the enzyme in a single step from a subcellular fraction enriched for atrial granules and lysosomes. Hence, the enzyme was purified 2000-fold in 90% overall yield, and subjected to N-terminal sequence analysis through 26 residues. The sequence determined, XXPEAAGLPG[R, L]GNPVP[F, G]R[Q, I]XY[G, E]XR(N, A]V, indicates that the atrial enzyme is unique, showing little sequence homology to other proteins in the database.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888138
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