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  • American Association for the Advancement of Science (AAAS)  (5)
  • Cambridge University Press  (3)
  • 1995-1999  (8)
  • 1
    Electronic Resource
    Electronic Resource
    Inference in Models with Nearly Integrated Regressors (1995)
    New York : Cambridge University Press
    Econometric theory 11 (1995), S. 1131-1147 
    Details
    ISSN: 0266-4666
    Source: Cambridge Journals Digital Archives
    Topics: Economics
    Notes: This paper examines regression tests of whether x forecasts y when the largest autoregressive root of the regressor is unknown. It is shown that previously proposed two-step procedures, with first stages that consistently classify x as I(1) or I(0), exhibit large size distortions when regressors have local-to-unit roots, because of asymptotic dependence on a nuisance parameter that cannot be estimated consistently. Several alternative procedures, based on Bonferroni and Scheffe methods, are therefore proposed and investigated. For many parameter values, the power loss from using these conservative tests is small.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1017/S0266466600009981
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    Paper (German National Licenses)
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  • 2
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    Molecular architecture of the rotary motor in ATP synthase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-27
    Description: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, D -- Leslie, A G -- Walker, J E -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1700-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576729" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Mitochondria/enzymology ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proton-Motive Force ; Proton-Translocating ATPases/*chemistry/metabolism ; Protons ; Saccharomyces cerevisiae/enzymology
    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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  • 3
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    Immune response and myoblasts that express Fas ligand (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, S M -- Hoffmann, A -- Le, D -- Springer, M L -- Stock, P G -- Blau, H M -- F32 HL08991/HL/NHLBI NIH HHS/ -- R01-CA59717/CA/NCI NIH HHS/ -- R01-HD18179/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1322-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411754" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/biosynthesis ; Apoptosis ; Cell Differentiation ; Cell Transplantation ; Fas Ligand Protein ; *Graft Rejection ; Immune Tolerance ; Islets of Langerhans/cytology ; *Islets of Langerhans Transplantation ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Muscle Fibers, Skeletal/*cytology/metabolism ; Muscle, Skeletal/*cytology/metabolism ; Neutrophils/*immunology ; 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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    Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, J -- Stock, D -- Jap, B -- Zwickl, P -- Baumeister, W -- Huber, R -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung fur Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725097" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Chaperonin 60/chemistry ; Computer Graphics ; Crystallography, X-Ray ; Cysteine Endopeptidases/*chemistry/metabolism ; Endopeptidases/*chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Leupeptins/chemistry/metabolism ; *Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protease Inhibitors/chemistry/metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/metabolism ; Thermoplasma/*enzymology
    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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    Proteasome from Thermoplasma acidophilum: a threonine protease (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme. Mutation of the residue to serine led to a fully active enzyme, which was over ten times more sensitive to the serine protease inhibitor 3,4-dichloroisocoumarin. In combination with the crystal structure of a proteasome-inhibitor complex, the data show that the nucleophilic attack is mediated by the amino-terminal threonine of processed beta subunits. The conservation pattern of this residue in eukaryotic sequences suggests that at least three of the seven eukaryotic beta-type subunit branches should be proteolytically inactive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemuller, E -- Lupas, A -- Stock, D -- Lowe, J -- Huber, R -- Baumeister, W -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung fur Strukturbiologie Max-Planck Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Coumarins/pharmacology ; Endopeptidases/*chemistry/metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Mutagenesis ; Protein Folding ; Sequence Alignment ; Serine Proteinase Inhibitors/pharmacology ; Thermoplasma/*enzymology
    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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    Signaling across membranes: a one and a two and a (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, J -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):370-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA. jstock@watson.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927993" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Catalysis ; Chemoreceptor Cells ; Dimerization ; *Escherichia coli Proteins ; Humans ; Ligands ; Membrane Proteins/chemistry/genetics/*metabolism ; Protein Kinases/metabolism ; Receptors, Cell Surface/chemistry/*metabolism ; Receptors, Somatotropin/chemistry/metabolism ; Signal Transduction/*physiology
    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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  • 7
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    Atmospheric 14CO2 Variations in the Equatorial Region (1995)
    Cambridge University Press
    Details
    Publication Date: 1995-01-01
    Description: We present here first results of 14CO2 monitoring at two sampling sites in the equatorial region of the South American continent (station Aychapicho, Ecuador and station Llano del Hato, Venezuela). We also include the data for two other stations representing undisturbed marine atmosphere at mid-latitudes of both hemispheres, far from large continental sources and sinks of CO2 (station Izaña, Tenerife, Spain and station Cape Grim, Tasmania). Between 1991 and 1993, 14CO2 levels in the tropical troposphere were generally higher by 2–5‰ when compared to mid-latitudes of both hemispheres. This apparent maximum of 14C in the tropics can be explained by two major factors: 1) emissions of 14C-free fossil fuel CO2, restricted mainly to mid-latitudes of the northern hemisphere; and 2) 14C depletion due to gas exchange with circumpolar Antarctic upwelling water, influencing mainly mid- and high southern latitudes. The δ14C record so far available for the Aychapicho station provides direct evidence for a regional reduction of atmospheric 14CO2 levels due to gas exchange with 14C-depleted equatorial surface ocean in the upwelling regions and dilution with the 14C-depleted CO2 released in these areas. Recurrent ENSO events, turning on and off the 14C-depleted CO2 source in the tropical Pacific, lead to relatively large temporal variations of the atmospheric 14C level in this region.
    Print ISSN: 0033-8222
    Electronic ISSN: 1945-5755
    Topics: Archaeology , Energy, Environment Protection, Nuclear Power Engineering , Geosciences
    Published by Cambridge University Press
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  • 8
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    Declining Trend in the 13C/12C Ratio of Atmospheric Carbon Dioxide from Tree Rings of South African Widdringtonia cedarbergensis (1999)
    Cambridge University Press
    Details
    Publication Date: 1999-09-01
    Description: Stable carbon isotope chronologies using tree ring wood cellulose have proved useful for developing hypotheses on climate and environment change. However, within both the Southern Hemisphere and Africa there has been very little tree-ring-based isotope research. Here we report the first high-resolution (annual) 13C/12C chronology for both Africa and the Southern Hemisphere. The 77-yr stable carbon isotope chronology was developed from six Widdringtonia cedarbergensis trees from a site in the Cedarberg Mountains, Western Cape Province, South Africa. The results indicate that 13C/12C ratios are not different from 1900 to 1949. After 1949, however, values become significantly more negative to 1977. The isotopic record from the pooled trees at the Die Bos site does not correlate with rainfall. This correlation is not significant even when the Widdringtonia stable carbon isotope record is de-trended for the anthropogenic CO2 contribution. The Widdringtonia record does, however, correlate significantly with atmospheric 13C/12C CO2 values derived from ice core data, tree ring 13C/12C chronologies from the Northern Hemisphere, and recent Southern Hemisphere records.
    Print ISSN: 0033-5894
    Electronic ISSN: 1096-0287
    Topics: Geography , Geosciences
    Published by Cambridge University Press
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