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  • American Association for the Advancement of Science  (21)
  • American Association for the Advancement of Science (AAAS)  (18)
  • 1995-1999  (39)
  • 1
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    Association of malaria parasite population structure, HLA, and immunological antagonism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Host-parasite coevolution has been likened to a molecular arms race, with particular parasite genes evolving to evade specific host defenses. Study of the variants of an antigenic epitope of Plasmodium falciparum that induces a cytotoxic T cell response supports this view. In African children with malaria, the variants present are influenced by the presence of a human leukocyte antigen (HLA) type that restricts the immune response to this epitope. The distribution of parasite variants may be further influenced by the ability of cohabiting parasite strains to facilitate each other's survival by down-regulating cellular immune responses, using altered peptide ligand antagonism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilbert, S C -- Plebanski, M -- Gupta, S -- Morris, J -- Cox, M -- Aidoo, M -- Kwiatkowski, D -- Greenwood, B M -- Whittle, H C -- Hill, A V -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1173-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Windmill Road, Oxford OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469800" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antigens, Protozoan/genetics/*immunology ; Biological Evolution ; Child ; Epitopes ; Evolution, Molecular ; Gambia ; Genes, Protozoan ; Genetic Variation ; HLA-B35 Antigen/*immunology ; Humans ; Ligands ; Malaria, Falciparum/*immunology/parasitology ; Models, Biological ; Plasmodium falciparum/genetics/*immunology ; Protozoan Proteins/genetics/*immunology ; T-Lymphocytes, Cytotoxic/*immunology
    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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  • 2
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    Equatorius: a new hominoid genus from the Middle Miocene of Kenya (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-28
    Description: A partial hominoid skeleton just older than 15 million years from sediments in the Tugen Hills of north central Kenya mandates a revision of the hominoid genus Kenyapithecus, a possible early member of the great ape-human clade. The Tugen Hills specimen represents a new genus, which also incorporates all material previously referable to Kenyapithecus africanus. The new taxon is derived with respect to earlier Miocene hominoids but is primitive with respect to the younger species Kenyapithecus wickeri and therefore is a late member of the stem hominoid radiation in the East African Miocene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ward, S -- Brown, B -- Hill, A -- Kelley, J -- Downs, W -- New York, N.Y. -- Science. 1999 Aug 27;285(5432):1382-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, Northeastern Ohio Universities College of Medicine, Post Office Box 95, Rootstown, OH 44272, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10464093" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone and Bones/anatomy & histology ; Dentition ; *Fossils ; History, Ancient ; Hominidae/anatomy & histology/*classification ; Humans ; Kenya ; Mandible/anatomy & histology ; Paleodontology ; Skeleton ; Terminology as Topic ; Tooth/anatomy & histology
    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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  • 3
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    Distinct mechanism for antidepressant activity by blockade of central substance P receptors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: The localization of substance P in brain regions that coordinate stress responses and receive convergent monoaminergic innervation suggested that substance P antagonists might have psychotherapeutic properties. Like clinically used antidepressant and anxiolytic drugs, substance P antagonists suppressed isolation-induced vocalizations in guinea pigs. In a placebo-controlled trial in patients with moderate to severe major depression, robust antidepressant effects of the substance P antagonist MK-869 were consistently observed. In preclinical studies, substance P antagonists did not interact with monoamine systems in the manner seen with established antidepressant drugs. These findings suggest that substance P may play an important role in psychiatric disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kramer, M S -- Cutler, N -- Feighner, J -- Shrivastava, R -- Carman, J -- Sramek, J J -- Reines, S A -- Liu, G -- Snavely, D -- Wyatt-Knowles, E -- Hale, J J -- Mills, S G -- MacCoss, M -- Swain, C J -- Harrison, T -- Hill, R G -- Hefti, F -- Scolnick, E M -- Cascieri, M A -- Chicchi, G G -- Sadowski, S -- Williams, A R -- Hewson, L -- Smith, D -- Carlson, E J -- Hargreaves, R J -- Rupniak, N M -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1640-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Merck Research Laboratories, West Point, PA 19456, USA. Mark_Kramer@merck.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733503" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Amygdala/drug effects/metabolism ; Animals ; Antidepressive Agents, Second-Generation/adverse ; effects/metabolism/pharmacology/*therapeutic use ; Behavior, Animal/drug effects ; Brain/drug effects/metabolism ; Depressive Disorder/*drug therapy/etiology/metabolism ; Female ; Gerbillinae ; Guinea Pigs ; Humans ; Male ; Middle Aged ; Morpholines/adverse effects/metabolism/pharmacology/*therapeutic use ; *Neurokinin-1 Receptor Antagonists ; Norepinephrine/physiology ; Paroxetine/therapeutic use ; Receptors, Neurokinin-1/metabolism ; Serotonin/physiology ; Stress, Psychological/drug therapy ; Substance P/*antagonists & inhibitors/metabolism ; Vocalization, Animal/drug effects
    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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  • 4
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    Fas ligand: a sensor for DNA damage critical in skin cancer etiology (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-07
    Description: DNA-damaged cells can either repair the DNA or be eliminated through a homeostatic control mechanism termed "cellular proofreading." Elimination of DNA-damaged cells after ultraviolet radiation (UVR) through sunburn cell (apoptotic keratinocyte) formation is thought to be pivotal for the removal of precancerous skin cells. Sunburn cell formation was found to be dependent on Fas ligand (FasL), a pro-apoptotic protein induced by DNA damage. Chronic exposure to UVR caused 14 of 20 (70 percent) FasL-deficient mice and 1 of 20 (5 percent) wild-type mice to accumulate p53 mutations in the epidermis. Thus, FasL-mediated apoptosis is important for skin homeostasis, suggesting that the dysregulation of Fas-FasL interactions may be central to the development of skin cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, L L -- Ouhtit, A -- Loughlin, S M -- Kripke, M L -- Ananthaswamy, H N -- Owen-Schaub, L B -- CA45623/CA/NCI NIH HHS/ -- CA52457/CA/NCI NIH HHS/ -- F32 AI09351/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 6;285(5429):898-900.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, University of Texas, M. D. Anderson Cancer Center, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10436160" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/genetics/physiology ; Apoptosis ; *DNA Damage ; Epidermis/*cytology/metabolism/radiation effects ; Fas Ligand Protein ; *Genes, p53 ; Keratinocytes/*cytology/metabolism/radiation effects ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mice, Inbred C3H ; Mutation ; Skin Neoplasms/*etiology/pathology ; Ultraviolet Rays ; Up-Regulation
    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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  • 5
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    Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-19
    Description: Prion propagation involves the conversion of cellular prion protein (PrPC) into a disease-specific isomer, PrPSc, shifting from a predominantly alpha-helical to beta-sheet structure. Here, conditions were established in which recombinant human PrP could switch between the native alpha conformation, characteristic of PrPC, and a compact, highly soluble, monomeric form rich in beta structure. The soluble beta form (beta-PrP) exhibited partial resistance to proteinase K digestion, characteristic of PrPSc, and was a direct precursor of fibrillar structures closely similar to those isolated from diseased brains. The conversion of PrPC to beta-PrP in suitable cellular compartments, and its subsequent stabilization by intermolecular association, provide a molecular mechanism for prion propagation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jackson, G S -- Hosszu, L L -- Power, A -- Hill, A F -- Kenney, J -- Saibil, H -- Craven, C J -- Waltho, J P -- Clarke, A R -- Collinge, J -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1999 Mar 19;283(5409):1935-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Prion Disease Group, Department of Neurogenetics, Imperial College School of Medicine at St. Mary's, London W2 1NY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10082469" target="_blank"〉PubMed〈/a〉
    Keywords: Circular Dichroism ; Endopeptidase K/metabolism ; Humans ; Hydrogen-Ion Concentration ; Molecular Weight ; Nuclear Magnetic Resonance, Biomolecular ; Oxidation-Reduction ; PrPC Proteins/chemistry ; PrPSc Proteins/chemistry ; Prions/*chemistry ; *Protein Conformation ; Protein Folding ; Protein Isoforms/chemistry ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Solubility ; Spectrum Analysis
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  • 6
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    Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended amino-terminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamble, T R -- Yoo, S -- Vajdos, F F -- von Schwedler, U K -- Worthylake, D K -- Wang, H -- McCutcheon, J P -- Sundquist, W I -- Hill, C P -- R01 AI40333/AI/NIAID NIH HHS/ -- R01 AI43036/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):849-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346481" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Capsid/*chemistry/genetics ; Cell Line ; Cloning, Molecular ; Cloning, Organism ; Crystallography, X-Ray ; Dimerization ; HIV-1/*chemistry/genetics/physiology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptidylprolyl Isomerase/chemistry ; *Protein Conformation ; Virus Replication
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    Electronic ISSN: 1095-9203
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  • 7
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    Environmental contributions to the obesity epidemic (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: The current epidemic of obesity is caused largely by an environment that promotes excessive food intake and discourages physical activity. Although humans have evolved excellent physiological mechanisms to defend against body weight loss, they have only weak physiological mechanisms to defend against body weight gain when food is abundant. Control of portion size, consumption of a diet low in fat and energy density, and regular physical activity are behaviors that protect against obesity, but it is becoming difficult to adopt and maintain these behaviors in the current environment. Because obesity is difficult to treat, public health efforts need to be directed toward prevention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, J O -- Peters, J C -- DK38088/DK/NIDDK NIH HHS/ -- DK42549/DK/NIDDK NIH HHS/ -- DK48520/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 May 29;280(5368):1371-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Colorado Clinical Nutrition Research Unit, University of Colorado Health Sciences Center, Denver, CO 80262, USA. james.hill@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9603719" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; Body Weight ; *Diet ; Dietary Fats/administration & dosage ; Energy Metabolism ; *Exercise ; Female ; Humans ; *Hyperphagia/etiology ; *Life Style ; Male ; Obesity/*epidemiology/*etiology/genetics/prevention & control
    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
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    Gathering airs schemes for averting asteroid doom (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, D K -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1562-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777852" target="_blank"〉PubMed〈/a〉
    Keywords: *Earth (Planet) ; *Minor Planets
    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
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    Pacific warming unsettles ecosystems (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, D K -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1911-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17770096" target="_blank"〉PubMed〈/a〉
    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
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    Copying articles (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, R -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):773.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846514" target="_blank"〉PubMed〈/a〉
    Keywords: Copyright/*legislation & jurisprudence ; Periodicals as Topic ; *Societies, Scientific ; United States
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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