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  • Animals  (12)
  • ASTRONOMY
  • LUNAR AND PLANETARY EXPLORATION
  • Solar Physics
  • American Association for the Advancement of Science (AAAS)  (12)
  • 1995-1999  (12)
  • 1980-1984
  • 1995  (12)
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (12)
Years
  • 1995-1999  (12)
  • 1980-1984
Year
  • 1
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    A middle stone age worked bone industry from Katanda, Upper Semliki Valley, Zaire (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: Three archaeological sites at Katanda on the Upper Semliki River in the Western Rift Valley of Zaire have provided evidence for a well-developed bone industry in a Middle Stone Age context. Artifacts include both barbed and unbarbed points as well as a daggerlike object. Dating by both direct and indirect means indicate an age of approximately 90,000 years or older. Together with abundant fish (primarily catfish) remains, the bone technology indicates that a complex subsistence specialization had developed in Africa by this time. The level of behavioral competence required is consistent with that of upper Paleolithic Homo sapiens sapiens. These data support an African origin of behaviorally as well as biologically modern humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yellen, J E -- Brooks, A S -- Cornelissen, E -- Mehlman, M J -- Stewart, K -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):553-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Archaeology Program, National Science Foundation, Arlington, VA 22230, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725100" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Archaeology ; *Behavior ; Democratic Republic of the Congo ; History, Ancient ; *Hominidae ; Humans
    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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    Peptide binding and presentation by mouse CD1 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-14
    Description: CD1 molecules are distantly related to the major histocompatibility complex (MHC) class I proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids. Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castano, A R -- Tangri, S -- Miller, J E -- Holcombe, H R -- Jackson, M R -- Huse, W D -- Kronenberg, M -- Peterson, P A -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542403" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigen Presentation ; Antigens, CD/chemistry/*immunology/metabolism ; Antigens, CD1 ; Cell Line ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptides/chemistry/*immunology/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection
    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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    Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-helix protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Basic helix-loop-helix (bHLH) proteins are instrumental in determining cell type during development. A bHLH protein, termed NeuroD, for neurogenic differentiation, has now been identified as a differentiation factor for neurogenesis because (i) it is expressed transiently in a subset of neurons in the central and peripheral nervous systems at the time of their terminal differentiation into mature neurons and (ii) ectopic expression of neuroD in Xenopus embryos causes premature differentiation of neuronal precursors. Furthermore, neuroD can convert presumptive epidermal cells into neurons and also act as a neuronal determination gene. However, unlike another previously identified proneural gene (XASH-3), neuroD seems competent to bypass the normal inhibitory influences that usually prevent neurogenesis in ventral and lateral ectoderm and is capable of converting most of the embryonic ectoderm into neurons. The data suggest that neuroD may participate in the terminal differentiation step during vertebrate neuronal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, J E -- Hollenberg, S M -- Snider, L -- Turner, D L -- Lipnick, N -- Weintraub, H -- New York, N.Y. -- Science. 1995 May 12;268(5212):836-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754368" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Cell Adhesion Molecules, Neuronal/biosynthesis ; Cell Differentiation/*genetics ; Cloning, Molecular ; Ectoderm/*cytology ; Gene Expression Regulation, Developmental ; *Helix-Loop-Helix Motifs/genetics ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*genetics/physiology ; Nervous System/cytology/embryology ; Neural Crest/cytology ; Neurons/*cytology/metabolism ; Sequence Alignment ; Xenopus
    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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    Zinc and Alzheimer's disease (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maggio, J E -- Esler, W P -- Stimson, E R -- Jennings, J M -- Ghilardi, J R -- Mantyh, P W -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1920-1; author reply 1921-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604269" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amyloid beta-Peptides/*metabolism ; Animals ; Humans ; Protein Binding ; Rats ; Solubility ; Zinc/*metabolism/pharmacology
    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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    Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-03
    Description: Many members of the cytokine receptor superfamily initiate intracellular signaling by activating members of the Jak family of tyrosine kinases. Activation of the same Jaks by multiple cytokines raises the question of how these cytokines activate distinct intracellular signaling pathways. Selection of particular substrates--the transcriptional activator Stat3 and protein tyrosine phosphatase PTP1D--that characterize responses to the ciliary neurotrophic factor-interleukin-6 cytokine family depended not on which Jak was activated, but was instead determined by specific tyrosine-based motifs in the receptor components--gp130 and LIFR--shared by these cytokines. Further, these tyrosine-based motifs were modular, because addition of a Stat3-specifying motif to another cytokine receptor, that for erythropoietin, caused it to activate Stat3 in a ligand-dependent fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stahl, N -- Farruggella, T J -- Boulton, T G -- Zhong, Z -- Darnell, J E Jr -- Yancopoulos, G D -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1349-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871433" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, CD ; Cell Line ; Cytokine Receptor gp130 ; DNA-Binding Proteins/*metabolism ; *Growth Inhibitors ; Interleukin-6/pharmacology ; Intracellular Signaling Peptides and Proteins ; Leukemia Inhibitory Factor ; *Lymphokines ; Membrane Glycoproteins/chemistry/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Point Mutation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Cytokine/chemistry/*metabolism ; Receptors, OSM-LIF ; Recombinant Fusion Proteins/metabolism ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/*metabolism ; 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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  • 6
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    Participation of the protein Go in multiple aspects of behavior in C. elegans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: The goa-1 gene encoding the alpha subunit of the heterotrimeric guanosine triphosphate-binding protein (G protein) Go from Caenorhabditis elegans is expressed in most neurons, and in the muscles involved in egg laying and male mating. Reduction-of-function mutations in goa-1 caused a variety of behavioral defects including hyperactive movement, premature egg laying, and male impotence. Expression of the activated Go alpha subunit (G alpha o) in transgenic nematodes resulted in lethargic movement, delayed egg laying, and reduced mating efficiency. Induced expression of activated G alpha o in adults was sufficient to cause these phenotypes, indicating that G alpha o mediates behavior through its role in neuronal function and the functioning of specialized muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, J E -- Korswagen, H C -- Liu, K S -- Hajdu-Cronin, Y M -- Simon, M I -- Plasterk, R H -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; Disorders of Sex Development ; Female ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Molecular Sequence Data ; Movement ; Muscles/innervation/physiology ; Mutation ; Neurons/physiology ; Oviposition ; Phenotype ; Serotonin/pharmacology ; Sexual Behavior, Animal
    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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  • 7
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    Simultaneous identification of bacterial virulence genes by negative selection (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: An insertional mutagenesis system that uses transposons carrying unique DNA sequence tags was developed for the isolation of bacterial virulence genes. The tags from a mixed population of bacterial mutants representing the inoculum and bacteria recovered from infected hosts were detected by amplification, radiolabeling, and hybridization analysis. When applied to a murine model of typhoid fever caused by Salmonella typhimurium, mutants with attenuated virulence were revealed by use of tags that were present in the inoculum but not in bacteria recovered from infected mice. This approach resulted in the identification of new virulence genes, some of which are related to, but functionally distinct from, the inv/spa family of S. typhimurium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hensel, M -- Shea, J E -- Gleeson, C -- Jones, M D -- Dalton, E -- Holden, D W -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):400-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Infectious Diseases and Bacteriology, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618105" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *DNA Transposable Elements ; *Genes, Bacterial ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Mutagenesis, Insertional ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Salmonella Infections, Animal/*microbiology ; Salmonella typhimurium/genetics/*pathogenicity ; Sequence Tagged Sites ; Virulence/genetics
    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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    Contribution of STAT SH2 groups to specific interferon signaling by the Jak-STAT pathway (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-03
    Description: In response to specific ligands, various STAT proteins (signal transducers and activators of transcription) are phosphorylated on tyrosine by Jak protein kinases and translocated to the nucleus to direct gene transcription. Selection of a STAT at the interferon gamma receptor as well as specific STAT dimer formation depended on the presence of particular SH2 groups (phosphotyrosine-binding domains), whereas the amino acid sequence surrounding the phosphorylated tyrosine on the STAT could vary. Thus, SH2 groups in STAT proteins may play crucial roles in specificity at the receptor kinase complex and in subsequent dimerization, whereas the kinases are relatively nonspecific.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heim, M H -- Kerr, I M -- Stark, G R -- Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- AI34420/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1347-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; DNA-Binding Proteins/chemistry/*metabolism ; Interferon-alpha/*pharmacology ; Interferon-gamma/*pharmacology ; Janus Kinase 1 ; Janus Kinase 2 ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Proteins/metabolism ; *Proto-Oncogene Proteins ; Receptors, Interferon/metabolism ; Recombinant Fusion Proteins/metabolism ; STAT1 Transcription Factor ; Signal Transduction ; Trans-Activators/chemistry/*metabolism ; 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
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    Separation of caveolae from associated microdomains of GPI-anchored proteins (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: In situ coating of the surface of endothelial cells in rat lung with cationic colloidal silica particles was used to separate caveolae from detergent-insoluble membranes rich in glycosyl phosphatidylinositol (GPI)-anchored proteins but devoid of caveolin. Immunogold electron microscopy showed that ganglioside GM1-enriched caveolae associated with an annular plasmalemmal domain enriched in GPI-anchored proteins. The purified caveolae contained molecular components required for regulated transport, including various lipid-anchored signaling molecules. Such specialized distinct microdomains may exist separately or together in the plasma membrane to organize signaling molecules and to process surface-bound ligands differentially.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schnitzer, J E -- McIntosh, D P -- Dvorak, A M -- Liu, J -- Oh, P -- AI33372/AI/NIAID NIH HHS/ -- HL43278/HL/NHLBI NIH HHS/ -- HL52766/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1435-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Harvard Medical School, Beth Israel Hospital, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660128" target="_blank"〉PubMed〈/a〉
    Keywords: 5'-Nucleotidase/analysis ; Animals ; Caveolin 1 ; *Caveolins ; Cell Fractionation ; Cell Membrane/*chemistry/*ultrastructure ; Colloids ; Detergents ; Endothelium, Vascular/ultrastructure ; Glycosylphosphatidylinositols/*analysis ; Membrane Proteins/*analysis ; Microscopy, Immunoelectron ; Rats ; Receptors, Cell Surface/analysis ; Receptors, Urokinase Plasminogen Activator ; Signal Transduction ; Silicon Dioxide ; Solubility
    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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    Receptor endocytosis and dendrite reshaping in spinal neurons after somatosensory stimulation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-16
    Description: In vivo somatosensory stimuli evoked the release of substance P from primary afferent neurons that terminate in the spinal cord and stimulated endocytosis of substance P receptors in rat spinal cord neurons. The distal dendrites that showed substance P receptor internalization underwent morphological reorganization, changing from a tubular structure to one characterized by swollen varicosities connected by thin segments. This internalization and dendritic structural reorganization provided a specific image of neurons activated by substance P. Thus receptor internalization can drive reversible structural changes in central nervous system neurons in vivo. Both of these processes may be involved in neuronal plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mantyh, P W -- DeMaster, E -- Malhotra, A -- Ghilardi, J R -- Rogers, S D -- Mantyh, C R -- Liu, H -- Basbaum, A I -- Vigna, S R -- Maggio, J E -- NS14627/NS/NINDS NIH HHS/ -- NS21445/NS/NINDS NIH HHS/ -- NS23970/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1629-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Neurobiology Laboratory, Veterans Administration Medical Center, Minneapolis, MN 55417, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539937" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Capsaicin/pharmacology ; Dendrites/metabolism/*ultrastructure ; *Endocytosis ; GTP-Binding Proteins/metabolism ; Male ; Neuronal Plasticity ; Neurons/*metabolism/ultrastructure ; Physical Stimulation ; Rats ; Rats, Sprague-Dawley ; Receptors, Neurokinin-1/*metabolism ; Spinal Cord/cytology/*metabolism ; Substance P/pharmacology
    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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