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  • Animals  (1,183)
  • EARTH RESOURCES AND REMOTE SENSING  (925)
  • 1990-1994  (754)
  • 1980-1984  (1,354)
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  • 11
    Publication Date: 1992-02-28
    Description: Many organisms construct structural ceramic (biomineral) composites from seemingly mundane materials; cell-mediated processes control both the nucleation and growth of mineral and the development of composite microarchitecture. Living systems fabricate biocomposites by: (i) confining biomineralization within specific subunit compartments; (ii) producing a specific mineral with defined crystal size and orientation; and (iii) packaging many incremental units together in a moving front process to form fully densified, macroscopic structures. By adapting biological principles, materials scientists are attempting to produce novel materials. To date, neither the elegance of the biomineral assembly mechanisms nor the intricate composite microarchitectures have been duplicated by nonbiological processing. However, substantial progress has been made in the understanding of how biomineralization occurs, and the first steps are now being taken to exploit the basic principles involved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heuer, A H -- Fink, D J -- Laraia, V J -- Arias, J L -- Calvert, P D -- Kendall, K -- Messing, G L -- Blackwell, J -- Rieke, P C -- Thompson, D H -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1098-105.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Matrix ; Calcification, Physiologic ; *Ceramics ; Chickens ; Crystallography
    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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  • 12
    Publication Date: 1994-09-02
    Description: As a step toward developing poliovirus as a vaccine vector, poliovirus recombinants were constructed by fusing exogenous peptides (up to 400 amino acids) and an artificial cleavage site for viral protease 3Cpro to the amino terminus of the viral polyprotein. Viral replication proceeded normally. An extended polyprotein was produced in infected cells and proteolytically processed into the complete array of viral proteins plus the foreign peptide, which was excluded from mature virions. The recombinants retained exogenous sequences through successive rounds of replication in culture and in vivo. Infection of animals with recombinants elicited a humoral immune response to the foreign peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andino, R -- Silvera, D -- Suggett, S D -- Achacoso, P L -- Miller, C J -- Baltimore, D -- Feinberg, M B -- AI22346/AI/NIAID NIH HHS/ -- AI35545/AI/NIAID NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073288" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Bacterial/biosynthesis ; Antibodies, Viral/biosynthesis ; Antigens, Bacterial/genetics/immunology ; Antigens, Viral/genetics/immunology ; Base Sequence ; Cloning, Molecular ; *Genetic Engineering ; Genetic Vectors ; HeLa Cells ; Humans ; Macaca fascicularis ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Poliovirus/*genetics/immunology/physiology ; Poliovirus Vaccine, Oral/*genetics ; *Protein Biosynthesis ; Proteins/metabolism ; Recombinant Proteins/biosynthesis/metabolism ; Vaccines, Synthetic/genetics/*immunology ; Virus Replication
    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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  • 13
    Publication Date: 1993-12-24
    Description: A human Wilms tumor cell line (RM1) was developed to test the tumor suppressor activity of WT1, a zinc finger transcription factor that is expressed in the developing human kidney and is mutationally inactivated in a subset of Wilms tumors. Transfection of each of four wild-type WT1 isoforms suppressed the growth of RM1 cells. The endogenous WT1 transcript in these cells was devoid of exon 2 sequences, a splicing alteration that was also detected in varying amounts in all Wilms tumors tested but not in normal kidney. Production of this abnormal transcript, which encodes a functionally altered protein, may represent a distinct mechanism for inactivating WT1 in Wilms tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haber, D A -- Park, S -- Maheswaran, S -- Englert, C -- Re, G G -- Hazen-Martin, D J -- Sens, D A -- Garvin, A J -- CA37887/CA/NCI NIH HHS/ -- CA58596/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2057-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Massachusetts General Hospital Cancer Center, Boston 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266105" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division/genetics ; DNA-Binding Proteins/biosynthesis/*genetics/physiology ; Genes, Wilms Tumor/genetics/*physiology ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasm Transplantation ; RNA, Messenger/genetics ; Tumor Cells, Cultured ; WT1 Proteins ; Wilms Tumor/*genetics/*pathology
    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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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-12-17
    Description: Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg. The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, A -- McRee, D E -- Vacquier, V D -- Stout, C D -- HD12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1864-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037-1093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266073" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Computer Graphics ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Mollusca ; Mucoproteins/*chemistry/metabolism ; Protein Structure, Secondary ; Vitelline Membrane/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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  • 15
    Publication Date: 1994-06-24
    Description: Fossils and artifacts recovered from the middle Awash Valley of Ethiopia's Afar depression sample the Middle Pleistocene transition from Homo erectus to Homo sapiens. Ar/Ar ages, biostratigraphy, and tephrachronology from this area indicate that the Pleistocene Bodo hominid cranium and newer specimens are approximately 0.6 million years old. Only Oldowan chopper and flake assemblages are present in the lower stratigraphic units, but Acheulean bifacial artifacts are consistently prevalent and widespread in directly overlying deposits. This technological transition is related to a shift in sedimentary regime, supporting the hypothesis that Middle Pleistocene Oldowan assemblages represent a behavioral facies of the Acheulean industrial complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, J D -- de Heinzelin, J -- Schick, K D -- Hart, W K -- White, T D -- WoldeGabriel, G -- Walter, R C -- Suwa, G -- Asfaw, B -- Vrba, E -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1907-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009220" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ethiopia ; *Fossils ; Geology/history ; History, Ancient ; Hominidae/*anatomy & histology ; Humans ; Skull/anatomy & histology
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  • 16
    Publication Date: 1992-03-13
    Description: Leukemia inhibitory factor (LIF) and interleukin-6 (IL-6) are multifunctional cytokines with many similar activities. LIF is structurally and functionally related to another cytokine, Oncostatin M (OSM), that binds to the high-affinity LIF receptor but not to the low-affinity LIF receptor. A complementary DNA was isolated that encodes the high-affinity converting subunit of the LIF receptor. The converter conferred high-affinity binding of both LIF and OSM when expressed with the low-affinity LIF receptor and is identical to the signal transducing subunit of the IL-6 receptor, gp130. The gp130 subunit alone confers low-affinity binding of OSM when expressed in COS-7 cells. This receptor system resembles the high-affinity receptors for granulocyte-macrophage colony-stimulating factor, IL-3, and IL-5, which share a common subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gearing, D P -- Comeau, M R -- Friend, D J -- Gimpel, S D -- Thut, C J -- McGourty, J -- Brasher, K K -- King, J A -- Gillis, S -- Mosley, B -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1434-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Research and Development Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1542794" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Binding, Competitive ; Cell Line, Transformed ; Cytokine Receptor gp130 ; Growth Inhibitors/*metabolism ; Interleukin-6/*metabolism ; Leukemia Inhibitory Factor ; Lymphokines/*metabolism ; Membrane Glycoproteins/*metabolism ; Oncostatin M ; Peptides/*metabolism ; Radioligand Assay ; *Receptors, Cytokine ; Receptors, Immunologic/*metabolism ; Receptors, OSM-LIF ; Recombinant Proteins/metabolism ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
    Publication Date: 1993-07-16
    Description: The cytoplasmic tyrosine kinase, Bruton's tyrosine kinase (Btk, formerly bpk or atk), is crucial for B cell development. Loss of kinase activity results in the human immunodeficiency, X-linked agammaglobulinemia, characterized by a failure to produce B cells. In the murine X-linked immunodeficiency (XID), B cells are present but respond abnormally to activating signals. The Btk gene, btk, was mapped to the xid region of the mouse X chromosome by interspecific backcross analysis. A single conserved residue within the amino terminal unique region of Btk was mutated in XID mice. This change in xid probably interferes with normal B cell signaling mediated by Btk protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rawlings, D J -- Saffran, D C -- Tsukada, S -- Largaespada, D A -- Grimaldi, J C -- Cohen, L -- Mohr, R N -- Bazan, J F -- Howard, M -- Copeland, N G -- AR36834/AR/NIAMS NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 16;261(5119):358-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332901" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*enzymology/immunology ; Base Sequence ; Cell Line ; Chromosome Mapping ; Crosses, Genetic ; Exons ; Female ; Genetic Linkage ; Immunologic Deficiency Syndromes/enzymology/*genetics/immunology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Inbred DBA ; Mice, Mutant Strains ; Molecular Sequence Data ; Protein-Tyrosine Kinases/chemistry/*genetics/metabolism ; *X Chromosome
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  • 18
    Publication Date: 1983-12-23
    Description: Endotoxin-free thymosin fraction 5 elevated corticotropin, beta-endorphin, and cortisol in a dose- and time-dependent fashion when administered intravenously to prepubertal cynomolgus monkeys. Two synthetic component peptides of thymosin fraction 5 had no acute effects on pituitary function, suggesting that some other peptides in thymosin fraction 5 were responsible for its corticotropin-releasing activity. In agreement with these observations, total thymectomy of juvenile macaques was associated with decreases in plasma cortisol, corticotropin, and beta-endorphin. These findings indicate that the prepubertal primate thymus contains corticotropin-releasing activity that may contribute to a physiological immunoregulatory circuit between the developing immunological and pituitary-adrenal systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Healy, D L -- Hodgen, G D -- Schulte, H M -- Chrousos, G P -- Loriaux, D L -- Hall, N R -- Goldstein, A L -- CA 24974/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Dec 23;222(4630):1353-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318312" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenocorticotropic Hormone/*blood ; Animals ; Dose-Response Relationship, Drug ; Endorphins/blood ; Female ; Hydrocortisone/blood ; Kinetics ; Macaca fascicularis ; Thymectomy ; Thymosin/analogs & derivatives/*pharmacology ; Thymus Gland/*physiology ; beta-Endorphin
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  • 19
    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; Structure-Activity Relationship
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  • 20
    Publication Date: 1984-11-30
    Description: A single recessive gene, lpr, induces an autoimmune-lymphoproliferative syndrome in several strains of mice. The lymphoid organs of lpr/lpr mice contained cells with increased amounts of myb RNA, which codes for a protein found in the nucleus. A similar human lymphoproliferative disorder also had an increase in c-myb expression. Mouse T cells induced by mitogens to proliferate did not express large amounts of myb RNA, indicating that marked myb expression is not a general feature of lymphocyte activation and proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mountz, J D -- Steinberg, A D -- Klinman, D M -- Smith, H R -- Mushinski, J F -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1087-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantibodies/*genetics ; Autoimmune Diseases/*genetics ; Female ; *Genes, Recessive ; Lymphocytes/immunology ; Lymphoproliferative Disorders/*genetics ; Mice ; Mice, Inbred Strains ; Nucleic Acid Hybridization ; *Oncogenes ; Species Specificity ; Spleen/immunology ; *Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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