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  • Animals  (126)
  • METEOROLOGY AND CLIMATOLOGY
  • SOLAR PHYSICS
  • 2005-2009
  • 1995-1999  (169)
  • 1980-1984
  • 1925-1929
  • 1995  (169)
Collection
Keywords
Publisher
Years
  • 2005-2009
  • 1995-1999  (169)
  • 1980-1984
  • 1925-1929
Year
  • 1
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    An STS-based map of the human genome (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: A physical map has been constructed of the human genome containing 15,086 sequence-tagged sites (STSs), with an average spacing of 199 kilobases. The project involved assembly of a radiation hybrid map of the human genome containing 6193 loci and incorporated a genetic linkage map of the human genome containing 5264 loci. This information was combined with the results of STS-content screening of 10,850 loci against a yeast artificial chromosome library to produce an integrated map, anchored by the radiation hybrid and genetic maps. The map provides radiation hybrid coverage of 99 percent and physical coverage of 94 percent of the human genome. The map also represents an early step in an international project to generate a transcript map of the human genome, with more than 3235 expressed sequences localized. The STSs in the map provide a scaffold for initiating large-scale sequencing of the human genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hudson, T J -- Stein, L D -- Gerety, S S -- Ma, J -- Castle, A B -- Silva, J -- Slonim, D K -- Baptista, R -- Kruglyak, L -- Xu, S H -- Hu, X -- Colbert, A M -- Rosenberg, C -- Reeve-Daly, M P -- Rozen, S -- Hui, L -- Wu, X -- Vestergaard, C -- Wilson, K M -- Bae, J S -- Maitra, S -- Ganiatsas, S -- Evans, C A -- DeAngelis, M M -- Ingalls, K A -- Nahf, R W -- Horton, L T Jr -- Anderson, M O -- Collymore, A J -- Ye, W -- Kouyoumjian, V -- Zemsteva, I S -- Tam, J -- Devine, R -- Courtney, D F -- Renaud, M T -- Nguyen, H -- O'Connor, T J -- Fizames, C -- Faure, S -- Gyapay, G -- Dib, C -- Morissette, J -- Orlin, J B -- Birren, B W -- Goodman, N -- Weissenbach, J -- Hawkins, T L -- Foote, S -- Page, D C -- Lander, E S -- HG00017/HG/NHGRI NIH HHS/ -- HG00098/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1945-54.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead-MIT Center for Genome Research, Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533086" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Chromosome Mapping ; Chromosomes, Artificial, Yeast ; Databases, Factual ; Gene Expression ; Genetic Markers ; *Genome, Human ; *Human Genome Project ; Humans ; Hybrid Cells ; Polymerase Chain Reaction ; *Sequence Analysis, DNA ; *Sequence Tagged Sites
    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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  • 2
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    Liposomes revisited (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lasic, D D -- Papahadjopoulos, D -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1275-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MegaBios Corporation, Burlingame, CA 94010.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871422" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Doxorubicin/administration & dosage ; *Drug Carriers ; *Genetic Therapy ; Humans ; Lipid Bilayers/chemistry ; *Liposomes/chemistry/pharmacokinetics ; Neoplasms/drug therapy ; 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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    Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: Fertilization is initiated by the species-specific binding of sperm to the extracellular coat of the egg. One sperm receptor for the mouse egg is beta-1,4-galactosyltransferase (GalTase), which binds O-linked oligosaccharides on the egg coat glycoprotein ZP3. ZP3 binding induces acrosomal exocytosis through the activation of a pertussis toxin-sensitive heterotrimeric guanine nucleotide-binding protein (G protein). The cytoplasmic domain of sperm surface GalTase bound to and activated a heterotrimeric G protein complex that contained the Gi alpha subunit. Aggregation of GalTase by multivalent ligands elicited G protein activation. Sperm from transgenic mice that overexpressed GalTase had higher rates of G protein activation than did wild-type sperm, which rendered transgenic sperm hypersensitive to their ZP3 ligand. Thus, the cytoplasmic domain of cell surface GalTase appears to enable it to function as a signal-transducing receptor for extracellular oligosaccharide ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, X -- Dubois, D H -- Miller, D J -- Shur, B D -- R01 HD22590/HD/NICHD NIH HHS/ -- R01 HD23479/HD/NICHD NIH HHS/ -- T32 HD07324/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569899" target="_blank"〉PubMed〈/a〉
    Keywords: Acrosome/physiology ; Adenosine Diphosphate Ribose/metabolism ; Amino Acid Sequence ; Animals ; Cell Membrane/enzymology/metabolism ; Egg Proteins/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Ligands ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; N-Acetyllactosamine Synthase/*metabolism ; Peptide Fragments/metabolism ; Pertussis Toxin ; *Receptors, Cell Surface ; Signal Transduction ; Spermatozoa/enzymology/*metabolism ; Virulence Factors, Bordetella/pharmacology ; Zona Pellucida/*chemistry
    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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    Inhibition of transcription elongation by the VHL tumor suppressor protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Germline mutations in the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of tumors, including renal carcinoma, hemangioblastoma of the central nervous system, and pheochromocytoma. Here, a cellular transcription factor, Elongin (SIII), is identified as a functional target of the VHL protein. Elongin (SIII) is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C) that activate transcription elongation by RNA polymerase II. The VHL protein was shown to bind tightly and specifically to the Elongin B and C subunits and to inhibit Elongin (SIII) transcriptional activity in vitro. These findings reveal a potentially important transcriptional regulatory network in which the VHL protein may play a key role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duan, D R -- Pause, A -- Burgess, W H -- Aso, T -- Chen, D Y -- Garrett, K P -- Conaway, R C -- Conaway, J W -- Linehan, W M -- Klausner, R D -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1402-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Urologic Oncology Section, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Gene Expression Regulation ; *Genes, Tumor Suppressor ; HeLa Cells ; Humans ; *Ligases ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics/*metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Transcription Factors/chemistry/isolation & purification/*metabolism ; *Transcription, Genetic ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/*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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  • 5
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    Adaptive evolution of color vision genes in higher primates (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: The intron 4 sequences of the three polymorphic alleles at the X-linked color photo-pigment locus in the squirrel monkey and the marmoset reveal that the alleles in each species are exceptionally divergent. The data further suggest either that each triallelic system has arisen independently in these two New World monkey lineages, or that in each species at least seven deletions and insertions (14 in the two species) in intron 4 have been transferred and homogenized among the alleles by gene conversion or recombination. In either case, the alleles in each species apparently have persisted more than 5 million years and probably have been maintained by overdominant selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shyue, S K -- Hewett-Emmett, D -- Sperling, H G -- Hunt, D M -- Bowmaker, J K -- Mollon, J D -- Li, W H -- EY10317/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1265-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genetics Center, School of Public Health, University of Texas, Houston 77225, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652574" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Amino Acid Sequence ; Animals ; *Biological Evolution ; Callithrix ; Color Perception/*genetics ; Eye Proteins/*genetics ; Gene Conversion ; Genetic Linkage ; Humans ; Introns ; Male ; Molecular Sequence Data ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retinal Pigments/*genetics ; Rod Opsins ; Saimiri ; Sequence Deletion ; Species Specificity ; X Chromosome
    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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  • 6
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    Impaired energy homeostasis in C/EBP alpha knockout mice (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-25
    Description: Mice homozygous for the targeted deletion of the c/ebp alpha gene, which expresses the CCAAT/enhancer-binding protein alpha (C/EBP alpha), did not store hepatic glycogen and died from hypoglycemia within 8 hours after birth. In these mutant mice, the amounts of glycogen synthase messenger RNA were 50 to 70 percent of normal and the transcriptional induction of the genes for two gluconeogenic enzymes, phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, was delayed. The hepatocytes and adipocytes of the mutant mice failed to accumulate lipid and the expression of the gene for uncoupling protein, the defining marker of brown adipose tissue, was reduced. This study demonstrates that C/EBP alpha is critical for the establishment and maintenance of energy homeostasis in neonates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, N D -- Finegold, M J -- Bradley, A -- Ou, C N -- Abdelsayed, S V -- Wilde, M D -- Taylor, L R -- Wilson, D R -- Darlington, G J -- DK 45285/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 25;269(5227):1108-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652557" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Adipose Tissue, Brown/metabolism ; Animals ; Animals, Newborn ; Blood Glucose/metabolism ; CCAAT-Enhancer-Binding Proteins ; Carrier Proteins/genetics ; DNA-Binding Proteins/genetics/*physiology ; *Energy Metabolism ; Female ; Gene Expression Regulation ; Glucose-6-Phosphatase/genetics ; Glycogen Synthase/genetics/metabolism ; Homeostasis ; Humans ; Ion Channels ; Lipid Metabolism ; Liver/metabolism ; Liver Glycogen/metabolism ; Male ; Membrane Proteins/genetics ; Mice ; Mice, Knockout ; Mitochondrial Proteins ; Nuclear Proteins/genetics/*physiology ; Phosphoenolpyruvate Carboxykinase (GTP)/genetics ; RNA, Messenger/metabolism ; Serum Albumin/genetics
    Print ISSN: 0036-8075
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  • 7
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    Immune system impairment and hepatic fibrosis in mice lacking the dioxin-binding Ah receptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: The aryl hydrocarbon (Ah) receptor (AHR) mediates many carcinogenic and teratogenic effects of environmentally toxic chemicals such as dioxin. An AHR-deficient (Ahr-/-) mouse line was constructed by homologous recombination in embryonic stem cells. Almost half of the mice died shortly after birth, whereas survivors reached maturity and were fertile. The Ahr-/- mice showed decreased accumulation of lymphocytes in the spleen and lymph nodes, but not in the thymus. The livers of Ahr-/- mice were reduced in size by 50 percent and showed bile duct fibrosis Ahr-/- mice were also nonresponsive with regard to dioxin-mediated induction of genes encoding enzymes that catalyze the metabolism of foreign compounds. Thus, the AHR plays an important role in the development of the liver and the immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez-Salguero, P -- Pineau, T -- Hilbert, D M -- McPhail, T -- Lee, S S -- Kimura, S -- Nebert, D W -- Rudikoff, S -- Ward, J M -- Gonzalez, F J -- P30 ES06096/ES/NIEHS NIH HHS/ -- R01 ES06811/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1995 May 5;268(5211):722-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732381" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Gene Expression Regulation/physiology ; Immunity/*physiology ; Liver/*physiology ; Liver Cirrhosis, Experimental/genetics/pathology ; Lymphoid Tissue/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Receptors, Aryl Hydrocarbon/genetics/*physiology
    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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  • 8
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    Involvement of CRAF1, a relative of TRAF, in CD40 signaling (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: CD40 is a receptor on the surface of B lymphocytes, the activation of which leads to B cell survival, growth, and differentiation. A yeast two-hybrid screen identified a gene, CRAF1, encoding a protein that interacts directly with the CD40 cytoplasmic tail through a region of similarity to the tumor necrosis factor-alpha (TNF-alpha) receptor-associated factors. Overexpression of a truncated CRAF1 gene inhibited CD40-mediated up-regulation of CD23. A region of CRAF1 was similar to the TNF-alpha receptor-associated factors TRAF1 and TRAF2 and so defined a shared TRAF-C domain that was necessary and sufficient for CD40 binding and homodimerization. The CRAF1 sequence also predicted a long amphipathic helix, a pattern of five zinc fingers, and a zinc ring finger. It is likely that other members of the TNF receptor superfamily use CRAF-related proteins in their signal transduction processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, G -- Cleary, A M -- Ye, Z S -- Hong, D I -- Lederman, S -- Baltimore, D -- 5-T32-GM07367/GM/NIGMS NIH HHS/ -- A122346/PHS HHS/ -- R01-CA55713/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1494-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7533327" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/*metabolism ; Antigens, CD40 ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Humans ; Mice ; Molecular Sequence Data ; Protein Structure, Secondary ; Proteins/chemistry/genetics/*physiology ; Receptors, IgE/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; TNF Receptor-Associated Factor 3 ; Up-Regulation ; Zinc Fingers
    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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  • 9
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    E5531, a pure endotoxin antagonist of high potency (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-07
    Description: Shock due to Gram-negative bacterial sepsis is a consequence of acute inflammatory response to lipopolysaccharide (LPS) or endotoxin released from bacteria. LPS is a major constituent of the outer membrane of Gram-negative bacteria, and its terminal disaccharide phospholipid (lipid A) portion contains the key structural features responsible for toxic activity. Based on the proposed structure of nontoxic Rhodobacter capsulatus lipid A, a fully stabilized endotoxin antagonist E5531 has been synthesized. In vitro, E5531 demonstrated potent antagonism of LPS-mediated cellular activation in a variety of systems. In vivo, E5531 protected mice from LPS-induced lethality and, in cooperation with an antibiotic, protected mice from a lethal infection of viable Escherichia coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christ, W J -- Asano, O -- Robidoux, A L -- Perez, M -- Wang, Y -- Dubuc, G R -- Gavin, W E -- Hawkins, L D -- McGuinness, P D -- Mullarkey, M A -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):80-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Elsai Research Institute, Andover, MA 01810-2441, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701344" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BCG Vaccine/immunology ; Cytokines/secretion ; Drug Design ; Endotoxins/*antagonists & inhibitors ; Escherichia coli Infections/immunology ; Gram-Negative Bacteria/immunology ; Humans ; In Vitro Techniques ; Lipid A/*analogs & derivatives/chemical synthesis/chemistry/pharmacology ; Lipopolysaccharides/antagonists & inhibitors ; Macrophages/immunology ; Male ; Mice ; Mice, Inbred C57BL ; Monocytes/immunology ; Moxalactam/pharmacology ; Nitric Oxide/metabolism ; Rhodobacter capsulatus/immunology ; Tumor Necrosis Factor-alpha/secretion
    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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