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  • Base Sequence  (162)
  • Female  (148)
  • Models, Molecular  (56)
  • American Association for the Advancement of Science (AAAS)  (328)
  • 1990-1994  (328)
  • 1994  (328)
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (328)
Years
  • 1990-1994  (328)
Year
  • 101
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    Padlock probes: circularizing oligonucleotides for localized DNA detection (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-30
    Description: Nucleotide sequence information derived from DNA segments of the human and other genomes is accumulating rapidly. However, it frequently proves difficult to use such short DNA segments to identify clones in genomic libraries or fragments in blots of the whole genome or for in situ analysis of chromosomes. Oligonucleotide probes, consisting of two target-complementary segments, connected by a linker sequence, were designed. Upon recognition of the specific nucleic acid molecule the ends of the probes were joined through the action of a ligase, creating circular DNA molecules catenated to the target sequence. These probes thus provide highly specific detection with minimal background.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nilsson, M -- Malmgren, H -- Samiotaki, M -- Kwiatkowski, M -- Chowdhary, B P -- Landegren, U -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2085-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beijer Laboratory, Department of Medical Genetics, Biomedical Center, Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7522346" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cells, Cultured ; Chromosomes, Human, Pair 12 ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA/*analysis ; DNA, Circular/*analysis ; Genetic Vectors ; Humans ; In Situ Hybridization ; Lymphocytes ; Membrane Proteins/genetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Oligonucleotide Probes/chemistry ; Repetitive Sequences, Nucleic Acid ; Templates, Genetic
    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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  • 102
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    Reversion of the mouse pink-eyed unstable mutation induced by low doses of x-rays (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: Deletions and other genome rearrangements can be caused by radiation and are associated with carcinogenesis and inheritable diseases. The pink-eyed unstable (p(un)) mutation in the mouse is caused by a gene duplication and reverts to wild type by deletion of one copy. Reversion events in the mouse embryo were detected as black spots on the fur of the animals or microscopically as partially black hair in a background of colorless hair. The frequency of partially black hair was increased by x-rays at very low doses. A linear dose-response relation was found between 1 and 100 centigray.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schiestl, R H -- Khogali, F -- Carls, N -- ES06593/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Toxicology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Radiation ; Embryo, Mammalian/radiation effects ; Female ; *Gene Deletion ; Hair Color/genetics/radiation effects ; Male ; Maternal Exposure ; Melanocytes/radiation effects ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Multigene Family ; Mutagenicity Tests ; Mutation/*radiation effects
    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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  • 103
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    Digenic retinitis pigmentosa due to mutations at the unlinked peripherin/RDS and ROM1 loci (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: In spite of recent advances in identifying genes causing monogenic human disease, very little is known about the genes involved in polygenic disease. Three families were identified with mutations in the unlinked photoreceptor-specific genes ROM1 and peripherin/RDS, in which only double heterozygotes develop retinitis pigmentosa (RP). These findings indicate that the allelic and nonallelic heterogeneity known to be a feature of monogenic RP is complicated further by interactions between unlinked mutations causing digenic RP. Recognition of the inheritance pattern exemplified by these three families might facilitate the identification of other examples of digenic inheritance in human disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kajiwara, K -- Berson, E L -- Dryja, T P -- EY00169/EY/NEI NIH HHS/ -- EY08683/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1604-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Berman-Gund Laboratory for the Study of Retinal Degenerations, Harvard Medical School, Massachusetts Eye and Ear Infirmary, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202715" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Electroretinography ; Eye Proteins/chemistry/*genetics ; Female ; Genes, Dominant ; Genes, Recessive ; Genetic Linkage ; Heterozygote ; Humans ; Intermediate Filament Proteins/chemistry/*genetics ; Male ; *Membrane Glycoproteins ; Membrane Proteins/chemistry/*genetics ; Molecular Sequence Data ; Mutation ; *Nerve Tissue Proteins ; Pedigree ; Peripherins ; Retinitis Pigmentosa/*genetics ; Rod Cell Outer Segment/chemistry ; Tetraspanins
    Print ISSN: 0036-8075
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  • 104
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    Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: Concentration of urine in mammals is regulated by the antidiuretic hormone vasopressin. Binding of vasopressin to its V2 receptor leads to the insertion of water channels in apical membranes of principal cells in collecting ducts. In nephrogenic diabetes insipidus (NDI), the kidney fails to concentrate urine in response to vasopressin. A male patient with an autosomal recessive form of NDI was found to be a compound heterozygote for two mutations in the gene encoding aquaporin-2, a water channel. Functional expression studies in Xenopus oocytes revealed that each mutation resulted in nonfunctional water channel proteins. Thus, aquaporin-2 is essential for vasopressin-dependent concentration of urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deen, P M -- Verdijk, M A -- Knoers, N V -- Wieringa, B -- Monnens, L A -- van Os, C H -- van Oost, B A -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, University of Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140421" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aquaporin 2 ; Aquaporin 6 ; *Aquaporins ; Base Sequence ; Cloning, Molecular ; Deamino Arginine Vasopressin/*pharmacology ; Diabetes Insipidus/*genetics/physiopathology ; Female ; Genes, Recessive ; Heterozygote ; Humans ; Kidney/metabolism/*physiology ; *Kidney Concentrating Ability ; Male ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Oocytes ; Pedigree ; Point Mutation ; Protein Structure, Secondary ; RNA, Complementary/genetics ; Water/metabolism ; Xenopus laevis
    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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  • 105
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    Electromagnetic fields. Breast cancer link claimed, criticized (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1658.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209240" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*etiology ; Electromagnetic Fields/*adverse effects ; Female ; Humans ; Male ; Melatonin/biosynthesis ; *Neoplasms, Radiation-Induced ; *Occupational Exposure ; Pineal Gland/metabolism/radiation effects
    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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  • 106
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    Prevention of lipopolysaccharide-induced lethal toxicity by tyrosine kinase inhibitors (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-27
    Description: Septic shock results from excessive stimulation of the host immune system, especially macrophages, by lipopolysaccharide (LPS), or endotoxin, which resides on the outer membrane of bacteria. Protein tyrosine kinase inhibitors of the tyrphostin AG 126 family protect mice against LPS-induced lethal toxicity. The protection correlates with the ability of these agents to block LPS-induced production of tumor necrosis factor alpha (TNF-alpha) and nitric oxide in macrophages as well as LPS-induced production of TNF-alpha in vivo. Furthermore, this inhibitory effect correlated with the potency of AG 126 to block LPS-induced tyrosine phosphorylation of a p42MAPK protein substrate in the murine macrophage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Novogrodsky, A -- Vanichkin, A -- Patya, M -- Gazit, A -- Osherov, N -- Levitzki, A -- New York, N.Y. -- Science. 1994 May 27;264(5163):1319-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Felsenstein Medical Research Center, Petach Tikva, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191285" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzylidene Compounds/*pharmacology ; Biological Assay ; Cell Line ; Cell Survival/drug effects ; Dose-Response Relationship, Drug ; Enzyme-Linked Immunosorbent Assay ; Female ; Lipopolysaccharides/*toxicity ; Macrophage Activation ; Macrophages, Peritoneal/*drug effects/metabolism ; Mice ; Mice, Inbred C57BL ; Mitogen-Activated Protein Kinase 1 ; Nitric Oxide/*biosynthesis ; Nitriles/*pharmacology ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/*antagonists & inhibitors/metabolism ; Tumor Necrosis Factor-alpha/analysis/*biosynthesis/toxicity ; *Tyrphostins
    Print ISSN: 0036-8075
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  • 107
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    Pesticides and breast cancer: no link? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):499-500.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160007" target="_blank"〉PubMed〈/a〉
    Keywords: African Continental Ancestry Group ; Asian Continental Ancestry Group ; Breast Neoplasms/blood/*chemically induced/ethnology ; Case-Control Studies ; DDT/adverse effects ; Dichlorodiphenyl Dichloroethylene/adverse effects/*blood ; European Continental Ancestry Group ; Female ; Humans ; Pesticide Residues/adverse effects/*blood ; Polychlorinated Biphenyls/adverse effects ; Risk Factors
    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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  • 108
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    Encapsulation of methane and other small molecules in a self-assembling superstructure (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-04
    Description: Physical inclusion of small molecules in larger structural lattices is well known in the crystalline state and is a common feature of the chemistry of zeolites. In the liquid state, a variety of synthetic macrocyclic molecules are available to complex and contain smaller guest species. An alternative strategy for binding is explored: assembly of cavity-forming structures from small subunits. Encapsulation of small guest molecules such as methane can be achieved with a synthetic structure that assembles reversibly through hydrogen bonding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Branda, N -- Wyler, R -- Rebek, J Jr -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1267-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122107" target="_blank"〉PubMed〈/a〉
    Keywords: Benzyl Compounds/chemistry ; Chemistry, Physical ; Chloroform ; Hydrogen Bonding ; Imidazoles/chemistry ; Magnetic Resonance Spectroscopy ; Methane/*chemistry ; Models, Molecular ; Molecular Conformation ; Molecular Structure ; Physicochemical Phenomena ; Polymers/*chemistry ; Temperature ; Thermodynamics
    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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  • 109
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    Risking everything? Risk behavior, behavior change, and AIDS (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: Inquiry into the determinants of risk-related sexual behavior is important for the development of interventions to reduce the incidence of new cases of human immunodeficiency virus infection. Recent social and behavioral research has revealed much about the individual and social factors influencing risk-taking. Findings from these studies have been important in the development of new educational and community-based interventions for communities at risk in the developed and developing worlds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aggleton, P -- O'Reilly, K -- Slutkin, G -- Davies, P -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):341-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Global Programme on AIDS, World Health Organization, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023156" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/prevention & ; control/*transmission ; Cultural Characteristics ; Developing Countries ; Disease Outbreaks ; Female ; Global Health ; Humans ; Male ; *Risk-Taking ; *Sexual Behavior ; Socioeconomic Factors
    Print ISSN: 0036-8075
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  • 110
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    Activation of the myogenic lineage by MEF2A, a factor that induces and cooperates with MyoD (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: Muscle enhancer factor-2A (MEF2A), a member of the MADS family, induced myogenic development when ectopically expressed in clones of nonmuscle cells of human clones, a function previously limited to the muscle basic helix-loop-helix (bHLH) proteins. During myogenesis, MEF2A and bHLH proteins cooperatively activate skeletal muscle genes and physically interact through the MADS domain of MEF2A and the three myogenic amino acids of the muscle bHLH proteins. Thus, skeletal myogenesis is mediated by two distinct families of mutually inducible and interactive muscle transcription factors, either of which can initiate the developmental cascade.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaushal, S -- Schneider, J W -- Nadal-Ginard, B -- Mahdavi, V -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1236-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973707" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Haplorhini ; Helix-Loop-Helix Motifs ; Humans ; MADS Domain Proteins ; MEF2 Transcription Factors ; Mice ; Molecular Sequence Data ; Muscle, Skeletal/*cytology/metabolism ; MyoD Protein/biosynthesis/*metabolism ; Myogenic Regulatory Factors ; Myogenin/biosynthesis/genetics/metabolism ; Transcription Factors/genetics/*metabolism ; Transfection
    Print ISSN: 0036-8075
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  • 111
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    Recombination between viral RNA and transgenic plant transcripts (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-11
    Description: Transformed plants expressing the 3' two-thirds of the cowpea chlorotic mottle virus (CCMV) capsid gene were inoculated with a CCMV deletion mutant lacking the 3' one-third of the capsid gene. Although the deletion inoculum replicates in inoculated cells, systemic infections occur only if recombination restores a functional capsid gene. Four of 125 inoculated transgenic plants, representing three different transgenic lines, became systemically infected. Analysis of viral RNA confirmed that RNA recombination had united the transgenic messenger RNA and the challenging virus through aberrant homologous recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, A E -- Allison, R F -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Michigan State University, East Lansing 48824-1312.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128222" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Bromovirus/*genetics/physiology ; Capsid/genetics ; Gene Deletion ; Genes, Viral ; Molecular Sequence Data ; Mutation ; Plants, Genetically Modified/genetics/*microbiology ; Plants, Toxic ; RNA, Messenger/*genetics ; RNA, Viral/*genetics ; *Recombination, Genetic ; Tobacco/genetics/microbiology ; Virus Replication
    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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  • 112
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    Blockage of NF-kappa B signaling by selective ablation of an mRNA target by 2-5A antisense chimeras (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: Activation of 2-5A-dependent ribonuclease by 5'-phosphorylated, 2',5'-linked oligoadenylates, known as 2-5A, is one pathway of interferon action. Unaided uptake into HeLa cells of 2-5A linked to an antisense oligonucleotide resulted in the selective ablation of messenger RNA for the double-stranded RNA (dsRNA)-dependent protein kinase PKR. Similarly, purified, recombinant human 2-5A-dependent ribonuclease was induced to selectively cleave PKR messenger RNA. Cells depleted of PKR activity were unresponsive to activation of nuclear factor-kappa B (NF-kappa B) by the dsRNA poly(I):poly(C), which provides direct evidence that PKR is a transducer for the dsRNA signaling of NF-kappa B.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maran, A -- Maitra, R K -- Kumar, A -- Dong, B -- Xiao, W -- Li, G -- Williams, B R -- Torrence, P F -- Silverman, R H -- AI 28253/AI/NIAID NIH HHS/ -- AI 34039-02/AI/NIAID NIH HHS/ -- CA 44059/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):789-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Cleveland Clinic Foundation, OH 44195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7914032" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/chemical synthesis/*pharmacology ; Base Sequence ; Endoribonucleases/metabolism ; Enzyme Activation ; HeLa Cells ; Humans ; Kinetics ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotides, Antisense/chemical synthesis/*pharmacology ; Oligoribonucleotides/chemical synthesis/*pharmacology ; Protein-Serine-Threonine Kinases/*genetics ; RNA, Messenger/drug effects ; Signal Transduction/*drug effects ; eIF-2 Kinase
    Print ISSN: 0036-8075
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  • 113
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    Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schumacher, M A -- Choi, K Y -- Zalkin, H -- Brennan, R G -- GM 24658/GM/NIGMS NIH HHS/ -- GM 49244/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):763-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/genetics/metabolism ; Base Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; *Escherichia coli Proteins ; Hydrogen Bonding ; Hypoxanthine ; Hypoxanthines/metabolism ; Lac Repressors ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Operator Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Repressor Proteins/*chemistry/genetics/metabolism
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  • 114
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    CD26 antigen and HIV fusion? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Broder, C C -- Nussbaum, O -- Gutheil, W G -- Bachovchin, W W -- Berger, E A -- New York, N.Y. -- Science. 1994 May 20;264(5162):1156-9; author reply 1162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909959" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*physiology ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; *Cell Fusion ; Cell Line ; Dipeptidyl Peptidase 4 ; Gene Products, env/*physiology ; Giant Cells/physiology ; HIV-1/*physiology ; Humans ; Hybrid Cells ; Molecular Sequence Data
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  • 115
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    The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is very similar to a family of bacterial beta-glucanases with the main-chain topology of the plant legume lectins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Divne, C -- Stahlberg, J -- Reinikainen, T -- Ruohonen, L -- Pettersson, G -- Knowles, J K -- Teeri, T T -- Jones, T A -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):524-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Uppsala University, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036495" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Cellobiose/analogs & derivatives/chemistry/metabolism ; Cellulose/metabolism ; Cellulose 1,4-beta-Cellobiosidase ; Computer Graphics ; Crystallography, X-Ray ; Glycoside Hydrolases/*chemistry/metabolism ; Hydrogen Bonding ; Iodobenzenes/chemistry/metabolism ; Models, Molecular ; Protein Structure, Secondary ; Trichoderma/*enzymology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Breast cancer gene offers surprises (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1796-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091205" target="_blank"〉PubMed〈/a〉
    Keywords: BRCA1 Protein ; Breast Neoplasms/*genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 17 ; Female ; Genes ; Genes, Tumor Suppressor ; Genetic Predisposition to Disease ; Humans ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*genetics ; Transcription Factors/*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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    NMR solution structure of a peptide nucleic acid complexed with RNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: Peptide nucleic acids (PNA) incorporating nucleic acid bases into an achiral polyamide backbone bind to DNA in a sequence-dependent manner. The structure of a PNA-ribonucleic acid (RNA) complex was determined with nuclear magnetic resonance methods. A hexameric PNA formed a 1:1 complex with a complementary RNA that is an antiparallel, right-handed double helix with Watson-Crick base pairing similar to the "A" form structure of RNA duplexes. The achiral PNA backbone assumed a distinct conformation upon binding that differed from previously proposed models and provides a basis for further structure-based design of antisense agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, S C -- Thomson, S A -- Veal, J M -- Davis, D G -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):777-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Research Institute, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7519361" target="_blank"〉PubMed〈/a〉
    Keywords: Magnetic Resonance Spectroscopy ; Models, Molecular ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemistry ; Peptides/*chemistry ; RNA/*chemistry
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    Linkage analysis of IL4 and other chromosome 5q31.1 markers and total serum immunoglobulin E concentrations (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: Sib-pair analysis of 170 individuals from 11 Amish families revealed evidence for linkage of five markers in chromosome 5q31.1 with a gene controlling total serum immunoglobulin E (IgE) concentration. No linkage was found between these markers and specific IgE antibody concentrations. Analysis of total IgE within a subset of 128 IgE antibody-negative sib pairs confirmed evidence for linkage to 5q31.1, especially to the interleukin-4 gene (IL4). A combination of segregation and maximum likelihood analyses provided further evidence for this linkage. These analyses suggest that IL4 or a nearby gene in 5q31.1 regulates IgE production in a nonantigen-specific (noncognate) fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marsh, D G -- Neely, J D -- Breazeale, D R -- Ghosh, B -- Freidhoff, L R -- Ehrlich-Kautzky, E -- Schou, C -- Krishnaswamy, G -- Beaty, T H -- 1 P41 RR03655/RR/NCRR NIH HHS/ -- AI20059/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 May 20;264(5162):1152-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Asthma and Allergy Center, School of Medicine, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178175" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Allergens/immunology ; Base Sequence ; Child ; Child, Preschool ; *Chromosomes, Human, Pair 5 ; Female ; Genes, MHC Class II ; *Genetic Linkage ; Genetic Markers ; Humans ; Hypersensitivity, Immediate/genetics ; Immunoglobulin E/*blood ; Interleukin-4/*genetics ; Likelihood Functions ; Lod Score ; Male ; Middle Aged ; Molecular Sequence Data
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-01
    Description: Deletion of the promoter and the first exon of the DNA polymerase beta gene (pol beta) in the mouse germ line results in a lethal phenotype. With the use of the bacteriophage-derived, site-specific recombinase Cre in a transgenic approach, the same mutation can be selectively introduced into a particular cellular compartment-in this case, T cells. The impact of the mutation on those cells can then be analyzed because the mutant animals are viable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, H -- Marth, J D -- Orban, P C -- Mossmann, H -- Rajewsky, K -- New York, N.Y. -- Science. 1994 Jul 1;265(5168):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8016642" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA Nucleotidyltransferases/genetics/metabolism ; DNA Polymerase I/*genetics/metabolism ; Female ; *Gene Deletion ; Genetic Engineering/*methods ; Homozygote ; *Integrases ; Male ; Mice ; Mice, Knockout ; Mice, Transgenic ; Mutation ; Recombination, Genetic ; Stem Cells/enzymology ; T-Lymphocytes/*enzymology ; Transfection ; *Viral Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Gene for familial psoriasis susceptibility mapped to the distal end of human chromosome 17q (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: A gene involved in psoriasis susceptibility was localized to the distal region of human chromosome 17q as a result of a genome-wide linkage analysis with polymorphic microsatellites and eight multiply affected psoriasis kindreds. In the family which showed the strongest evidence for linkage, the recombination fraction between a psoriasis susceptibility locus and D17S784 was 0.04 with a maximum two-point lod score of 5.33. There was also evidence for genetic heterogeneity and although none of the linked families showed any association with HLA-Cw6, two unlinked families showed weak levels of association. This study demonstrates that in some families, psoriasis susceptibility is due to variation at a single major genetic locus other than the human lymphocyte antigen locus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomfohrde, J -- Silverman, A -- Barnes, R -- Fernandez-Vina, M A -- Young, M -- Lory, D -- Morris, L -- Wuepper, K D -- Stastny, P -- Menter, A -- P01-AI2327/AI/NIAID NIH HHS/ -- R01 HL47145/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 May 20;264(5162):1141-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of Texas Southwestern Medical Center, Dallas 75235-8591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178173" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 17 ; DNA Primers ; DNA, Satellite/genetics ; Disease Susceptibility ; Female ; Genetic Linkage ; Genetic Markers ; HLA-C Antigens/genetics ; Haplotypes ; Humans ; Lod Score ; Male ; Molecular Sequence Data ; Pedigree ; Polymorphism, Genetic ; Psoriasis/*genetics ; Software
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Fertilization and ion channels (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nuccitelli, R -- Ferguson, J E -- New York, N.Y. -- Science. 1994 Feb 18;263(5149):988.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8310299" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Female ; *Fertilization ; Male ; Oocytes/*physiology ; Sodium Channels/*physiology ; Spermatozoa/metabolism ; Xenopus laevis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Animal tests take back seat to clinical data (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seachrist, L -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1525.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202703" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/chemically induced/prevention & control ; Endometrial Neoplasms/chemically induced ; Female ; Humans ; Liver Neoplasms, Experimental/chemically induced ; Rats ; Tamoxifen/therapeutic use/*toxicity
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    Long-term behavioral recovery in parkinsonian rats by an HSV vector expressing tyrosine hydroxylase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: One therapeutic approach to treating Parkinson's disease is to convert endogenous striatal cells into levo-3,4-dihydroxyphenylalanine (L-dopa)-producing cells. A defective herpes simplex virus type 1 vector expressing human tyrosine hydroxylase was delivered into the partially denervated striatum of 6-hydroxydopamine-lesioned rats, used as a model of Parkinson's disease. Efficient behavioral and biochemical recovery was maintained for 1 year after gene transfer. Biochemical recovery included increases in both striatal tyrosine hydroxylase enzyme activity and in extracellular dopamine concentrations. Persistence of human tyrosine hydroxylase was revealed by expression of RNA and immunoreactivity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2638002/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2638002/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉During, M J -- Naegele, J R -- O'Malley, K L -- Geller, A I -- EY09749/EY/NEI NIH HHS/ -- NS06208/NS/NINDS NIH HHS/ -- NS28227/NS/NINDS NIH HHS/ -- R01 NS034025/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1399-403.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7669103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Corpus Striatum/*enzymology/metabolism ; Denervation ; Disease Models, Animal ; Dopamine/metabolism ; Gene Transfer Techniques ; *Genetic Therapy ; Genetic Vectors ; Humans ; Levodopa/metabolism ; Male ; Molecular Sequence Data ; *Motor Activity ; Neurons/enzymology ; Parkinson Disease/metabolism/*therapy ; Rats ; Rats, Sprague-Dawley ; Simplexvirus/*genetics ; Tyrosine 3-Monooxygenase/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Scientific misconduct. NIH tightens clinical trials monitoring (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seachrist, L -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):499.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160006" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/prevention & control/radiotherapy/surgery ; Clinical Trials as Topic/*standards ; Combined Modality Therapy ; Endometrial Neoplasms/chemically induced ; Female ; Humans ; Investigational New Drug Application ; Mastectomy, Segmental ; National Institutes of Health (U.S.)/*organization & administration ; *Scientific Misconduct ; Tamoxifen/adverse effects ; United States
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    Effective tumor vaccine generated by fusion of hepatoma cells with activated B cells (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-28
    Description: Fusion of BERH-2 rat hepatocellular carcinoma cells with activated B cells produced hybrid cells that lost their tumorigenicity and became immunogenic. Syngeneic rats injected with BERH-2-B hybrid cells became resistant to challenge with parental BERH-2 cells, and rats with established BERH-2 hepatomas were cured by subsequent injection of BERH-2-B cells. Both CD4+ and CD8+ cells were essential for the induction of protective immunity; however, only CD8+ cells were required for the eradication of BERH-2 tumors. The generation of hybrid tumor cells that elicit antitumor immune responses may be a useful strategy for cancer immunotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, Y -- Wu, M -- Chen, H -- Wang, X -- Liu, G -- Li, G -- Ma, J -- Sy, M S -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):518-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tumor Immunology and Biotherapy Center, Eastern Institute of Hepatobiliary Surgery, Shanghai, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7507262" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD80/analysis ; B-Lymphocytes/*immunology ; CD4-Positive T-Lymphocytes/immunology ; Cell Fusion ; Female ; Histocompatibility Antigens Class II/analysis ; Hybrid Cells/*immunology ; Immunotherapy, Active ; Liver Neoplasms, Experimental/*immunology/prevention & control/therapy ; Lymphocyte Activation ; Neoplasm Transplantation ; Rats ; Rats, Wistar ; T-Lymphocyte Subsets/immunology ; Tumor Cells, Cultured ; Vaccination ; Vaccines/*immunology
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    Manic depression. Highs and lows on the research roller coaster (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1693-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209248" target="_blank"〉PubMed〈/a〉
    Keywords: Bipolar Disorder/*genetics ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Chromosomes, Human, Pair 18 ; Female ; Genetic Markers ; *Genetic Techniques ; *Genome, Human ; Humans ; Lod Score ; Male
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    Noradrenergic regulation of cholinergic differentiation (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: When the sympathetic nerves that innervate rat sweat glands reach their targets, they are induced to switch from using norepinephrine as their neurotransmitter to acetylcholine. Catecholamines (such as norepinephrine) released by nerves growing to the sweat gland induce this phenotypic conversion by stimulating production of a cholinergic differentiation factor [sweat gland factor (SGF)] by gland cells. Here, culture of gland cells with sympathetic, but not sensory, neurons induced SGF production. Blockage of alpha 1- or beta-adrenergic receptors prevented acquisition of the cholinergic phenotype in sympathetic neurons co-cultured with sweat glands, and sweat glands from sympathectomized animals lacked SGF. Thus, reciprocal instructive interactions, mediated in part by small molecule neurotransmitters, direct the development of this synapse.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Habecker, B A -- Landis, S C -- NS-023678/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1602-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, Case Western Reserve University School of Medicine, Cleveland, OH 44106-4975.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202714" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Base Sequence ; Cell Differentiation ; Cells, Cultured ; Culture Media, Conditioned ; Glycoproteins/*biosynthesis ; Molecular Sequence Data ; Neuregulins ; Neurons/cytology/physiology ; Neurons, Afferent/cytology/physiology ; Parasympathetic Nervous System/cytology/*physiology ; Phenotype ; Rats ; Receptors, Adrenergic/*physiology ; Sweat Glands/cytology/*innervation/metabolism ; Sympathectomy ; Sympathetic Nervous System/cytology/*physiology
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    On the trail of a second susceptibility gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, C -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1798.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091206" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 13 ; Female ; Genes, Tumor Suppressor ; Genetic Markers ; Genetic Predisposition to Disease ; Humans ; Male ; Mutation
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    Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: HIV integrase is the enzyme responsible for inserting the viral DNA into the host chromosome; it is essential for HIV replication. The crystal structure of the catalytically active core domain (residues 50 to 212) of HIV-1 integrase was determined at 2.5 A resolution. The central feature of the structure is a five-stranded beta sheet flanked by helical regions. The overall topology reveals that this domain of integrase belongs to a superfamily of polynucleotidyl transferases that includes ribonuclease H and the Holliday junction resolvase RuvC. The active site region is identified by the position of two of the conserved carboxylate residues essential for catalysis, which are located at similar positions in ribonuclease H. In the crystal, two molecules form a dimer with a extensive solvent-inaccessible interface of 1300 A2 per monomer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dyda, F -- Hickman, A B -- Jenkins, T M -- Engelman, A -- Craigie, R -- Davies, D R -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1981-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, NIDDK, NIH, Bethesda, MD 20892-0560.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801124" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Nucleotidyltransferases/*chemistry ; HIV-1/*enzymology ; Hydrogen Bonding ; Integrases ; Models, Molecular ; Molecular Sequence Data ; Protein Folding ; Protein Structure, Secondary ; Ribonuclease H/chemistry ; Solubility ; Virus Integration
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    A hearty endorsement for aspirin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272863" target="_blank"〉PubMed〈/a〉
    Keywords: Aspirin/*therapeutic use ; Cardiovascular Diseases/*prevention & control ; Female ; Humans ; Male ; Meta-Analysis as Topic ; Risk Factors ; Thrombosis/*prevention & control ; United States ; United States Food and Drug Administration
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    RNA editing: transfer of genetic information from gRNA to precursor mRNA in vitro (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: RNA editing in the mitochondrion of Trypanosoma brucei extensively alters the adenosine triphosphate synthase (ATPase) subunit 6 precursor messenger RNA (pre-mRNA) by addition of 447 uridines and removal of 28 uridines. In vivo, the guide RNA gA6[14] is thought to specify the deletion of two uridines from the editing site closest to the 3' end. In this study, an in vitro system was developed that accurately removed uridines from this editing site in synthetic ATPase 6 pre-mRNA when gA6[14] and ATP were added. Mutations in both the guide RNA and the pre-mRNA editing site suggest that base-pairing interactions control the number of uridines deleted in vitro. Thus, guide RNAs are required for RNA editing and for the transfer of genetic information to pre-mRNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seiwert, S D -- Stuart, K -- GM 42188/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):114-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06536-0182.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7524149" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/genetics ; Adenosine Triphosphate/metabolism ; Animals ; Base Composition ; Base Sequence ; Mitochondria/genetics ; Molecular Sequence Data ; Mutation ; RNA/chemistry/*genetics/metabolism ; *RNA Editing ; RNA Precursors/chemistry/*genetics/metabolism ; RNA, Guide/chemistry/*genetics/metabolism ; RNA, Protozoan/chemistry/genetics/metabolism ; Trypanosoma brucei brucei/*genetics/metabolism ; Uridine/metabolism
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  • 132
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    The mating of a fly (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-17
    Description: Courtship in Drosophila is influenced by a wide variety of genes, in that many different kinds of pleiotropic mutations lead to defective courtship. This may seem to be a truism, but the broad temporal and spatial expression of most of the fly's "neuro genes" makes it difficult to exclude elements of such genes' actions as materially underlying reproductive behavior. "Courtship genes" that seem to play more particular roles were originally identified as sensory, learning, or rhythm mutations; their reproductive abnormalities have been especially informative for revealing components of male or female actions that might otherwise have gone unnoticed. Further behavioral mutations seemed originally to be courtship-specific, turned out not to have that property, and have led to a broadened perspective on the nature and action of Drosophila's sex-determination genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, J C -- GM-21473/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1702-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brandeis University, Waltham, MA 02254-9110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209251" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila melanogaster/anatomy & histology/*genetics/physiology ; Female ; *Genes, Insect ; Male ; Mutation ; Nervous System Physiological Phenomena ; Phenotype ; Sex Characteristics ; Sex Determination Analysis ; *Sexual Behavior, Animal
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  • 133
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    Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: A homozygous mutation in the kinase domain of ZAP-70, a T cell receptor-associated protein tyrosine kinase, produced a distinctive form of human severe combined immunodeficiency. Manifestations of this disorder included profound immunodeficiency, absence of peripheral CD8+ T cells, and abundant peripheral CD4+ T cells that were refractory to T cell receptor-mediated activation. These findings demonstrate that ZAP-70 is essential for human T cell function and suggest that CD4+ and CD8+ T cells depend on different intracellular signaling pathways to support their development or survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elder, M E -- Lin, D -- Clever, J -- Chan, A C -- Hope, T J -- Weiss, A -- Parslow, T G -- AI29313/AI/NIAID NIH HHS/ -- GM43574/GM/NIGMS NIH HHS/ -- RR01271/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of California, San Francisco 94143-0110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202712" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Female ; Frameshift Mutation ; Gene Deletion ; Homozygote ; Humans ; Infant ; Male ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Severe Combined Immunodeficiency/*genetics/immunology ; Signal Transduction ; T-Lymphocyte Subsets/*immunology ; Transfection ; Tumor Cells, Cultured ; ZAP-70 Protein-Tyrosine Kinase
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    The paradox of critical mass for women in science (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Etzkowitz, H -- Kemelgor, C -- Neuschatz, M -- Uzzi, B -- Alonzo, J -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):51-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sociology Board, State University of New York at Purchase 10577.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939644" target="_blank"〉PubMed〈/a〉
    Keywords: *Education, Graduate ; *Faculty ; Female ; Humans ; Male ; *Science ; Universities ; *Women ; Women, Working
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    National Institutes of Health. New law brings affirmative action to clinical research (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303263" target="_blank"〉PubMed〈/a〉
    Keywords: Clinical Trials, Phase III as Topic/*legislation & jurisprudence/methods ; Female ; Humans ; Male ; *Minority Groups ; *National Institutes of Health (U.S.) ; United States ; *Women's Health
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  • 136
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    The stereochemical course of group II intron self-splicing (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-12-09
    Description: The stereochemical specificities and reaction courses for both self-splicing steps of a group II intron have been determined by phosphorothioate substitution at the 5' and 3' splice site phosphodiester bonds. Both steps of the splicing reaction proceeded with a phosphorothioate in the Sp configuration but were blocked by the Rp diastereomer. Both steps also proceeded with inversion of stereochemical configuration around phosphorus, consistent with a concerted transesterification reaction. These results are identical to those found for nuclear precursor mRNA (pre-mRNA) splicing and provide support for the hypothesis that group II introns and nuclear pre-mRNA introns share a common evolutionary history.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Padgett, R A -- Podar, M -- Boulanger, S C -- Perlman, P S -- GM31480/GM/NIGMS NIH HHS/ -- GM45371/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1685-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527587" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Exons ; *Introns ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/chemistry ; Oxygen/chemistry ; Phosphorus/chemistry ; RNA/*chemistry/genetics ; *RNA Splicing ; Sulfur/chemistry ; Thionucleotides/chemistry
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    Environmental estrogens (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hansen, L G -- Jansen, H T -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):526.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939693" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/chemically induced ; Dichlorodiphenyl Dichloroethylene/adverse effects ; Dioxins/adverse effects ; Environmental Exposure/adverse effects ; Environmental Pollutants/*adverse effects/metabolism ; Estrogen Antagonists/metabolism ; Estrogens/*adverse effects/metabolism ; Female ; Humans
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  • 138
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    MHC class I expression in mice lacking the proteasome subunit LMP-7 (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-08-26
    Description: Proteasomes degrade endogenous proteins. Two subunits, LMP-2 and LMP-7, are encoded in a region of the major histocompatibility complex (MHC) that is critical for class I-restricted antigen presentation. Mice with a targeted deletion of the gene encoding LMP-7 have reduced levels of MHC class I cell-surface expression and present the endogenous antigen HY inefficiently; addition of peptides to splenocytes deficient in LMP-7 restores wild-type class I expression levels. This demonstrates the involvement of LMP-7 in the MHC class I presentation pathway and suggests that LMP-7 functions as an integral part of the peptide supply machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fehling, H J -- Swat, W -- Laplace, C -- Kuhn, R -- Rajewsky, K -- Muller, U -- von Boehmer, H -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1234-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066463" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Animals ; Antigen Presentation ; Antigen-Presenting Cells/immunology ; Base Sequence ; Carrier Proteins/genetics ; *Cysteine Endopeptidases ; Female ; Gene Deletion ; H-2 Antigens/*biosynthesis/immunology ; H-Y Antigen/immunology ; Lymphocytes/immunology ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; *Multienzyme Complexes ; Proteasome Endopeptidase Complex ; Proteins/genetics/*physiology
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  • 139
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    Molecular basis of mammalian sexual determination: activation of Mullerian inhibiting substance gene expression by SRY (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: The pathway of male sexual development in mammals is initiated by SRY, a gene on the short arm of the Y chromosome. Its expression in the differentiating gonadal ridge directs testicular morphogenesis, characterized by elaboration of Mullerian inhibiting substance (MIS) and testosterone. SRY and MIS each belong to conserved gene families that function in the control of growth and differentiation. Structural and biochemical studies of the DNA binding domain of SRY (the HMG box) revealed a protein-DNA interaction consisting of partial side chain intercalation into a widened minor groove. Functional studies of SRY in a cell line from embryonic gonadal ridge demonstrated activation of a gene-regulatory pathway leading to expression of MIS. SRY molecules containing mutations associated with human sex reversal have altered structural interactions with DNA and failed to induce transcription of MIS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haqq, C M -- King, C Y -- Ukiyama, E -- Falsafi, S -- Haqq, T N -- Donahoe, P K -- Weiss, M A -- GM51558/GM/NIGMS NIH HHS/ -- HD30812/HD/NICHD NIH HHS/ -- P30HD28138/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1494-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Surgical Research Laboratory, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985018" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Mullerian Hormone ; Base Sequence ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Female ; *Gene Expression Regulation, Developmental ; Genitalia, Male/*embryology ; *Glycoproteins ; Growth Inhibitors/biosynthesis/*genetics ; Humans ; Male ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mullerian Ducts ; *Nuclear Proteins ; Sex Differentiation/*genetics ; Sex-Determining Region Y Protein ; Testicular Hormones/biosynthesis/*genetics ; Transcription Factors/chemistry/*genetics/metabolism
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    Identification of two GTP-binding proteins in the chloroplast protein import machinery (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: Two of four proteins that associated with translocation intermediates during protein import across the outer chloroplast envelope membrane were identified as guanosine triphosphate (GTP)-binding proteins. Both proteins are integral membrane proteins of the outer chloroplast membrane, and both are partially exposed on the chloroplast surface where they were accessible to thermolysin digestion. Engagement of the outer membrane's import machinery by an import substrate was inhibited by slowly hydrolyzable or non-hydrolyzable GTP analogs. Thus, these GTP-binding proteins may function in protein import into chloroplasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kessler, F -- Blobel, G -- Patel, H A -- Schnell, D J -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1035-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973656" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Base Sequence ; Biological Transport ; Chloroplasts/chemistry/*metabolism ; GTP-Binding Proteins/analysis/chemistry/*metabolism ; Guanosine Triphosphate/metabolism ; Intracellular Membranes/chemistry/*metabolism ; Membrane Proteins/analysis/chemistry/*metabolism ; Molecular Sequence Data ; *Monomeric GTP-Binding Proteins ; Plant Proteins/chemistry/*metabolism ; Sequence Alignment
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  • 141
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    Mutation of a mutL homolog in hereditary colon cancer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-18
    Description: Some cases of hereditary nonpolyposis colorectal cancer (HNPCC) are due to alterations in a mutS-related mismatch repair gene. A search of a large database of expressed sequence tags derived from random complementary DNA clones revealed three additional human mismatch repair genes, all related to the bacterial mutL gene. One of these genes (hMLH1) resides on chromosome 3p21, within 1 centimorgan of markers previously linked to cancer susceptibility in HNPCC kindreds. Mutations of hMLH1 that would disrupt the gene product were identified in such kindreds, demonstrating that this gene is responsible for the disease. These results suggest that defects in any of several mismatch repair genes can cause HNPCC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papadopoulos, N -- Nicolaides, N C -- Wei, Y F -- Ruben, S M -- Carter, K C -- Rosen, C A -- Haseltine, W A -- Fleischmann, R D -- Fraser, C M -- Adams, M D -- CA35494/CA/NCI NIH HHS/ -- CA47527/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1625-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Oncology Center, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128251" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; *Adenosine Triphosphatases ; Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics ; Base Sequence ; Carrier Proteins ; Chromosome Mapping ; *Chromosomes, Human, Pair 3 ; Codon ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; *DNA Repair ; *DNA-Binding Proteins ; *Escherichia coli Proteins ; Female ; Frameshift Mutation ; *Genes ; Genetic Markers ; Humans ; Male ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Mutation ; Neoplasm Proteins/chemistry/*genetics ; Nuclear Proteins ; Open Reading Frames ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/genetics ; Sequence Deletion ; Tumor Cells, Cultured
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    Flu virus invasion: halfway there (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carr, C M -- Kim, P S -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):234-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939658" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism/virology ; Endocytosis ; Endosomes/virology ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral/chemistry/*physiology ; Hydrogen-Ion Concentration ; *Membrane Fusion ; Models, Biological ; Models, Molecular ; Orthomyxoviridae/immunology/*physiology ; Protein Conformation ; Viral Envelope Proteins/chemistry/*physiology
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    DNA targets for certain bZIP proteins distinguished by an intrinsic bend (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-05-20
    Description: In spite of the large amount of sequence conservation among the DNA binding segments of basic region leucine zipper (bZIP) proteins, these proteins can discriminate differently between target sequences that differ in half-site spacing. Here it is shown that the half-site spacing preferences of bZIP proteins are the result of (i) the differential intrinsic curvature in target binding sites that differ by insertion or deletion of a single base pair and (ii) the ability of some bZIP proteins to overcome this intrinsic curvature through a mechanism dependent on basic segment residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paolella, D N -- Palmer, C R -- Schepartz, A -- New York, N.Y. -- Science. 1994 May 20;264(5162):1130-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178171" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factor 2 ; Amino Acid Sequence ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Cyclic AMP Response Element-Binding Protein/chemistry/*metabolism ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Fungal Proteins/chemistry/*metabolism ; G-Box Binding Factors ; *Leucine Zippers ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Protein Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins c-jun/chemistry/metabolism ; *Saccharomyces cerevisiae Proteins ; *Transcription Factors
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    Population policy options (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-06
    Description: In the review by Kristie Macrakis of Beyond the Wall: Memoirs of an East and West German Spy by Werner Stiller, with Jefferson Adams (editor and translator) [Brassey's (US), McLean, VA, 1992; Maxwell Macmillan, London, UK, 1992] (17 Dec., p. 1908), it is stated that physicist Rolf Dobbertin, who denies any spying, was "sent to Paris in 1956 to study at the expense of the Stasi," was "sentenced to 12 years in prison," and "sat in a French jail for five years before he was released in 1991." Legal documents show that Dobbertin, who was arrested in January 1979 for acts of "communication with agents of a foreign power, dealings that could be harmful [intelligence de nature a nuire] to the military or diplomatic situation of France or to its essential economic interest," was jailed until May 1983. He was subsequently tried in 1990 and sentenced to 12 years in prison, but was acquitted of the above charge by a special Assize Court in a second trial in November 1991. According to Dobbertin, he studied continuously at the University of Rostock from 1952 until 1958, and then taught at the University of Berlin for one year before beginning his work in 1959 at the Centre Nationale de la Recherche Scientifigue in France, where he continues to be employed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Treisman, M -- New York, N.Y. -- Science. 1994 May 6;264(5160):760.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171327" target="_blank"〉PubMed〈/a〉
    Keywords: *Developing Countries ; *Family Characteristics ; Female ; Humans ; Male ; *Population Control ; *Social Security
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    ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: Protein tyrosine kinases (PTKs) play an integral role in T cell activation and differentiation. Defects in the Src-family PTKs in mice and in T cell lines have resulted in variable defects in thymic development and in T cell antigen receptor (TCR) signal transduction. Here, three siblings are described with an autosomal recessive form of severe combined immunodeficiency disease (SCID) in which ZAP-70, a non-Src PTK, is absent as a result of mutations in the ZAP-70 gene. This absence is associated with defects in TCR signal transduction, suggesting an important functional role for ZAP-70.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A C -- Kadlecek, T A -- Elder, M E -- Filipovich, A H -- Kuo, W L -- Iwashima, M -- Parslow, T G -- Weiss, A -- AR-20684/AR/NIAMS NIH HHS/ -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1599-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202713" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/metabolism ; Cell Line ; Child ; Female ; Gene Deletion ; *Genes, Recessive ; Humans ; Lymphocyte Activation ; Male ; Molecular Sequence Data ; Mutation ; Point Mutation ; Protein-Tyrosine Kinases/deficiency/*genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Severe Combined Immunodeficiency/*genetics/immunology ; *Signal Transduction ; T-Lymphocyte Subsets/immunology ; ZAP-70 Protein-Tyrosine Kinase
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  • 146
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    Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-01
    Description: The Epstein-Barr virus (EBV) transactivator protein, termed Epstein-Barr virus nuclear antigen 2 (EBNA2), plays a critical role in the regulation of latent viral transcription and in the immortalization of EBV-infected B cells. Unlike most transcription factors, EBNA2 does not bind directly to its cis-responsive DNA element but requires a cellular factor, termed C-promoter binding factor 1 (CBF1). Here, CBF1 was purified and was found to directly interact with EBNA2. CBF1 is identical to a protein thought to be involved in immunoglobulin gene rearrangement, RBPJ kappa. Contrary to previous reports, CBF1-RBPJ kappa did not bind to the recombination signal sequences but instead bound to sites in the EBV C-promoter and in the CD23 promoter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henkel, T -- Ling, P D -- Hayward, S D -- Peterson, M G -- CA42245/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 1;265(5168):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik Inc, South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8016657" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*genetics ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/chemistry/*genetics/isolation & purification/*metabolism ; Epstein-Barr Virus Nuclear Antigens ; HeLa Cells ; Herpesvirus 4, Human/*genetics/immunology ; Humans ; Immunoglobulin J Recombination Signal Sequence-Binding Protein ; Molecular Sequence Data ; *Nuclear Proteins ; *Promoter Regions, Genetic ; Receptors, IgE/genetics ; Regulatory Sequences, Nucleic Acid ; *Transcriptional Activation
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  • 147
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    TLC1: template RNA component of Saccharomyces cerevisiae telomerase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: Telomeres, the natural ends of linear eukaryotic chromosomes, are essential for chromosome stability. Because of the nature of DNA replication, telomeres require a specialized mechanism to ensure their complete duplication. Telomeres are also capable of silencing the transcription of genes that are located near them. In order to identify genes in the budding yeast Saccharomyces cerevisiae that are important for telomere function, a screen was conducted for genes that, when expressed in high amounts, would suppress telomeric silencing. This screen lead to the identification of the gene TLC1 (telomerase component 1). TLC1 encodes the template RNA of telomerase, a ribonucleoprotein required for telomere replication in a variety of organisms. The discovery of TLC1 confirms the existence of telomerase in S. cerevisiae and may facilitate both the analysis of this enzyme and an understanding of telomere structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, M S -- Gottschling, D E -- CA 14599/CA/NCI NIH HHS/ -- GM43893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):404-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545955" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Fungal/genetics/metabolism ; DNA Nucleotidylexotransferase/chemistry/*genetics/metabolism ; Gene Expression Regulation, Fungal ; *Genes, Fungal ; Molecular Sequence Data ; RNA, Fungal/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Suppression, Genetic ; Telomere/genetics/metabolism ; Templates, Genetic
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    Boron therapy gets early test (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flam, F -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1799.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091207" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Boron Neutron Capture Therapy ; Brain Neoplasms/*radiotherapy ; Clinical Trials as Topic ; Ethics, Medical ; Female ; Glioblastoma/*radiotherapy ; Humans ; Investigational New Drug Application ; Rats ; United States ; United States Food and Drug Administration
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  • 149
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    Protein-DNA recognition: new perspectives and underlying themes (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Hippel, P H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):769-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303292" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Thermodynamics
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  • 150
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    Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: The most frequently occurring resistance of Gram-negative bacteria against tetracyclines is triggered by drug recognition of the Tet repressor. This causes dissociation of the repressor-operator DNA complex and enables expression of the resistance protein TetA, which is responsible for active efflux of tetracycline. The 2.5 angstrom resolution crystal structure of the homodimeric Tet repressor complexed with tetracycline-magnesium reveals detailed drug recognition. The orientation of the operator-binding helix-turn-helix motifs of the repressor is inverted in comparison with other DNA binding proteins. The repressor-drug complex is unable to interact with DNA because the separation of the DNA binding motifs is 5 angstroms wider than usually observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinrichs, W -- Kisker, C -- Duvel, M -- Muller, A -- Tovar, K -- Hillen, W -- Saenger, W -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Kristallographie, Freie Universitat Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153629" target="_blank"〉PubMed〈/a〉
    Keywords: Antiporters/*chemistry/genetics/metabolism ; Bacterial Proteins/*chemistry/genetics/metabolism ; Crystallography, X-Ray ; DNA, Bacterial/metabolism ; Helix-Loop-Helix Motifs ; Hydrogen Bonding ; Magnesium/chemistry ; Models, Molecular ; Mutation ; Operator Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Repressor Proteins/*chemistry/genetics/metabolism ; Tetracycline/*chemistry/metabolism ; *Tetracycline Resistance/genetics
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    Molecule makers learn the rules of a crooked game (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flam, F -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1563-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128241" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Models, Molecular ; Protein Conformation ; *Protein Engineering ; *Protein Folding ; Protein Structure, Secondary
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  • 152
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    Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-09
    Description: The gene aquaporin-1 encodes channel-forming integral protein (CHIP), a member of a large family of water transporters found throughout nature. Three rare individuals were identified who do not express CHIP-associated Colton blood group antigens and whose red cells exhibit low osmotic water permeabilities. Genomic DNA analyses demonstrated that two individuals were homozygous for different nonsense mutations (exon deletion or frameshift), and the third had a missense mutation encoding a nonfunctioning CHIP molecule. Surprisingly, none of the three suffers any apparent clinical consequence, which raises questions about the physiological importance of CHIP and implies that other mechanisms may compensate for its absence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, G M -- Smith, B L -- Zeidel, M L -- Moulds, J J -- Agre, P -- DK32753/DK/NIDDK NIH HHS/ -- HL33991/HL/NHLBI NIH HHS/ -- HL48268/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7521540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaporin 1 ; *Aquaporins ; Base Sequence ; Blood Group Antigens ; Cell Membrane Permeability ; Erythrocyte Membrane/chemistry/physiology ; Exons ; Female ; Homozygote ; Humans ; Ion Channels/blood/*genetics/urine ; Kidney Tubules/chemistry ; Molecular Sequence Data ; Mutation ; Oocytes ; Phenotype ; Polymerase Chain Reaction ; Xenopus
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  • 153
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    High-resolution structure of the oligomerization domain of p53 by multidimensional NMR (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel beta sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clore, G M -- Omichinski, J G -- Sakaguchi, K -- Zambrano, N -- Sakamoto, H -- Appella, E -- Gronenborn, A M -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):386-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023159" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Graphics ; DNA/chemistry/metabolism ; Genes, p53 ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Protein Conformation ; Protein Structure, Secondary ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism
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  • 154
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    Vibrationally coherent photochemistry in the femtosecond primary event of vision (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: Femtosecond pump-probe experiments reveal the impulsive production of photoproduct in the primary event in vision. The retinal chromophore of rhodopsin was excited with a 35-femtosecond pulse at 500 nanometers, and transient changes in absorption were measured with 10-femtosecond probe pulses. At probe wavelengths within the photo-product absorption band, oscillatory features with a period of 550 femtoseconds (60 wavenumbers) were observed whose phase and amplitude demonstrate that they are the result of nonstationary vibrational motion in the ground state of the photoproduct. The observation of coherent vibrational motion of the photoproduct supports the idea that the primary step in vision is a vibrationally coherent process and that the high quantum yield of the cis--〉trans isomerization in rhodopsin is a consequence of the extreme speed of the excited-state torsional motion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Q -- Schoenlein, R W -- Peteanu, L A -- Mathies, R A -- Shank, C V -- EY-02051/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):422-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Materials Sciences Division, Lawrence Berkeley Laboratory, University of California, 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939680" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Fourier Analysis ; Isomerism ; *Light ; Models, Molecular ; Photic Stimulation ; Photochemistry ; Rhodopsin/analogs & derivatives/*chemistry ; Spectrum Analysis ; Vision, Ocular/*physiology
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    The Sverdlovsk anthrax outbreak of 1979 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: In April and May 1979, an unusual anthrax epidemic occurred in Sverdlovsk, Union of Soviet Socialist Republics. Soviet officials attributed it to consumption of contaminated meat. U.S. agencies attributed it to inhalation of spores accidentally released at a military microbiology facility in the city. Epidemiological data show that most victims worked or lived in a narrow zone extending from the military facility to the southern city limit. Farther south, livestock died of anthrax along the zone's extended axis. The zone paralleled the northerly wind that prevailed shortly before the outbreak. It is concluded that the escape of an aerosol of anthrax pathogen at the military facility caused the outbreak.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meselson, M -- Guillemin, J -- Hugh-Jones, M -- Langmuir, A -- Popova, I -- Shelokov, A -- Yampolskaya, O -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1202-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973702" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aerosols ; Aged ; *Air Microbiology ; Animals ; Animals, Domestic ; Anthrax/*epidemiology/history/microbiology/transmission/veterinary ; *Bacillus anthracis/immunology ; Bacterial Vaccines ; Biological Warfare ; *Disease Outbreaks/veterinary ; Female ; History, 20th Century ; Humans ; Male ; Meteorological Concepts ; Middle Aged ; Retrospective Studies ; Spores, Bacterial ; USSR/epidemiology ; Wind
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  • 156
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    Naturally occurring variation in bristle number and DNA polymorphisms at the scabrous locus of Drosophila melanogaster (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: The association between quantitative genetic variation in bristle number and molecular variation at a candidate neurogenic locus, scabrous, was examined in Drosophila melanogaster. Approximately 32 percent of the genetic variation in abdominal bristle number (21 percent for sternopleural bristle number) among 47 second chromosomes from a natural population was correlated with DNA sequence polymorphisms at this locus. Several polymorphic sites associated with large phenotypic effects occurred at intermediate frequency. Quantitative genetic variation in natural populations caused by alleles that have large effects at a few loci and that segregate at intermediate frequencies conflicts with the classical infinitesimal model of the genetic basis of quantitative variation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lai, C -- Lyman, R F -- Long, A D -- Langley, C H -- Mackay, T F -- GM45146/GM/NIGMS NIH HHS/ -- GM45344/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1697-702.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Population Biology, University of California at Davis 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992053" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; DNA/genetics ; *Drosophila Proteins ; Drosophila melanogaster/anatomy & histology/*genetics ; Female ; *Genes, Insect ; *Genetic Variation ; *Glycoproteins ; Haplotypes ; Linkage Disequilibrium ; Male ; Molecular Sequence Data ; Phenotype ; *Polymorphism, Genetic ; Proteins/*genetics ; Restriction Mapping ; Sense Organs/anatomy & histology
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  • 157
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    Coupling of local folding to site-specific binding of proteins to DNA (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-02-11
    Description: Thermodynamic studies have demonstrated the central importance of a large negative heat capacity change (delta C degree assoc) in site-specific protein-DNA recognition. Dissection of the large negative delta C degree assoc and the entropy change of protein-ligand and protein-DNA complexation provide a thermodynamic signature identifying processes in which local folding is coupled to binding. Estimates of the number of residues that fold on binding obtained from this analysis agree with structural data. Structural comparisons indicate that these local folding transitions create key parts of the protein-DNA interface. The energetic implications of this "induced fit" model for DNA site recognition are considered.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spolar, R S -- Record, M T Jr -- GM23467/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):777-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303294" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; *Protein Folding ; Thermodynamics
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  • 158
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    Stopping premature births before it's too late (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radetsky, P -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1486-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985015" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biomarkers/analysis ; Clinical Trials as Topic ; Collagenases/analysis ; Female ; Fibronectins/analysis ; Gap Junctions/physiology ; Genital Diseases, Female/complications/drug therapy ; Humans ; Matrix Metalloproteinase 9 ; Nitric Oxide/analysis ; Obstetric Labor, Premature/etiology/*prevention & control ; Oxytocin/antagonists & inhibitors ; Pregnancy ; Pregnancy Complications, Infectious/drug therapy ; Uterine Contraction
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  • 159
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    Adaptive reversion of a frameshift mutation in Escherichia coli by simple base deletions in homopolymeric runs (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: Spontaneous mutations are thought to occur primarily in growing cells. However, spontaneous mutations also arise in nutritionally deprived cells, and in some cases this process appears to be adaptive. Here it is reported that when a Lac- strain of Escherichia coli is under selection for lactose use, the spectrum of Lac+ mutations that arises is different, and simpler, than that arising without selection. Mutations appearing during selection were mainly one-base deletions in runs of iterated bases. Similar mutations occurring in repetitive DNA elements are associated with a variety of human hereditary diseases and are increased in cells that cannot correct heteroduplex DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2990682/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2990682/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foster, P L -- Trimarchi, J M -- R01 GM054084/GM/NIGMS NIH HHS/ -- R01 GM054084-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):407-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Health, Boston University School of Public Health, MA 02118.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023164" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/*genetics/growth & development/metabolism ; Frameshift Mutation ; Lac Operon ; Lactose/metabolism ; Molecular Sequence Data ; *Mutation ; Recombination, Genetic ; *Selection, Genetic ; *Sequence Deletion ; beta-Galactosidase/metabolism
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    Malaria pathogenesis (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-06-24
    Description: Malaria is a disease caused by repeated cycles of growth of the parasite Plasmodium in the erythrocyte. Various cellular and molecular strategies allow the parasite to evade the human immune response for many cycles of parasite multiplication. Under certain circumstances Plasmodium infection causes severe anemia or cerebral malaria; the expression of disease is influenced by both parasite and host factors, as exemplified by the exacerbation of disease during pregnancy. This article provides an overview of malaria pathogenesis, synthesizing the recent field, laboratory, and epidemiological data that will lead to the development of strategies to reduce mortality and morbidity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, L H -- Good, M F -- Milon, G -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1878-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Malaria Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009217" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia/etiology ; Animals ; Antibodies, Protozoan/immunology ; Erythrocytes/*parasitology ; Female ; Host-Parasite Interactions ; Humans ; Infant, Newborn ; Malaria/complications/immunology/*parasitology ; Malaria, Cerebral/etiology/parasitology ; Malaria, Falciparum/complications/immunology/*parasitology ; Plasmodium/growth & development/immunology/*pathogenicity ; Plasmodium falciparum/growth & development/immunology/pathogenicity ; Pregnancy ; Pregnancy Complications, Parasitic/immunology/parasitology ; Recurrence
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  • 161
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    Adenosine inhibition of mesopontine cholinergic neurons: implications for EEG arousal (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: Increased discharge activity of mesopontine cholinergic neurons participates in the production of electroencephalographic (EEG) arousal; such arousal diminishes as a function of the duration of prior wakefulness or of brain hyperthermia. Whole-cell and extracellular recordings in a brainstem slice show that mesopontine cholinergic neurons are under the tonic inhibitory control of endogenous adenosine, a neuromodulator released during brain metabolism. This inhibitory tone is mediated postsynaptically by an inwardly rectifying potassium conductance and by an inhibition of the hyperpolarization-activated current. These data provide a coupling mechanism linking neuronal control of EEG arousal with the effects of prior wakefulness, brain hyperthermia, and the use of the adenosine receptor blockers caffeine and theophylline.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612520/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612520/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rainnie, D G -- Grunze, H C -- McCarley, R W -- Greene, R W -- R01 MH039683/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):689-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, Harvard University, Brockton, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303279" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*physiology ; Animals ; Arousal/*physiology ; Calcium/metabolism ; Electric Conductivity ; *Electroencephalography/drug effects ; Female ; Frontal Lobe/physiology ; In Vitro Techniques ; Male ; Membrane Potentials ; Neurons/*physiology ; Parasympathetic Nervous System/*physiology ; Potassium/metabolism ; Rats
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    Retention of unassembled components of integral membrane proteins by calnexin (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-01-21
    Description: Quality control mechanisms prevent the cell surface expression of incompletely assembled multisubunit receptors such as the T cell receptor (TCR). The molecular chaperone function of calnexin (IP90, p88), a 90-kilodalton protein that resides in the endoplasmic reticulum (ER), in the retention of representative chains of the TCR-CD3 complex in the ER was tested. Truncation mutants of calnexin, when transiently expressed in COS cells, were exported from the ER and either accumulated in the Golgi or progressed to the cell surface. CD3 epsilon chains cotransfected with the forms of calnexin that were not retained in the ER exited the ER and colocalized with calnexin. Since engineered calnexin determined the intracellular localization of the proteins associated with it, it is concluded that calnexin interacts with incompletely assembled TCR components and retains them in the ER.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rajagopalan, S -- Xu, Y -- Brenner, M B -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):387-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Rheumatology and Immunology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8278814" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3/*metabolism ; Base Sequence ; Calcium-Binding Proteins/analysis/chemistry/*metabolism ; Calnexin ; Cell Line ; Cell Membrane/metabolism ; Endoplasmic Reticulum/*metabolism ; Golgi Apparatus/metabolism ; Histocompatibility Antigens Class I/metabolism ; Lysosomes/metabolism ; Membrane Proteins/analysis/chemistry/*metabolism ; Molecular Sequence Data ; Nuclear Envelope/metabolism ; Receptor-CD3 Complex, Antigen, T-Cell/*metabolism ; Recombinant Proteins/metabolism ; Transfection
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  • 163
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    Clinical trial monitoring: hit or miss? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1534-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202707" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/surgery ; Clinical Trials as Topic/economics/*standards ; Clinical Trials, Phase III as Topic/standards ; Costs and Cost Analysis ; Ethics Committees, Research ; Federal Government ; Female ; *Government Regulation ; Humans ; Informed Consent ; Mastectomy, Segmental ; Multicenter Studies as Topic/economics/*standards ; National Institutes of Health (U.S.)/economics/*standards ; Peer Review, Research ; Randomized Controlled Trials as Topic/standards ; Scientific Misconduct ; United States ; United States Food and Drug Administration
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  • 164
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    Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-21
    Description: After injury to the cell membrane, rapid resealing of the membrane occurs with little loss of intracellular contents. This process has been studied by measurement of the rate of dye loss after membrane puncture in both the sea urchin embryo and 3T3 fibroblasts. Resealing of disrupted cell membranes requires external calcium that can be antagonized by magnesium. Block of multifunctional calcium/calmodulin kinase, which regulates exocytotic vesicle availability at synapses, and of kinesin, which is required for outward-directed transport of vesicles, inhibited membrane resealing. Resealing was also inhibited by botulinum neurotoxins B and A, suggesting that the two synaptosomal-associated proteins synaptobrevin and SNAP-25 also participate in resealing. This pattern of inhibition indicates that the calcium-dependent mechanisms for cell membrane resealing may involve vesicle delivery, docking, and fusion, similar to the exocytosis of neurotransmitters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinhardt, R A -- Bi, G -- Alderton, J M -- R01 AR41129/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):390-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7904084" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Botulinum Toxins/pharmacology ; Calcium/*metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Division/drug effects ; Cell Membrane/drug effects/*physiology ; Female ; Kinesin/physiology ; Magnesium/pharmacology ; Membrane Proteins/physiology ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/physiology ; Neurotransmitter Agents/*metabolism ; Oligopeptides/pharmacology ; Ovum ; R-SNARE Proteins ; Sea Urchins ; Synaptic Transmission ; Synaptosomal-Associated Protein 25 ; Zygote
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    An interleukin-4-induced transcription factor: IL-4 Stat (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: Interleukin-4 (IL-4) is an immunomodulatory cytokine secreted by activated T lymphocytes, basophils, and mast cells. It plays an important role in modulating the balance of T helper (Th) cell subsets, favoring expansion of the Th2 lineage relative to Th1. Imbalance of these T lymphocyte subsets has been implicated in immunological diseases including allergy, inflammation, and autoimmune disease. IL-4 may mediate its biological effects, at least in part, by activating a tyrosine-phosphorylated DNA binding protein. This protein has now been purified and its encoding gene cloned. Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat. Study of the inhibitory activities of phosphotyrosine-containing peptides derived from the intracellular domain of the IL-4 receptor provided evidence for direct coupling of receptor and transcription factor during the IL-4 Stat activation cycle. Such observations indicate that IL-4 Stat has the same functional domain for both receptor coupling and dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hou, J -- Schindler, U -- Henzel, W J -- Ho, T C -- Brasseur, M -- McKnight, S L -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1701-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085155" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cross-Linking Reagents ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Humans ; Interleukin-4/*pharmacology ; Interleukin-4 Receptor alpha Subunit ; Models, Biological ; Molecular Sequence Data ; Monocytes/metabolism ; Phosphopeptides/metabolism/pharmacology ; Phosphorylation ; Polymers ; Receptors, Cell Surface ; Receptors, Interleukin-4 ; Receptors, Mitogen/*metabolism ; STAT6 Transcription Factor ; Trans-Activators/chemistry/genetics/isolation & purification/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism
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  • 166
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    Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-07-15
    Description: The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a model system for genetic and biochemical analysis of protein folding. The x-ray structure of a shortened TSP (residues 109 to 666) was determined to a 2.0 angstrom resolution. Each subunit of the homotrimer contains a large parallel beta helix. The interdigitation of the polypeptide chains at the carboxyl termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinbacher, S -- Seckler, R -- Miller, S -- Steipe, B -- Huber, R -- Reinemer, P -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):383-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023158" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacteriophage P22 ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Glycoside Hydrolases/*chemistry/genetics ; Models, Molecular ; Point Mutation ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Viral Proteins/*chemistry/genetics ; *Viral Tail Proteins
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  • 167
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    Natural vertical transmission of western equine encephalomyelitis virus in mosquitoes (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: The mechanism by which western equine encephalomyelitis (WEE) virus and other mosquito-borne alphaviruses (Togaviridae) survive during periods of vector inactivity is unknown. Recently, three strains of WEE virus were isolated from adult Aedes dorsalis collected as larvae from a salt marsh in a coastal region of California. This provides evidence of vertical transmission of WEE virus in mosquitoes in nature. Vertical transmission in Ae. dorsalis and closely related mosquito species may be an important mechanism for the maintenance of WEE virus in temperate regions in North America where horizontal transmission of the virus is seasonal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fulhorst, C F -- Hardy, J L -- Eldridge, B F -- Presser, S B -- Reeves, W C -- AI-03028/AI/NIAID NIH HHS/ -- AI-26154/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):676-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Public Health, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303276" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/*microbiology ; Animals ; California ; Encephalitis Virus, Western Equine/isolation & purification/*physiology ; Encephalomyelitis, Equine/transmission ; Female ; Insect Vectors/*microbiology ; Larva/microbiology ; Male ; Seasons
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  • 168
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    Cystic fibrosis heterozygote resistance to cholera toxin in the cystic fibrosis mouse model (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: The effect of the number of cystic fibrosis (CF) alleles on cholera toxin (CT)-induced intestinal secretion was examined in the CF mouse model. CF mice that expressed no CF transmembrane conductance regulator (CFTR) protein did not secrete fluid in response to CT. Heterozygotes expressed 50 percent of the normal amount of CFTR protein in the intestinal epithelium and secreted 50 percent of the normal fluid and chloride ion in intestinal epithelium and secreted 50 percent of the normal fluid and chloride ion and fluid secretion suggests that CF heterozygotes might possess a selective advantage of resistance to cholera.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabriel, S E -- Brigman, K N -- Koller, B H -- Boucher, R C -- Stutts, M J -- DK46003/DK/NIDDK NIH HHS/ -- HL34322/HL/NHLBI NIH HHS/ -- HL42384/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):107-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of North Carolina, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7524148" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Body Fluids/*secretion ; Chloride Channels/metabolism ; Chlorides/*metabolism ; Cholera Toxin/*toxicity ; Crosses, Genetic ; Cyclic AMP/metabolism ; Cystic Fibrosis/*genetics/physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator ; Female ; Heterozygote ; Intestinal Mucosa/*secretion ; Intestine, Small/secretion ; Male ; Membrane Proteins/*genetics/metabolism ; Mice
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  • 169
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    Reconstitution of transcription factor SL1: exclusive binding of TBP by SL1 or TFIID subunits (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: RNA polymerase I and II transcription factors SL1 and TFIID, respectively, are composed of the TATA-binding protein (TBP) and a set of TBP-associated factors (TAFs) responsible for promoter recognition. How the universal transcription factor TBP becomes committed to a TFIID or SL1 complex has not been known. Complementary DNAs encoding each of the three TAFIs that are integral components of SL1 have not been isolated. Analysis of subunit interactions indicated that the three TAFIs can bind individually and specifically to TBP. In addition, these TAFIs interact with each other to form a stable TBP-TAF complex. When TBP was bound first by either TAFI110, 63, or 48, subunits of TFIID such as TAFII250 and 150 did not bind TBP. Conversely, if TBP first formed a complex with TAFII250 or 150, the subunits of SL1 did not bind TBP. These results suggest that a mutually exclusive binding specificity for TBP intrinsic to SL1 and TFIID subunits directs the formation of promoter- and RNA polymerase-selective TBP-TAF complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Comai, L -- Zomerdijk, J C -- Beckmann, H -- Zhou, S -- Admon, A -- Tjian, R -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1966-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California at Berkeley 94720-3204.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801123" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; DNA, Complementary/genetics ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; *Pol1 Transcription Initiation Complex Proteins ; Promoter Regions, Genetic ; Protein Binding ; RNA Polymerase I/metabolism ; TATA Box ; *TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; Transcription Factor TFIID ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; Transcription, Genetic
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  • 170
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    Association of poly(CA).poly(TG) DNA fragments into four-stranded complexes bound by HMG1 and 2 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-15
    Description: The tandemly repeated DNA sequence poly(CA).poly(TG) is found in tracts up to 60 base pairs long, dispersed at thousands of sites throughout the genomes of eukaryotes. Double-stranded DNA fragments containing such sequences associated spontaneously with each other in vitro, in the absence of protein, forming stable four-stranded structures that were detected by gel electrophoresis and electron microscopy. These structures were recognized specifically by the nuclear nonhistone high mobility group (HMG) proteins 1 and 2 as evidenced by gel retardation. Such sequence-specific complexes might be involved in vivo in recombination or other processes requiring specific association of two double-stranded DNA molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaillard, C -- Strauss, F -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):433-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Jacques Monod, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153633" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry/metabolism ; Electrophoresis, Polyacrylamide Gel ; High Mobility Group Proteins/chemistry/*metabolism ; Microscopy, Electron ; Molecular Sequence Data ; Nucleic Acid Conformation ; Polydeoxyribonucleotides/*chemistry/metabolism ; *Repetitive Sequences, Nucleic Acid
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  • 171
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    Maternal rescue of transforming growth factor-beta 1 null mice (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-24
    Description: Maternal sources of transforming growth factor-beta 1 (TGF-beta 1) are shown here to contribute to the normal appearance and perinatal survival of TGF-beta 1 null newborn mice. Labeled TGF-beta 1 crossed the placenta and was recovered intact from various tissues after oral administration to mouse pups. TGF beta-1 protein was also detected in cells recovered from breast milk. In immunohistochemical analyses, TGF-beta 1 null embryos and null newborn pups born to TGF-beta 1 heterozygotes stained positive for TGF-beta 1, whereas those born to a null female were negative and had severe cardiac abnormalities. These results suggest an important role for maternal sources of TGF-beta 1 during development and, more generally, provide evidence for maternal rescue of targeted gene disruption in the fetus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letterio, J J -- Geiser, A G -- Kulkarni, A B -- Roche, N S -- Sporn, M B -- Roberts, A B -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1936-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemoprevention, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009224" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Embryonic and Fetal Development ; Female ; Fetus/*metabolism ; Heart Defects, Congenital/etiology ; Heterozygote ; Homozygote ; *Maternal-Fetal Exchange ; Mice ; Milk/chemistry ; Pregnancy ; Transforming Growth Factor beta/analysis/biosynthesis/*metabolism
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    Catalytic activity of an RNA domain derived from the U6-U4 RNA complex (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: U6 RNA contains two regions that are essential for proper splicing of nuclear precursor messenger RNA (pre-mRNA). A comparison of putative secondary structures of the U6-U4 RNA complexes from different phyla revealed a conserved domain that is similar to the catalytic hammerhead RNA motif. Although no catalytic activity was detected in the mammalian U6-U4 RNA complexes, two nucleotide changes in U6 RNA and one in U4 RNA conferred cleavage activity to the complex. Furthermore, the highly conserved domain of the wild-type complex, without the accompanying flanking regions, cleaved an RNA substrate and exhibited other characteristics of the hammerhead ribozyme. The possible involvement of this structure in pre-mRNA splicing is also discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, J H -- Cedergren, R -- Nadal-Ginard, B -- R01 AR36865-08/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):77-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272868" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Humans ; Introns ; Magnesium/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Splicing ; RNA, Catalytic/chemistry/*metabolism ; RNA, Small Nuclear/chemistry/*metabolism ; Yeasts/genetics
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    Lung cancer risk for female smokers (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Risch, H A -- Howe, G R -- Jain, M -- Burch, J D -- Holowaty, E J -- Miller, A B -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1206-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122096" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Lung Neoplasms/*etiology/mortality ; Male ; Risk Factors ; Sex Factors ; Smoking/*adverse effects
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  • 174
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    A subset of CD4+ thymocytes selected by MHC class I molecules (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-25
    Description: To complete their maturation, most immature thymocytes depend on the simultaneous engagement of their antigen receptor [alpha beta T cell receptor (TCR)] and their CD4 or CD8 coreceptors with major histocompatibility complex class II or I ligands, respectively. However, a normal subset of mature alpha beta TCR+ thymocytes did not follow these rules. These thymocytes expressed NK1.1 and a restricted set of alpha beta TCRs that are intrinsically class I-reactive because their positive selection was class I-dependent but CD8-independent. These cells were CD4+ and CD4-8- but never CD8+, because the presence of CD8 caused negative selection. Thus, neither CD4 nor CD8 contributes signals that direct their maturation into the CD4+ and CD4-8- lineages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bendelac, A -- Killeen, N -- Littman, D R -- Schwartz, R H -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1774-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7907820" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/analysis ; Antigens, CD4/analysis ; Antigens, CD8/analysis ; Antigens, Ly ; Antigens, Surface ; CD4-Positive T-Lymphocytes/cytology/*immunology ; Female ; Histocompatibility Antigens Class I/*physiology ; Lectins, C-Type ; Ligands ; Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; NK Cell Lectin-Like Receptor Subfamily B ; Phenotype ; Proteins/analysis ; Receptors, Antigen, T-Cell, alpha-beta/analysis/*physiology ; T-Lymphocyte Subsets/cytology/*immunology
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    Design of a G.C-specific DNA minor groove-binding peptide (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-28
    Description: A four-ring tripeptide containing alternating imidazole and pyrrole carboxamides specifically binds six-base pair 5'-(A,T)GCGC(A,T)-3' sites in the minor groove of DNA. The designed peptide has a specificity completely reversed from that of the tripyrrole distamycin, which binds A,T sequences. Structural studies with nuclear magnetic resonance revealed that two peptides bound side-by-side and in an antiparallel orientation in the minor groove. Each of the four imidazoles in the 2:1 ligand-DNA complex recognized a specific guanine amino group in the GCGC core through a hydrogen bond. Targeting a designated four-base pair G.C tract by this synthetic ligand supports the generality of the 2:1 peptide-DNA motif for sequence-specific minor groove recognition of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geierstanger, B H -- Mrksich, M -- Dervan, P B -- Wemmer, D E -- GM-27681/GM/NIGMS NIH HHS/ -- GM-43129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):646-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Group in Biophysics, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939719" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Computer Graphics ; DNA/chemistry/*metabolism ; Drug Design ; Hydrogen Bonding ; Imidazoles/chemical synthesis/*chemistry/metabolism ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligopeptides/chemical synthesis/*chemistry/metabolism ; Protein Conformation ; Pyrroles/chemical synthesis/*chemistry/metabolism
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    Environmental estrogens stir debate (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, R -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):308-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023147" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Wild/physiology ; Environmental Pollutants/*adverse effects/metabolism/toxicity ; Estrogens/*adverse effects/metabolism/toxicity ; Female ; Humans ; Male ; Pregnancy ; Prenatal Exposure Delayed Effects ; Reproduction/*drug effects ; Sperm Count/drug effects ; Testicular Neoplasms/epidemiology/etiology
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    Target of the transcriptional activation function of phage lambda cI protein (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: Activation of transcription initiation by the cI protein of phage lambda is thought to be mediated by a direct interaction between cl and RNA polymerase at the PRM promoter. Two negatively charged amino acid residues in the DNA binding domain of cI play a key role in activation, suggesting that these residues contact RNA polymerase. The subunit of RNA polymerase involved was identified by selecting polymerase mutants that restored the activation function of a mutant form of cI protein. Although previous studies suggest that several activators interact with the alpha subunit of RNA polymerase, the results here suggest that cI interacts with the sigma subunit. An arginine to histidine change near the carboxyl terminus of sigma specifically suppresses an aspartic acid to asparagine change in the activation region of cI. This finding supports the direct-contact model and suggests that a cluster of positively charged residues near the carboxyl terminus of sigma is the target of the negatively charged activation region of cI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, M -- Moyle, H -- Susskind, M M -- GM36811/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):75-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California, Los Angeles 90089-1340.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272867" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage P22/genetics ; Bacteriophage lambda/*genetics ; Base Sequence ; *DNA-Binding Proteins ; DNA-Directed RNA Polymerases/genetics/metabolism ; Models, Genetic ; Molecular Sequence Data ; Promoter Regions, Genetic ; Repressor Proteins/chemistry/*genetics/metabolism ; Sigma Factor/chemistry/*genetics/metabolism ; Suppression, Genetic ; Transcription Factors/chemistry/*genetics/metabolism ; *Transcriptional Activation ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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    Rise and fall of the Y chromosome (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1994 Jan 14;263(5144):171-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8284667" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila melanogaster/genetics ; Female ; Humans ; Male ; Mutation ; *Recombination, Genetic ; Sex Determination Analysis ; *Y Chromosome
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    Kin selection, social structure, gene flow, and the evolution of chimpanzees (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: Hypotheses about chimpanzee social behavior, phylogeography, and evolution were evaluated by noninvasive genotyping of free-ranging individuals from 20 African sites. Degrees of relatedness among individuals in one community were inferred from allele-sharing at eight nuclear simple sequence repeat (SSR) loci. Males are related on the order of half-siblings, and homozygosity is significantly increased at several SSR loci compared to Hardy-Weinberg expectations. These data support the kin-selection hypothesis for the evolution of cooperation among males. Sequence variation patterns at two mitochondrial loci indicate historically high long-distance gene flow and clarify the relationships among three allopatric subspecies. The unexpectedly large genetic distance between the western subspecies, Pan troglodytes verus, and the other two subspecies suggests a divergence time of about 1.58 million years. This result, if confirmed at nuclear loci and supported by eco-behavioral data, implies that P. t. verus should be elevated to full species rank.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morin, P A -- Moore, J J -- Chakraborty, R -- Jin, L -- Goodall, J -- Woodruff, D S -- 1T32 HG00005-02/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1193-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7915048" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Alleles ; Animals ; Base Sequence ; *Biological Evolution ; DNA/analysis/genetics ; Female ; *Genetic Variation ; Hair/chemistry ; Male ; Molecular Sequence Data ; Pan troglodytes/classification/*genetics/psychology ; Phylogeny ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; *Social Behavior ; Tanzania
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    Crystal structure of the principal neutralization site of HIV-1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-04-01
    Description: The crystal structure of a complex between a 24-amino acid peptide from the third variable (V3) loop of human immunodeficiency virus-type 1 (HIV-1) gp 120 and the Fab fragment of a broadly neutralizing antibody (59.1) was determined to 3 angstrom resolution. The tip of the V3 loop containing the Gly-Pro-Gly-Arg-Ala-Phe sequence adopts a double-turn conformation, which may be the basis of its conservation in many HIV-1 isolates. A complete map of the HIV-1 principal neutralizing determinant was constructed by stitching together structures of V3 loop peptides bound to 59.1 and to an isolate-specific (MN) neutralizing antibody (50.1). Structural conservation of the overlapping epitopes suggests that this biologically relevant conformation could be of use in the design of synthetic vaccines and drugs to inhibit HIV-1 entry and virus-related cellular fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghiara, J B -- Stura, E A -- Stanfield, R L -- Profy, A T -- Wilson, I A -- GM-46192/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):82-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7511253" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/immunology ; Antigen-Antibody Complex/*chemistry/immunology ; Antigen-Antibody Reactions ; Computer Graphics ; Crystallography, X-Ray ; Epitopes/chemistry/immunology ; HIV Antibodies/*chemistry/immunology ; HIV Envelope Protein gp120/*chemistry/immunology ; HIV-1/*chemistry/immunology ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/*chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Neutralization Tests ; Peptide Fragments/*chemistry/immunology ; Protein Conformation ; Protein Structure, Secondary
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    Suppression of hyphal formation in Candida albicans by mutation of a STE12 homolog (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: A Candida albicans gene (CPH1) was cloned that encodes a protein homologous to Saccharomyces cerevisiae Ste12p, a transcription factor that is the target of the pheromone response mitogen-activated protein kinase cascade. CPH1 complements both the mating defect of ste12 haploids and the filamentous growth defect of ste12/ste12 diploids. Candida albicans strains without a functional CPH1 gene (cph1/cph1) show suppressed hyphal formation on solid medium. However, cph1/cph1 strains can still form hyphae in liquid culture and in response to serum. Thus, filamentous growth may be activated in C. albicans by the same signaling kinase cascade that activates Ste12p in S. cerevisiae; however, alternative pathways may exist in C. albicans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, H -- Kohler, J -- Fink, G R -- GM402661/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1723-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992058" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Candida albicans/cytology/genetics/*growth & development ; Cloning, Molecular ; Culture Media ; Fungal Proteins/chemistry/*genetics/physiology ; *Genes, Fungal ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Saccharomyces cerevisiae/cytology/genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/chemistry/*genetics/physiology
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    High-resolution molecular discrimination by RNA (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-03-11
    Description: Species of RNA that bind with high affinity and specificity to the bronchodilator theophylline were identified by selection from an oligonucleotide library. One RNA molecule binds to theophylline with a dissociation constant Kd of 0.1 microM. This binding affinity is 10,000-fold greater than the RNA molecule's affinity for caffeine, which differs from theophylline only by a methyl group at nitrogen atom N-7. Analysis by nuclear magnetic resonance indicates that this RNA molecule undergoes a significant change in its conformation or dynamics upon theophylline binding. Binding studies of compounds chemically related to theophylline have revealed structural features required for the observed binding specificity. These results demonstrate the ability of RNA molecules to exhibit an extremely high degree of ligand recognition and discrimination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenison, R D -- Gill, S C -- Pardi, A -- Polisky, B -- AI01051/AI/NIAID NIH HHS/ -- AI33098/AI/NIAID NIH HHS/ -- RR03283/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1425-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NeXagen, Inc., Boulder, CO 80301.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7510417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Binding, Competitive ; DNA, Complementary/chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; RNA/chemistry/*metabolism ; Sequence Analysis, DNA ; Theophylline/chemistry/*metabolism ; Xanthines/chemistry/metabolism
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    Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6 (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-04-01
    Description: The STAT family of proteins carries out a dual function: signal transduction and activation of transcription. A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor (EGF) and interleukin-6 (IL-6) but not interferon gamma (IFN-gamma). It is likely that this phosphoprotein forms homodimers as well as heterodimers with the first described member of the STAT family, Stat91 (renamed Stat1 alpha), which is activated by the IFNs and EGF. Differential activation of different STAT proteins in response to different ligands should help to explain specificity in nuclear signaling from the cell surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhong, Z -- Wen, Z -- Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):95-8.〈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/8140422" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/isolation & purification/*metabolism ; Epidermal Growth Factor/*pharmacology ; Humans ; Interferon-gamma ; Interleukin-6/*pharmacology ; Mice ; Molecular Sequence Data ; Phosphorylation ; Regulatory Sequences, Nucleic Acid ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Sequence Alignment ; Trans-Activators/metabolism ; Transfection ; Tumor Cells, Cultured ; Tyrosine/metabolism
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    DNA bending by asymmetric phosphate neutralization (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-12-16
    Description: DNA is often bent when complexed with proteins. Understanding the forces responsible for DNA bending would be of fundamental value in exploring the interplay of these macromolecules. A series of experiments was devised to test the hypothesis that proteins with cationic surfaces can induce substantial DNA bending by neutralizing phosphates on one DNA face. Repulsions between phosphates in the remaining anionic helix are predicted to result in an unbalanced compression force acting to deform the DNA toward the protein. This hypothesis is supported by the results of electrophoretic experiments in which DNA spontaneously bends when one helical face is partially modified by incorporation of neutral phosphate analogs. Phasing with respect to a site of intrinsic DNA curvature (hexadeoxyadenylate tract) permits estimation of the electrostatic bend angle, and demonstrates that such modified DNAs are deformed toward the neutralized surface, as predicted. Similar model systems may be useful in exploring the extent to which phosphate neutralization can account for DNA bending by particular proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strauss, J K -- Maher, L J 3rd -- GM47814/GM/NIGMS NIH HHS/ -- P30 CA36727-08/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1829-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68198-6805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997878" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cations/chemistry ; DNA/*chemistry ; DNA-Binding Proteins/chemistry ; Electrochemistry ; Electrophoresis, Polyacrylamide Gel ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleosomes/chemistry ; Oligodeoxyribonucleotides ; Organophosphorus Compounds/chemistry ; Phosphates/*chemistry ; Thermodynamics
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    The TATA-binding protein: a general transcription factor in eukaryotes and archaebacteria (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-27
    Description: The TATA-binding protein TBP appears to be essential for all transcription in eukaryotic cell nuclei, which suggests that its function was established early in evolution. Archaebacteria constitute a kingdom of organisms distinct from eukaryotes and eubacteria. Archaebacterial gene regulatory sequences often map to TATA box-like motifs. Here it is shown that the archaebacterium Pyrococcus woesei expresses a protein with structural and functional similarity to eukaryotic TBP molecules. This suggests that TBP's role in transcription was established before the archaebacterial and eukaryotic lineages diverged and that the transcription systems of archaebacteria and eukaryotes are fundamentally homologous.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowlands, T -- Baumann, P -- Jackson, S P -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1994 May 27;264(5163):1326-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome/CRC Institute, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191287" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/genetics ; Amino Acid Sequence ; Arabidopsis/genetics ; Archaea/chemistry/*genetics/metabolism ; Base Sequence ; *Biological Evolution ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Eukaryotic Cells/*metabolism ; Genes, Bacterial ; Molecular Sequence Data ; Polymerase Chain Reaction ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins ; *TATA Box ; TATA-Box Binding Protein ; Transcription Factor TFIIB ; *Transcription Factor TFIIIB ; Transcription Factors/chemistry/*genetics/metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/genetics
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  • 186
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    Coaxially stacked RNA helices in the catalytic center of the Tetrahymena ribozyme (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: Coaxial stacking of helical elements is a determinant of three-dimensional structure in RNA. In the catalytic center of the Tetrahymena group I intron, helices P4 and P6 are part of a tertiary structural domain that folds independently of the remainder of the intron. When P4 and P6 were fused with a phosphodiester linkage, the resulting RNA retained the detailed tertiary interactions characteristic of the native P4-P6 domain and even required lower magnesium ion concentrations for folding. These results indicate that P4 and P6 are coaxial in the P4-P6 domain and, therefore, in the native ribozyme. Helix fusion could provide a general method for identifying pairs of coaxially stacked helices in biological RNA molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, F L -- Wang, Y H -- Griffith, J D -- Cech, T R -- GM31819/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085157" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Edetic Acid ; Electrophoresis, Polyacrylamide Gel ; Ferrous Compounds ; Introns ; Magnesium/pharmacology ; Molecular Sequence Data ; *Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/ultrastructure ; RNA, Protozoan/*chemistry/ultrastructure ; Tetrahymena/*genetics
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  • 187
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    Crystal structure of a catalytic antibody with a serine protease active site (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-19
    Description: The three-dimensional structure of an unusually active hydrolytic antibody with a phosphonate transition state analog (hapten) bound to the active site has been solved to 2.5 A resolution. The antibody (17E8) catalyzes the hydrolysis of norleucine and methionine phenyl esters and is selective for amino acid esters that have the natural alpha-carbon L configuration. A plot of the pH-dependence of the antibody-catalyzed reaction is bell-shaped with an activity maximum at pH 9.5; experiments on mechanism lend support to the formation of a covalent acyl-antibody intermediate. The structural and kinetic data are complementary and support a hydrolytic mechanism for the antibody that is remarkably similar to that of the serine proteases. The antibody active site contains a Ser-His dyad structure proximal to the phosphorous atom of the bound hapten that resembles two of the three components of the Ser-His-Asp catalytic triad of serine proteases. The antibody active site also contains a Lys residue to stabilize oxyanion formation, and a hydrophobic binding pocket for specific substrate recognition of norleucine and methionine side chains. The structure identifies active site residues that mediate catalysis and suggests specific mutations that may improve the catalytic efficiency of the antibody. This high resolution structure of a catalytic antibody-hapten complex shows that antibodies can converge on active site structures that have arisen through natural enzyme evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, G W -- Guo, J -- Huang, W -- Fletterick, R J -- Scanlan, T S -- DK39304/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1059-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Catalytic/*chemistry/immunology/metabolism ; Binding Sites ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Haptens/metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Serine Endopeptidases/*chemistry/metabolism
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  • 188
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    Role of a conserved retinoic acid response element in rhombomere restriction of Hoxb-1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: After activation in mesoderm and neuroectoderm, expression of the Hoxb-1 gene is progressively restricted to rhombomere (r) 4 in the hindbrain. Analysis of the chick and mouse Hoxb-1 genes identified positive and negative regulatory regions that cooperate to mediate segment-restricted expression during rhombomere formation. An enhancer generates expression extending into r3 and r5, and a repressor limits this domain to r4. The repressor contains a conserved retinoic acid response element, point mutations in which allow expression to spread into adjacent rhombomeres. Retinoids and their nuclear receptors may therefore participate in sharpening segment-restricted expression of Hoxb-1 during rhombomere boundary formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Studer, M -- Popperl, H -- Marshall, H -- Kuroiwa, A -- Krumlauf, R -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1728-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lab of Developmental Neurobiology, National Institute for Medical Research, Mill Hill, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7916164" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chick Embryo ; Enhancer Elements, Genetic ; Gene Expression Regulation ; *Genes, Homeobox ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Neural Crest/metabolism ; Oligonucleotides/metabolism ; Point Mutation ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Retinoic Acid/metabolism ; *Regulatory Sequences, Nucleic Acid ; Retinoid X Receptors ; Rhombencephalon/*embryology/metabolism ; *Transcription Factors ; Tretinoin/*pharmacology
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  • 189
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    An experimental study of inbreeding depression in a natural habitat (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: Inbreeding is known to lead to decreased survival and reproduction in captive populations of animals. It is also important to know whether inbreeding has deleterious effects in natural habitats. An estimate was made of the effects of inbreeding in white-footed mice, Peromyscus leucopus noveboracensis, derived from a wild population. This study demonstrates that inbreeding had a significant detrimental effect on the survivorship of mice reintroduced into a natural habitat. This effect was more severe than the effect observed in laboratory studies of the population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jimenez, J A -- Hughes, K A -- Alaks, G -- Graham, L -- Lacy, R C -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):271-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Illinois-Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939661" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Animals ; Body Weight ; Female ; *Inbreeding ; Likelihood Functions ; Male ; Peromyscus/genetics/*physiology ; Regression Analysis ; Survival Rate
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  • 190
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    Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-28
    Description: A gene encoding a protein related to the serpin family of protease inhibitors was identified as a candidate tumor suppressor gene that may play a role in human breast cancer. The gene product, called maspin, is expressed in normal mammary epithelial cells but not in most mammary carcinoma cell lines. Transfection of MDA-MB-435 mammary carcinoma cells with the maspin gene did not alter the cells' growth properties in vitro, but reduced the cells' ability to induce tumors and metastasize in nude mice and to invade through a basement membrane matrix in vitro. Analysis of human breast cancer specimens revealed that loss of maspin expression occurred most frequently in advanced cancers. These results support the hypothesis that maspin functions as a tumor suppressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, Z -- Anisowicz, A -- Hendrix, M J -- Thor, A -- Neveu, M -- Sheng, S -- Rafidi, K -- Seftor, E -- Sager, R -- CA39814/CA/NCI NIH HHS/ -- P01 CA22427/CA/NCI NIH HHS/ -- R01 CA59702/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 28;263(5146):526-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cancer Genetics, Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8290962" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Breast/*chemistry ; Breast Neoplasms/*chemistry/pathology ; Down-Regulation ; Epithelium/chemistry ; Female ; Gene Expression ; Genes, Tumor Suppressor ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasm Metastasis ; Neoplasm Transplantation ; Neoplasms, Experimental/pathology ; Proteins/analysis/genetics/*physiology ; Sequence Analysis ; Serpins/analysis/genetics/*physiology ; Transfection ; Tumor Cells, Cultured
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  • 191
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    Analysis and expression of a cloned pre-T cell receptor gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: The T cell antigen receptor (TCR) beta chain regulates early T cell development in the absence of the TCR alpha chain. The developmentally controlled gene described here encodes the pre-TCR alpha (pT alpha) chain, which covalently associates with TCR beta and with the CD3 proteins forms a pre-TCR complex that transduces signals in immature thymocytes. Unlike the lambda 5 pre-B cell receptor protein, the pT alpha chain is a type I transmembrane protein whose cytoplasmic tail contains two potential phosphorylation sites and a Src homology 3 (SH3)-domain binding sequence. Pre-TCR alpha transfection experiments indicated that surface expression of the pre-TCR is controlled by additional developmentally regulated proteins. Identification of the pT alpha gene represents an essential step in the structure-function analysis of the pre-TCR complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saint-Ruf, C -- Ungewiss, K -- Groettrup, M -- Bruno, L -- Fehling, H J -- von Boehmer, H -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1208-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite INSERM 373, Institut Necker, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973703" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3/metabolism ; Base Sequence ; Cell Line ; *Cloning, Molecular ; DNA, Complementary/genetics ; *Gene Expression Regulation, Developmental ; Gene Rearrangement ; Membrane Glycoproteins/chemistry/*genetics/metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Open Reading Frames ; Phosphorylation ; Polymerase Chain Reaction ; Rabbits ; Receptors, Antigen, T-Cell, alpha-beta/chemistry/*genetics/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology ; Transfection
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  • 192
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    Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-30
    Description: The complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII reveals that it contains 269 predicted or known genes (300 base pairs or larger). Fifty-nine of these genes (22 percent) were previously identified. Of the 210 novel genes, 65 are predicted to encode proteins that are similar to other proteins of known or predicted function. Sixteen genes appear to be relatively recently duplicated. On average, there is one gene approximately every 2 kilobases. Although the coding density and base composition across the chromosome are not uniform, no regular pattern of variation is apparent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnston, M -- Andrews, S -- Brinkman, R -- Cooper, J -- Ding, H -- Dover, J -- Du, Z -- Favello, A -- Fulton, L -- Gattung, S -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2077-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091229" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Fungal ; DNA, Fungal/genetics ; *Genes, Fungal ; Introns ; Multigene Family ; Open Reading Frames ; RNA, Fungal/genetics ; RNA, Transfer/genetics ; Saccharomyces cerevisiae/*genetics
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  • 193
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    DNA fingerprinting (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovell, W S -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):201-2; author reply 202-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939647" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Dna ; DNA Fingerprinting/*statistics & numerical data ; Gene Frequency ; Humans ; Jurisprudence ; Probability
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  • 194
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    Coordinate initiation of Drosophila development by regulated polyadenylation of maternal messenger RNAs (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-23
    Description: Pattern formation in Drosophila depends initially on the translational activation of maternal messenger RNAs (mRNAs) whose protein products determine cell fate. Three mRNAs that dictate anterior, dorsoventral, and terminal specification--bicoid, Toll, and torso, respectively--showed increases in polyadenylate [poly(A)] tail length concomitant with translation. In contrast, posteriorly localized nanos mRNA, although also translationally activated, was not regulated by poly(A) status. These results implicate at least two mechanisms of mRNA activation in flies. Studies with bicoid mRNA showed that cytoplasmic polyadenylation is necessary for translation, establishing this pathway as essential for embryogenesis. Combined, these experiments identify a regulatory pathway that can coordinate initiation of maternal pattern formation systems in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salles, F J -- Lieberfarb, M E -- Wreden, C -- Gergen, J P -- Strickland, S -- GM51584/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1996-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University Medical Center at Stony Brook, NY 11794-8651.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801127" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cytoplasm/metabolism ; Drosophila/*embryology/genetics ; *Drosophila Proteins ; Embryonic Development ; Female ; *Homeodomain Proteins ; Insect Hormones/genetics ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Morphogenesis ; Ovary/metabolism ; Poly A/*metabolism ; *Protein Biosynthesis ; Protein-Tyrosine Kinases/genetics ; RNA, Messenger/genetics/*metabolism ; *RNA-Binding Proteins ; *Receptor Protein-Tyrosine Kinases ; *Receptors, Cell Surface ; Toll-Like Receptors ; *Trans-Activators
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  • 195
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    Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-21
    Description: Collagenase is a zinc-dependent endoproteinase and is a member of the matrix metalloproteinase (MMP) family of enzymes. The MMPs participate in connective tissue remodeling events and aberrant regulation has been associated with several pathologies. The 2.4 angstrom resolution structure of the inhibited enzyme revealed that, in addition to the catalytic zinc, there is a second zinc ion and a calcium ion which play a major role in stabilizing the tertiary structure of collagenase. Despite scant sequence homology, collagenase shares structural homology with two other endoproteinases, bacterial thermolysin and crayfish astacin. The detailed description of protein-inhibitor interactions present in the structure will aid in the design of compounds that selectively inhibit individual members of the MMP family. Such inhibitors will be useful in examining the function of MMPs in pathological processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovejoy, B -- Cleasby, A -- Hassell, A M -- Longley, K -- Luther, M A -- Weigl, D -- McGeehan, G -- McElroy, A B -- Drewry, D -- Lambert, M H -- New York, N.Y. -- Science. 1994 Jan 21;263(5145):375-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Research Institute, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8278810" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/metabolism ; Collagenases/*chemistry/metabolism ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Matrix Metalloproteinase 8 ; Matrix Metalloproteinase Inhibitors ; Metalloendopeptidases/chemistry ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermolysin/chemistry ; Zinc/metabolism
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  • 196
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    Mapping the lectin-like activity of tumor necrosis factor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-11
    Description: Tumor necrosis factor (TNF), but not lymphotoxin (LT), is directly trypanolytic for salivarian trypanosomes. This activity was not blocked by soluble 55-kilodalton and 75-kilodalton TNF receptors, but was potently inhibited by N,N'-diacetylchitobiose, an oligosaccharide that binds TNF. Comparative sequence analysis of TNF and LT localized the trypanocidal region, and synthetic peptides were trypanolytic. TNF molecules in which the trypanocidal region was mutated or deleted retained tumoricidal activity. Thus, trypanosome-TNF interactions occur via a TNF domain, probably with lectin-like affinity, which is functionally and spatially distinct from the mammalian TNF receptor binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lucas, R -- Magez, S -- De Leys, R -- Fransen, L -- Scheerlinck, J P -- Rampelberg, M -- Sablon, E -- De Baetselier, P -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):814-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Immunology, University of Brussels, Sint-Genesius-Rode, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303299" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Disaccharides ; Glucans/metabolism/pharmacology ; L Cells (Cell Line) ; Lectins/chemistry/metabolism/*pharmacology ; Lymphotoxin-alpha/pharmacology ; Mice ; Molecular Sequence Data ; Mutation ; Peptide Fragments/chemistry/pharmacology ; Receptors, Tumor Necrosis Factor/metabolism ; Trypanosoma brucei brucei/*drug effects ; Tumor Necrosis Factor-alpha/chemistry/genetics/metabolism/*pharmacology
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  • 197
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    Induction of an olfactory memory by the activation of a metabotropic glutamate receptor (1994)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1994-07-08
    Description: Female mice form an olfactory memory of male pheromones at mating; exposure to the pheromones of a strange male after that mating will block pregnancy. The formation of this memory is mediated by the accessory olfactory system, in which an increase in norepinephrine after mating reduces inhibitory transmission of gamma-aminobutyric acid from the granule cells to the mitral cells. This study shows that the activation of mGluR2, a metabotropic glutamate receptor that suppresses the gamma-aminobutyric acid inhibition of the mitral cells, permits the formation of a specific olfactory memory without the occurrence of mating by infusion of mGluR2 agonists into the female's accessory olfactory bulb. This memory faithfully reflects the memory formed at mating.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaba, H -- Hayashi, Y -- Higuchi, T -- Nakanishi, S -- New York, N.Y. -- Science. 1994 Jul 8;265(5169):262-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Kochi Medical School, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023145" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cycloleucine/analogs & derivatives/pharmacology ; Cyclopropanes/pharmacology ; Estrus ; Female ; Glycine/analogs & derivatives/pharmacology ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; Neuronal Plasticity ; Olfactory Bulb/cytology/*physiology ; Phentolamine/pharmacology ; Pheromones/*pharmacology ; Pregnancy ; Pregnancy, Animal/drug effects/*physiology ; Receptors, AMPA/metabolism ; Receptors, Glutamate/*metabolism ; Receptors, Kainic Acid/metabolism ; Sexual Behavior, Animal/drug effects/*physiology ; gamma-Aminobutyric Acid/metabolism
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  • 198
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    Orientation selectivity of cortical neurons during intracellular blockade of inhibition (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: Neurons in the primary visual cortex of the cat are selectively activated by stimuli with particular orientations. This selectivity can be disrupted by the application of antagonists of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) to a local region of the cortex. In order to determine whether inhibitory inputs are necessary for a single cortical neuron to show orientation selectivity, GABA receptors were blocked intracellularly during whole cell recording. Although the membrane potential, spontaneous activity, subfield antagonism, and directional selectivity of neurons were altered after they were perfused internally with the blocking solution, 18 out of 18 neurons remained selective for stimulus orientation. These results indicate that excitatory inputs are sufficient to generate orientation selectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, S -- Toth, L -- Sheth, B -- Sur, M -- EY06363/EY/NEI NIH HHS/ -- EY07023/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):774-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8047882" target="_blank"〉PubMed〈/a〉
    Keywords: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid/pharmacology ; Animals ; Cats ; Cesium/pharmacology ; Electric Stimulation ; Evoked Potentials/drug effects/physiology ; Female ; Fluorides/pharmacology ; Form Perception/physiology ; In Vitro Techniques ; Muscimol/pharmacology ; Neural Inhibition/drug effects/*physiology ; Neurons/drug effects/*physiology ; Orientation/physiology ; Photic Stimulation ; Picrotoxin/pharmacology ; Rats ; Visual Cortex/*cytology/drug effects/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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  • 199
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    Cortical reorganization and deafferentation in adult macaques (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lund, J P -- Sun, G D -- Lamarre, Y -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):546-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036500" target="_blank"〉PubMed〈/a〉
    Keywords: Afferent Pathways ; Animals ; *Brain Mapping ; Denervation ; Face/innervation ; Female ; Jaw/innervation ; Macaca mulatta ; Neuronal Plasticity ; Neurons, Afferent/*physiology ; Somatosensory Cortex/*physiology ; Thumb/innervation ; Trigeminal Nerve/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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  • 200
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    Control of cell behavior during vertebrate development by Slug, a zinc finger gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-06
    Description: Slug, a vertebrate gene encoding a zinc finger protein of the Snail family, is expressed in the neural crest and in mesodermal cells emigrating from the primitive streak. Early chick embryos were incubated with antisense oligonucleotides to chick Slug. These oligonucleotides specifically inhibit the normal change in cell behavior that occurs at the two sites in the emerging body plan in which the gene is expressed. This change, which is the transition from epithelial to mesenchymal character, occurs at the formation of mesoderm during gastrulation and on emigration of the neutral crest from the neural tube.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nieto, M A -- Sargent, M G -- Wilkinson, D G -- Cooke, J -- New York, N.Y. -- Science. 1994 May 6;264(5160):835-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto Cajal, Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7513443" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/analysis ; Antigens, CD57 ; Antigens, Differentiation, T-Lymphocyte/analysis ; Base Sequence ; Blastoderm/cytology ; Cell Movement ; Central Nervous System/*embryology ; Chick Embryo ; Gastrula/*cytology ; Gene Expression ; In Situ Hybridization ; Mesoderm/*cytology ; Molecular Sequence Data ; Neural Crest/cytology/immunology ; Oligonucleotides, Antisense/pharmacology ; Transcription Factors/chemistry/*genetics ; Transcription, Genetic ; Zinc Fingers/*genetics
    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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