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  • Mutation  (83)
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Association of Petroleum Geologists (AAPG)
  • Elsevier
  • 2015-2019
  • 1995-1999  (83)
  • 1990-1994
  • 1995  (83)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Association of Petroleum Geologists (AAPG)
  • Elsevier
  • Springer  (5)
  • Wiley-Blackwell  (4)
Years
  • 2015-2019
  • 1995-1999  (83)
  • 1990-1994
Year
  • 1
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    The chromodomain protein Swi6: a key component at fission yeast centromeres (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Centromeres attach chromosomes to the spindle during mitosis, thereby ensuring the equal distribution of chromosomes into daughter cells. Transcriptionally silent heterochromatin of unknown function is associated with centromeres in many organisms. In the fission yeast Schizosaccharomyces pombe, the silent mating-type loci, centromeres, and telomeres are assembled into silent heterochromatin-like domains. The Swi6 chromodomain protein affects this silencing, and now it is shown that Swi6p localizes with these three chromosomal regions. In cells lacking Swi6p, centromeres lag on the spindle during anaphase and chromosomes are lost at high rates. Thus, Swi6p is located at fission yeast centromeres and is required for their proper function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekwall, K -- Javerzat, J P -- Lorentz, A -- Schmidt, H -- Cranston, G -- Allshire, R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1429-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Human Genetics Unit, Western General Hospital, Edinburgh, Scotland, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660126" target="_blank"〉PubMed〈/a〉
    Keywords: Centromere/chemistry/*physiology ; Chromosomes, Fungal ; Fluorescent Antibody Technique ; Fungal Proteins/analysis/genetics/*physiology ; Genes, Fungal ; Genes, Mating Type, Fungal ; Heterochromatin/chemistry ; In Situ Hybridization, Fluorescence ; Interphase ; Mitosis ; Mutation ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/genetics/*physiology ; Telomere/chemistry ; Transcription Factors/analysis/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    The nematode Caenorhabditis elegans and its genome (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: Over the past two decades, the small soil nematode Caenorhabditis elegans has become established as a major model system for the study of a great variety of problems in biology and medicine. One of its most significant advantages is its simplicity, both in anatomy and in genomic organization. The entire haploid genetic content amounts to 100 million base pairs of DNA, about 1/30 the size of the human value. As a result, C. elegans has also provided a pilot system for the construction of physical maps of larger animal and plant genomes, and subsequently for the complete sequencing of those genomes. By mid-1995, approximately one-fifth of the complete DNA sequence of this animal had been determined. Caenorhabditis elegans provides a test bed not only for the development and application of mapping and sequencing technologies, but also for the interpretation and use of complete sequence information. This article reviews the progress so far toward a realizable goal--the total description of the genome of a simple animal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hodgkin, J -- Plasterk, R H -- Waterston, R H -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):410-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics ; *Chromosome Mapping ; Gene Expression ; *Genes, Helminth ; *Genome ; Mutation ; *Sequence Analysis, DNA
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  • 3
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    A neuropeptide gene defined by the Drosophila memory mutant amnesiac (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Mutations in genes required for associative learning and memory in Drosophila exist, but isolation of the genes has been difficult because most are defined by a single, chemically induced allele. Here, a simplified genetic screen was used to identify candidate genes involved in learning and memory. Second site suppressors of the dunce (dnc) female sterility phenotype were isolated with the use of transposon mutagenesis. One suppressor mutation that was recovered mapped in the amnesiac (amn) gene. Cloning of the locus revealed that amn encodes a previously uncharacterized neuropeptide gene. Thus, with the cloning of amn, specific neuropeptides are implicated in the memory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feany, M B -- Quinn, W G -- New York, N.Y. -- Science. 1995 May 12;268(5212):869-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Codon ; DNA Transposable Elements ; DNA, Complementary/genetics ; Drosophila/*genetics/physiology ; *Drosophila Proteins ; Female ; *Genes, Insect ; Growth Hormone-Releasing Hormone/chemistry/genetics ; Male ; Memory/*physiology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Neuropeptides/chemistry/*genetics ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Sequence Homology, Amino Acid ; Suppression, Genetic
    Print ISSN: 0036-8075
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  • 4
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    Masking of the CBF1/RBPJ kappa transcriptional repression domain by Epstein-Barr virus EBNA2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2) is a transcriptional activator that is essential for EBV-driven B cell immortalization. EBNA2 is targeted to responsive promoters through interaction with a cellular DNA binding protein, C promoter binding factor 1 (CBF1). A transcriptional repression domain has been identified within CBF1. This domain also interacts with EBNA2, and repression is masked by EBNA2 binding. Thus, EBNA2 acts by countering transcriptional repression. Mutation at amino acid 233 of CBF1 abolishes repression and correlates with a loss-of-function mutation in the Drosophila homolog Su(H).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsieh, J J -- Hayward, S D -- CA42245/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725102" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Epstein-Barr Virus Nuclear Antigens ; *Gene Expression Regulation ; HeLa Cells ; Humans ; Immunoglobulin J Recombination Signal Sequence-Binding Protein ; Models, Genetic ; Mutation ; *Nuclear Proteins ; Promoter Regions, Genetic ; Trans-Activators/chemistry/*metabolism ; *Transcription, Genetic ; Transfection
    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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  • 5
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    Defects in the barrier (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roop, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):474-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7529942" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Membrane/metabolism ; Humans ; Ichthyosis/*genetics/metabolism/pathology ; Ichthyosis, Lamellar/*genetics/metabolism/pathology ; Intermediate Filaments/metabolism/ultrastructure ; Keratinocytes/metabolism/*ultrastructure ; Keratins/genetics ; Lipid Metabolism ; Mutation ; Transglutaminases/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Mutations of keratinocyte transglutaminase in lamellar ichthyosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Lamellar ichthyosis is a severe congenital skin disorder characterized by generalized large scales and variable redness. Affected individuals in three families exhibited drastically reduced keratinocyte transglutaminase (TGK) activity. In two of these families, expression of TGK transcripts was diminished or abnormal and no TGK protein was detected. Homozygous or compound heterozygous mutations of the TGK gene were identified in all families. These data suggest that defects in TGK cause lamellar ichthyosis and that intact cross-linkage of cornified cell envelopes is required for epidermal tissue homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, M -- Rettler, I -- Bernasconi, K -- Frenk, E -- Lavrijsen, S P -- Ponec, M -- Bon, A -- Lautenschlager, S -- Schorderet, D F -- Hohl, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):525-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, Centre Hospitalier Universitaire Vandois (CHUV), Hopital de Beaumont, Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824952" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; Codon ; Female ; Gene Deletion ; Genetic Linkage ; Heterozygote ; Homozygote ; Humans ; Ichthyosis, Lamellar/enzymology/*genetics ; Introns ; Keratinocytes/*enzymology/ultrastructure ; Male ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Protein Precursors/metabolism ; Transglutaminases/*genetics/metabolism
    Print ISSN: 0036-8075
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  • 7
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    The white gene of Ceratitis capitata: a phenotypic marker for germline transformation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Reliable germline transformation is required for molecular studies and ultimately for genetic control of economically important insects, such as the Mediterranean fruit fly (medfly) Ceratitis capitata. A prerequisite for the establishment and maintenance of transformant lines is selectable or phenotypically dominant markers. To this end, a complementary DNA clone derived from the medfly white gene was isolated, which showed substantial similarity to white genes in Drosophila melanogaster and other Diptera. It is correlated with a spontaneous mutation causing white eyes in the medfly and can be used to restore partial eye color in transgenic Drosophila carrying a null mutation in the endogenous white gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwiebel, L J -- Saccone, G -- Zacharopoulou, A -- Besansky, N J -- Favia, G -- Collins, F H -- Louis, C -- Kafatos, F C -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2005-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533095" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Cloning, Molecular ; Diptera/chemistry/*genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics ; Eye Color/genetics ; Eye Proteins/chemistry/*genetics ; *Genes, Insect ; Genetic Markers ; Insect Hormones/chemistry/genetics ; Molecular Sequence Data ; Mutation ; Phenotype ; Sequence Alignment ; *Transformation, Genetic
    Print ISSN: 0036-8075
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  • 8
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    Requirement of Saccharomyces cerevisiae Ras for completion of mitosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: In the yeast Saccharomyces cerevisiae, Ras regulates adenylate cyclase, which is essential for progression through the G1 phase of the cell cycle. However, even when the adenosine 3',5'-monophosphate (cAMP) pathway was bypassed, the double disruption of RAS1 and RAS2 resulted in defects in growth at both low and high temperatures. Furthermore, the simultaneous disruption of RAS1, RAS2, and the RAS-related gene RSR1 was lethal at any temperature. The triple-disrupted cells were arrested late in the mitotic (M) phase, which was accompanied by an accumulation of cells with divided chromosomes and sustained histone H1 kinase activity. The lethality of the triple disruption was suppressed by the multicopies of CDC5, CDC15, DBF2, SPO12, and TEM1, all of which function in the completion of the M phase. Mammalian ras also suppressed the lethality, which suggests that a similar signaling pathway exists in higher eukaryotes. These results demonstrate that S. cerevisiae Ras functions in the completion of the M phase in a manner independent of the Ras-cAMP pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morishita, T -- Mitsuzawa, H -- Nakafuku, M -- Nakamura, S -- Hattori, S -- Anraku, Y -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1213-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Cellular Biology, National Institute of Neuroscience, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502049" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/genetics/metabolism ; Fungal Proteins/*genetics/physiology ; GTP Phosphohydrolases/genetics/physiology ; Genes, Fungal ; Genes, Suppressor ; *Genes, ras ; *Mitosis ; Mutation ; Phenotype ; Saccharomyces cerevisiae/*cytology/genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Temperature ; *rab GTP-Binding Proteins ; ras Proteins/*genetics/physiology
    Print ISSN: 0036-8075
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  • 9
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    Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Y -- Dostmann, W R -- Herberg, F W -- Durick, K -- Xuong, N H -- Ten Eyck, L -- Taylor, S S -- Varughese, K I -- GM07313/GM/NIGMS NIH HHS/ -- GM34921/GM/NIGMS NIH HHS/ -- RR01644/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):807-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0654, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638597" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/*chemistry/genetics/metabolism ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/analogs & derivatives/*metabolism ; Cyclic AMP-Dependent Protein Kinases/*chemistry ; Enzyme Activation ; Hydrogen Bonding ; *Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
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  • 10
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    Aberrant subcellular localization of BRCA1 in breast cancer (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The BRCA1 gene product was identified as a 220-kilodalton nuclear phosphoprotein in normal cells, including breast ductal epithelial cells, and in 18 of 20 tumor cell lines derived from tissues other than breast and ovary. In 16 of 17 breast and ovarian cancer lines and 17 of 17 samples of cells obtained from malignant effusions, however, BRCA1 localized mainly in cytoplasm. Absence of BRCA1 or aberrant subcellular location was also observed to a variable extent in histological sections of many breast cancer biopsies. These findings suggest that BRCA1 abnormalities may be involved in the pathogenesis of many breast cancers, sporadic as well as familial.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Chen, C F -- Riley, D J -- Allred, D C -- Chen, P L -- Von Hoff, D -- Osborne, C K -- Lee, W H -- CA58318/CA/NCI NIH HHS/ -- EY05758/EY/NEI NIH HHS/ -- P50CA58183/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio 78245, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein ; Base Sequence ; Breast/*chemistry ; Breast Neoplasms/*chemistry/ultrastructure ; Cell Fractionation ; Cell Line ; Cell Nucleus/chemistry ; Cytoplasm/*chemistry ; Female ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*analysis/genetics/metabolism ; Neoplasms/chemistry/ultrastructure ; Ovarian Neoplasms/chemistry/ultrastructure ; Pleural Effusion, Malignant/chemistry/pathology ; Transcription Factors/*analysis/genetics/metabolism ; Tumor Cells, Cultured
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  • 11
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    Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+] (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: The yeast non-Mendelian factor [psi+] has been suggested to be a self-modified protein analogous to mammalian prions. Here it is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the [psi+] factor. Over-production or inactivation of Hsp104 caused the loss of [psi+]. These results suggest that chaperone proteins play a role in prion-like phenomena, and that a certain level of chaperone expression can cure cells of prions without affecting viability. This may lead to antiprion treatments that involve the alteration of chaperone amounts or activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chernoff, Y O -- Lindquist, S L -- Ono, B -- Inge-Vechtomov, S G -- Liebman, S W -- New York, N.Y. -- Science. 1995 May 12;268(5212):880-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Illinois, Chicago 60607-7020, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754373" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/*biosynthesis/genetics/physiology ; Gene Expression ; Heat-Shock Proteins/genetics/*physiology ; Mutation ; Prions/*biosynthesis ; Saccharomyces cerevisiae/genetics/*physiology ; *Saccharomyces cerevisiae Proteins ; Suppression, Genetic
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  • 12
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    Pheromone response in yeast: association of Bem1p with proteins of the MAP kinase cascade and actin (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: Haploid cells of the yeast Saccharomyces cerevisiae respond to mating pheromones with polarized growth toward the mating partner. This morphological response requires the function of the cell polarity establishment protein Bem1p. Immunochemical and two-hybrid protein interaction assays revealed that Bem1p interacts with two components of the pheromone-responsive mitogen-activated protein (MAP) kinase cascade, Ste20p and Ste5p, as well as with actin. Mutants of Bem1p that are associated with defective pheromone-induced polarized morphogenesis interacted with Ste5p and actin but not with Ste20p. Thus, the association of Bem1p with Ste20p and Ste5p may contribute to the conveyance of spatial information that regulates polarized rearrangement of the actin cytoskeleton during yeast mating.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leeuw, T -- Fourest-Lieuvin, A -- Wu, C -- Chenevert, J -- Clark, K -- Whiteway, M -- Thomas, D Y -- Leberer, E -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1210-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502048" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; *Adaptor Proteins, Signal Transducing ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Carrier Proteins ; Cell Polarity ; Fungal Proteins/chemistry/genetics/*metabolism ; GTP-Binding Proteins/metabolism ; Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase Kinases ; Morphogenesis ; Mutation ; Peptides/pharmacology ; Pheromones/*pharmacology ; Protein-Serine-Threonine Kinases/*metabolism ; Saccharomyces cerevisiae/cytology/*metabolism ; *Saccharomyces cerevisiae Proteins
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  • 13
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    Cell movement tale told by bacterial tail protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604275" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Animals ; Bacterial Proteins ; Bacterial Vaccines/immunology ; Cell Movement/*physiology ; DNA-Binding Proteins/*genetics/physiology ; Escherichia coli/genetics/physiology ; Genes, Bacterial ; Humans ; Macaca mulatta ; Mutation ; Shigella flexneri/genetics/immunology/*physiology ; Transcription Factors/*genetics/physiology
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  • 14
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    Protein proves to be a key link in innate immunity (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):301-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618098" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/chemistry/genetics/*immunology ; Child ; Cloning, Molecular ; Complement Activation/*immunology ; Disease Susceptibility ; Humans ; *Immunity, Innate ; Immunologic Deficiency Syndromes/*etiology ; Mannose-Binding Lectins ; Mutation ; Phagocytosis/*immunology ; Protein Conformation ; Protein Structure, Secondary
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  • 15
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    Plant genetics. Shedding light on the ticking of internal timekeepers (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1091-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855588" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; *Biological Clocks/genetics ; Carrier Proteins/genetics ; *Circadian Rhythm/genetics ; *Genes, Plant ; Light-Harvesting Protein Complexes ; Luciferases/genetics ; Mutation ; *Photosynthetic Reaction Center Complex Proteins ; *Photosystem II Protein Complex ; *Plant Proteins ; Recombinant Fusion Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Sunlight and melanoma: an answer from MTS1 (p16) (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maestro, R -- Boiocchi, M -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):15-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809600" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/*genetics ; Cyclin-Dependent Kinase Inhibitor p16 ; *Genes, Tumor Suppressor ; Humans ; Melanoma/*etiology/genetics ; Mutation ; Neoplasms, Radiation-Induced/*genetics ; Protein Kinase Inhibitors ; Ultraviolet Rays/*adverse effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Structure of the Arabidopsis RPM1 gene enabling dual specificity disease resistance (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: Plants can recognize pathogens through the action of disease resistance (R) genes, which confer resistance to pathogens expressing unique corresponding avirulence (avr) genes. The molecular basis of this gene-for-gene specificity is unknown. The Arabidopsis thaliana RPM1 gene enables dual specificity to pathogens expressing either of two unrelated Pseudomonas syringae avr genes. Despite this function, RPM1 encodes a protein sharing molecular features with recently described single-specificity R genes. Surprisingly, RPM1 is lacking from naturally occurring, disease-susceptible Arabidopsis accessions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grant, M R -- Godiard, L -- Straube, E -- Ashfield, T -- Lewald, J -- Sattler, A -- Innes, R W -- Dangl, J L -- R29 GM 46451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):843-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Laboratory, Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638602" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*genetics/microbiology ; *Arabidopsis Proteins ; Base Sequence ; Genes, Bacterial ; *Genes, Plant ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Plant Diseases/*genetics ; Plant Proteins/chemistry/*genetics ; Plants, Genetically Modified ; Polymorphism, Restriction Fragment Length ; Pseudomonas/genetics/growth & development/pathogenicity ; Transformation, Genetic ; Virulence/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    Host range of a plant pathogenic fungus determined by a saponin detoxifying enzyme (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-20
    Description: Antifungal saponins occur in many plant species and may provide a preformed chemical barrier to attack by phytopathogenic fungi. Some fungal pathogens can enzymatically detoxify host plant saponins, which suggests that saponin detoxification may determine the host range of these fungi. A gene encoding a saponin detoxifying enzyme was cloned from the cereal-infecting fungus Gaeumannomyces graminis. Fungal mutants generated by targeted gene disruption were no longer able to infect the saponin-containing host oats but retained full pathogenicity to wheat (which does not contain saponins). Thus, the ability of a phytopathogenic fungus to detoxify a plant saponin can determine its host range.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowyer, P -- Clarke, B R -- Lunness, P -- Daniels, M J -- Osbourn, A E -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):371-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsburg Laboratory, John Innes Centre, Norwich, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824933" target="_blank"〉PubMed〈/a〉
    Keywords: Ascomycota/enzymology/*genetics/physiology ; Avena/*microbiology ; Cloning, Molecular ; *Fungal Proteins ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Neurospora crassa/genetics ; Saponins/*analysis/*antagonists & inhibitors/metabolism ; Transformation, Genetic ; Triticum/*microbiology ; beta-Glucosidase/*genetics/isolation & purification/metabolism
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  • 19
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    A regulatory role for ARF6 in receptor-mediated endocytosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: Adenosine diphosphate-ribosylation factor 6 (ARF6), ARF6 mutants, and ARF1 were transiently expressed in Chinese hamster ovary cells, and the effects on receptor-mediated endocytosis were assessed. Overexpressed ARF6 localized to the cell periphery and led to a redistribution of transferrin receptors to the cell surface and a decrease in the rate of uptake of transferrin. Similar results were obtained when a mutant defective in guanosine triphosphate hydrolysis was expressed. Expression of a dominant negative mutant, ARF6(T27N), resulted in an intracellular distribution of transferrin receptors and an inhibition of transferrin recycling to the cell surface. In contrast, overexpression of ARF1 had little or no effect on these parameters of endocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Souza-Schorey, C -- Li, G -- Colombo, M I -- Stahl, P D -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1175-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, 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/7855600" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Amino Acid Sequence ; Animals ; Base Sequence ; CHO Cells ; Cell Membrane/metabolism ; Cricetinae ; *Endocytosis ; GTP-Binding Proteins/analysis/genetics/*physiology ; Golgi Apparatus/metabolism/ultrastructure ; Kinetics ; Molecular Sequence Data ; Mutation ; Receptors, Transferrin/metabolism ; Transferrin/metabolism
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  • 20
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    Common virulence factors for bacterial pathogenicity in plants and animals (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: A Pseudomonas aeruginosa strain (UCBPP-PA14) is infectious both in an Arabidopsis thaliana leaf infiltration model and in a mouse full-thickness skin burn model. UCBPP-PA14 exhibits ecotype specificity for Arabidopsis, causing a range of symptoms from none to severe in four different ecotypes. In the mouse model, UCBPP-PA14 is as lethal as other well-studied P. aeruginosa strains. Mutations in the UCBPP-PA14 toxA, plcS, and gacA genes resulted in a significant reduction in pathogenicity in both hosts, indicating that these genes encode virulence factors required for the full expression of pathogenicity in both plants and animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rahme, L G -- Stevens, E J -- Wolfort, S F -- Shao, J -- Tompkins, R G -- Ausubel, F M -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1899-902.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604262" target="_blank"〉PubMed〈/a〉
    Keywords: *ADP Ribose Transferases ; Animals ; Arabidopsis/*microbiology ; Bacterial Proteins/genetics ; *Bacterial Toxins ; Base Sequence ; Burns/complications ; Exotoxins/genetics ; Male ; Mice ; Molecular Sequence Data ; Mutation ; Phospholipases/genetics ; Plant Diseases/*microbiology ; Pseudomonas Infections/*microbiology ; Pseudomonas aeruginosa/genetics/growth & development/*pathogenicity ; Virulence/genetics ; *Virulence Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Getting a grip on G protein function in C. elegans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1596-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886445" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Mutation ; *Signal Transduction
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  • 22
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    Participation of the protein Go in multiple aspects of behavior in C. elegans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: The goa-1 gene encoding the alpha subunit of the heterotrimeric guanosine triphosphate-binding protein (G protein) Go from Caenorhabditis elegans is expressed in most neurons, and in the muscles involved in egg laying and male mating. Reduction-of-function mutations in goa-1 caused a variety of behavioral defects including hyperactive movement, premature egg laying, and male impotence. Expression of the activated Go alpha subunit (G alpha o) in transgenic nematodes resulted in lethargic movement, delayed egg laying, and reduced mating efficiency. Induced expression of activated G alpha o in adults was sufficient to cause these phenotypes, indicating that G alpha o mediates behavior through its role in neuronal function and the functioning of specialized muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, J E -- Korswagen, H C -- Liu, K S -- Hajdu-Cronin, Y M -- Simon, M I -- Plasterk, R H -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; Disorders of Sex Development ; Female ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Molecular Sequence Data ; Movement ; Muscles/innervation/physiology ; Mutation ; Neurons/physiology ; Oviposition ; Phenotype ; Serotonin/pharmacology ; Sexual Behavior, Animal
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  • 23
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    Hold 'em and fold 'em: chaperones and signal transduction (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohen, S P -- Kralli, A -- Yamamoto, K R -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1303-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4255, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761850" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/genetics/*physiology ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/physiology ; HSP90 Heat-Shock Proteins/physiology ; *Heat-Shock Proteins ; Molecular Chaperones/*physiology ; Mutation ; Oncogene Protein pp60(v-src)/metabolism ; Protein Folding ; Receptors, Estrogen/metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Steroid/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 24
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    Guidelines for protein design: the energetics of beta sheet side chain interactions (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-10
    Description: To determine the interaction energy between cross-strand pairs of side chains on an antiparallel beta sheet, pairwise amino acid substitutions were made on the solvent-exposed face of the B1 domain of streptococcal protein G. The measured interaction energies were substantial (1.8 kilocalories per mole) and comparable to the magnitude of the beta sheet propensities. The experimental results paralleled the statistical frequency with which the residue pairs are found in beta sheets of known structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C K -- Regan, L -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):980-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481801" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/genetics ; Hot Temperature ; Hydrogen Bonding ; Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Engineering ; Protein Folding ; *Protein Structure, Secondary ; Streptococcus/chemistry ; Thermodynamics
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  • 25
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    Rescue of the En-1 mutant phenotype by replacement of En-1 with En-2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: The related mouse Engrailed genes En-1 and En-2 are expressed from the one- and approximately five-somite stages, respectively, in a similar presumptive mid-hindbrain domain. However, mutations in En-1 and En-2 produce different phenotypes. En-1 mutant mice die at birth with a large mid-hindbrain deletion, whereas En-2 mutants are viable, with cerebellar defects. To determine whether these contrasting phenotypes reflect differences in temporal expression or biochemical activity of the En proteins, En-1 coding sequences were replaced with En-2 sequences by gene targeting. This rescued all En-1 mutant defects, demonstrating that the difference between En-1 and En-2 stems from their divergent expression patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanks, M -- Wurst, W -- Anson-Cartwright, L -- Auerbach, A B -- Joyner, A L -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mt. Sinai Hospital, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/abnormalities/embryology ; Chimera ; Crosses, Genetic ; Female ; *Gene Expression Regulation, Developmental ; *Gene Targeting ; *Genes, Homeobox ; Homeodomain Proteins/*genetics/physiology ; Limb Deformities, Congenital ; Male ; Mice ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Phenotype ; Promoter Regions, Genetic ; Recombination, Genetic ; Stem Cells ; Sternum/abnormalities
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 26
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    Association of the yeast pheromone response G protein beta gamma subunits with the MAP kinase scaffold Ste5p (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: The mating response pathway of the yeast Saccharomyces cerevisiae includes a heterotrimeric guanine nucleotide-binding protein (G protein) that activates a mitogen-activated protein MAP kinase cascade by an unknown mechanism. An amino-terminal fragment of the MAP kinase scaffold protein Ste5p that interfered with pheromone-induced cell cycle arrest was identified. A haploid-specific interaction between the amino terminus of Ste5p and the G protein beta subunit Ste4p was also detected in a two-hybrid assay, and the product of a signaling-defective allele of STE4 was defective in this interaction. In cells with a constitutively activated pheromone response pathway, epitope-tagged Ste4p was coimmunoprecipitated with Ste5p. Thus, association of the G protein and the MAP kinase cassette via the scaffolding protein Ste5p may transmit the G protein signal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whiteway, M S -- Wu, C -- Leeuw, T -- Clark, K -- Fourest-Lieuvin, A -- Thomas, D Y -- Leberer, E -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1572-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667635" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Carrier Proteins ; Cell Division ; Fungal Proteins/genetics/*metabolism ; *GTP-Binding Protein beta Subunits ; *GTP-Binding Protein gamma Subunits ; GTP-Binding Proteins/genetics/*metabolism ; *Heterotrimeric GTP-Binding Proteins ; Molecular Sequence Data ; Mutation ; Pheromones/pharmacology ; Plasmids ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Signal Transduction ; Transformation, Genetic
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  • 27
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    Separation of origin recognition complex functions by cross-species complementation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Transcriptional silencing at the HMRa locus of Saccharomyces cerevisiae requires the function of the origin recognition complex (ORC), the replication initiator of yeast. Expression of a Drosophila melanogaster Orc2 complementary DNA in the yeast orc2-1 strain, which is defective for replication and silencing, complemented the silencing defect but not the replication defect; this result indicated that the replication and silencing functions of ORC were separable. The orc2-1 mutation mapped to the region of greatest homology between the Drosophila and yeast proteins. The silent state mediated by DmOrc2 was epigenetic; it was propagated during mitotic divisions in a relatively stable way, whereas the nonsilent state was metastable. In contrast, the silent state was erased during meiosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenhofer-Murray, A E -- Gossen, M -- Pak, D T -- Botchan, M R -- Rine, J -- GM31105/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1671-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502078" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *DNA Replication ; DNA-Binding Proteins/genetics/*physiology ; Drosophila Proteins ; Drosophila melanogaster/*genetics ; Fungal Proteins/genetics/physiology ; *Gene Expression Regulation ; Genes, Fungal ; Genes, Insect ; Genetic Complementation Test ; Mutation ; Origin Recognition Complex ; Regulatory Sequences, Nucleic Acid ; *Replication Origin ; Repressor Proteins/genetics/*physiology ; Saccharomyces cerevisiae/*genetics/physiology ; Saccharomyces cerevisiae Proteins ; Temperature ; Transformation, Genetic
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  • 28
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    Muscular dystrophies: diseases of the dystrophin-glycoprotein complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worton, R -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):755-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Hospital for Sick Children, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481760" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Chromosome Mapping ; Chromosomes, Human, Pair 13 ; Chromosomes, Human, Pair 4 ; Cytoskeletal Proteins/*genetics/physiology ; Dystroglycans ; Dystrophin/*genetics/physiology ; Humans ; Membrane Glycoproteins/*genetics/physiology ; Muscles/chemistry ; Muscular Dystrophies/*genetics/metabolism ; Mutation ; Phenotype ; Sarcoglycans ; Sequence Deletion
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  • 29
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    Inflammatory bowel disease and adenomas in mice expressing a dominant negative N-cadherin (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: Cadherins mediate cell adhesion and are essential for normal development. Embryonic stem cells were transfected with a dominant negative N-cadherin mutant (NCAD delta) under the control of promoters active in small intestinal epithelial cells and then introduced into C57BL/6 mouse blastocysts. Analysis of adult chimeric mice revealed that expression of NCAD delta along the entire crypt-villus axis, but not in the villus epithelium alone, produced an inflammatory bowel disease resembling Crohn's disease. NCAD delta perturbed proliferation, migration, and death programs in crypts, which lead to adenomas. This model provides insights about cadherin function in an adult organ and the factors underlying inflammatory bowel disease and intestinal neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hermiston, M L -- Gordon, J I -- DK30292/DK/NIDDK NIH HHS/ -- DK39760/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1203-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502046" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/*etiology/metabolism/pathology ; Animals ; Apoptosis ; Cadherins/biosynthesis/genetics/*physiology ; Cell Division ; Cell Line ; Cell Movement ; Chimera ; Crohn Disease/etiology/immunology/metabolism/pathology ; Immunity, Mucosal ; Inflammatory Bowel Diseases/*etiology/immunology/metabolism/pathology ; Intestinal Mucosa/immunology/metabolism/*pathology ; Intestinal Neoplasms/*etiology/metabolism/pathology ; Intestine, Small/pathology ; Jejunum/pathology ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mutation ; Stem Cells ; Transfection
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    Agriculture. Playing chicken with an epidemic (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wuethrich, B -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1594.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886444" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens/*virology ; Disease Outbreaks/prevention & control/*veterinary ; Influenza A virus/genetics/immunology/*pathogenicity ; Influenza in Birds/*epidemiology/prevention & control/virology ; Mexico/epidemiology ; Mutation ; Viral Vaccines ; Virulence
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: Thermodynamic mutant cycles provide a formalism for studying energetic coupling between amino acids on the interaction surface in a protein-protein complex. This approach was applied to the Shaker potassium channel and to a high-affinity peptide inhibitor (scorpion toxin) that binds to its pore entryway. The assignment of pairwise interactions defined the spatial arrangement of channel amino acids with respect to the known inhibitor structure. A strong constraint was placed on the Shaker channel pore-forming region by requiring its amino-terminal border to be 12 to 15 angstroms from the central axis. This method is directly applicable to sodium, calcium, and other ion channels where inhibitor or modulatory proteins bind with high affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hidalgo, P -- MacKinnon, R -- GM43949/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):307-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oocytes ; Potassium Channels/*chemistry/genetics/metabolism ; Scorpion Venoms/*metabolism ; Shaker Superfamily of Potassium Channels ; Thermodynamics ; Toxins, Biological/*metabolism ; Xenopus laevis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 32
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    Circadian clock mutants in Arabidopsis identified by luciferase imaging (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: The cycling bioluminescence of Arabidopsis plants carrying a firefly luciferase fusion construct was used to identify mutant individuals with aberrant cycling patterns. Both long- and short-period mutants were recovered. A semidominant short-period mutation, timing of CAB expression (toc1), was mapped to chromosome 5. The toc1 mutation shortens the period of two distinct circadian rhythms, the expression of chlorophyll a/b-binding protein (CAB) genes and the movements of primary leaves, although toc1 mutants do not show extensive pleiotropy for other phenotypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Millar, A J -- Carre, I A -- Strayer, C A -- Chua, N H -- Kay, S A -- GM44640/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1161-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Science Foundation (NSF) Center for Biological Timing, Department of Biology, University of Virginia, Charlottesville 22903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855595" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Biological Clocks/*genetics ; Carrier Proteins/*genetics ; Circadian Rhythm/*genetics ; Crosses, Genetic ; Darkness ; Gene Expression Regulation, Plant ; *Genes, Plant ; Light ; Light-Harvesting Protein Complexes ; Luciferases/genetics ; Luminescence ; Movement ; Mutation ; Phenotype ; *Photosynthetic Reaction Center Complex Proteins ; *Photosystem II Protein Complex ; Plant Leaves/physiology ; *Plant Proteins ; Plants, Genetically Modified ; Recombinant Fusion Proteins
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    Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-25
    Description: Vulval induction during Caenorhabditis elegans development is mediated by LET-23, a homolog of the mammalian epidermal growth factor receptor tyrosine kinase. The sli-1 gene is a negative regulator of LET-23 and is shown here to encode a protein similar to c-Cbl, a mammalian proto-oncoprotein. SLI-1 and c-Cbl share approximately 55 percent amino acid identity over a stretch of 390 residues, which includes a C3HC4 zinc-binding motif known as the RING finger, and multiple consensus binding sites for Src homology 3 (SH3) domains. SLI-1 and c-Cbl may define a new class of proteins that modify receptor tyrosine kinase-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoon, C H -- Lee, J -- Jongeward, G D -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Aug 25;269(5227):1102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Caenorhabditis elegans/*genetics/growth & development ; *Caenorhabditis elegans Proteins ; Conserved Sequence ; DNA, Complementary/genetics ; Female ; *Genes, Helminth ; *Genes, Regulator ; Helminth Proteins/chemistry/*genetics/metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Proto-Oncogene Proteins/chemistry/*genetics ; Proto-Oncogene Proteins c-cbl ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Alignment ; Signal Transduction ; *Ubiquitin-Protein Ligases ; Vulva/growth & development
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    Conversion of bacteriorhodopsin into a chloride ion pump (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: In the light-driven proton pump bacteriorhodopsin, proton transfer from the retinal Schiff base to aspartate-85 is the crucial reaction of the transport cycle. In halorhodopsin, a light-driven chloride ion pump, the equivalent of residue 85 is threonine. When aspartate-85 was replaced with threonine, the mutated bacteriorhodopsin became a chloride ion pump when expressed in Halobacterium salinarium and, like halorhodopsin, actively transported chloride ions in the direction opposite from the proton pump. Chloride was bound to it, as revealed by large shifts of the absorption maximum of the chromophore, and its photointermediates included a red-shifted state in the millisecond time domain, with its amplitude and decay rate dependent on chloride concentration. Bacteriorhodopsin and halorhodopsin thus share a common transport mechanism, and the interaction of residue 85 with the retinal Schiff base determines the ionic specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sasaki, J -- Brown, L S -- Chon, Y S -- Kandori, H -- Maeda, A -- Needleman, R -- Lanyi, J K -- GM29498/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):73-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Faculty of Science, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604281" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/chemistry ; Bacteriorhodopsins/chemistry/genetics/*metabolism ; Biological Transport ; Chlorides/*metabolism ; Halorhodopsins ; Hot Temperature ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Ion Pumps/chemistry/*metabolism ; Light ; Mutation ; Proton Pumps ; Schiff Bases ; Threonine/chemistry
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  • 35
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    Requirement of the yeast RTH1 5' to 3' exonuclease for the stability of simple repetitive DNA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-14
    Description: Simple repetitive DNA sequences are unstable in human colorectal cancers and a variety of other cancers. Mutations in the DNA mismatch repair genes MSH2, MLH1, and PMS1 result in elevated rates of spontaneous mutation and cause a marked increase in the instability of simple repeats. Compared with the wild type, a null mutation in the yeast RTH1 gene, which encodes a 5' to 3' exonuclease, was shown to increase the rate of instability of simple repetitive DNA by as much as 280 times and to increase the spontaneous mutation rate by 30 times. Epistasis analyses were consistent with the hypothesis that this RTH1-encoded nuclease has a role in the MSH2-MLH-1-PMS1 mismatch repair pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, R E -- Kovvali, G K -- Prakash, L -- Prakash, S -- CA 41261/CA/NCI NIH HHS/ -- GM 19261/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):238-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Science, University of Texas Medical Branch, Galveston 77555-1061, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618086" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; *Carrier Proteins ; *DNA Repair ; DNA, Fungal/genetics ; DNA-Binding Proteins/genetics ; Exodeoxyribonuclease V ; Exodeoxyribonucleases/*genetics/metabolism ; Fungal Proteins/genetics ; *Genes, Fungal ; MutS Homolog 2 Protein ; Mutation ; *Neoplasm Proteins ; *Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae/enzymology/*genetics ; *Saccharomyces cerevisiae Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Isolation of timeless by PER protein interaction: defective interaction between timeless protein and long-period mutant PERL (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The period (per) gene likely encodes a component of the Drosophila circadian clock. Circadian oscillations in the abundance of per messenger RNA and per protein (PER) are thought to arise from negative feedback control of per gene transcription by PER. A recently identified second clock locus, timeless (tim), apparently regulates entry of PER into the nucleus. Reported here are the cloning of complementary DNAs derived from the tim gene in a two-hybrid screen for PER-interacting proteins and the demonstration of a physical interaction between the tim protein (TIM) and PER in vitro. A restricted segment of TIM binds directly to a part of the PER dimerization domain PAS. PERL, a mutation that causes a temperature-sensitive lengthening of circadian period and a temperature-sensitive delay in PER nuclear entry, exhibits a temperature-sensitive defect in binding to TIM. These results suggest that the interaction between TIM and PER determines the timing of PER nuclear entry and therefore the duration of part of the circadian cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gekakis, N -- Saez, L -- Delahaye-Brown, A M -- Myers, M P -- Sehgal, A -- Young, M W -- Weitz, C J -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):811-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481773" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/genetics ; Cell Nucleus/metabolism ; Circadian Rhythm/*genetics ; Cloning, Molecular ; Cytoplasm/metabolism ; DNA, Complementary/genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics/*metabolism ; Feedback ; Gene Expression Regulation ; Genes, Insect ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Proteins/genetics/isolation & purification/*metabolism ; Recombinant Fusion Proteins/metabolism ; Temperature
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    Missing Alzheimer's gene found (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):917-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638610" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/ethnology/*genetics ; Amyloid beta-Peptides/biosynthesis ; Chromosomes, Human, Pair 1/*genetics ; DNA, Complementary ; Female ; Gene Expression ; Genes ; Germany/ethnology ; Humans ; Male ; Membrane Proteins/genetics ; Mutation ; Presenilin-1 ; Sequence Homology, Nucleic Acid
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    New Alzheimer's gene found (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1845-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604254" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/etiology/*genetics/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Biological Transport ; Brain/metabolism ; *Caenorhabditis elegans Proteins ; Chromosome Mapping ; *Chromosomes, Human, Pair 14 ; Genes ; Genetic Markers ; Humans ; Membrane Proteins/chemistry/*genetics/physiology ; Mutation ; Presenilin-1
    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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  • 39
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    Mismatch repair deficiency in phenotypically normal human cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: Tumor cells in patients with hereditary nonpolyposis colorectal cancer (HNPCC) are characterized by a genetic hypermutability caused by defects in DNA mismatch repair. A subset of HNPCC patients was found to have widespread mutations not only in their tumors, but also in their non-neoplastic cells. Although these patients had numerous mutations in all tissues examined, they had very few tumors. The hypermutability was associated with a profound defect in mismatch repair at the biochemical level. These results have implications for the relation between mutagenesis and carcinogenesis, and they suggest that mismatch repair deficiency is compatible with normal human development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parsons, R -- Li, G M -- Longley, M -- Modrich, P -- Liu, B -- Berk, T -- Hamilton, S R -- Kinzler, K W -- Vogelstein, B -- CA35494/CA/NCI NIH HHS/ -- CA62924/CA/NCI NIH HHS/ -- GM45190/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 May 5;268(5211):738-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins Oncology Center, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7632227" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line, Transformed ; Clone Cells ; Colorectal Neoplasms, Hereditary Nonpolyposis/*genetics ; DNA Repair/*genetics ; DNA, Satellite/analysis ; Humans ; Intestinal Mucosa/chemistry ; Lymphocytes/chemistry ; Molecular Sequence Data ; Mutation ; Phenotype ; Repetitive Sequences, Nucleic Acid
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  • 40
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    An ethylene-inducible component of signal transduction encoded by never-ripe (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: The ripening-impaired tomato mutant Never-ripe (Nr) is insensitive to the plant hormone ethylene. The gene that cosegregates with the Nr locus encodes a protein with homology to the Arabidopsis ethylene receptor ETR1 but is lacking the response regulator domain found in ETR1 and related prokaryotic two-component signal transducers. A single amino acid change in the sensor domain confers ethylene insensitivity when expressed in transgenic tomato plants. Modulation of NR gene expression during fruit ripening controls response to the hormone ethylene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkinson, J Q -- Lanahan, M B -- Yen, H C -- Giovannoni, J J -- Klee, H J -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1807-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monsanto Company, Chesterfield, MO 63198, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525371" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Base Sequence ; DNA Primers ; Ethylenes/*metabolism ; Genes, Plant ; Lycopersicon esculentum/*genetics/growth & development/metabolism ; Molecular Sequence Data ; Mutation ; Plant Proteins/*genetics/metabolism ; *Receptors, Cell Surface ; Sequence Homology, Amino Acid ; *Signal Transduction
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  • 41
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    Inhibition of transcription elongation by the VHL tumor suppressor protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Germline mutations in the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of tumors, including renal carcinoma, hemangioblastoma of the central nervous system, and pheochromocytoma. Here, a cellular transcription factor, Elongin (SIII), is identified as a functional target of the VHL protein. Elongin (SIII) is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C) that activate transcription elongation by RNA polymerase II. The VHL protein was shown to bind tightly and specifically to the Elongin B and C subunits and to inhibit Elongin (SIII) transcriptional activity in vitro. These findings reveal a potentially important transcriptional regulatory network in which the VHL protein may play a key role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duan, D R -- Pause, A -- Burgess, W H -- Aso, T -- Chen, D Y -- Garrett, K P -- Conaway, R C -- Conaway, J W -- Linehan, W M -- Klausner, R D -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1402-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Urologic Oncology Section, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Gene Expression Regulation ; *Genes, Tumor Suppressor ; HeLa Cells ; Humans ; *Ligases ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics/*metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Transcription Factors/chemistry/isolation & purification/*metabolism ; *Transcription, Genetic ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/*genetics
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  • 42
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    The TBP-TFIIA interaction in the response to acidic activators in vivo (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: A yeast TBP mutant (N2-1) is described here that is defective specifically in responding to acidic activators in vivo. N2-1 does not support activation by Gal4, Ace1, and Gcn4, but appears unaffected for constitutive transcription, repression by the Cyc8-Tup1 and Not complexes, and transcription by polymerase I (Pol) and Pol III. In vitro, N2-1 fails to interact with TFIIA, but it associates normally with a TATA element, an acidic activation domain, and TFIIB. Fusion of the small subunit of TFIIA to N2-1 restores activation function in vivo. Thus, an efficient interaction between TBP and TFIIA is required for transcriptional activation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stargell, L A -- Struhl, K -- GM30186/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):75-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604282" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/genetics/*metabolism/physiology ; DNA-Directed RNA Polymerases/metabolism ; Fungal Proteins/physiology ; Hydrogen-Ion Concentration ; Immediate-Early Proteins/physiology ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Nuclear Receptor Subfamily 4, Group A, Member 2 ; Protein Kinases/physiology ; *Repressor Proteins ; Saccharomyces cerevisiae/*genetics/growth & development ; *Saccharomyces cerevisiae Proteins ; *TATA Box ; TATA-Box Binding Protein ; Trans-Activators/*physiology ; Transcription Factor TFIIA ; Transcription Factors/genetics/*metabolism/physiology ; *Transcriptional Activation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The ethylene signal transduction pathway in plants (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-05-05
    Description: Ethylene (C2H4), the chemically simplest plant hormone, is among the best-characterized plant growth regulators. It participates in a variety of stress responses and developmental processes. Genetic studies in Arabidopsis have defined a number of genes in the ethylene signal transduction pathway. Isolation of two of these genes has revealed that plants sense this gas through a combination of proteins that resemble both prokaryotic and eukaryotic signaling proteins. Ethylene signaling components are likely conserved for responses as diverse as cell elongation, cell fate patterning in the root epidermis, and fruit ripening. Genetic manipulation of these genes will provide agriculture with new tools to prevent or modify ethylene responses in a variety of plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, J R -- New York, N.Y. -- Science. 1995 May 5;268(5211):667-75.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Pennsylvania, Philadelphia 19104-6018, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732375" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Ethylenes ; Molecular Sequence Data ; Mutation ; Plant Development ; Plant Growth Regulators/*physiology ; *Plant Physiological Phenomena ; Plants/genetics ; Signal Transduction/*physiology
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    Localization of protein implicated in establishment of cell type to sites of asymmetric division (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-27
    Description: Asymmetric division in Bacillus subtilis generates progeny cells with dissimilar fates. SpoIIE, a membrane protein required for the establishment of cell type, was shown to localize near sites of potential polar division. SpoIIE initially localizes in a bipolar pattern, coalescing at marks in the cell envelope at which asymmetric division can take place. Then, during division, SpoIIE becomes restricted to the polar septum and is lost from the distal pole. Thus, when division is complete, SpoIIE sits at the boundary between the progeny from which it dictates cell fate by the activation of a cell-specific transcription factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arigoni, F -- Pogliano, K -- Webb, C D -- Stragier, P -- Losick, R -- GM18568/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):637-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Physico-Chimique, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570022" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/*chemistry/cytology/genetics/*physiology ; Bacterial Proteins/*analysis/physiology ; *Cell Division ; Cell Membrane/chemistry ; Gene Expression ; Microscopy, Fluorescence ; Mutation ; Recombinant Fusion Proteins/analysis ; Sigma Factor/physiology ; Spores, Bacterial/*chemistry ; *Transcription Factors
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    Positional cloning and sequence analysis of the Drosophila clock gene, timeless (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-11-03
    Description: The Drosophila genes timeless (tim) and period (per) interact, and both are required for production of circadian rhythms. Here the positional cloning and sequencing of tim are reported. The tim gene encodes a previously uncharacterized protein of 1389 amino acids, and possibly another protein of 1122 amino acids. The arrhythmic mutation tim01 is a 64-base pair deletion that truncates TIM to 749 amino acids. Absence of sequence similarity to the PER dimerization motif (PAS) indicates that direct interaction between PER and TIM would require a heterotypic protein association.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, M P -- Wager-Smith, K -- Wesley, C S -- Young, M W -- Sehgal, A -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, National Science Foundation Science and Technology Center for Biological Timing, and Laboratory of Genetics, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481771" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Clocks/*genetics ; Chromosome Mapping ; Circadian Rhythm/*genetics ; Cloning, Molecular ; *Drosophila Proteins ; Drosophila melanogaster/chemistry/*genetics/physiology ; *Genes, Insect ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Nuclear Proteins/chemistry/genetics ; Period Circadian Proteins ; Polymorphism, Restriction Fragment Length ; Proteins/chemistry/*genetics ; Sequence Analysis ; Sequence Deletion ; Sequence Homology, Amino Acid
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    Sodium-driven potassium uptake by the plant potassium transporter HKT1 and mutations conferring salt tolerance (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Sodium (Na+) at high millimolar concentrations in soils is toxic to most higher plants and severely reduces agricultural production worldwide. However, the molecular mechanisms for plant Na+ uptake remain unknown. Here, the wheat root high-affinity potassium (K+) uptake transporter HKT1 was shown to function as a high-affinity K(+)-Na+ cotransporter. High-affinity K+ uptake was activated by micromolar Na+ concentrations; moreover, high-affinity Na+ uptake was activated by K+ (half-activation constant, 2.8 microM K+). However, at physiologically detrimental concentrations of Na+, K+ accumulation mediated by HKT1 was blocked and low-affinity Na+ uptake occurred (Michaelis constant, approximately 16 mM Na+), which correlated to Na+ toxicity in plants. Point mutations in the sixth putative transmembrane domain of HKT1 that increase Na+ tolerance were isolated with the use of yeast as a screening system. Na+ uptake and Na+ inhibition of K+ accumulation indicate a possible role for HKT1 in physiological Na+ toxicity in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rubio, F -- Gassmann, W -- Schroeder, J I -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1660-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502075" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport/drug effects ; Carrier Proteins/genetics/*metabolism ; *Cation Transport Proteins ; Membrane Potentials ; Membrane Proteins/genetics/*metabolism ; Mutation ; Oocytes/metabolism ; Patch-Clamp Techniques ; Plant Proteins/genetics/*metabolism ; Potassium/*metabolism ; Recombinant Proteins/metabolism ; Rubidium/metabolism ; Sodium/*metabolism/*toxicity ; Spectrophotometry, Atomic ; *Symporters ; Xenopus ; Yeasts/metabolism
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    Mutations in the dystrophin-associated protein gamma-sarcoglycan in chromosome 13 muscular dystrophy (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: Severe childhood autosomal recessive muscular dystrophy (SCARMD) is a progressive muscle-wasting disorder common in North Africa that segregates with microsatellite markers at chromosome 13q12. Here, it is shown that a mutation in the gene encoding the 35-kilodalton dystrophin-associated glycoprotein, gamma-sarcoglycan, is likely to be the primary genetic defect in this disorder. The human gamma-sarcoglycan gene was mapped to chromosome 13q12, and deletions that alter its reading frame were identified in three families and one of four sporadic cases of SCARMD. These mutations not only affect gamma-sarcoglycan but also disrupt the integrity of the entire sarcoglycan complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noguchi, S -- McNally, E M -- Ben Othmane, K -- Hagiwara, Y -- Mizuno, Y -- Yoshida, M -- Yamamoto, H -- Bonnemann, C G -- Gussoni, E -- Denton, P H -- Kyriakides, T -- Middleton, L -- Hentati, F -- Ben Hamida, M -- Nonaka, I -- Vance, J M -- Kunkel, L M -- Ozawa, E -- NS23740/NS/NINDS NIH HHS/ -- P01-NS26630/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):819-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neuroscience, National Center for Neurology and Psychiatry, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 13 ; *Cytoskeletal Proteins ; DNA, Complementary/genetics ; Dystrophin/chemistry/genetics/metabolism ; Humans ; Linkage Disequilibrium ; Membrane Glycoproteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Molecular Weight ; Muscle, Skeletal/chemistry/metabolism ; Muscular Dystrophies/*genetics ; Mutation ; Phenotype ; Rabbits ; Sarcoglycans ; Sequence Deletion
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    The myth of Eve: molecular biology and human origins (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-22
    Description: It has been proposed that modern humans descended from a single woman, the "mitochondrial Eve" who lived in Africa 100,000 to 200,000 years ago. The human immune system DRB1 genes are extremely polymorphic, with gene lineages that coalesce into an ancestor who lived around 60 million years ago, a time before the divergence of the apes from the Old World monkeys. The theory of gene coalescence suggests that, throughout the last 60 million years, human ancestral populations had an effective size of 100,000 individuals or greater. Molecular evolution data favor the African origin of modern humans, but the weight of the evidence is against a population bottleneck before their emergence. The mitochondrial Eve hypothesis emanates from a confusion between gene genealogies and individual genealogies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ayala, F J -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1930-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, Irvine, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533083" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Cercopithecidae/genetics ; Computer Simulation ; DNA, Mitochondrial/genetics ; DNA-Binding Proteins/genetics ; *Evolution, Molecular ; Female ; Fossils ; Genes, MHC Class II ; Genetics, Population ; HLA-DR Antigens/genetics ; HLA-DRB1 Chains ; *Hominidae/genetics ; Humans ; Kruppel-Like Transcription Factors ; Male ; Mutation ; Selection, Genetic ; Transcription Factors
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    Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-01-20
    Description: Multiple endocrine neoplasia types 2A and 2B (MEN2A and MEN2B) and familial medullary thyroid carcinoma are dominantly inherited cancer syndromes. All three syndromes are associated with mutations in RET, which encodes a receptor-like tyrosine kinase. The altered RET alleles were shown to be transforming genes in NIH 3T3 cells as a consequence of constitutive activation of the RET kinase. The MEN2A mutation resulted in RET dimerization at steady state, whereas the MEN2B mutation altered RET catalytic properties both quantitatively and qualitatively. Oncogenic conversion of RET in these neoplastic syndromes establishes germline transmission of dominant transforming genes in human cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santoro, M -- Carlomagno, F -- Romano, A -- Bottaro, D P -- Dathan, N A -- Grieco, M -- Fusco, A -- Vecchio, G -- Matoskova, B -- Kraus, M H -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):381-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centro di Endocrinologia ed Oncologia Sperimentale, Consiglio Nazionale delle Ricerche (CNR), Napoli, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824936" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Alleles ; Animals ; Cell Transformation, Neoplastic/*genetics ; *Drosophila Proteins ; Genetic Vectors ; Humans ; Mice ; Multiple Endocrine Neoplasia Type 2a/*genetics ; Multiple Endocrine Neoplasia Type 2b/*genetics ; Mutation ; Phosphorylation ; Proto-Oncogene Proteins/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-ret ; *Proto-Oncogenes ; Receptor Protein-Tyrosine Kinases/chemistry/*genetics/metabolism ; Substrate Specificity ; Transfection ; Tumor Cells, Cultured
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    Bisexual fruit flies point to brain courtship centers (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):791-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846522" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bisexuality ; Brain/physiology ; Crosses, Genetic ; Drosophila melanogaster/genetics/*physiology ; Female ; *Genes, Insect ; Male ; Mutation ; Sex Attractants/physiology ; Sexual Behavior, Animal ; Smell
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    ILR1, an amidohydrolase that releases active indole-3-acetic acid from conjugates (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-06-23
    Description: In plants, the growth regulator indole-3-acetic acid (IAA) is found both free and conjugated to a variety of amino acids, peptides, and carbohydrates. IAA conjugated to leucine has effects in Arabidopsis thaliana similar to those of free IAA. The ilr1 mutant is insensitive to exogenous IAA-Leu and was used to positionally clone the Arabidopsis ILR1 gene. ILR1 encodes a 48-kilodalton protein that cleaves IAA-amino acid conjugates in vitro and is homologous to bacterial amidohydrolase enzymes. DNA sequences similar to that of ILR1 are found in other plant species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartel, B -- Fink, G R -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1745-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792599" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Amino Acids ; Arabidopsis/enzymology/*genetics ; *Arabidopsis Proteins ; Base Sequence ; Cloning, Molecular ; *Genes, Plant ; Hydrolysis ; Indoleacetic Acids/*metabolism/pharmacology ; Leucine/metabolism ; Molecular Sequence Data ; Mutation ; Plant Growth Regulators/*metabolism ; Sequence Alignment
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    Strain-dependent epithelial defects in mice lacking the EGF receptor (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-07-14
    Description: Mice and cells lacking the epidermal growth factor receptor (EGFR) were generated to examine its physiological role in vivo. Mutant fetuses are retarded in growth and die at mid-gestation in a 129/Sv genetic background, whereas in a 129/Sv x C57BL/6 cross some survive until birth and even to postnatal day 20 in a 129/Sv x C57BL/6 x MF1 background. Death in utero probably results from a defect in the spongiotrophoblast layer of the placenta. Newborn mutant mice have open eyes, rudimentary whiskers, immature lungs, and defects in the epidermis, correlating with the expression pattern of the EGFR as monitored by beta-galactosidase activity. These defects are probably cell-autonomous because chimeric mice generated with EGFR-/- embryonic stem cells contribute small amounts of mutant cells to some organs. These results indicate that the EGFR regulates epithelial proliferation and differentiation and that the genetic background influences the resulting phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sibilia, M -- Wagner, E F -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):234-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Pathology (IMP), Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618085" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; *Embryonic and Fetal Development ; *Epithelial Cells ; Female ; Gene Targeting ; Hematopoiesis ; Lung/cytology/embryology ; Male ; Mice ; Mice, Inbred Strains ; Mutation ; Phenotype ; Placenta/physiology ; Receptor, Epidermal Growth Factor/genetics/*physiology ; Skin/cytology/embryology ; Species Specificity ; Stem Cells/cytology ; Trophoblasts/cytology
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    Converting Escherichia coli RNA polymerase into an enhancer-responsive enzyme: role of an NH2-terminal leucine patch in sigma 54 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-10
    Description: The protein sigma 54 associates with Escherichia coli core RNA polymerase to form a holoenzyme that binds promoters but is inactive in the absence of enhancer activation. Here, mutants of sigma 54 enabled polymerases to transcribe without enhancer protein and adenosine triphosphate. The mutations are in leucines within the NH2-terminal glutamine-rich domain of sigma 54. Multiple leucine substitutions mimicked the effect of enhancer protein, which suggests that the enhancer protein functions to disrupt a leucine patch. The results indicate that sigma 54 acts both as an inhibitor of polymerase activity and as a receptor that interacts with enhancer protein to overcome this inhibition, and that these two activities jointly confer enhancer responsiveness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J T -- Syed, A -- Hsieh, M -- Gralla, J D -- GM35754/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):992-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481805" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacterial Proteins/physiology ; DNA-Binding Proteins/*physiology ; DNA-Directed RNA Polymerases/chemistry/genetics/*metabolism ; *Enhancer Elements, Genetic ; Escherichia coli/*enzymology/genetics/growth & development ; Escherichia coli Proteins ; Leucine/chemistry ; Molecular Sequence Data ; Mutation ; PII Nitrogen Regulatory Proteins ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Sigma Factor/chemistry/genetics/*metabolism ; *Trans-Activators ; Transcription Factors/*physiology ; Transcription, Genetic
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    Association between X-linked mixed deafness and mutations in the POU domain gene POU3F4 (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-03
    Description: Deafness with fixation of the stapes (DFN3) is the most frequent X-linked form of hearing impairment. The underlying gene has been localized to a 500-kilobase segment of the Xq21 band. Here, it is reported that a candidate gene for this disorder, Brain 4 (POU3F4), which encodes a transcription factor with a POU domain, maps to the same interval. In five unrelated patients with DFN3 but not in 50 normal controls, small mutations were found that result in truncation of the predicted protein or in nonconservative amino acid substitutions. These findings indicate that POU3F4 mutations are a molecular cause of DFN3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Kok, Y J -- van der Maarel, S M -- Bitner-Glindzicz, M -- Huber, I -- Monaco, A P -- Malcolm, S -- Pembrey, M E -- Ropers, H H -- Cremers, F P -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):685-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, University Hospital Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839145" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; DNA Mutational Analysis ; Deafness/*genetics ; Female ; Genetic Linkage ; Humans ; Male ; Molecular Sequence Data ; Mutation ; POU Domain Factors ; Pedigree ; Point Mutation ; Polymerase Chain Reaction ; Sequence Deletion ; Transcription Factors/chemistry/*genetics ; *X Chromosome
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    Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: The Escherichia coli guanosine triphosphate (GTP)-binding proteins Ffh and FtsY have been proposed to catalyze the cotranslational targeting of proteins to the bacterial plasma membrane. A mutation was introduced into the GTP-binding domain of FtsY that altered its nucleotide specificity from GTP to xanthosine triphosphate (XTP). The mutant FtsY protein stimulated GTP hydrolysis by a ribonucleoprotein consisting of Ffh and 4.5S RNA in a reaction that required XTP, and it hydrolyzed XTP in a reaction that required both the Ffh-4.5S ribonucleoprotein and GTP. Thus, nucleotide triphosphate hydrolysis by Ffh and FtsY is likely to occur in reciprocally coupled reactions in which the two interacting guanosine triphosphatases act as regulatory proteins for each other.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Powers, T -- Walter, P -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1422-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California Medical School, San Francisco 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660124" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/genetics/*metabolism ; Base Sequence ; Enzyme Activation ; *Escherichia coli Proteins ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanosine Triphosphate/*metabolism ; Hydrolysis ; Molecular Sequence Data ; Mutation ; Receptors, Cytoplasmic and Nuclear/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Ribonucleotides/metabolism/pharmacology ; Signal Recognition Particle/*metabolism
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    Chromosomal control of meiotic cell division (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Chromosomes have multiple roles both in controlling the cell assembly and structure of the spindle and in determining chromosomal position on the spindle in many meiotic cells and in some types of mitotic cells. Moreover, functionally significant chromosome-microtubule interactions are not limited to the kinetochore but are also mediated by proteins localized along the arms of chromosomes. Finally, chromosomes also play a crucial role in control of the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKim, K S -- Hawley, R S -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1595-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of California at Davis 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502068" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Animals ; *Cell Cycle ; Chromosomes/*physiology/ultrastructure ; DNA-Binding Proteins/physiology ; Kinesin/physiology ; Kinetochores/physiology ; *Meiosis ; Metaphase ; Microtubule Proteins/physiology ; Microtubules/physiology/ultrastructure ; Mutation ; Nuclear Proteins/physiology ; Spindle Apparatus/physiology/ultrastructure
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    The evolution of molecular computation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stemmer, W P -- New York, N.Y. -- Science. 1995 Dec 1;270(5241):1510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7491501" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Sequence ; *Dna ; *Evolution, Molecular ; Gene Library ; Genome, Human ; Humans ; *Mathematical Computing ; Mutation ; Selection, Genetic
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    Candidate gene for the chromosome 1 familial Alzheimer's disease locus (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-18
    Description: A candidate gene for the chromosome 1 Alzheimer's disease (AD) locus was identified (STM2). The predicted amino acid sequence for STM2 is homologous to that of the recently cloned chromosome 14 AD gene (S182). A point mutation in STM2, resulting in the substitution of an isoleucine for an asparagine (N141l), was identified in affected people from Volga German AD kindreds. This N141l mutation occurs at an amino acid residue that is conserved in human S182 and in the mouse S182 homolog. The presence of missense mutations in AD subjects in two highly similar genes strongly supports the hypothesis that mutations in both are pathogenic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy-Lahad, E -- Wasco, W -- Poorkaj, P -- Romano, D M -- Oshima, J -- Pettingell, W H -- Yu, C E -- Jondro, P D -- Schmidt, S D -- Wang, K -- AG0513C/AG/NIA NIH HHS/ -- R01-AG11762/AG/NIA NIH HHS/ -- R01-AG11899/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geriatric Research Education, and Clinical Center (182B), Veterans Affairs Medical Center, Seattle, WA 98108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638622" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/ethnology/*genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Cloning, Molecular ; DNA, Complementary/genetics ; Female ; Gene Expression ; Germany/ethnology ; Humans ; Lod Score ; Male ; Membrane Proteins/chemistry/*genetics ; Middle Aged ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Presenilin-2
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    Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-06
    Description: Cdc2 is the cyclin-dependent kinase that controls entry of cells into mitosis. Phosphorylation of Cdc2 on threonine-14 and tyrosine-15 inhibits the activity of the enzyme and prevents premature initiation of mitosis. Although Wee1 has been identified as the kinase that phosphorylates tyrosine-15 in various organisms, the threonine-14-specific kinase has not been isolated. A complementary DNA was cloned from Xenopus that encodes Myt1, a member of the Wee1 family that was discovered to phosphorylate Cdc2 efficiently on both threonine-14 and tyrosine-15. Myt1 is a membrane-associated protein that contains a putative transmembrane segment. Immunodepletion studies suggested that Myt1 is the predominant threonine-14-specific kinase in Xenopus egg extracts. Myt1 activity is highly regulated during the cell cycle, suggesting that this relative of Wee1 plays a role in mitotic control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueller, P R -- Coleman, T R -- Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):86-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569953" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/*metabolism ; *Cell Cycle Proteins ; Cell Membrane/enzymology ; Cloning, Molecular ; Cyclins/metabolism ; Interphase ; Mitosis ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Oocytes/enzymology ; Phosphorylation ; Phosphothreonine/metabolism ; Phosphotyrosine/metabolism ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins
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    Solution structure of the activator contact domain of the RNA polymerase alpha subunit (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-01
    Description: The structure of the carboxyl-terminal domain of the Escherichia coli RNA polymerase alpha subunit (alpha CTD), which is regarded as the contact site for transcription activator proteins and for the promoter UP element, was determined by nuclear magnetic resonance spectroscopy. Its compact structure of four helices and two long arms enclosing its hydrophobic core shows a folding topology distinct from those of other DNA-binding proteins. The UP element binding site was found on the surface comprising helix 1, the amino-terminal end of helix 4, and the preceding loop. Mutation experiments indicated that the contact sites for transcription activator proteins are also on the same surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeon, Y H -- Negishi, T -- Shirakawa, M -- Yamazaki, T -- Fujita, N -- Ishihama, A -- Kyogoku, Y -- New York, N.Y. -- Science. 1995 Dec 1;270(5241):1495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7491496" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/metabolism ; DNA-Directed RNA Polymerases/*chemistry/genetics/metabolism ; Escherichia coli/enzymology ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Promoter Regions, Genetic ; Protein Folding ; Protein Structure, Secondary ; Solutions ; Trans-Activators/metabolism
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    HIV population dynamics in vivo: implications for genetic variation, pathogenesis, and therapy (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Several recent reports indicate that the long, clinically latent phase that characterizes human immunodeficiency virus (HIV) infection of humans is not a period of viral inactivity, but an active process in which cells are being infected and dying at a high rate and in large numbers. These results lead to a simple steady-state model in which infection, cell death, and cell replacement are in balance, and imply that the unique feature of HIV is the extraordinarily large number of replication cycles that occur during infection of a single individual. This turnover drives both the pathogenic process and (even more than mutation rate) the development of genetic variation. This variation includes the inevitable and, in principle, predictable accumulation of mutations such as those conferring resistance to antiviral drugs whose presence before therapy must be considered in the design of therapeutic strategies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coffin, J M -- R35 CA 44385/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):483-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824947" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/drug therapy/immunology/*virology ; Antiviral Agents/pharmacology/therapeutic use ; CD4 Lymphocyte Count ; CD4-Positive T-Lymphocytes/immunology/*virology ; Cell Death ; DNA, Viral/blood ; Drug Resistance, Microbial ; Genetic Variation ; HIV/drug effects/genetics/*physiology ; HIV Infections/drug therapy/immunology/*virology ; Humans ; Kinetics ; Mutation ; Proviruses/genetics/physiology ; RNA, Viral/blood ; Viremia/virology ; Virus Replication
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    Mutations in the sulfonylurea receptor gene in familial persistent hyperinsulinemic hypoglycemia of infancy (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Familial persistent hyperinsulinemic hypoglycemia of infancy (PHHI), an autosomal recessive disorder characterized by unregulated insulin secretion, is linked to chromosome 11p14-15.1. The newly cloned high-affinity sulfonylurea receptor (SUR) gene, a regulator of insulin secretion, was mapped to 11p15.1 by means of fluorescence in situ hybridization. Two separate SUR gene splice site mutations, which segregated with disease phenotype, were identified in affected individuals from nine different families. Both mutations resulted in aberrant processing of the RNA sequence and disruption of the putative second nucleotide binding domain of the SUR protein. Abnormal insulin secretion in PHHI appears to be caused by mutations in the SUR gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, P M -- Cote, G J -- Wohllk, N -- Haddad, B -- Mathew, P M -- Rabl, W -- Aguilar-Bryan, L -- Gagel, R F -- Bryan, J -- DK38146/DK/NIDDK NIH HHS/ -- DK44311/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):426-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Specialties, University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716548" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; DNA Mutational Analysis ; DNA, Complementary/genetics ; Genotype ; Humans ; Hyperinsulinism/*genetics ; Hypoglycemia/*genetics ; Infant ; Insulin/secretion ; Molecular Sequence Data ; Mutation ; Pancreatic Diseases/*genetics ; Phenotype ; Point Mutation ; Potassium Channels/chemistry/*genetics ; *Potassium Channels, Inwardly Rectifying ; RNA Splicing ; Receptors, Drug/chemistry/*genetics ; Sulfonylurea Compounds/metabolism ; Sulfonylurea Receptors
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    Targeted disruption of mouse EGF receptor: effect of genetic background on mutant phenotype (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-14
    Description: Gene targeting was used to create a null allele at the epidermal growth factor receptor locus (Egfr). The phenotype was dependent on genetic background. EGFR deficiency on a CF-1 background resulted in peri-implantation death due to degeneration of the inner cell mass. On a 129/Sv background, homozygous mutants died at mid-gestation due to placental defects; on a CD-1 background, the mutants lived for up to 3 weeks and showed abnormalities in skin, kidney, brain, liver, and gastrointestinal tract. The multiple abnormalities associated with EGFR deficiency indicate that the receptor is involved in a wide range of cellular activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Threadgill, D W -- Dlugosz, A A -- Hansen, L A -- Tennenbaum, T -- Lichti, U -- Yee, D -- LaMantia, C -- Mourton, T -- Herrup, K -- Harris, R C -- GM14630/GM/NIGMS NIH HHS/ -- HD07104/HD/NICHD NIH HHS/ -- HD26722/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):230-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Case Western Reserve University, Cleveland, OH 44106-4955, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618084" target="_blank"〉PubMed〈/a〉
    Keywords: Abnormalities, Multiple/*genetics ; Animals ; Base Sequence ; Brain/abnormalities/cytology ; Cell Division ; Digestive System/cytology ; Digestive System Abnormalities ; *Embryonic and Fetal Development ; Female ; *Gene Targeting ; Hair/abnormalities ; Homozygote ; Kidney/cytology ; Lung/cytology ; Male ; Mice ; Molecular Sequence Data ; Mutation ; Phenotype ; Receptor, Epidermal Growth Factor/deficiency/*genetics/*physiology ; Skin/cytology ; Skin Abnormalities
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    Annual genetics meeting: some puzzles, some answers (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1120-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502034" target="_blank"〉PubMed〈/a〉
    Keywords: Acrocephalosyndactylia/*genetics ; Fathers ; Female ; *Genetics, Medical ; Humans ; Male ; Mutation ; Myotonic Dystrophy/*genetics ; Myotonin-Protein Kinase ; Protein-Serine-Threonine Kinases/genetics ; RNA/metabolism ; Receptor Protein-Tyrosine Kinases/genetics ; Receptor, Fibroblast Growth Factor, Type 2 ; Receptors, Fibroblast Growth Factor/genetics ; Repetitive Sequences, Nucleic Acid
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    Silver as a probe of pore-forming residues in a potassium channel (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: In voltage-dependent potassium channels, the molecular determinants of ion selectivity are found in the P (pore) region, a stretch of 21 contiguous residues. Cysteine was introduced at each P region position in a Shaker potassium channel. Residues projecting side chains into the pore were identified by means of channel inhibition by a sulfhydryl-reactive potassium ion analog, silver ion. The pattern of silver ion reactivity contradicts a beta barrel architecture of potassium channel pores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Q -- Miller, C -- GM-31768/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):304-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02254, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cysteine/pharmacology ; Mutation ; Oocytes ; Patch-Clamp Techniques ; Potassium Channels/*chemistry/genetics/physiology ; Shaker Superfamily of Potassium Channels ; *Silver ; Xenopus laevis
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    Yeast checkpoint genes in DNA damage processing: implications for repair and arrest (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-01
    Description: Yeast checkpoint control genes were found to affect processing of DNA damage as well as cell cycle arrest. An assay that measures DNA damage processing in vivo showed that the checkpoint genes RAD17, RAD24, and MEC3 activated an exonuclease that degrades DNA. The degradation is probably a direct consequence of checkpoint protein function, because RAD17 encodes a putative 3'-5' DNA exonuclease. Another checkpoint gene, RAD9, had a different role: It inhibited the degradation by RAD17, RAD24, and MEC3. A model of how processing of DNA damage may be linked to both DNA repair and cell cycle arrest is proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lydall, D -- Weinert, T -- GM 45276-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 1;270(5241):1488-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of Arizona, Tucson 85721, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7491494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle Proteins ; *DNA Damage ; *DNA Repair ; DNA, Fungal/*metabolism ; DNA-Binding Proteins ; Exonucleases/chemistry/genetics/metabolism ; Fungal Proteins/chemistry/*genetics ; *G2 Phase ; *Genes, Fungal ; Molecular Sequence Data ; Mutation ; Yeasts/cytology/*genetics/metabolism
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    Appropriate partners make good matches (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karran, P -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1857-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund, Clare Hall Laboratories, Hertfordshire, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604258" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Colorectal Neoplasms/*genetics ; Colorectal Neoplasms, Hereditary Nonpolyposis/genetics ; *DNA Repair/genetics ; DNA, Neoplasm/*metabolism ; DNA-Binding Proteins/genetics/physiology ; Germ-Line Mutation ; Humans ; Molecular Sequence Data ; MutS Homolog 2 Protein ; Mutation ; Nucleic Acid Heteroduplexes/metabolism ; Phenotype ; Proto-Oncogene Proteins/genetics/physiology ; Tumor Cells, Cultured
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    Discovery of AT gene sparks biomedical research bonanza (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-06-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1700-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792589" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia/*genetics ; Ataxia Telangiectasia Mutated Proteins ; Breast Neoplasms/*genetics ; Cell Cycle Proteins ; Cell Division ; Cloning, Molecular ; DNA Damage ; DNA Repair ; DNA-Binding Proteins ; Female ; Genetic Predisposition to Disease ; Genetic Testing ; Heterozygote ; Humans ; Mutation ; Phosphatidylinositol 3-Kinases ; Phosphotransferases (Alcohol Group Acceptor)/genetics/metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/*genetics ; Radiation Tolerance ; Signal Transduction ; Tumor Suppressor Proteins ; X-Rays
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    New clues found to Huntington's (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502028" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology ; Humans ; Huntington Disease/*metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/immunology/*metabolism ; Nuclear Proteins/chemistry/genetics/immunology/*metabolism ; Spinocerebellar Degenerations/metabolism
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    New clock gene cloned (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-11-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):732-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481759" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/*genetics ; Cell Nucleus/metabolism ; Circadian Rhythm/*genetics ; Cloning, Molecular ; Cytoplasm/metabolism ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/metabolism ; Gene Expression Regulation ; *Genes, Insect ; Mutation ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Proteins/*genetics/metabolism
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    Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-01
    Description: The phosphorylation of the human estrogen receptor (ER) serine residue at position 118 is required for full activity of the ER activation function 1 (AF-1). This Ser118 is phosphorylated by mitogen-activated protein kinase (MAPK) in vitro and in cells treated with epidermal growth factor (EGF) and insulin-like growth factor (IGF) in vivo. Overexpression of MAPK kinase (MAPKK) or of the guanine nucleotide binding protein Ras, both of which activate MAPK, enhanced estrogen-induced and antiestrogen (tamoxifen)-induced transcriptional activity of wild-type ER, but not that of a mutant ER with an alanine in place of Ser118. Thus, the activity of the amino-terminal AF-1 of the ER is modulated by the phosphorylation of Ser118 through the Ras-MAPK cascade of the growth factor signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kato, S -- Endoh, H -- Masuhiro, Y -- Kitamoto, T -- Uchiyama, S -- Sasaki, H -- Masushige, S -- Gotoh, Y -- Nishida, E -- Kawashima, H -- Metzger, D -- Chambon, P -- New York, N.Y. -- Science. 1995 Dec 1;270(5241):1491-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Agricultural Chemistry, Tokyo University of Agriculture, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7491495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; Estradiol/analogs & derivatives/pharmacology ; Estrogen Antagonists/pharmacology ; Humans ; Mitogen-Activated Protein Kinase Kinases ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Polyunsaturated Alkamides ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-raf ; Proto-Oncogene Proteins p21(ras)/metabolism ; Receptors, Estrogen/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Serine/*metabolism ; Somatomedins/pharmacology ; Tamoxifen/analogs & derivatives/pharmacology ; *Transcriptional Activation/drug effects ; Transfection
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    HERG, a human inward rectifier in the voltage-gated potassium channel family (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: In contrast to other members of the Eag family of voltage-gated, outwardly rectifying potassium channels, the human eag-related gene (HERG) has now been shown to encode an inwardly rectifying potassium channel. The properties of HERG channels are consistent with the gating properties of Eag-related and other outwardly rectifying, S4-containing potassium channels, but with the addition of an inactivation mechanism that attenuates potassium efflux during depolarization. Because mutations in HERG cause a form of long-QT syndrome, these properties of HERG channel function may be critical to the maintenance of normal cardiac rhythmicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trudeau, M C -- Warmke, J W -- Ganetzky, B -- Robertson, G A -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Wisconsin Medical School, Madison 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604285" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Barium/pharmacology ; Cesium/pharmacology ; Ether-A-Go-Go Potassium Channels ; Humans ; *Ion Channel Gating ; Long QT Syndrome/genetics/physiopathology ; Membrane Potentials ; Mutation ; Oocytes ; Patch-Clamp Techniques ; Potassium Channels/drug effects/genetics/*physiology ; *Potassium Channels, Inwardly Rectifying ; Ranidae
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  • 73
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    Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Small changes in the peptide-major histocompatibility complex (MHC) molecule ligands recognized by antigen-specific T cell receptors (TCRs) can convert fully activating complexes into partially activating or even inhibitory ones. This study examined early TCR-dependent signals induced by such partial agonists or antagonists. In contrast to typical agonist ligands, both an antagonist and several partial agonists stimulated a distinct pattern of zeta chain phosphorylation and failed to activate associated ZAP-70 kinase. These results identify a specific step in the early tyrosine phosphorylation cascade that is altered after TCR engagement with modified peptide-MHC molecule complexes. This finding may explain the different biological responses to TCR occupancy by these variant ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madrenas, J -- Wange, R L -- Wang, J L -- Isakov, N -- Samelson, L E -- Germain, R N -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):515-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lymphocyte Biology Section, 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/7824949" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Clone Cells ; Cytochrome c Group/pharmacology ; Enzyme Activation ; Histocompatibility Antigens Class II/genetics/immunology/*pharmacology ; Interleukin-2/biosynthesis ; L Cells (Cell Line) ; Ligands ; Lymphocyte Activation ; Membrane Proteins/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Peptide Fragments/pharmacology ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell/agonists/antagonists & inhibitors/*metabolism ; Signal Transduction ; T-Lymphocytes, Helper-Inducer/*immunology ; Tyrosine/metabolism ; ZAP-70 Protein-Tyrosine Kinase
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  • 74
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    Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-28
    Description: The role of mitogen-activated protein (MAP) kinase cascades in integrating distinct upstream signals was studied in yeast. Mutants that were not able to activate PBS2 MAP kinase kinase (MAPKK; Pbs2p) at high osmolarity were characterized. Pbs2p was activated by two independent signals that emanated from distinct cell-surface osmosensors. Pbs2p was activated by MAP kinase kinase kinases (MAPKKKs) Ssk2p and Ssk22p that are under the control of the SLN1-SSK1 two-component osmosensor. Alternatively, Pbs2p was activated by a mechanism that involves the binding of its amino terminal proline-rich motif to the Src homology 3 (SH3) domain of a putative transmembrane osmosensor Sho1p.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maeda, T -- Takekawa, M -- Saito, H -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):554-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624781" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cloning, Molecular ; Enzyme Activation ; Fungal Proteins/metabolism ; Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase Kinases ; Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Mutation ; Osmolar Concentration ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; *Saccharomyces cerevisiae Proteins ; Signal Transduction
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  • 75
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    Rhythmic expression of timeless: a basis for promoting circadian cycles in period gene autoregulation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The clock gene timeless (tim) is required for circadian rhythmicity in Drosophila. The accumulation of tim RNA followed a circadian rhythm, and the phase and period of the tim RNA rhythm were indistinguishable from those that have been reported for per. The tim RNA oscillations were found to be dependent on the presence of PER and TIM proteins, which demonstrates feedback control of tim by a mechanism previously shown to regulate per expression. The cyclic expression of tim appears to dictate the timing of PER protein accumulation and nuclear localization, suggesting that tim promotes circadian rhythms of per and tim transcription by restricting per RNA and PER protein accumulation to separate times of day.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sehgal, A -- Rothenfluh-Hilfiker, A -- Hunter-Ensor, M -- Chen, Y -- Myers, M P -- Young, M W -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, University of Pennsylvania Medical Center, Philadelphia 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481772" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/genetics ; Circadian Rhythm/*genetics ; Darkness ; *Drosophila Proteins ; Drosophila melanogaster/*genetics/physiology ; *Gene Expression Regulation ; *Genes, Insect ; Mutation ; Nuclear Proteins/*genetics/metabolism ; Period Circadian Proteins ; Proteins/*genetics/metabolism ; RNA/genetics/metabolism
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    Dependence of peptide binding by MHC class I molecules on their interaction with TAP (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-06
    Description: Major histocompatibility complex (MHC) class I molecules bind peptides that are delivered from the cytosol into the endoplasmic reticulum by the MHC-encoded transporter associated with antigen processing (TAP). Peptide capture by immature heterodimers of class I heavy chains and beta 2-microglobulin may be facilitated by their physical association with TAP. A genetic defect in a human mutant cell line causes the complete failure of diverse class I heterodimers to associate with TAP. This deficiency impairs the ability of the class I heterodimers to efficiently capture peptides and results from loss of function of an unidentified gene or genes linked to the MHC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grandea, A G 3rd -- Androlewicz, M J -- Athwal, R S -- Geraghty, D E -- Spies, T -- AI30581/AI/NIAID NIH HHS/ -- AI38508/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):105-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569935" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*metabolism ; Amino Acid Sequence ; Calcium-Binding Proteins/metabolism ; Calnexin ; Cell Line ; Endoplasmic Reticulum/metabolism ; HLA Antigens/metabolism ; HLA-A1 Antigen/metabolism ; HLA-B Antigens/metabolism ; HLA-B8 Antigen/metabolism ; HLA-G Antigens ; Histocompatibility Antigens Class I/*metabolism ; Humans ; Ligands ; *Major Histocompatibility Complex/genetics ; Molecular Sequence Data ; Mutation ; Peptides/*metabolism ; Transfection ; beta 2-Microglobulin/metabolism
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  • 77
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    Commitment of CNS progenitors along the dorsoventral axis of Drosophila neuroectoderm (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: In the Drosophila embryo, the central nervous system (CNS) develops from a population of neural stem cells (neuroblasts) and midline progenitor cells. Here, the fate and extent of determination of CNS progenitors along the dorsoventral axis was assayed. Dorsal neuroectodermal cells transplanted into the ventral neuroectoderm or into the midline produced CNS lineages consistent with their new position. However, ventral neuroectodermal cells and midline cells transplanted to dorsal sites of the neuroectoderm migrated ventrally and produced CNS lineages consistent with their origin. Thus, inductive signals at the ventral midline and adjacent neuroectoderm may confer ventral identities to CNS progenitors as well as the ability to assume and maintain characteristic positions in the developing CNS. Furthermore, ectopic transplantations of wild-type midline cells into single minded (sim) mutant embryos suggest that the ventral midline is required for correct positioning of the cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Udolph, G -- Luer, K -- Bossing, T -- Technau, G M -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Genetik, Universitat Mainz, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652576" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Movement ; Cell Transplantation ; Central Nervous System/embryology ; Drosophila/*embryology ; Ectoderm/cytology/*physiology ; Gastrula/cytology ; Mutation ; Neuroglia/cytology ; Neurons/*cytology ; Stem Cell Transplantation ; Stem Cells/*cytology/physiology ; Transplantation, Heterotopic
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  • 78
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    Induction of ectopic eyes by targeted expression of the eyeless gene in Drosophila (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-24
    Description: The Drosophila gene eyeless (ey) encodes a transcription factor with both a paired domain and a homeodomain. It is homologous to the mouse Small eye (Pax-6) gene and to the Aniridia gene in humans. These genes share extensive sequence identity, the position of three intron splice sites is conserved, and these genes are expressed similarly in the developing nervous system and in the eye during morphogenesis. Loss-of-function mutations in both the insect and in the mammalian genes have been shown to lead to a reduction or absence of eye structures, which suggests that ey functions in eye morphogenesis. By targeted expression of the ey complementary DNA in various imaginal disc primordia of Drosophila, ectopic eye structures were induced on the wings, the legs, and on the antennae. The ectopic eyes appeared morphologically normal and consisted of groups of fully differentiated ommatidia with a complete set of photoreceptor cells. These results support the proposition that ey is the master control gene for eye morphogenesis. Because homologous genes are present in vertebrates, ascidians, insects, cephalopods, and nemerteans, ey may function as a master control gene throughout the metazoa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halder, G -- Callaerts, P -- Gehring, W J -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1788-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Drosophila/*embryology/*genetics ; Eye/embryology ; Gene Expression Regulation/physiology ; Genes, Homeobox/physiology ; Genes, Insect/*physiology ; Genes, Reporter ; Microscopy, Electron, Scanning ; Mutation ; Photoreceptor Cells, Invertebrate/embryology ; beta-Galactosidase/genetics
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    Minisatellites and human disease (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-09-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krontiris, T G -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1682-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Tufts University School of Medicine, Boston, MA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569893" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Consensus Sequence ; DNA, Satellite/*genetics/metabolism ; Diabetes Mellitus, Type 1/*genetics ; Gene Conversion ; Genetic Predisposition to Disease ; Humans ; Linkage Disequilibrium ; Minisatellite Repeats/*genetics ; Mutation ; Neoplasms/*genetics ; Transcription Factors/metabolism ; Transcriptional Activation
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  • 80
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    Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: A mismatch-binding heterodimer of hMSH2 and a 160-kilodalton polypeptide has been isolated from HeLa cells by virtue of its ability to restore mismatch repair to nuclear extracts of hMSH2-deficient LoVo colorectal tumor cells. This heterodimer, designated hMutS alpha, also restores mismatch repair to extracts of alkylation-tolerant MT1 lymphoblastoid cells and HCT-15 colorectal tumor cells, which are selectively defective in the repair of base-base and single-nucleotide insertion-deletion mismatches. Because HOT-15 cells appear to be free of hMSH2 mutations, this selective repair defect is likely a result of a deficiency of the hMutS alpha 160-kilodalton subunit, and mutations in the corresponding gene may confer hypermutability and cancer predisposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drummond, J T -- Li, G M -- Longley, M J -- Modrich, P -- GM45190/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1909-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604264" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Colorectal Neoplasms/chemistry/*genetics ; DNA Damage ; DNA Repair/*genetics ; DNA, Neoplasm/*metabolism ; DNA-Binding Proteins/chemistry/*isolation & purification/physiology ; HeLa Cells ; Humans ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Nucleic Acid Heteroduplexes/metabolism ; Sequence Deletion ; Tumor Cells, Cultured
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  • 81
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    Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: I kappa B-alpha inhibits transcription factor NF-kappa B by retaining it in the cytoplasm. Various stimuli, typically those associated with stress or pathogens, rapidly inactivate I kappa B-alpha. This liberates NF-kappa B to translocate to the nucleus and initiate transcription of genes important for the defense of the organism. Activation of NF-kappa B correlates with phosphorylation of I kappa B-alpha and requires the proteolysis of this inhibitor. When either serine-32 or serine-36 of I kappa B-alpha was mutated, the protein did not undergo signal-induced phosphorylation or degradation, and NF-kappa B could not be activated. These results suggest that phosphorylation at one or both of these residues is critical for activation of NF-kappa B.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, K -- Gerstberger, S -- Carlson, L -- Franzoso, G -- Siebenlist, U -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1485-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-1876.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878466" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Humans ; *I-kappa B Proteins ; Ionomycin/pharmacology ; Mice ; Molecular Sequence Data ; Mutation ; NF-kappa B/*antagonists & inhibitors/metabolism ; Phosphorylation ; Point Mutation ; Signal Transduction ; T-Lymphocytes ; Tetradecanoylphorbol Acetate/pharmacology ; Transcriptional Activation ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology
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  • 82
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    Control of electron transfer between the L- and M-sides of photosynthetic reaction centers (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-18
    Description: An aspartic acid residue has been introduced near ring V of the L-side accessory bacteriochlorophyll (BCHlL) or the photosynthetic reaction center in a rhodobacter capsulatus mutant in which a His also replaces Leu 212 on the M-polypeptide. The initial stage of charge separation in the G(M201)D/L(M212)H double mutant yields approximately 70 percent electron transfer to the L-side cofactors, approximately 15 percent rapid deactivation to the ground state, and approximately 15 percent electron transfer to the so-called inactive M-side bacteriopheophytin (BPhM). It is suggested here that the Asp introduced at M201 modulates the reduction potential of BCHlL, thereby changing the energetics of charge separation. The results demonstrate that an individual amino acid residue can, through its influence on the free energies of the charge-separated states, effectively dictate the balance between the forward electron transfer reactions on the L-side of the RC, the charge-recombination processes, and electron transfer to the M-side chromophores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heller, B A -- Holten, D -- Kirmaier, C -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):940-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Washington University, St Louis, MO 63130, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638616" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriochlorophylls/chemistry/*metabolism ; Electron Transport ; Light-Harvesting Protein Complexes ; Mutation ; Pheophytins/chemistry/*metabolism ; Photochemistry ; Photosynthetic Reaction Center Complex Proteins/chemistry/*metabolism ; Rhodobacter capsulatus/genetics/*metabolism ; Spectrum Analysis ; Thermodynamics
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  • 83
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    Delayed helix formation of mutant collagen (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinmann, B -- Raghunath, M -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):258.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809634" target="_blank"〉PubMed〈/a〉
    Keywords: Collagen/*chemistry/genetics ; Humans ; Mutation ; Osteogenesis Imperfecta/metabolism ; Peptides/chemistry/genetics ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary
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