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  • Articles  (19)
  • Mutation  (19)
  • 1995-1999  (19)
  • 1995  (19)
  • Natural Sciences in General  (19)
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  • Articles  (19)
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  • 1995-1999  (19)
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Journal
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  • 1
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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
    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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    Inhibition of transcription elongation by the VHL tumor suppressor protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Germline mutations in the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of tumors, including renal carcinoma, hemangioblastoma of the central nervous system, and pheochromocytoma. Here, a cellular transcription factor, Elongin (SIII), is identified as a functional target of the VHL protein. Elongin (SIII) is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C) that activate transcription elongation by RNA polymerase II. The VHL protein was shown to bind tightly and specifically to the Elongin B and C subunits and to inhibit Elongin (SIII) transcriptional activity in vitro. These findings reveal a potentially important transcriptional regulatory network in which the VHL protein may play a key role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duan, D R -- Pause, A -- Burgess, W H -- Aso, T -- Chen, D Y -- Garrett, K P -- Conaway, R C -- Conaway, J W -- Linehan, W M -- Klausner, R D -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1402-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Urologic Oncology Section, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Gene Expression Regulation ; *Genes, Tumor Suppressor ; HeLa Cells ; Humans ; *Ligases ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics/*metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Transcription Factors/chemistry/isolation & purification/*metabolism ; *Transcription, Genetic ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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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
    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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  • 4
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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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    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
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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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
    Print ISSN: 0036-8075
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  • 9
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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
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    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
    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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