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  • Articles  (82)
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  • American Association for the Advancement of Science (AAAS)  (82)
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  • Articles  (82)
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  • American Association for the Advancement of Science (AAAS)  (82)
  • American Association for the Advancement of Science
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  • 1
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    A "selfish" B chromosome that enhances its transmission by eliminating the paternal genome (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-22
    Description: In the parasitic wasp, Nasonia vitripennis, males are haploid and usually develop from unfertilized eggs, whereas females are diploid and develop from fertilized eggs. Some individuals in this species carry a genetic element, termed psr (paternal sex ratio), which is transmitted through sperm and causes condensation and subsequent loss of paternal chromosomes in fertilized eggs, thus converting diploid females into haploid males. In this report the psr trait was shown to be caused by a supernumerary chromosome. This B chromosome contains at least three repetitive DNA sequences that do not cross-hybridize to each other or to the host genome. The psr chromosome apparently produces a trans-acting product responsible for condensation of the paternal chromosomes, but is itself insensitive to the effect. Because the psr chromosome enhances its transmission by eliminating the rest of the genome, it can be considered the most "selfish" genetic element yet described.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nur, U -- Werren, J H -- Eickbush, D G -- Burke, W D -- Eickbush, T H -- GM31867/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 22;240(4851):512-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Rochester, NY 14627.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3358129" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes/*physiology ; Cloning, Molecular ; DNA, Satellite ; Diploidy ; Haploidy ; Hymenoptera/*genetics ; Molecular Sequence Data ; Repetitive Sequences, Nucleic Acid ; Sex Determination Analysis ; *Sex Ratio ; Wasps/*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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  • 2
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    Molecular cloning of odorant-binding protein: member of a ligand carrier family (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-15
    Description: Odorant-binding protein (OBP) is found in nasal epithelium, and it selectively binds odorants. Three complementary DNAs encoding rat odorant-binding protein have now been cloned and sequenced. One clone contains an open reading frame predicted to encode an 18,091-dalton protein. RNA blot analysis confirms the localization of OBP messenger RNA in the nasal epithelium. This OBP has 33 percent amino acid identity to alpha 2-microglobulin, a secreted plasma protein. Other members of an alpha 2-microglobulin superfamily bind and transport hydrophobic ligands. Thus, OBP probably binds and carries odorants within the nasal epithelium to putative olfactory receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pevsner, J -- Reed, R R -- Feinstein, P G -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- GM-07626/GM/NIGMS NIH HHS/ -- P01 CA16519-13/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):336-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388043" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*genetics ; Cloning, Molecular ; Ligands ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nasal Mucosa/*physiology ; Rats ; *Receptors, Odorant ; Smell/*physiology
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  • 3
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    Transient expression shows ligand gating and allosteric potentiation of GABAA receptor subunits (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-02
    Description: Human gamma-aminobutyric acid A (GABAA) receptor subunits were expressed transiently in cultured mammalian cells. This expression system allows the simultaneous characterization of ligand-gated ion channels by electrophysiology and by pharmacology. Thus, coexpression of the alpha and beta subunits of the GABAA receptor generated GABA-gated chloride channels and binding sites for GABAA receptor ligands. Channels consisting of only alpha or beta subunits could also be detected. These homomeric channels formed with reduced efficiencies compared to the heteromeric receptors. Both of these homomeric GABA-responsive channels were potentiated by barbiturate, indicating that sites for both ligand-gating and allosteric potentiation are present on receptors assembled from either subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pritchett, D B -- Sontheimer, H -- Gorman, C M -- Kettenmann, H -- Seeburg, P H -- Schofield, P R -- New York, N.Y. -- Science. 1988 Dec 2;242(4883):1306-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neuroendocrinology, ZMBH, University of Heidelberg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2848320" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Blotting, Northern ; Cells, Cultured ; Chloride Channels ; Chlorides/*physiology ; Cloning, Molecular ; Electric Conductivity ; Humans ; Macromolecular Substances ; Membrane Proteins/*physiology ; Muscimol/metabolism ; Receptors, GABA-A/*physiology/ultrastructure ; Structure-Activity Relationship ; Transfection
    Print ISSN: 0036-8075
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  • 4
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    Grafting genetically modified cells to the damaged brain: restorative effects of NGF expression (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-16
    Description: Fibroblasts were genetically modified to secrete nerve growth factor (NGF) by infection with a retroviral vector and then implanted into the brains of rats that had surgical lesions of the fimbria-fornix. The grafted cells survived and produced sufficient NGF to prevent the degeneration of cholinergic neurons that would die without treatment. In addition, the protected cholinergic cells sprouted axons that projected in the direction of the cellular source of NGF. These results indicate that a combination of gene transfer and intracerebral grafting may provide an effective treatment for some disorders of the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, M B -- Friedmann, T -- Robertson, R C -- Tuszynski, M -- Wolff, J A -- Breakefield, X O -- Gage, F H -- AG06088/AG/NIA NIH HHS/ -- HD20034/HD/NICHD NIH HHS/ -- NS24279/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1575-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of California School of Medicine, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201248" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholinesterase/metabolism ; Animals ; Brain/cytology/enzymology/*pathology ; Cell Survival ; DNA/genetics ; Fibroblasts/metabolism/*transplantation ; Genetic Vectors ; Histocytochemistry ; Moloney murine leukemia virus/genetics ; Nerve Growth Factors/genetics/*physiology ; Rats
    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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    Site-directed mutagenesis of two trans-regulatory genes (tat-III,trs) of HIV-1 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-19
    Description: Point mutations were introduced into the overlapping trans-regulatory genes (tat-III and trs) of human immunodeficiency virus type 1 (HIV-1), and the mutants were evaluated for virus expression. The results showed that tat-III has a positive transacting role and is required for transcriptional activation. A chain terminating mutation early in the trs gene resulted in an increase in transcription of viral messenger RNA as measured by nuclear transcription experiments, but only one major species of viral messenger RNA (1.8 kilobases) was detected, and little or no viral structural proteins were made. Thus, the trs gene product is essential for expression of virus structural proteins but, at the same time, may have a negative trans-regulatory role in transcription. Cotransfection of the point mutant proviruses defective in tat or trs with each other or with a complementary DNA clone containing tat and trs sequences restored the normal transcription pattern and subsequent virus production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sadaie, M R -- Benter, T -- Wong-Staal, F -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):910-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tumor Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3277284" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Acquired Immunodeficiency Syndrome/immunology ; Animals ; Cell Line ; Chloramphenicol O-Acetyltransferase ; Codon ; DNA/genetics ; *Genes, Regulator ; *Genes, Viral ; HIV/*genetics ; Humans ; Immunosorbent Techniques ; *Mutation ; Plasmids ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Transcription, Genetic ; Transfection
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  • 6
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    A newly characterized HLA DQ beta allele associated with pemphigus vulgaris (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-26
    Description: The inheritance of particular alleles of major histocompatibility complex class II genes increases the risk for various human autoimmune diseases; however, only a small percentage of individuals having an allele associated with susceptibility develop disease. The identification of allelic variants more precisely correlated with disease susceptibility would greatly facilitate clinical screening and diagnosis. Oligonucleotide-primed gene amplification in vitro was used to determine the nucleotide sequence of a class II variant found almost exclusively in patients with the autoimmune skin disease pemphigus vulgaris. In addition to clinical implications, the disease-restricted distribution of this variant should provide insight into the molecular mechanisms underlying associations between diseases and HLA-class II genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sinha, A A -- Brautbar, C -- Szafer, F -- Friedmann, A -- Tzfoni, E -- Todd, J A -- Steinman, L -- McDevitt, H O -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1026-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2894075" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Autoimmune Diseases/*genetics/immunology ; Base Sequence ; DNA/genetics ; Gene Amplification ; Genetic Variation ; HLA-D Antigens/*genetics ; HLA-DQ Antigens/*genetics/immunology ; HLA-DR Antigens/immunology ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Pemphigus/*genetics/immunology ; Polymorphism, Restriction Fragment Length
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  • 7
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    Cloning of a lymphoid-specific cDNA encoding a protein binding the regulatory octamer DNA motif (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-29
    Description: An octamer DNA sequence plays a critical role in directing transcription of immunoglobulin genes in B lymphocytes. A new technique of direct binding of radioactive DNA was used to screen a complementary DNA expression library from the BJAB cell line in lambda gt11 phage to derive molecular cDNA clones representing a putative B lymphocyte-specific octamer binding protein. The plaques were screened with DNA containing four copies of the octamer sequence and positive phage recombinants were identified. The fusion protein produced on inducing a lysogen of one phage bound to a monomeric octamer probe. The cDNA insert from this phage hybridized to messenger RNA found in B lymphocytes, but not in most other cells. Thus, this cDNA derives from a gene (oct-2) that specifies an octamer binding protein expressed preferentially in B lymphocytes, proving that, for at least one gene, a cell-specific transcription factor exists and its amount is controlled through messenger RNA availability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Staudt, L M -- Clerc, R G -- Singh, H -- LeBowitz, J H -- Sharp, P A -- Baltimore, D -- P01-CA42063/CA/NCI NIH HHS/ -- P30-CAL4051/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):577-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399892" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA/genetics ; DNA-Binding Proteins/*physiology ; Gene Expression Regulation ; *Genes ; Humans ; Lymphocytes/*physiology ; *Regulatory Sequences, Nucleic Acid ; Transcription Factors/*physiology
    Print ISSN: 0036-8075
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  • 8
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    Cloning of a membrane protein that induces a slow voltage-gated potassium current (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: A rat kidney messenger RNA that induces a slowly activating, voltage-dependent potassium current on its expression in Xenopus oocytes was identified by combining molecular cloning with an electrophysiological assay. The cloned complementary DNA encodes a novel membrane protein that consists of 130 amino acids with a single putative transmembrane domain. This protein differs from the known ion channel proteins but is involved in the induction of selective permeation of potassium ions by membrane depolarization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takumi, T -- Ohkubo, H -- Nakanishi, S -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Immunology, Kyoto University Faculty of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Electric Conductivity ; Membrane Potentials ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Potassium Channels/*physiology ; Rats ; Xenopus laevis
    Print ISSN: 0036-8075
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  • 9
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    Structural rearrangement of the retinoblastoma gene in human breast carcinoma (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: Structural changes of the human retinoblastoma gene have been demonstrated previously in retinoblastoma and some clinically related tumors including osteosarcoma. Structural aberrations of the retinoblastoma locus (RB1) were observed in 25% of breast tumor cell lines studied and 7% of the primary tumors. These changes include homozygous internal deletions and total deletion of RB1; a duplication of an exon was observed in one of the cell lines. In all cases, structural changes either resulted in the absence or truncation of the RB1 transcript. No obvious defect in RB1 was detected by DNA blot analysis in primary tumors or cell lines from Wilms' tumor, cervical carcinoma, or hepatoma. These results further support the concept that the human RB1 gene has pleiotropic effects on specific types of cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉T'Ang, A -- Varley, J M -- Chakraborty, S -- Murphree, A L -- Fung, Y K -- CA44754/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):263-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology/Oncology, Childrens Hospital of Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175651" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*genetics ; Chromosome Aberrations ; Chromosomes, Human, Pair 13 ; DNA/genetics ; DNA Probes ; Exons ; Eye Neoplasms/*genetics ; Female ; *Gene Rearrangement ; Homozygote ; Humans ; Lymphatic Metastasis ; Menopause ; Mutation ; Nucleic Acid Hybridization ; Retinoblastoma/*genetics ; Risk Factors ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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  • 10
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    In situ transcription: specific synthesis of complementary DNA in fixed tissue sections (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: A technique, in situ transcription, is described, in which reverse transcription of mRNAs is achieved within fixed tissue sections. An oligonucleotide complementary to proopiomelanocortin (POMC) mRNA was used as a primer for the specific synthesis of radiolabeled POMC cDNA in fixed sections of rat pituitary, thus permitting the rapid anatomical localization of POMC mRNA by autoradiography. Intermediate lobe signal intensities were sensitive to dopaminergic drugs, demonstrating that the method can be used for studies of mRNA regulation. The transcripts may also be eluted from tissue sections for a variety of uses, including the identification and cloning of autoradiographically localized cDNAs from small amounts of tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tecott, L H -- Barchas, J D -- Eberwine, J H -- DA-05010/DA/NIDA NIH HHS/ -- MH-23861/MH/NIMH NIH HHS/ -- MH09099/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nancy Pritzker Laboratory of Behavioral Neurochemistry, Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2454508" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/*biosynthesis ; Deoxycytidine/metabolism ; Electrophoresis, Polyacrylamide Gel ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Oligonucleotides/genetics ; Pituitary Gland/*metabolism ; Pro-Opiomelanocortin/*genetics ; RNA, Messenger/*metabolism ; RNA-Directed DNA Polymerase/metabolism ; Rats ; *Transcription, Genetic
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  • 11
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    Reshaping human antibodies: grafting an antilysozyme activity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-25
    Description: The production of therapeutic human monoclonal antibodies by hybridoma technology has proved difficult, and this has prompted the "humanizing" of mouse monoclonal antibodies by recombinant DNA techniques. It was shown previously that the binding site for a small hapten could be grafted from the heavy-chain variable domain of a mouse antibody to that of a human myeloma protein by transplanting the hypervariable loops. It is now shown that a large binding site for a protein antigen (lysozyme) can also be transplanted from mouse to human heavy chain. The success of such constructions may be facilitated by an induced-fit mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verhoeyen, M -- Milstein, C -- Winter, G -- New York, N.Y. -- Science. 1988 Mar 25;239(4847):1534-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Cambridge, England.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2451287" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal/genetics/immunology ; Base Sequence ; Binding Sites, Antibody ; Binding, Competitive ; Cloning, Molecular ; DNA, Recombinant ; Epitopes/immunology ; Humans ; Immunoglobulin G/genetics/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Molecular Sequence Data ; Muramidase/*immunology ; Plasmids ; Recombinant Proteins ; Transfection
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  • 12
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    Tandem array of human visual pigment genes at Xq28 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Unequal crossing-over within a head-to-tail tandem array of the homologous red and green visual pigment genes has been proposed to explain the observed variation in green-pigment gene number among individuals and the prevalence of red-green fusion genes among color-blind subjects. This model was tested by probing the structure of the red and green pigment loci with long-range physical mapping techniques. The loci were found to constitute a gene array with an approximately 39-kilobase repeat length. The position of the red pigment gene at the 5' edge of the array explains its lack of variation in copy number. Restriction maps of the array in four individuals who differ in gene number are consistent with a head-to-tail configuration of the genes. These results provide physical evidence in support of the model and help to explain the high incidence of color blindness in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vollrath, D -- Nathans, J -- Davis, R W -- GM21891/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1669-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2837827" target="_blank"〉PubMed〈/a〉
    Keywords: Color Vision Defects/*genetics ; Crossing Over, Genetic ; DNA/genetics ; DNA Restriction Enzymes ; Electrophoresis, Agar Gel ; Exons ; Female ; Genetic Variation ; Humans ; Male ; Nucleic Acid Hybridization ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retinal Pigments/*genetics ; *X Chromosome
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  • 13
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    Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-29
    Description: Zeins, the storage proteins of maize, are totally lacking in the essential amino acids lysine and tryptophan. Lysine codons and lysine- and tryptophan-encoding oligonucleotides were introduced at several positions into a 19-kilodalton zein complementary DNA by oligonucleotide-mediated mutagenesis. A 450-base pair open reading frame from a simian virus 40 (SV40) coat protein was also engineered into the zein coding region. Messenger RNAs for the modified zeins were synthesized in vitro with an SP6 RNA polymerase system and injected into Xenopus laevis oocytes. The modifications did not affect the translation, signal peptide cleavage, or stability of the zeins. The ability of the modified zeins to assemble into structures similar to maize protein bodies was assayed by two criteria: assembly into membrane-bound vesicles resistant to exogenously added protease, and ability to self-aggregate into dense structures. All of the modified zeins were membrane-bound; only the one containing a 17-kilodalton SV40 protein fragment was unable to aggregate. These findings suggest that it may be possible to create high-lysine corn by genetic engineering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, J C -- Galili, G -- Kawata, E E -- Cuellar, R E -- Shotwell, M A -- Larkins, B A -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):662-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2834822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/metabolism ; DNA/genetics ; DNA, Recombinant ; Female ; Genetic Engineering ; *Lysine/genetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Oocytes/*metabolism ; Peptide Hydrolases/metabolism ; RNA, Messenger/genetics ; Simian virus 40/genetics ; Xenopus laevis ; Zea mays ; Zein/genetics/*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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  • 14
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    Translocation and rearrangement of myeloperoxidase gene in acute promyelocytic leukemia (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-06
    Description: Acute promyelocytic leukemia (subtype M3) is characterized by malignant promyelocytes exhibiting an abundance of abnormally large or aberrant primary granules. Myeloperoxidase (MPO) activity of these azurophilic granules, as assessed by cytochemical staining, is unusually intense. In addition, M3 is universally associated with a chromosomal translocation, t(15;17)(q22;q11.2). In this report, the MPO gene was localized to human chromosome 17 (q12-q21), the region of the breakpoint on chromosome 17 in the t(15;17), by somatic cell hybrid analysis and in situ chromosomal hybridization. By means of MPO complementary DNA clones for in situ hybridization and Southern blot analysis, the effect of this specific translocation on the MPO gene was examined. In all cases of M3 examined, MPO is translocated to chromosome 15. Genomic blot analyses indicate rearrangement of MPO in leukemia cells of two of four cases examined. These findings suggest that MPO may be pivotal in the pathogenesis of acute promyelocytic leukemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weil, S C -- Rosner, G L -- Reid, M S -- Chisholm, R L -- Lemons, R S -- Swanson, M S -- Carrino, J J -- Diaz, M O -- Le Beau, M M -- 1R01 CA44475/CA/NCI NIH HHS/ -- CA09273/CA/NCI NIH HHS/ -- CA16910/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 May 6;240(4853):790-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Northwestern University Medical Center, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2896388" target="_blank"〉PubMed〈/a〉
    Keywords: Bone Marrow/analysis ; Chromosome Mapping ; Chromosomes, Human, Pair 15 ; Chromosomes, Human, Pair 17 ; DNA/genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; Humans ; Leukemia, Myeloid, Acute/*enzymology/genetics ; Nucleic Acid Hybridization ; Peroxidase/*genetics ; Plasmids ; Polymorphism, Restriction Fragment Length ; *Translocation, Genetic
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  • 15
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    Human ribosomal RNA genes: orientation of the tandem array and conservation of the 5' end (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-01
    Description: The multiple copies of the human ribosomal RNA genes (rDNA) are arranged as tandem repeat clusters that map to the middle of the short arms of chromosomes 13, 14, 15, 21, and 22. Concerted evolution of the gene family is thought to be mediated by interchromosomal recombination between rDNA repeat units, but such events would also result in conservation of the sequences distal to the rDNA on these five pairs of chromosomes. To test this possibility, a DNA fragment spanning the junction between rDNA and distal flanking sequence has been cloned and characterized. Restriction maps, sequence data, and gene mapping studies demonstrate that (i) the rRNA genes are transcribed in a telomere-to-centromere direction, (ii) the 5' end of the cluster and the adjacent non-rDNA sequences are conserved on the five pairs of chromosomes, and (iii) the 5' end of the cluster is positioned about 3.7 kb upstream from the transcription initiation site of the first repeat unit. The data support a model of concerted evolution by interchromosomal recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worton, R G -- Sutherland, J -- Sylvester, J E -- Willard, H F -- Bodrug, S -- Dube, I -- Duff, C -- Kean, V -- Ray, P N -- Schmickel, R D -- HD-13506/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 1;239(4835):64-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics Department, Hospital for Sick Children, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3336775" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Chromosomes, Human, Pair 13 ; Chromosomes, Human, Pair 14 ; Chromosomes, Human, Pair 15 ; Chromosomes, Human, Pair 21 ; Chromosomes, Human, Pair 22 ; Cloning, Molecular ; DNA, Ribosomal/*genetics ; Genes ; Humans ; RNA, Ribosomal/*genetics ; Sequence Homology, Nucleic Acid ; Transcription, 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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  • 16
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    Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-22
    Description: The parasitic protozoon Trypanosoma brucei contains a highly organized membrane skeleton, consisting of a dense array of parallel, singlet microtubules that are laterally interconnected and that are also in tight contact with the overlying cell membrane. A high molecular weight, heat-stable protein from this membrane skeleton was isolated that is localized along the microtubules. Protease digestion experiments and sequencing of a cloned gene segment showed that most of the protein is built up by more than 50 nearly identical tandem repeats with a periodicity of 38 amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, A -- Hemphill, A -- Wyler, T -- Seebeck, T -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur allgemeine Mikrobiologie, Universitat Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3393912" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Compartmentation ; Cell Membrane/ultrastructure ; Cloning, Molecular ; Microscopy, Electron ; Microtubule-Associated Proteins/*analysis/genetics ; Microtubules/ultrastructure ; Molecular Sequence Data ; Molecular Weight ; Repetitive Sequences, Nucleic Acid ; Trypanosoma brucei brucei/*analysis/genetics/ultrastructure
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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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    Duchenne muscular dystrophy gene expression in normal and diseased human muscle (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-18
    Description: A probe for the 5' end of the Duchenne muscular dystrophy (DMD) gene was used to study expression of the gene in normal human muscle, myogenic cell cultures, and muscle from patients with DMD. Expression was found in RNA from normal fetal muscle, adult cardiac and skeletal muscle, and cultured muscle after myoblast fusion. In DMD muscle, expression of this portion of the gene was also revealed by in situ RNA hybridization, particularly in regenerating muscle fibers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, M O -- Sylvester, J E -- Heiman-Patterson, T -- Shi, Y J -- Fieles, W -- Stedman, H -- Burghes, A -- Ray, P -- Worton, R -- Fischbeck, K H -- GM32592/GM/NIGMS NIH HHS/ -- NS08075/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 18;239(4846):1418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurology Department, Hospital of the University of Pennsylvania, Philadelphia, 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2450401" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; DNA/genetics ; DNA, Recombinant ; *Gene Expression Regulation ; Humans ; Muscles/embryology/*metabolism ; Muscular Dystrophies/*genetics ; Myocardium/metabolism ; Nucleic Acid Hybridization ; RNA/metabolism ; RNA, Messenger/metabolism ; Regeneration ; Transcription, Genetic
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  • 18
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    Protection of cattle against rinderpest with vaccinia virus recombinants expressing the HA or F gene (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: Rinderpest is a highly contagious ruminant viral disease manifested by a rapid course and greater than 90% mortality. Infectious vaccinia virus recombinants were constructed that express either the hemagglutinin or the fusion gene of rinderpest virus. All cattle vaccinated with either recombinant or with the combined recombinants produced neutralizing antibodies against rinderpest virus and were protected against the disease when challenged with more than 1000 times the lethal dose of the virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yilma, T -- Hsu, D -- Jones, L -- Owens, S -- Grubman, M -- Mebus, C -- Yamanaka, M -- Dale, B -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1058-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterinary Microbiology and Immunology, University of California, Davis 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194758" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cloning, Molecular ; Hemagglutinins, Viral/genetics/*immunology ; Immunologic Memory ; Rinderpest/*prevention & control ; Vaccination ; *Vaccines ; *Vaccines, Synthetic ; Vaccinia virus/genetics ; Viral Fusion Proteins/genetics/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Insulin-resistant diabetes due to a point mutation that prevents insulin proreceptor processing (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-06
    Description: A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser. Epstein-Barr virus-transformed lymphocytes from this patient synthesize an insulin receptor precursor that is normally glycosylated and inserted into the plasma membrane but is not cleaved to mature alpha and beta subunits. Insulin binding to these cells is severely reduced but can be increased about fivefold by gentle treatment with trypsin, accompanied by the appearance of normal alpha subunits. These results indicate that proteolysis of the proreceptor is necessary for its normal full insulin-binding sensitivity and signal-transducing activity and that a cellular protease that is more stringent in its specificity than trypsin is required to process the receptor precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshimasa, Y -- Seino, S -- Whittaker, J -- Kakehi, T -- Kosaki, A -- Kuzuya, H -- Imura, H -- Bell, G I -- Steiner, D F -- AM 13914/AM/NIADDK NIH HHS/ -- AM 20595/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1988 May 6;240(4853):784-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283938" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; DNA/genetics ; Diabetes Mellitus/*genetics/metabolism ; Female ; Glycosylation ; Humans ; Insulin/metabolism ; Insulin Resistance/*genetics ; Lymphocytes/metabolism ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Protein Precursors/*genetics/metabolism ; RNA, Messenger/metabolism ; Receptor, Insulin/*genetics/metabolism ; Trypsin/metabolism
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  • 20
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    Novel regulators of bone formation: molecular clones and activities (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-16
    Description: Protein extracts derived from bone can initiate the process that begins with cartilage formation and ends in de novo bone formation. The critical components of this extract, termed bone morphogenetic protein (BMP), that direct cartilage and bone formation as well as the constitutive elements supplied by the animal during this process have long remained unclear. Amino acid sequence has been derived from a highly purified preparation of BMP from bovine bone. Now, human complementary DNA clones corresponding to three polypeptides present in this BMP preparation have been isolated, and expression of the recombinant human proteins have been obtained. Each of the three (BMP-1, BMP-2A, and BMP-3) appears to be independently capable of inducing the formation of cartilage in vivo. Two of the encoded proteins (BMP-2A and BMP-3) are new members of the TGF-beta supergene family, while the third, BMP-1, appears to be a novel regulatory molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wozney, J M -- Rosen, V -- Celeste, A J -- Mitsock, L M -- Whitters, M J -- Kriz, R W -- Hewick, R M -- Wang, E A -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1528-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tissue Growth and Repair Program, Genetics Institute, Inc., Cambridge, MA 02140.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201241" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone Morphogenetic Proteins ; Cartilage/cytology/drug effects ; Cell Line ; DNA/genetics ; Growth Substances/*genetics ; Humans ; Molecular Sequence Data ; *Osteogenesis ; Proteins/*genetics/pharmacology ; Recombinant Proteins/pharmacology ; Sequence Homology, Nucleic Acid ; Transforming Growth Factors/genetics
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  • 21
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    Low plasma cholesterol levels caused by a short deletion in the apolipoprotein B gene (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-29
    Description: Familial hypobetalipoproteinemia is a syndrome in which the plasma levels of apolipoprotein B (apo-B) and cholesterol are abnormally low. A truncated species of apo-B was identified in the plasma lipoproteins of members of a kindred with familial hypobetalipoproteinemia. DNA sequencing studies on genomic clones and enzymatically amplified genomic DNA samples revealed a four-base pair deletion in the apo-B gene. This short deletion, which results in a frameshift and a premature stop codon, accounts for the truncated apo-B species and explains the low apo-B and low cholesterol levels in this family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, S G -- Northey, S T -- McCarthy, B J -- HL-01672-03/HL/NHLBI NIH HHS/ -- HL-14197/HL/NHLBI NIH HHS/ -- HL-38781-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):591-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399894" target="_blank"〉PubMed〈/a〉
    Keywords: Apolipoproteins B/*genetics ; Cholesterol/*blood ; Chromosome Deletion ; Cloning, Molecular ; Heterozygote ; Humans ; Hypobetalipoproteinemias/*genetics ; Hypolipoproteinemias/*genetics ; Mutation ; Pedigree
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  • 22
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    Gene transfer is coming on target (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):191-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175649" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chimera ; DNA/genetics ; Drug Resistance/genetics ; *Genetic Therapy ; Globins/genetics ; Growth ; Hypoxanthine Phosphoribosyltransferase/genetics ; Mice ; *Transfection
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  • 23
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    Gene identity confirmed (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Jan 22;239(4838):351.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3336788" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; *Genes ; Humans ; Receptors, Antigen, T-Cell/*genetics
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  • 24
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    Orphan interferon finds a new home (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Jan 1;239(4835):25-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3276001" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Products/physiology ; Cloning, Molecular ; Cytokines ; Humans ; Interferon Type I/*physiology ; Viral Interference
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  • 25
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    MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-21
    Description: Expression of a complementary DNA (cDNA) encoding the mouse MyoD1 protein in a variety of fibroblast and adipoblast cell lines converts them to myogenic cells. Polyclonal antisera to fusion proteins containing the MyoD1 sequence show that MyoD1 is a phosphoprotein present in the nuclei of proliferating myoblasts and differentiated myotubes but not expressed in 10T1/2 fibroblasts or other nonmuscle cell types. Functional domains of the MyoD1 protein were analyzed by site-directed deletional mutagenesis of the MyoD1 cDNA. Deletion of a highly basic region (residues 102 to 135) interferes with both nuclear localization and induction of myogenesis. Deletion of a short region (residues 143 to 162) that is similar to a conserved region in the c-Myc family of proteins eliminates the ability of the MyoD1 protein to initiate myogenesis but does not alter nuclear localization. Deletions of regions spanning the remainder of MyoD1 did not affect nuclear localization and did not inhibit myogenesis. Furthermore, expression of only 68 amino acids of MyoD1, containing the basic and the Myc similarity domains, is sufficient to activate myogenesis in stably transfected 10T1/2 cells. Genetic analysis maps the MyoD1 gene to mouse chromosome 7 and human chromosome 11.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tapscott, S J -- Davis, R L -- Thayer, M J -- Cheng, P F -- Weintraub, H -- Lassar, A B -- New York, N.Y. -- Science. 1988 Oct 21;242(4877):405-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175662" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cells, Cultured ; Chromosome Mapping ; DNA/genetics ; Fibroblasts/cytology ; *Genes ; Humans ; Mice ; Muscles/cytology ; *MyoD Protein ; Nuclear Proteins/*genetics/physiology ; *Oncogenes ; Phosphoproteins/*genetics/physiology
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  • 26
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    Expression of a calcium-mobilizing parathyroid hormone-like peptide in lactating mammary tissue (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: A survey of rat tissues by RNA analysis, aimed at uncovering the physiological function of the parathyroid hormone-like peptide (PTH-LP) associated with hypercalcemia of malignancy, revealed the presence of a 1.5-kilobase messenger RNA encoding this peptide in lactating mammary glands. PTH-LP messenger RNA is expressed in mammary tissue only during lactation; it appears and disappears rapidly (2 to 4 hours) as a function of the sucking stimulus. The identity of this messenger RNA was confirmed by cloning the rat PTH-LP complementary DNA, which predicts a peptide with strong similarity to the human homolog. Moreover, extracts from lactating mammary tissue stimulated parathyroid hormone-dependent adenylate cyclase. These findings suggest that PTH-LP plays a physiological role in lactation, possibly as a hormone for the mobilization or transfer (or both) of calcium to the milk.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thiede, M A -- Rodan, G A -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bone Biology and Osteoporosis Research, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175653" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/*metabolism ; Cloning, Molecular ; DNA/genetics ; Female ; *Gene Expression Regulation ; Humans ; Lactation/*metabolism ; Mammary Glands, Animal/*metabolism ; Molecular Sequence Data ; Neoplasm Proteins/*genetics/physiology ; Parathyroid Hormone-Related Protein ; Pregnancy ; RNA, Messenger/genetics/*metabolism ; Rats ; Sequence Homology, Nucleic Acid ; Tissue Distribution
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  • 27
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    Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-08
    Description: Mammalian cell lines (BSC-40, NG108-15, and GH4C1) that cannot process the murine neuroendocrine peptide precursor prepro-opiomelanocortin (mPOMC) when its synthesis is directed by a vaccinia virus vector were coinfected with a second recombinant vaccinia virus carrying the yeast KEX2 gene, which encodes an endopeptidase that cleaves at pairs of basic amino acid residues. mPOMC was cleaved intracellularly to a set of product peptides normally found in vivo, including mature gamma-lipotropin and beta-endorphin1-31. In GH4C1 cells (a rat pituitary line), product peptides were incorporated into stored secretory granules. These results suggest that the inability of any particular cell line to process a prohormone precursor is due to the absence of a suitable endogenous processing enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, G -- Thorne, B A -- Thomas, L -- Allen, R G -- Hruby, D E -- Fuller, R -- Thorner, J -- AI20563/AI/NIAID NIH HHS/ -- DK37274/DK/NIDDK NIH HHS/ -- HD18438/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):226-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3291117" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cloning, Molecular ; DNA, Recombinant ; Endopeptidases/*metabolism ; In Vitro Techniques ; Pro-Opiomelanocortin/*metabolism ; Protein Precursors/*metabolism ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/enzymology
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    Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-29
    Description: A thermostable DNA polymerase was used in an in vitro DNA amplification procedure, the polymerase chain reaction. The enzyme, isolated from Thermus aquaticus, greatly simplifies the procedure and, by enabling the amplification reaction to be performed at higher temperatures, significantly improves the specificity, yield, sensitivity, and length of products that can be amplified. Single-copy genomic sequences were amplified by a factor of more than 10 million with very high specificity, and DNA segments up to 2000 base pairs were readily amplified. In addition, the method was used to amplify and detect a target DNA molecule present only once in a sample of 10(5) cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saiki, R K -- Gelfand, D H -- Stoffel, S -- Scharf, S J -- Higuchi, R -- Horn, G T -- Mullis, K B -- Erlich, H A -- New York, N.Y. -- Science. 1988 Jan 29;239(4839):487-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cetus Corporation, Department of Human Genetics, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2448875" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA/*genetics ; DNA, Recombinant ; DNA-Directed DNA Polymerase/*metabolism ; Electrophoresis, Agar Gel ; Globins/genetics ; *Hot Temperature ; Humans ; *Nucleic Acid Amplification Techniques ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; RNA/genetics ; Thermus/enzymology
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    cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-29
    Description: Interleukin-1 alpha and -1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis. A direct expression strategy was used to clone the receptor for IL-1 from mouse T cells. The product of the cloned complementary DNA binds both IL-1 alpha and IL-1 beta in a manner indistinguishable from that of the native T cell IL-1 receptor. The extracellular, IL-1 binding portion of the receptor is 319 amino acids in length and is composed of three immunoglobulin-like domains. The cytoplasmic portion of the receptor is 217 amino acids long.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J E -- March, C J -- Cosman, D -- Widmer, M B -- MacDonald, H R -- McMahan, C J -- Grubin, C E -- Wignall, J M -- Jackson, J L -- Call, S M -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):585-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2969618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Genes, Immunoglobulin ; Interleukin-1/*physiology ; Mice ; Molecular Sequence Data ; *Multigene Family ; Receptors, Immunologic/*genetics ; Receptors, Interleukin-1
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    Conversion of a PI-anchored protein to an integral membrane protein by a single amino acid mutation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-05
    Description: Qa-2, a cell-surface glycoprotein anchored by phosphatidylinositol (PI), is structurally related to the class I transplantation antigens H-2 K, D, and L, which are integral membrane glycoproteins. The predicted transmembrane segment of Qa-2 differs from those of H-2 K, D, and L by the presence of an aspartate in place of a valine at position 295. A single base change that replaced this aspartate with valine resulted in cell-surface Qa-2 molecules that were insensitive to hydrolysis by a PI-specific phospholipase C and more resistant to papain cleavage, properties shared by H-2D. Cells expressing Asp----Val mutant Qa-2 proteins were still able to attach a PI anchor to endogenous proteins such as Thy-1 and J11D. It therefore appears that this single amino acid change converts Qa-2 from a PI-linked form into an integral membrane protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waneck, G L -- Stein, M E -- Flavell, R A -- AI24562/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):697-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biogen Research Corporation, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399901" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antigens, Surface/genetics ; *Aspartic Acid ; Cell Line ; DNA/genetics ; H-2 Antigens ; *Histocompatibility Antigens/genetics ; *Histocompatibility Antigens Class I ; Membrane Proteins/genetics/*metabolism ; Mutation ; Papain/metabolism ; Phosphatidylinositols/*metabolism ; Thymoma ; Thymus Neoplasms ; Transfection ; Tumor Cells, Cultured ; Type C Phospholipases/metabolism ; *Valine
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    Many transcription factors interact synergistically with steroid receptors (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-09
    Description: Progesterone (PRE) or glucocorticoid receptor (GRE) DNA binding sites are often found clustered with binding sites for other transcription factors. Individual protein binding sites were tested without the influence of adjacent factors by analyzing isolated combinations of several transcription factor binding sites with PREs or GREs. All show strong synergistic effects on steroid induction. The degree of synergism is inversely related to the strength of the GRE. Thus, a steroid responsive unit can be composed of several modules that, if positioned correctly, act synergistically.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schule, R -- Muller, M -- Kaltschmidt, C -- Renkawitz, R -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Biochemie, Martinsried, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201230" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Cloning, Molecular ; Genes ; HeLa Cells/metabolism ; Humans ; Molecular Sequence Data ; Plasmids ; Receptors, Glucocorticoid/*genetics/metabolism ; Receptors, Progesterone/*genetics/metabolism ; Transcription Factors/*genetics/metabolism ; Transfection
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    Diabetic mouse incorrectly typed (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prochazka, M -- Leiter, E H -- Serreze, D V -- Coleman, D L -- Jackson, R A -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):945.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jackson Laboratory, Bar Harbor, ME 04609.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crosses, Genetic ; DNA/genetics ; Diabetes Mellitus, Type 1/*genetics ; *Genes, Recessive ; Major Histocompatibility Complex ; Mice ; Recombination, Genetic
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    Wound macrophages express TGF-alpha and other growth factors in vivo: analysis by mRNA phenotyping (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-05
    Description: The presence of macrophages is required for the regeneration of many cell types during wound healing. Macrophages have been reported to express a wide range of mitogenic factors and cytokines, but none of these factors has been shown in vivo to sustain all the wound-healing processes. It has been suggested that transforming growth factor-alpha (TGF-alpha) may mediate angiogenesis, epidermal regrowth, and formation of granulation tissue in vivo. Macrophages isolated from a wound site, and not exposed to cell culture conditions, expressed messenger RNA transcripts for TGF-alpha, TGF-beta, platelet-derived growth factor A-chain, and insulin-like growth factor-1. The expression of these transcripts was determined by a novel method for RNA analysis in which low numbers of mouse macrophages were isolated from wound cylinders, their RNA was purified and reverse-transcribed, and the complementary DNA was amplified in a polymerase chain reaction primed with growth factor sequence-specific primers. This single-cell RNA phenotyping procedure is rapid and has the potential for quantification, and mRNA transcripts from a single cell or a few cells can be unambiguously demonstrated, with the simultaneous analysis of several mRNA species. Macrophages from wounds expressed TGF-alpha antigen, and wound fluids contained TGF-alpha. Elicited macrophages in culture also expressed TGF-alpha transcripts and polypeptide in a time-dependent manner after stimulation with modified low-density lipoproteins and lipopolysaccharide endotoxin, which are characteristic of the activators found in injured tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rappolee, D A -- Mark, D -- Banda, M J -- Werb, Z -- AR 32746/AR/NIAMS NIH HHS/ -- GM 27345/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):708-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Radiobiology and Environmental Health, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3041594" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; DNA/genetics ; Enzyme-Linked Immunosorbent Assay ; Epidermal Growth Factor/biosynthesis/genetics ; Fibroblast Growth Factors/biosynthesis/genetics ; Fibroblasts/metabolism ; Fluorescent Antibody Technique ; Growth Substances/*biosynthesis/genetics ; Insulin-Like Growth Factor I/biosynthesis/genetics ; Macrophages/*metabolism ; Male ; Mice ; Nucleic Acid Hybridization ; *Peptide Biosynthesis ; Peptides/genetics ; Platelet-Derived Growth Factor/biosynthesis/genetics ; Protein Biosynthesis ; RNA, Messenger/*biosynthesis ; Rabbits ; Transcription, Genetic ; Transforming Growth Factors ; *Wound Healing ; Wounds and Injuries/*pathology
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    Genomic amplification with transcript sequencing (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-29
    Description: A sequencing method called genomic amplification with transcript sequencing (GAWTS) is described that is based on amplification with the polymerase chain reaction (PCR). GAWTS bypasses cloning and increases the rate of sequence acquisition by at least fivefold. The method involves the attachment of a phage promoter onto at least one of the PCR primers. The segments amplified by PCR are transcribed to further increase the signal and to provide an abundance of single-stranded template for reverse transcriptase-mediated dideoxy sequencing. An end-labeled reverse transcriptase primer complementary to the desired sequence generates the additional specificity required to generate unambiguous sequence data. GAWTS can be performed on as little as a nanogram of genomic DNA. The rate of GAWTS can be increased by coamplification and cotranscription of multiple regions as illustrated by two regions of the factor IX gene. Since GAWTS lends itself well to automation, further increases in the rate of sequence acquisition can be expected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stoflet, E S -- Koeberl, D D -- Sarkar, G -- Sommer, S S -- New York, N.Y. -- Science. 1988 Jan 29;239(4839):491-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Mayo Clinic/Foundation, Rochester, MN 55905.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3340835" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; DNA-Directed DNA Polymerase/metabolism ; DNA-Directed RNA Polymerases ; Electrophoresis, Agar Gel ; Exons ; Factor IX/*genetics ; Hemophilia A/genetics ; Humans ; Molecular Sequence Data ; Mutation ; *Nucleic Acid Amplification Techniques ; T-Phages/enzymology ; *Transcription, Genetic
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    Molecular cloning of the zeta chain of the T cell antigen receptor (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-26
    Description: The T cell antigen receptor is a multi-subunit receptor complex present on the surface of all mature and many developing T cells. It consists of clonotypic heterodimers noncovalently linked to five invariant chains that are encoded by four genes and referred to as the CD3 complex. The CD3 gamma, delta, and epsilon chains have been molecularly characterized. In this report the molecular cloning of a complementary DNA encoding the zeta chain of the murine T cell antigen receptor is described. The predicted protein sequence of the zeta chain suggests a structure distinct from those of any of the previously described receptor subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weissman, A M -- Baniyash, M -- Hou, D -- Samelson, L E -- Burgess, W H -- Klausner, R D -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3278377" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Membrane/metabolism ; Chromatography, High Pressure Liquid ; *Cloning, Molecular ; Cyanogen Bromide ; DNA/genetics ; Electrophoresis, Polyacrylamide Gel ; Immunosorbent Techniques ; Macromolecular Substances ; *Membrane Proteins ; Mice ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; Peptide Fragments ; Protein Biosynthesis ; RNA, Messenger/genetics ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/analysis ; Transcription, Genetic ; Tumor Cells, Cultured
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    Gene encoding the beta subunit of S100 protein is on chromosome 21: implications for Down syndrome (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-11
    Description: S100 protein is a calcium-binding protein found predominantly in the vertebrate nervous system. Genomic and complementary DNA probes were used in conjunction with a panel of rodent-human somatic cell hybrids to assign the gene for the beta subunit of S100 protein to the distal half of the long arm of human chromosome 21. This gene was identified as a candidate sequence which, when expressed in the trisomic state, may underlie the neurologic disturbances in Down syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allore, R -- O'Hanlon, D -- Price, R -- Neilson, K -- Willard, H F -- Cox, D R -- Marks, A -- Dunn, R J -- 140-17001/PHS HHS/ -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2964086" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; Down Syndrome/*genetics ; Humans ; Macromolecular Substances ; Nucleic Acid Hybridization ; S100 Proteins/*genetics
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    Cone cell-specific genes expressed in retinoblastoma (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-01
    Description: Retinoblastoma, an intraocular tumor that occurs in children, has long been regarded, on the basis of morphological criteria, as a malignancy of the photoreceptor cell lineage. Here it is shown that when this tumor is grown in vitro, the cells express highly specialized photoreceptor cell genes. Transcripts for the transducin alpha subunit, TC alpha, which is specific to the cone cell, as well as transcripts for the red or green cone cell photopigment, were found in seven out of seven low-passage retinoblastoma cell lines. No marker genes specific to rod cell were expressed, suggesting that retinoblastoma has a cone cell lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bogenmann, E -- Lochrie, M A -- Simon, M I -- EY04950/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):76-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology Oncology, Childrens Hospital of Los Angeles, CA 90027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2451289" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/genetics ; Gene Expression Regulation ; Humans ; Membrane Proteins/*genetics ; Nucleic Acid Hybridization ; Photoreceptor Cells/*metabolism ; RNA/genetics ; Retinoblastoma/*genetics ; Transcription, Genetic ; Transducin ; Tumor Cells, Cultured
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    Single subunits of the GABAA receptor form ion channels with properties of the native receptor (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-28
    Description: The alpha and beta subunits of the gamma-aminobutyric acidA (GABAA) receptor were expressed individually in Xenopus oocytes by injection of RNA synthesized from their cloned DNAs. GABA-sensitive chloride channels were detected several days after injection with any one of three different alpha RNAs (alpha 1, alpha 2, and alpha 3) or with beta RNA. The channels induced by each of the alpha-subunit RNAs were indistinguishable, they had multiple conductance levels (10, 19, 28, and 42 picosiemens), and their activity was potentiated by pentobarbital and inhibited by picrotoxin. The beta channels usually expressed poorly but showed similar single channel conductance levels (10, 18, 27, and 40 picosiemens), potentiation by pentobarbital and inhibition by picrotoxin. The finding that both alpha and beta subunits, examined separately, form GABA-sensitive ion channels with permeation properties and regulatory sites characteristic of the native receptor suggests that the amino acid sequences that confer these properties are within the homologous domains shared by the subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blair, L A -- Levitan, E S -- Marshall, J -- Dionne, V E -- Barnard, E A -- NS20962/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 28;242(4878):577-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Molecular Neurobiology Unit, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845583" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chloride Channels ; Chlorides/*physiology ; Cloning, Molecular ; Dose-Response Relationship, Drug ; Electric Conductivity ; Macromolecular Substances ; Membrane Proteins/*physiology ; Picrotoxin/pharmacology ; RNA, Messenger/administration & dosage ; Receptors, GABA-A/*physiology ; Structure-Activity Relationship ; Xenopus laevis ; gamma-Aminobutyric Acid/pharmacology
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    Repair of the secretion defect in the Z form of alpha 1-antitrypsin by addition of a second mutation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-23
    Description: Homozygous inheritance of the Z-type mutant form of the alpha 1-antitrypsin (alpha 1AT) gene results in the most common form of alpha 1AT deficiency, a human hereditary disease associated with a high risk for the development of emphysema and an increased incidence of neonatal hepatitis. The alpha 1AT-synthesizing cells of individuals with the Z gene have normal alpha 1AT messenger RNA levels, but alpha 1AT secretion is markedly reduced secondary to accumulation of newly synthesized alpha 1AT in the rough endoplasmic reticulum. Crystallographic analysis of alpha 1AT predicts that in normal alpha 1AT, a negatively charged Glu342 is adjacent to positively charged Lys290. Thus the Glu342----Lys342 Z mutation caused the loss of a normal salt bridge, resulting in the intracellular aggregation of the Z molecule. The prediction was made that a second mutation in the alpha 1AT genet that changed the positively charged Lys290 to a negatively charged Glu290 would correct the secretion defect. When the second mutation was added to the Z-type complementary DNA, the resulting gene directed the synthesis and secretion of amounts of alpha 1AT similar to that directed by the normal alpha 1AT complementary DNA in an in vitro eukaryotic expression system. This suggests the possibility that a human hereditary disease can be corrected by inserting an additional mutation in the same gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brantly, M -- Courtney, M -- Crystal, R G -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1700-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pulmonary Branch, National Heart, Lung, and Blood Institute, Bethesda, MD.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2904702" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Codon ; DNA/genetics ; Electrochemistry ; Endoplasmic Reticulum/metabolism ; Glutamates ; Glutamic Acid ; Humans ; Lysine ; *Mutation ; Protein Conformation ; RNA, Messenger/metabolism ; Structure-Activity Relationship ; Transfection ; alpha 1-Antitrypsin/*genetics/secretion ; alpha 1-Antitrypsin Deficiency
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    Molecular cloning of human and rat complementary DNA encoding androgen receptors (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: Complementary DNAs (cDNAs) encoding androgen receptors were obtained from human testis and rat ventral prostate cDNA libraries. The amino acid sequence deduced from the nucleotide sequences of the cDNAs indicated the presence of a cysteine-rich DNA-binding domain that is highly conserved in all steroid receptors. The human cDNA was transcribed and the RNA product was translated in cell-free systems to yield a 76-kilodalton protein. The protein was immunoprecipitable by human autoimmune antibodies to the androgen receptor. The protein bound androgens specifically and with high affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, C S -- Kokontis, J -- Liao, S T -- DK-09461/DK/NIDDK NIH HHS/ -- DK-37694/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):324-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353726" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; *Cloning, Molecular ; DNA/genetics ; *Genes ; Humans ; Male ; Molecular Sequence Data ; Molecular Weight ; Rats ; Receptors, Androgen/*genetics/metabolism ; Sequence Homology, Nucleic Acid ; Species Specificity ; Testis/metabolism
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    Identification of germline and somatic mutations affecting the retinoblastoma gene (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-30
    Description: Retinoblastoma (RB) is a malignant tumor of developing retina that arises when abnormalities resulting in loss of function affect both alleles of the gene at the retinoblastoma locus (RB1) on chromosome 13q. The majority of RB tumors do not show gross alterations in a 4.7-kb fragment (4.7R), which is a candidate RB1 gene. To search for more subtle mutations, the ribonuclease protection method was used to analyze 4.7R messenger RNA from RB tumors. Five of 11 RB tumors, which exhibit normal 4.7R DNA and normal-sized RNA transcripts, showed abnormal ribonuclease cleavage patterns. Three of the five mutations affected the same region of the messenger RNA, consistent with an effect on splicing involving an as yet unidentified 5' exon. The high frequency of mutations in 4.7R supports the identification of 4.7R as the RB1 gene. However, the unusual nature of some of the abnormalities of 4.7 R alleles indicates that the accepted sequence of genetic events involved in the genesis of RB may require reevaluation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunn, J M -- Phillips, R A -- Becker, A J -- Gallie, B L -- New York, N.Y. -- Science. 1988 Sep 30;241(4874):1797-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hospital for Sick Children, Research Institute, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175621" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; DNA, Neoplasm/genetics ; Humans ; Mutation ; Retinoblastoma/*genetics
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    Virus-specific splicing inhibitor in extracts from cells infected with HIV-1 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-16
    Description: Human immunodeficiency virus type 1 (HIV-1), in contrast with most other retroviruses, encodes trans-regulatory proteins for virus gene expression. It is shown in this study, by means of an in vitro splicing system, that nuclear extracts obtained from cells infected with HIV-1 contain a factor (or factors) that specifically inhibits splicing of a synthetic SP6/HIV pre-messenger RNA (pre-mRNA)-containing donor and acceptor splice sites in the coding region for the envelope protein. It is also shown that the SP6/HIV pre-mRNA is not capable of assembly in a ribonucleoprotein complex, spliceosome, in extracts from infected cells. These findings raise the possibility that specific inhibition of pre-mRNA splicing in the envelope protein coding region by HIV-1 trans-regulatory factors might be one control mechanism for efficient production of structural viral proteins and virion assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gutman, D -- Goldenberg, C J -- AI-24479/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1492-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Miami School of Medicine, FL 33101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047873" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/physiology ; Cloning, Molecular ; DNA Mutational Analysis ; Gene Expression Regulation ; HIV/*genetics ; HeLa Cells ; Humans ; RNA Processing, Post-Transcriptional ; *RNA Splicing ; RNA, Viral/*genetics ; Ribonucleoproteins/physiology
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    Hormone-sensitive lipase: sequence, expression, and chromosomal localization to 19 cent-q13.3 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-16
    Description: Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin. The 757-amino acid sequence predicted from a cloned rat adipocyte complementary DNA showed no homology with any other known lipase or protein. The activity-controlling phosphorylation site was localized to Ser563 in a markedly hydrophilic domain, and a lipid-binding consensus site was tentatively identified. One or several messenger RNA species (3.3, 3.5, or 3.9 kilobases) were expressed in adipose and steroidogenic tissues and heart and skeletal muscle. The human hormone-sensitive lipase gene mapped to chromosome 19 cent-q13.3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holm, C -- Kirchgessner, T G -- Svenson, K L -- Fredrikson, G -- Nilsson, S -- Miller, C G -- Shively, J E -- Heinzmann, C -- Sparkes, R S -- Mohandas, T -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1503-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical and Physiological Chemistry, University of Lund, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3420405" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 19 ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Rats ; Sterol Esterase/*genetics
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  • 44
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    A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-26
    Description: A 50-nucleotide untranslated region is shown to be present within the coding sequence of Escherichia coli bacteriophage T4 gene 60, which encodes one of the subunits for its type II DNA topoisomerase. This interruption is part of the transcribed messenger RNA and appears not to be removed before translation. Thus, the usual colinearity between messenger RNA and the encoded protein sequence apparently does not exist in this case. The interruption is bracketed by a direct repeat of five base pairs. A mechanism is proposed in which folding of the untranslated region brings together codons separated by the interruption so that the elongating ribosome may skip the 50 nucleotides during translation. The alternative possibility, that the protein is efficiently translated from a very minor and undetectable form of processed messenger RNA, seems unlikely, but has not been completely ruled out.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, W M -- Ao, S Z -- Casjens, S -- Orlandi, R -- Zeikus, R -- Weiss, R -- Winge, D -- Fang, M -- GM 21960/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1005-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular, Viral and Molecular Biology, University of Utah Medical Center, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon ; DNA/genetics ; DNA Topoisomerases, Type I/*genetics ; DNA, Recombinant ; *Genes, Viral ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmids ; Protein Biosynthesis ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; T-Phages/enzymology/*genetics ; Transcription, Genetic
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  • 45
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    Molecular characterization of a functional cDNA encoding the serotonin 1c receptor (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-29
    Description: Neurons that release serotonin as a neurotransmitter project to most regions of the central and peripheral nervous system and mediate diverse neural functions. The physiological effects of serotonin are initiated by the activation of multiple, distinct receptor subtypes. Cloning in RNA expression vectors was combined with a sensitive electrophysiological assay in Xenopus oocytes in order to isolate a functional cDNA clone encoding the 5HTlc serotonin receptor. Injection of RNA transcribed in vitro from this clone into Xenopus oocytes elicits serotonin sensitivity. Mouse fibroblasts transformed with this clone bind serotonin agonists and antagonists and exhibit an increase in intracellular Ca2+ concentrations in response to serotonin. The sequence of the 5HTlc receptor reveals that it belongs to the family of G protein-coupled receptors, which are thought to traverse the cytoplasmic membrane seven times. Moreover, in situ hybridization and RNA blot analysis indicate that the 5HTlc receptor is expressed in neurons in many regions of the central nervous system and suggest that this subclass of receptor may mediate many of the central actions of serotonin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julius, D -- MacDermott, A B -- Axel, R -- Jessell, T M -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):558-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399891" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Fibroblasts/physiology ; Gene Expression Regulation ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Oocytes/physiology ; Phosphoproteins/physiology ; Rats ; Receptors, Serotonin/*genetics ; Serotonin/*physiology ; Xenopus laevis
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  • 46
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    A chemoattractant receptor controls development in Dictyostelium discoideum (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-16
    Description: During the early stages of its developmental program, Dictyostelium discoideum expresses cell surface cyclic adenosine monophosphate (cyclic AMP) receptors. It has been suggested that these receptors coordinate the aggregation of individual cells into a multicellular organism and regulate the expression of a large number of developmentally regulated genes. The complementary DNA (cDNA) for the cyclic AMP receptor has now been cloned from lambda gt-11 libraries by screening with specific antiserum. The 2-kilobase messenger RNA (mRNA) that encodes the receptor is undetectable in growing cells, rises to a maximum at 3 to 4 hours of development, and then declines. In vitro transcribed complementary RNA, when hybridized to cellular mRNA, specifically arrests in vitro translation of the receptor polypeptide. When the cDNA is expressed in Dictyostelium cells, the undifferentiated cells specifically bind cyclic AMP. Cell lines transformed with a vector that expresses complementary mRNA (antisense) do not express the cyclic AMP receptor protein. These cells fail to enter the aggregation stage of development during starvation, whereas control and wild-type cells aggregate and complete the developmental program within 24 hours. The phenotype of the antisense transformants suggests that the cyclic AMP receptor is essential for development. The deduced amino acid sequence of the receptor reveals a high percentage of hydrophobic residues grouped in seven domains, similar to the rhodopsins and other receptors believed to interact with G proteins. It shares amino acid sequence identity and is immunologically cross-reactive with bovine rhodopsin. A model is proposed in which the cyclic AMP receptor crosses the bilayer seven times with a serine-rich cytoplasmic carboxyl terminus, the proposed site of ligand-induced receptor phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, P S -- Sun, T J -- Saxe, C L 3rd -- Kimmel, A R -- Johnson, R L -- Devreotes, P N -- GM 34933/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1467-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Dictyostelium/*growth & development/physiology ; Membrane Proteins/physiology ; Molecular Sequence Data ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; Solubility
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  • 47
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    Fertilization events induced by neurotransmitters after injection of mRNA in Xenopus eggs (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-22
    Description: Fertilization initiates in the egg a dramatic increase in intracellular calcium that opens ion channels and causes exocytosis. To explore the possibility that these events might involve a receptor-mediated pathway, receptors for serotonin or acetylcholine (M1 muscarinic) were expressed in the Xenopus egg; serotonin or acetylcholine then could initiate a series of responses similar to those normally initiated by sperm. Thus, there may be an endogenous receptor in the egg membrane that is activated by sperm, and the serotonin or M1 muscarinic receptor may replace the sperm receptor in this pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kline, D -- Simoncini, L -- Mandel, G -- Maue, R A -- Kado, R T -- Jaffe, L A -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Connecticut Health Center, Farmington 06032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3134693" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cytoplasmic Granules/physiology ; Endocytosis ; Exocytosis ; Female ; *Fertilization ; GTP-Binding Proteins/physiology ; Genetic Engineering ; Inositol Phosphates/physiology ; Male ; Membrane Potentials ; Receptors, Muscarinic/*physiology ; Receptors, Serotonin/*physiology ; Sperm-Ovum Interactions ; Xenopus laevis
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    The primary structure and heterogeneity of tau protein from mouse brain (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-15
    Description: Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer's disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive alpha-helical or beta-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, G -- Cowan, N -- Kirschner, M -- GM32099/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):285-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3122323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Brain Chemistry ; Codon ; DNA/genetics ; DNA, Recombinant ; Mice ; Microtubule-Associated Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins/genetics ; Protein Conformation ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; tau Proteins
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    Evidence that the M2 membrane-spanning region lines the ion channel pore of the nicotinic receptor (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-16
    Description: Site-directed mutagenesis and expression in Xenopus oocytes were used to study acetylcholine receptors in which serine residues (i) were replaced by alanines (alpha, delta subunits) or (ii) replaced a phenylalanine (beta subunit) at a postulated polar site within the M2 transmembrane helix. As the number of serines decreased, there were decreases in the residence time and consequently the equilibrium binding affinity of QX-222, a quaternary ammonium anesthetic derivative thought to bind within the open channel. Receptors with three serine-to-alanine mutations also displayed a selective decrease in outward single-channel currents. Both the direction of this rectification and the voltage dependence of QX-222 blockade suggest that the residues mutated are within the aqueous pore of the receptor and near its cytoplasmic (inner) surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leonard, R J -- Labarca, C G -- Charnet, P -- Davidson, N -- Lester, H A -- NS-11756/NS/NINDS NIH HHS/ -- NS-8083/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2462281" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*physiology ; Cloning, Molecular ; Electric Conductivity ; Female ; Ion Channels/*physiology ; Kinetics ; Membrane Potentials ; Mutation ; Oocytes/physiology ; RNA, Messenger/genetics ; Receptors, Nicotinic/genetics/*physiology ; Transcription, Genetic ; Xenopus
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    Induction of gene amplification by arsenic (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-01
    Description: Arsenic is a well-established carcinogen in humans, but there is little evidence for its carcinogenicity in animals and it is inactive as an initiator or tumor promoter in two-stage models of carcinogenicity in mice. Two arsenic salts (sodium arsenite and sodium arsenate) induced a high frequency of methotrexate-resistant 3T6 cells, which were shown to have amplified copies of the dihydrofolate reductase gene. The ability of arsenic to induce gene amplification may relate to its carcinogenic effects in humans since amplification of oncogenes is observed in many human tumors. The inability of arsenic to induce gene mutations may relate to the negative results of arsenic in long-term animal studies and suggests that these experiments may not detect some environmental agents that act late in the carcinogenic process in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, T C -- Tanaka, N -- Lamb, P W -- Gilmer, T M -- Barrett, J C -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):79-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388020" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arsenates/*pharmacology ; Arsenic/*pharmacology ; *Arsenites ; Cell Line ; DNA/genetics ; Drug Resistance ; Gene Amplification/*drug effects ; Humans ; Methotrexate ; Mice ; Neoplasms, Experimental/chemically induced/genetics ; Nucleic Acid Hybridization ; Oncogenes ; *Sodium Compounds ; Tetrahydrofolate Dehydrogenase/*genetics
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    Heterologous expression of excitability proteins: route to more specific drugs? (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-26
    Description: Many clinically important drugs act on the intrinsic membrane proteins (ion channels, receptors, and ion pumps) that control cell excitability. A major goal of pharmacology has been to develop drugs that are more specific for a particular subtype of excitability molecule. DNA cloning has revealed that many excitability proteins are encoded by multigene families and that the diversity of previously recognized pharmacological subtypes is matched, and probably surpassed, by the diversity of messenger RNAs that encode excitability molecules. In general, the diverse subtypes retain their properties when the excitability proteins are expressed in foreign cells such as oocytes and mammalian cell lines. Such heterologous expression may therefore become a tool for testing drugs against specific subtypes. In a systematic research program to exploit this possibility, major considerations include alternative processing of messenger RNA for excitability proteins, coupling to second-messenger systems, and expression of enough protein to provide material for structural studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lester, H A -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1057-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2457947" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Physiological Phenomena ; Cloning, Molecular ; Drug-Related Side Effects and Adverse Reactions ; GTP-Binding Proteins/genetics/physiology ; Gene Expression Regulation ; *Genetic Variation ; Humans ; Ion Channels/drug effects/physiology ; Membrane Proteins/*genetics/physiology ; *Pharmacology ; Receptors, Cell Surface/drug effects/genetics/physiology
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  • 52
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    A previously undetected MHC gene with an unusual periodic structure (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-08
    Description: The major histocompatibility complex is a chromosomal segment embodying several gene clusters among which those with immune functions are the best characterized. This region is suspected to host other as yet undetected genes whose characterization may shed light on the population genetics and evolution of the whole gene complex and thus on its unexplained character of marker locus for a number of diseases of nonimmune or unknown pathogenesis. A novel gene was identified that is transcribed in all tissues tested and is located in mouse and man between the CA and Bf genes of the H-2 and HLA complexes, respectively. From the nucleotide sequence, derived from liver complementary DNA clones, it is predicted that this novel single-copy gene encodes a 42-kilodalton polypeptide that bears no recognizable relation to the protein families known so far, but it displays striking hallmarks of natural selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levi-Strauss, M -- Carroll, M C -- Steinmetz, M -- Meo, T -- New York, N.Y. -- Science. 1988 Apr 8;240(4849):201-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U 276, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353717" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Genes ; Liver/physiology ; *Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; Periodicity ; Selection, Genetic
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    Family relationships are a biological conundrum (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):671.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; DNA/genetics ; Genes ; Globins/genetics ; Hominidae/*classification/genetics ; Humans
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    Molecular clocks turn a quarter century (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1988 Feb 5;239(4840):561-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3340843" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA/genetics ; Humans ; *Models, Genetic ; Time Factors
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    Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-11-11
    Description: The microtubule-associated protein MAP2 is a prominent large-sized component of purified brain microtubules that, like the 36- to 38-kilodalton tau proteins, bears antigenic determinants found in association with the neurofibrillary tangles of Alzheimer's disease. The complete sequence of mouse brain MAP2 was determined from a series of overlapping cloned complementary DNAs. The sequence of the carboxyl-terminal 185 amino acids is very similar (67 percent) to a corresponding region of tau protein, and includes a series of three imperfect repeats, each 18 amino acids long and separated by 13 or 14 amino acids. A subcloned fragment spanning the first two of the 18-amino acid repeats was expressed as a polypeptide by translation in vitro. This polypeptide copurified with microtubules through two successive cycles of polymerization and depolymerization, whereas a control polypeptide derived from the amino-terminal region of MAP2 completely failed to copurify. These data imply that the carboxyl-terminal domain containing the 18-amino acid repeats constitutes the microtubule binding site in MAP2. The occurrence of these repeats in tau protein suggests that these may be a general feature of microtubule binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewis, S A -- Wang, D H -- Cowan, N J -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3142041" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; DNA/genetics ; Mice ; Microtubule-Associated Proteins/genetics/*metabolism ; Microtubules/*metabolism ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins ; Protein Biosynthesis ; Repetitive Sequences, Nucleic Acid ; Sequence Homology, Nucleic Acid ; Tubulin/metabolism ; tau Proteins
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    Type-restricted neutralization of molecular clones of human immunodeficiency virus (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-15
    Description: In a study of the immunologic significance of the genetic diversity present within single isolates of human immunodeficiency virus type 1 (HIV-1), the neutralization of viruses derived from molecular clones of the HIV-1 strain HTLV-IIIB by an extensive panel of sera was compared. Sera from HIV-1-infected patients and from goats immunized with polyacrylamide gel-purified HIV-1 envelope glycoprotein (gp120), native gp120, or gp120-derived recombinant peptides, showed marked heterogeneity in neutralizing activity against these closely related viruses. The change of a single amino acid residue in gp120 may account for such "clonal restriction" of neutralizing activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Looney, D J -- Fisher, A G -- Putney, S D -- Rusche, J R -- Redfield, R R -- Burke, D S -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Viral Diseases, Walter Reed Army Institute of Research, Washington, DC 20307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388046" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Viral/*immunology ; Binding, Competitive ; Cloning, Molecular ; HIV/genetics/*immunology ; HIV Seropositivity/immunology ; Humans ; Molecular Sequence Data ; Neutralization Tests ; Oligopeptides/chemical synthesis/immunology
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    A single receptor binds both insulin-like growth factor II and mannose-6-phosphate (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-04
    Description: Amino acid sequences deduced from rat complementary DNA clones encoding the insulin-like growth factor II (IGF-II) receptor closely resemble those of the bovine cation-independent mannose-6-phosphate receptor (Man-6-P receptorCI), suggesting they are identical structures. It is also shown that IGF-II receptors are adsorbed by immobilized pentamannosyl-6-phosphate and are specifically eluted with Man-6-P. Furthermore, Man-6-P specifically increases by about two times the apparent affinity of the purified rat placental receptor for 125I-labeled IGF-II. These results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P-containing proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacDonald, R G -- Pfeffer, S R -- Coussens, L -- Tepper, M A -- Brocklebank, C M -- Mole, J E -- Anderson, J K -- Chen, E -- Czech, M P -- Ullrich, A -- CA 39240/CA/NCI NIH HHS/ -- DK 30648/DK/NIDDK NIH HHS/ -- DK 34063/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Massachusetts Medical Center, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2964083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/genetics/*metabolism ; Cell Membrane/analysis/metabolism ; Chromatography, Affinity ; DNA/genetics ; Female ; Hexosephosphates/*metabolism ; Insulin-Like Growth Factor II/*metabolism ; Mannosephosphates/*metabolism ; Molecular Sequence Data ; Placenta/analysis ; Pregnancy ; Rats ; Receptor, IGF Type 2 ; Receptor, Insulin/genetics/*metabolism ; Receptors, Somatomedin ; Sequence Homology, Nucleic Acid ; Somatomedins/*metabolism
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    Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-05-13
    Description: The biosynthetic rates for both the transferrin receptor (TfR) and ferritin are regulated by iron. An iron-responsive element (IRE) in the 5' untranslated portion of the ferritin messenger RNA (mRNA) mediates iron-dependent control of its translation. In this report the 3' untranslated region of the mRNA for the human TfR was shown to be necessary and sufficient for iron-dependent control of mRNA levels. Deletion studies identified a 678-nucleotide fragment of the TfR complementary DNA that is critical for this iron regulation. Five potential stem-loops that resemble the ferritin IRE are contained within the region critical for TfR regulation. Each of two of the five TfR elements was independently inserted into the 5' untranslated region of an indicator gene transcript. In this location they conferred iron regulation of translation. Thus, an mRNA element has been implicated in the mediation of distinct regulatory phenomena dependent on the context of the element within the transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casey, J L -- Hentze, M W -- Koeller, D M -- Caughman, S W -- Rouault, T A -- Klausner, R D -- Harford, J B -- New York, N.Y. -- Science. 1988 May 13;240(4854):924-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2452485" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics ; DNA, Recombinant ; Ferritins/biosynthesis/*genetics ; Growth Hormone/genetics ; Humans ; Iron/*pharmacology ; Mice ; Plasmids ; Protein Biosynthesis/*drug effects ; RNA/*genetics ; RNA, Messenger/*genetics ; Receptors, Transferrin/biosynthesis/*genetics ; *Regulatory Sequences, Nucleic Acid ; Transcription, Genetic ; Transfection ; Transformation, Genetic
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    Expression of the murine Duchenne muscular dystrophy gene in muscle and brain (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-18
    Description: Complementary DNA clones were isolated that represent the 5' terminal 2.5 kilobases of the murine Duchenne muscular dystrophy (Dmd) messenger RNA (mRNA). Mouse Dmd mRNA was detectable in skeletal and cardiac muscle and at a level approximately 90 percent lower in brain. Dmd mRNA is also present, but at much lower than normal levels, in both the muscle and brain of three different strains of dystrophic mdx mice. The identification of Dmd mRNA in brain raises the possibility of a relation between human Duchenne muscular dystrophy (DMD) gene expression and the mental retardation found in some DMD males. These results also provide evidence that the mdx mutations are allelic variants of mouse Dmd gene mutations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chamberlain, J S -- Pearlman, J A -- Muzny, D M -- Gibbs, R A -- Ranier, J E -- Caskey, C T -- Reeves, A A -- New York, N.Y. -- Science. 1988 Mar 18;239(4846):1416-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Genetics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3347839" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; DNA/genetics ; DNA, Recombinant ; *Gene Expression Regulation ; Intellectual Disability/genetics ; Mice ; Mice, Inbred ICR ; Mice, Mutant Strains ; Muscles/*metabolism ; Muscular Dystrophy, Animal/*genetics ; Mutation ; Nucleic Acid Hybridization ; RNA, Messenger/metabolism ; Ribonuclease, Pancreatic/metabolism
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    Genome rearrangement and nitrogen fixation in Anabaena blocked by inactivation of xisA gene (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-09
    Description: Two genome rearrangements involving 11- and 55-kilobase DNA elements occur during the terminal differentiation of an Anabaena photosynthetic vegetative cell into a nitrogen-fixing heterocyst. The xisA gene, located on the nifD 11-kilobase DNA element, was inactivated by recombination between the chromosome and a copy of the xisA gene that was mutated by inserting an antibiotic gene cassette. Site-directed inactivation of the Anabaena xisA gene blocked rearrangement of the 11-kilobase element and nitrogen fixation, but did not affect rearrangement of the 55-kilobase element, heterocyst differentiation, or heterocyst pattern formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golden, J W -- Wiest, D R -- GM36890/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1421-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Texas A&M University, College Station 77843.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144039" target="_blank"〉PubMed〈/a〉
    Keywords: Cyanobacteria/*genetics/growth & development ; DNA/genetics ; *Gene Rearrangement ; *Genes ; *Genes, Bacterial ; Immunoblotting ; Nitrogen Fixation/*genetics ; Phenotype ; Restriction Mapping
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    Yeast HAP2 and HAP3: transcriptional activators in a heteromeric complex (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-15
    Description: Transcription of the yeast C upsilon C1 gene (iso-1-cytochrome c) is regulated in part by the upstream activation site UAS2. Activity of UAS2 requires both the HAP2 and HAP3 activators, which bind to UAS2 in an interdependent manner. To distinguish whether these factors bound to UAS2 cooperatively or formed a complex in the absence of DNA, HAP2 and HAP3 were tagged by gene fusion to LexA and beta-galactosidase, respectively, and purified through four chromatographic steps. The copurification of LexA-HAP2, HAP3 beta-galactosidase, and UAS2 binding activity shows that HAP2 and HAP3 associate in the absence of DNA to form a multisubunit activation complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, S -- Guarente, L -- 5RO1 GM3044-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):317-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832951" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics ; Cloning, Molecular ; Cytochrome c Group/*genetics ; *Cytochromes c ; Galactosidases/*genetics ; *Genes ; *Genes, Fungal ; *Genes, Regulator ; *Saccharomyces cerevisiae Proteins ; *Serine Endopeptidases ; *Transcription, Genetic ; beta-Galactosidase/*genetics
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    The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-09
    Description: Mutants in the gene CDC34 of the yeast Saccharomyces cerevisiae are defective in the transition from G1 to the S phase of the cell cycle. This gene was cloned and shown to encode a 295-residue protein that has substantial sequence similarity to the product of the yeast RAD6 gene. The RAD6 gene is required for a variety of cellular functions including DNA repair and was recently shown to encode a ubiquitin-conjugating enzyme. When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes. The cell cycle function of CDC34 is thus likely to be mediated by the ubiquitin-conjugating activity of its product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goebl, M G -- Yochem, J -- Jentsch, S -- McGrath, J P -- Varshavsky, A -- Byers, B -- GM18541/GM/NIGMS NIH HHS/ -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 9;241(4871):1331-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842867" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cell Cycle ; Chromosome Mapping ; Cloning, Molecular ; *Genes, Fungal ; Molecular Sequence Data ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/*genetics ; Ubiquitins/*metabolism
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    Chromosomal gene transfer in Spiroplasma citri (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-19
    Description: The study of resistance marker rearrangement in Spiroplasma citri mutants provides evidence of transfer of chromosomal information followed by recombination. This is the first report of such a transfer in vivo in the mollicutes--that is, in the smallest self-replicating organisms. The double-resistant phenotypes obtained are stable even without selection pressure. The mechanism of gene transfer is insensitive to deoxyribonuclease, requires contact, and possibly, areas of fusion of the cell membranes; it shares properties with the transfer by protoplast fusion in Gram-positive bacteria. The extensive degenerative evolution of mollicutes has retained, in S. citri, bacterial functions of chromosomal transfer and recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barroso, G -- Labarere, J -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):959-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire, Universite de Bordeaux II-INRA, C.R.A. de Bordeaux, Pont-de-la-Maye, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3261453" target="_blank"〉PubMed〈/a〉
    Keywords: Arsenates/pharmacology ; *Chromosomes, Bacterial ; Cloning, Molecular ; Culture Media ; Drug Resistance, Microbial/genetics ; Herbicides/pharmacology ; Mutation ; Oxides/pharmacology ; Phenotype ; *Recombination, Genetic ; Spiroplasma/drug effects/*genetics ; Time Factors ; *Transfection ; Vanadates/pharmacology
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    Biologic features of HIV-1 that correlate with virulence in the host (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-01
    Description: Individuals infected with the human immunodeficiency virus type 1 (HIV-1) may be asymptomatic or have AIDS-related complex or the acquired immuno deficiency syndrome (AIDS). Little is known about the factors that influence progression of infection to AIDS. In this study of isolates of HIV-1 obtained at intervals during the infection of four individuals, the development of disease was found to be correlated with the emergence of HIV-1 variants that were more cytopathic in vitro as the disease progressed and that replicated more efficiently in a wide variety of different human cells. The biologic properties of HIV-1 in vitro thus appear to reflect its virulence in the host. Further studies of such sequentially isolated viruses may lead to the identification of viral genes that govern pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng-Mayer, C -- Seto, D -- Tateno, M -- Levy, J A -- P01 AI-24286/AI/NIAID NIH HHS/ -- R01 AI-24499/AI/NIAID NIH HHS/ -- R01 AI-25284/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):80-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, School of Medicine, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832945" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Complex/etiology/microbiology ; Acquired Immunodeficiency Syndrome/etiology/microbiology ; Cytopathogenic Effect, Viral ; DNA/genetics ; Genetic Variation ; HIV/genetics/*pathogenicity/physiology ; HIV Envelope Protein gp120 ; Humans ; Neutralization Tests ; Retroviridae Proteins/genetics
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    Expression of a distinctive BCR-ABL oncogene in Ph1-positive acute lymphocytic leukemia (ALL) (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-12
    Description: The Philadelphia chromosome (Ph1) is a translocation between chromosomes 9 and 22 that is found in chronic myelogenous leukemia (CML) and a subset of acute lymphocytic leukemia patients (ALL). In CML, this results in the expression of a chimeric 8.5-kilobase BCR-ABL transcript that encodes the P210BCR-ABL tyrosine kinase. The Ph1 chromosome in ALL expresses a distinct ABL-derived 7-kilobase messenger RNA that encodes the P185ALL-ABL protein. Since the expression of different oncogene products may play a role in the distinctive presentation of Ph1-positive ALL versus CML, it is necessary to understand the molecular basis for the expression of P185ALL-ABL. Both P210BCR-ABL and P185ALL-ABL are recognized by an antiserum directed to BCR determinants in the amino-terminal region of both proteins. Antisera to BCR determinants proximal to the BCR-ABL junction in CML immunoprecipitated P210BCR-ABL but not P185ALL-ABL. Nucleotide sequence analysis of complementary DNA clones made from RNA from the Ph1-positive ALL SUP-B15 cell line, and S1 nuclease protection analysis confirmed the presence of BCR-ABL chimeric transcripts in Ph1-positive ALL cells. In Ph1-positive ALL, ABL sequences were joined to BCR sequences approximately 1.5 kilobases 5' of the CML junction. P185ALL-ABL represents the product of a BCR-ABL fusion gene in Ph1-positive ALL that is distinct from the BCR-ABL fusion gene of CML.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, S S -- McLaughlin, J -- Timmons, M -- Pendergast, A M -- Ben-Neriah, Y -- Dow, L W -- Crist, W -- Rovera, G -- Smith, S D -- Witte, O N -- CA-20180/CA/NCI NIH HHS/ -- CA-21765/CA/NCI NIH HHS/ -- CA-34233/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 12;239(4841 Pt 1):775-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, UCLA 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3422516" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Humans ; Leukemia, Lymphoid/*genetics ; Molecular Sequence Data ; *Oncogenes ; *Philadelphia Chromosome ; RNA, Messenger/genetics ; *Transcription, Genetic
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    Insertional mutagenesis of the Drosophila genome with single P elements (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-04
    Description: A versatile genetic method for identifying and cloning Drosophila melanogaster genes affecting any recognizable phenotype is described. Strains are constructed in which the insertion of a single P transposable element has caused a new mutation, greatly simplifying the genetic and molecular analysis of the affected gene. Mutagenesis is initiated by crossing two strains, each of which contains a specially designed P element. One element (jumpstarter), encoding P element transposase, efficiently mobilizes the second nonautonomous transposon (mutator), whose structure facilitates selection and cloning of new insertion mutations. Random mutator transpositions are captured in individual stocks that no longer contain jumpstarter, where they remain stable. This method was used to construct 1300 single P element insertion stocks which were then screened for recessive mutations. A library of single-element insertion strains will allow the structure and function of Drosophila genes to be readily correlated, and should have many other applications in Drosophila molecular genetics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cooley, L -- Kelley, R -- Spradling, A -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1121-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830671" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes ; Cloning, Molecular ; DNA/genetics ; *DNA Transposable Elements ; DNA, Recombinant ; Drosophila melanogaster/*genetics ; *Mutation ; Transformation, Genetic
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    Evidence of estrogen receptors in normal human osteoblast-like cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-01
    Description: In seven strains of cultured normal human osteoblast-like cells, a mean of 1615 molecules of tritium-labeled 17 beta-estradiol per cell nucleus could be bound to specific nuclear sites. The nuclear binding of the labeled steroid was temperature-dependent, steroid-specific, saturable, and cell type-specific. These are characteristics of biologically active estrogen receptors. Pretreatment with 10 nanomolar estradiol in vitro increased the specific nuclear binding of progesterone in four of six cell strains, indicating an induction of functional progesterone receptors. RNA blot analysis demonstrated the presence of messenger RNA for the human estrogen receptor. The data suggest that estrogen acts directly on human bone cells through a classical estrogen receptor-mediated mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eriksen, E F -- Colvard, D S -- Berg, N J -- Graham, M L -- Mann, K G -- Spelsberg, T C -- Riggs, B L -- AG-04875/AG/NIA NIH HHS/ -- CA-90441/CA/NCI NIH HHS/ -- HD-9140/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):84-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrine Research Unit, Mayo Clinic, Rochester, MN 55905.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388021" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Cell Nucleus/metabolism ; Cells, Cultured ; DNA/genetics ; Dexamethasone/metabolism ; Diethylstilbestrol/metabolism ; Estradiol/metabolism/pharmacology ; Humans ; Nucleic Acid Hybridization ; Osteoblasts/drug effects/*metabolism ; Progesterone/metabolism ; Promegestone/metabolism ; RNA, Messenger/metabolism ; Receptors, Estrogen/drug effects/genetics/*metabolism ; Receptors, Progesterone/drug effects/metabolism ; Tritium
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    Isotypic exclusion of gamma delta T cell receptors in transgenic mice bearing a rearranged beta-chain gene (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-26
    Description: The rearrangement of T cell antigen receptor beta- and gamma-chain gene segments was studied in transgenic mice that bear a functional beta-chain gene. Virtually all CD3-positive T cells derived from transgenic mice express beta chains containing the transgene-encoded V beta 8.2 variable region on their surfaces and do not express endogenous beta-chain variable regions. Expression of endogenous V beta genes is inhibited at the level of somatic recombination during thymic ontogeny. Furthermore, rearrangements of the TCR gamma-chain genes are also markedly inhibited in these transgenic animals. Hence expression of the TCR beta transgene has led to allelic exclusion of alpha beta receptors and isotypic exclusion of gamma delta T cell receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fenton, R G -- Marrack, P -- Kappler, J W -- Kanagawa, O -- Seidman, J G -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1089-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2970670" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antibodies, Monoclonal ; Bacteriophage lambda/genetics ; Cloning, Molecular ; DNA, Recombinant ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Genes, Immunoglobulin ; Immunoassay ; Immunoglobulin Heavy Chains/genetics ; Liver/analysis ; Mice ; Mice, Transgenic ; Ovalbumin/immunology ; Receptors, Antigen, T-Cell/*genetics ; Recombination, Genetic ; T-Lymphocytes/metabolism ; Thymus Gland/analysis
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  • 69
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    Antiproliferative activity of a hybrid protein between interferon-gamma and tumor necrosis factor-beta (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-16
    Description: A hybrid protein between interferon-gamma and tumor necrosis factor-beta was made by ligating the respective genes and expressing the fused genes under the control of the trp promoter in Escherichia coli. The antiproliferative activity of the hybrid protein in vitro was greatly increased compared with either interferon-gamma or tumor necrosis factor-beta alone, and both antiviral activity and cytotoxic effect were retained in the hybrid protein. The hybrid protein may have potential clinical application.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, G S -- Gray, P W -- Shepard, H M -- Taylor, M W -- AI21898/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1501-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3138754" target="_blank"〉PubMed〈/a〉
    Keywords: *Antiviral Agents ; Cloning, Molecular ; *Growth Inhibitors ; Immunosorbent Techniques ; *Interferon-gamma ; Recombinant Fusion Proteins/pharmacology ; Structure-Activity Relationship ; *Tumor Necrosis Factor-alpha
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    Overexpression of low density lipoprotein (LDL) receptor eliminates LDL from plasma in transgenic mice (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-11
    Description: A complementary DNA encoding the human low density lipoprotein (LDL) receptor under control of the mouse metallothionein-I promoter was injected into fertilized mouse eggs, and a strain of mice expressing high levels of LDL receptors was established. After administration of cadmium, these mice cleared intravenously injected 125I-labeled LDL from blood eight to ten times more rapidly than did normal mice. The plasma concentrations of apoproteins B-100 and E, the two ligands for the LDL receptor, declined by more than 90 percent after cadmium treatment, but the concentration of another apoprotein, A-I, was unaffected. Therefore, overexpression of an endocytotic receptor can dramatically lower the ambient concentration of its ligand in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hofmann, S L -- Russell, D W -- Brown, M S -- Goldstein, J L -- Hammer, R E -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1277-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Female ; *Genes ; Humans ; Kinetics ; Lipoproteins, LDL/*blood ; Mice ; Mice, Transgenic ; Plasmids ; Receptors, LDL/*genetics/metabolism ; Reference Values ; Transcription, Genetic
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    A 115-kD polypeptide immunologically related to erythrocyte band 3 is present in Golgi membranes (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-02
    Description: Band 3 multigene family consists of several distinct but structurally related polypeptides which are probably involved in the transport of anions across the plasma membrane of both erythrocytes and nonerythroid cells. A novel member of this family of polypeptides that resides in the Golgi complex was identified with antibodies to Band 3. The Golgi antigen had a larger molecular size and was antigenically distinct from Band 3 in the amino-terminal domain. It was expressed most prominently in cells that secrete large amounts of sulfated proteins and proteoglycans. This polypeptide may participate in sulfate transport across Golgi membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellokumpu, S -- Neff, L -- Jamsa-Kellokumpu, S -- Kopito, R -- Baron, R -- DE-04724/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 2;242(4883):1308-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2461589" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anion Exchange Protein 1, Erythrocyte/*immunology ; Cloning, Molecular ; Golgi Apparatus/*ultrastructure ; Immunoenzyme Techniques ; Intracellular Membranes/*ultrastructure ; Ion Channels/*ultrastructure ; Molecular Weight ; Rats
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    Estrogen binding, receptor mRNA, and biologic response in osteoblast-like osteosarcoma cells (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-01
    Description: High specific activity estradiol labeled with iodine-125 was used to detect approximately 200 saturable, high-affinity (dissociation constant approximately equal to 1.0 nM) nuclear binding sites in rat (ROS 17/2.8) and human (HOS TE85) clonal osteoblast-like osteosarcoma cells. Of the steroids tested, only testosterone exhibited significant cross-reactivity with estrogen binding. RNA blot analysis with a complementary DNA probe to the human estrogen receptor revealed putative receptor transcripts of 6 to 6.2 kilobases in both rat and human osteosarcoma cells. Type I procollagen and transforming growth factor-beta messenger RNA levels were enhanced in cultured human osteoblast-like cells treated with 1 nM estradiol. Thus, estrogen can act directly on osteoblasts by a receptor-mediated mechanism and thereby modulate the extracellular matrix and other proteins involved in the maintenance of skeletal mineralization and remodeling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Komm, B S -- Terpening, C M -- Benz, D J -- Graeme, K A -- Gallegos, A -- Korc, M -- Greene, G L -- O'Malley, B W -- Haussler, M R -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):81-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Arizona College of Medicine, Tucson 85724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3164526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Cell Nucleus/metabolism ; DNA/genetics ; Estradiol/*metabolism/pharmacology ; Humans ; Iodine Radioisotopes ; Nucleic Acid Hybridization ; Osteoblasts/drug effects/*metabolism ; Osteosarcoma/*metabolism ; Peptides/genetics ; Procollagen/genetics ; RNA, Messenger/*metabolism ; Rats ; Receptors, Estrogen/genetics/*metabolism ; Transcription, Genetic ; Transforming Growth Factors ; Tumor Cells, Cultured
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    Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-09
    Description: A proteinase with high affinity for insulin has been proposed to play a role in the cellular processing of this hormone. A complementary DNA (cDNA) coding for this enzyme has been isolated and sequenced. The deduced amino acid sequence of the enzyme contained the sequences of 13 peptides derived from the isolated protein. The cDNA could be transcribed in vitro to yield a synthetic RNA that in cell-free translations produced a protein that coelectrophoresed with the native proteinase and could be immunoprecipitated with monoclonal antibodies to this enzyme. The deduced sequence of this proteinase did not contain the consensus sequences for any of the known classes of proteinases (that is, metallo, cysteine, aspartic, or serine), but it did show homology to an Escherichia coli proteinase (called protease III), which also cleaves insulin and is present in the periplasmic space. Thus, these two proteins may be members of a family of proteases that are involved in intercellular peptide signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Affholter, J A -- Fried, V A -- Roth, R A -- CA21765/CA/NCI NIH HHS/ -- DK01393/DK/NIDDK NIH HHS/ -- DK34926/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3059494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Endopeptidases/*genetics ; Escherichia coli/enzymology/*genetics ; Genes ; Humans ; Insulysin/*genetics ; *Metalloendopeptidases ; Molecular Sequence Data ; Peptide Hydrolases/*genetics ; Sequence Homology, Nucleic Acid
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    Heterogeneity of glycine receptors and their messenger RNAs in rat brain and spinal cord (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-14
    Description: Messenger RNAs isolated from adult or newborn rat spinal cord were fractionated in a sucrose gradient. The fractions were injected into Xenopus oocytes to determine their potencies for expression of glycine receptors (GlyRs), which were then examined electrophysiologically. The sedimentation profiles disclosed two classes of GlyR mRNAs, one heavy and the other light. The adult spinal cord was rich in heavy GlyR mRNA, whereas the light GlyR mRNA was more abundant in neonatal spinal cord and in adult cerebral cortex. Glycine receptors encoded by heavy and light mRNAs of adult spinal cord showed some electrophysiological differences. Thus there are two types of GlyRs encoded by mRNAs of different sizes, and the expression of these mRNAs is developmentally regulated. A tissue- and age-dependent distribution of heterogeneous GlyR mRNAs may imply diverse roles of the GlyRs in neuronal function in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akagi, H -- Miledi, R -- R01-NS23284/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):270-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychobiology, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845580" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Cell Membrane/physiology ; Centrifugation, Density Gradient ; Cerebral Cortex/*analysis ; DNA/genetics ; Electric Conductivity ; Glycine/pharmacology ; Nucleic Acid Hybridization ; Oocytes/drug effects/physiology ; RNA, Messenger/*genetics/isolation & purification ; Rats ; Receptors, Glycine ; Receptors, Neurotransmitter/*genetics/physiology ; Spinal Cord/*analysis ; Transcription, Genetic ; Xenopus laevis
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    A 13-kilodalton maize mitochondrial protein in E. coli confers sensitivity to Bipolaris maydis toxin (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-15
    Description: The Texas male-sterile cytoplasm (cms-T) of maize carries the cytoplasmically inherited trait of male sterility. Mitochondria isolated from cms-T maize are specifically sensitive to a toxin (BmT-toxin) produced by the fungal pathogen Bipolaris maydis, race T, and the carbamate insecticide methomyl. A mitochondrial gene unique to cms-T maize, which produces a 13-kilodalton polypeptide associated with cytoplasmic male sterility, was expressed in Escherichia coli. After addition of BmT-toxin or methomyl, inhibition of whole cell respiration and swelling of spheroplasts were observed in Escherichia coli cultures producing the novel mitochondrial protein; these effects are similar to those observed with isolated cms-T mitochondria. The amino-terminal region of the 13-kilodalton polypeptide appears to be essential for proper interaction with the BmT-toxin and methomyl. These results implicate the 13-kilodalton polypeptide in conferring toxin sensitivity to mitochondria of cms-T maize.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dewey, R E -- Siedow, J N -- Timothy, D H -- Levings, C S 3rd -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):293-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Crop Science, North Carolina State University, Raleigh 27695.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3276005" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*pharmacology ; Cloning, Molecular ; Codon ; Dicyclohexylcarbodiimide/pharmacology ; Escherichia coli/drug effects/*genetics/metabolism ; Methomyl/pharmacology ; Mitochondria/*analysis ; Molecular Weight ; Mycotoxins/*pharmacology ; Oxygen Consumption/drug effects ; Plant Proteins/*genetics/physiology ; Plants/analysis/drug effects/*genetics ; Plasmids ; Promoter Regions, Genetic ; Zea mays
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    Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits of a DHP-sensitive calcium channel (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-23
    Description: Complementary DNAs were isolated and used to deduce the primary structures of the alpha 1 and alpha 2 subunits of the dihydropyridine-sensitive, voltage-dependent calcium channel from rabbit skeletal muscle. The alpha 1 subunit, which contains putative binding sites for calcium antagonists, is a hydrophobic protein with a sequence that is consistent with multiple transmembrane domains and shows structural and sequence homology with other voltage-dependent ion channels. In contrast, the alpha 2 subunit is a hydrophilic protein without homology to other known protein sequences. Nucleic acid hybridization studies suggest that the alpha 1 and alpha 2 subunit mRNAs are expressed differentially in a tissue-specific manner and that there is a family of genes encoding additional calcium channel subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellis, S B -- Williams, M E -- Ways, N R -- Brenner, R -- Sharp, A H -- Leung, A T -- Campbell, K P -- McKenna, E -- Koch, W J -- Hui, A -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute Biotechnology/Industrial Associates, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2458626" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/*metabolism ; Calcium Channel Blockers/pharmacology ; Cloning, Molecular ; *Dna ; DNA Restriction Enzymes ; Dihydropyridines/pharmacology ; *Ion Channels/drug effects ; Molecular Sequence Data ; Organ Specificity ; *Peptide Mapping ; RNA, Messenger/biosynthesis ; Rabbits ; Sequence Homology, Nucleic Acid
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    The CD14 monocyte differentiation antigen maps to a region encoding growth factors and receptors (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-29
    Description: CD14 is a myelomonocytic differentiation antigen expressed by monocytes, macrophages, and activated granulocytes and is detectable with the monoclonal antibodies MO2, MY4, and LeuM3. Analyses of complementary DNA and genomic clones of CD14 show that it has a novel structure and that it maps to chromosome 5 within a region containing other genes encoding growth factors and receptors; it may therefore represent a new receptor important for myeloid differentiation. In addition, the CD14 gene is included in the "critical" region that is frequently deleted in certain myeloid leukemias.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goyert, S M -- Ferrero, E -- Rettig, W J -- Yenamandra, A K -- Obata, F -- Le Beau, M M -- R01-AI23859/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 29;239(4839):497-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Rheumatic Diseases, Hospital for Joint Diseases Orthopaedic Institute, New York, NY 10003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2448876" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens, CD14 ; Antigens, Differentiation/*genetics/immunology ; Cell Differentiation ; Chromosome Mapping ; Chromosomes, Human, Pair 5 ; DNA/genetics ; Electrophoresis, Polyacrylamide Gel ; Granulocytes/immunology ; Growth Substances/*genetics ; Humans ; Immunosorbent Techniques ; Leukemia/genetics ; Macrophages/immunology ; Mice ; Monocytes/*immunology ; Myelodysplastic Syndromes/genetics ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Receptors, Cell Surface/*genetics
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    Two mutant alleles of the insulin receptor gene in a patient with extreme insulin resistance (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-05-06
    Description: Insulin receptor complementary DNA has been cloned from an insulin-resistant patient with leprechaunism whose receptors exhibited multiple abnormalities in insulin binding. The patient is a compound heterozygote, having inherited two different mutant alleles of the insulin receptor gene. One allele contains a missense mutation encoding the substitution of glutamic acid for lysine at position 460 in the alpha subunit of the receptor. The second allele has a nonsense mutation causing premature chain termination after amino acid 671 in the alpha subunit, thereby deleting both the transmembrane and tyrosine kinase domains of the receptor. Interestingly, the father is heterozygous for this nonsense mutation and exhibits a moderate degree of insulin resistance. This raises the possibility that mutations in the insulin receptor gene may account for the insulin resistance in some patients with non-insulin-dependent diabetes mellitus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kadowaki, T -- Bevins, C L -- Cama, A -- Ojamaa, K -- Marcus-Samuels, B -- Kadowaki, H -- Beitz, L -- McKeon, C -- Taylor, S I -- New York, N.Y. -- Science. 1988 May 6;240(4853):787-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry and Molecular Pathophysiology Section, National Institute of Diabetes, Digestive, and Kidney Disease, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2834824" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cell Line ; Cell Membrane/metabolism ; Cell Transformation, Viral ; DNA/genetics ; Diabetes Mellitus, Type 2/*genetics ; Endocrine System Diseases/genetics ; Female ; Gene Amplification ; Growth Disorders/genetics ; Herpesvirus 4, Human ; Heterozygote ; Humans ; Hydrogen-Ion Concentration ; Insulin/blood ; Insulin Resistance/*genetics ; Lymphocytes/metabolism ; Monocytes/metabolism ; Mutation ; Receptor, Insulin/*genetics ; Syndrome ; Transfection
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    Distinct regions of Sp1 modulate DNA binding and transcriptional activation (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-16
    Description: Sp1 is a sequence-specific DNA binding protein that activates RNA polymerase II transcription from promoters that contain properly positioned GC boxes. A series of deletion mutants of Sp1 were expressed in Escherichia coli and used to identify separate regions of the protein that are important for three different biochemical activities. The sequence-specificity of DNA binding was conferred by Zn(II) fingers, whereas a different region of Sp1 appeared to regulate the affinity of DNA binding. The E. coli-synthesized Sp1 was able to stimulate initiation of RNA synthesis in vitro, and at least two distinct segments of the protein contributed to its transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kadonaga, J T -- Courey, A J -- Ladika, J -- Tjian, R -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1566-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3059495" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Deletion ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA-Binding Proteins/*genetics/metabolism ; *Gene Expression Regulation ; *Genes ; HeLa Cells/metabolism ; Humans ; Mutation ; Sp1 Transcription Factor ; Transcription Factors/*genetics/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 80
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    Conversion of normal behavior to shiverer by myelin basic protein antisense cDNA in transgenic mice (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-29
    Description: Myelin basic proteins (MBPs) are coded by the single gene necessary for myelin formation in the central nervous system of the mouse. An antisense MBP mini-gene was constructed and used to determine the function of antisense DNA in transgenic mice. Several transgenic offspring of a founder transgenic mouse, AS100, were converted from the normal to mutant shiverer phenotype. Antisense MBP messenger RNA was expressed in these mice, and the endogenous MBP messenger RNA, the MBP, and the myelination in the central nervous system were reduced.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Katsuki, M -- Sato, M -- Kimura, M -- Yokoyama, M -- Kobayashi, K -- Nomura, T -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):593-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of DNA Biology, School of Medicine, Tokai University, Isehara, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2456614" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brain/physiology ; DNA/genetics ; Gene Expression Regulation ; Mice ; Mice, Neurologic Mutants/*physiology ; Mice, Transgenic ; Molecular Sequence Data ; Myelin Basic Protein/genetics/*physiology ; Myelin Sheath/physiology ; Phenotype ; RNA/*genetics ; RNA, Antisense
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 81
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    The presence of fibroblast growth factor in the frog egg: its role as a natural mesoderm inducer (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: A complementary DNA clone corresponding to a 4.2-kilobase transcript that is present in the Xenopus oocyte and newly transcribed in the neurula stages of development has been isolated. This messenger RNA encodes a 155-amino acid protein that is 84% identical to the human basic fibroblast growth factor (bFGF). When expressed in Escherichia coli and purified, the Xenopus FGF induced mesoderm in animal cell blastomeres as measured by muscle actin expression. Immunoblots with an antibody to a Xenopus FGF peptide show that the oocyte and early embryo contain a store of the FGF polypeptide at high enough concentrations to induce mesoderm. The presence of FGF in the oocyte, together with the apparent lack of a secretory signal sequence in the protein, suggest that the regulation of mesoderm induction may involve novel mechanisms that occur after the translation of FGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimelman, D -- Abraham, J A -- Haaparanta, T -- Palisi, T M -- Kirschner, M W -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1053-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194757" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Blotting, Western ; Cloning, Molecular ; DNA/genetics ; DNA Probes ; Fibroblast Growth Factors/*physiology ; Gene Expression Regulation ; Mesoderm/*cytology ; Molecular Sequence Data ; Oocytes/physiology ; Xenopus laevis/*embryology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 82
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    Chimeric alpha 2-,beta 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-03
    Description: The alpha 2 and beta 2 adrenergic receptors, both of which are activated by epinephrine, but which can be differentiated by selective drugs, have opposite effects (inhibitory and stimulatory) on the adenylyl cyclase system. The two receptors are homologous with each other, rhodopsin, and other receptors coupled to guanine nucleotide regulatory proteins and they contain seven hydrophobic domains, which may represent transmembrane spanning segments. The function of specific structural domains of these receptors was determined after construction and expression of a series of chimeric alpha 2-,beta 2-adrenergic receptor genes. The specificity for coupling to the stimulatory guanine nucleotide regulatory protein lies within a region extending from the amino terminus of the fifth hydrophobic domain to the carboxyl terminus of the sixth. Major determinants of alpha 2- and beta 2-adrenergic receptor agonist and antagonist ligand binding specificity are contained within the seventh membrane spanning domain. Chimeric receptors should prove useful for elucidating the structural basis of receptor function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobilka, B K -- Kobilka, T S -- Daniel, K -- Regan, J W -- Caron, M G -- Lefkowitz, R J -- HL 16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1310-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2836950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Chimera ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Humans ; Molecular Sequence Data ; Pindolol/analogs & derivatives/metabolism ; Protein Conformation ; Receptors, Adrenergic, alpha/*genetics ; Receptors, Adrenergic, beta/*genetics ; Yohimbine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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