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  • Base Sequence  (172)
  • Cells, Cultured  (41)
  • American Association for the Advancement of Science (AAAS)  (204)
  • Annual Reviews
  • 1990-1994  (204)
  • 1980-1984
  • 1955-1959
  • 1930-1934
  • 1993  (204)
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  • American Association for the Advancement of Science (AAAS)  (204)
  • Annual Reviews
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  • 1990-1994  (204)
  • 1980-1984
  • 1955-1959
  • 1930-1934
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  • 1
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    Role of intracellular calcium in NI-35-evoked collapse of neuronal growth cones (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: A myelin-associated protein from the central nervous system, the neurite growth inhibitor NI-35, inhibits regeneration of lesioned neuronal fiber tracts in vivo and growth of neurites in vitro. Growth cones of cultured rat dorsal root ganglion neurons arrested their growth and collapsed when exposed to liposomes containing NI-35. Before morphological changes, the concentration of free intracellular calcium ([Ca2+]i) showed a rapid and large increase in growth cones exposed to liposomes containing NI-35. Neither an increase in [Ca2+]i nor collapse of growth cones was detected in the presence of antibodies to NI-35. Dantrolene, an inhibitor of calcium release from caffeine-sensitive intracellular calcium stores, protected growth cones from collapse evoked by NI-35. Depletion of these caffeine-sensitive intracellular calcium stores prevented the increase in [Ca2+]i evoked by NI-35. The NI-35-evoked cascade of intracellular messengers that mediates collapse of growth cones includes the crucial step of calcium release from intracellular stores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bandtlow, C E -- Schmidt, M F -- Hassinger, T D -- Schwab, M E -- Kater, S B -- NS24683/NS/NINDS NIH HHS/ -- NS28323/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):80-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brain Research Institute, University of Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418499" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caffeine/pharmacology ; Calcium/*metabolism ; Cells, Cultured ; Drug Carriers ; Fura-2 ; Ganglia, Spinal/*physiology ; Growth Inhibitors/*pharmacology ; Kinetics ; Liposomes ; Nerve Fibers/drug effects/*physiology/ultrastructure ; Neurons/drug effects/*physiology/ultrastructure ; Rats
    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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    Rate and mechanism of nonhomologous recombination during a single cycle of retroviral replication (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-08
    Description: Oncogenes discovered in retroviruses such as Rous sarcoma virus were generated by transduction of cellular proto-oncogenes into the viral genome. Several different kinds of junctions between the viral and proto-oncogene sequences have been found in different viruses. A system of retrovirus vectors and a protocol that mimicked this transduction during a single cycle of retrovirus replication was developed. The transduction involved the formation of a chimeric viral-cellular RNA, strand switching of the reverse transcription growing point from an infectious retrovirus to the chimeric RNA, and often a subsequent deletion during the rest of viral DNA synthesis. A short region of sequence identity was frequently used for the strand switching. The rate of this process was about 0.1 to 1 percent of the rate of homologous retroviral recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, J -- Temin, H M -- CA-07175/CA/NCI NIH HHS/ -- CA-22443/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):234-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉McArdle Laboratory for Cancer Research, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8421784" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Cinnamates ; *DNA Replication ; DNA, Viral/chemistry/genetics ; Drug Resistance/genetics ; Genes, Viral ; Genetic Vectors ; Hygromycin B/analogs & derivatives ; Kinetics ; Mice ; Molecular Sequence Data ; Moloney murine leukemia virus/genetics ; Neomycin ; Plasmids ; *Proto-Oncogenes ; RNA, Viral/analysis/genetics ; *Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroviridae/*genetics/physiology ; Transfection ; *Virus Replication
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  • 3
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    Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-22
    Description: Glycogen storage disease (GSD) type 1a is caused by the deficiency of D-glucose-6-phosphatase (G6Pase), the key enzyme in glucose homeostasis. Despite both a high incidence and morbidity, the molecular mechanisms underlying this deficiency have eluded characterization. In the present study, the molecular and biochemical characterization of the human G6Pase complementary DNA, its gene, and the expressed protein, which is indistinguishable from human microsomal G6Pase, are reported. Several mutations in the G6Pase gene of affected individuals that completely inactivate the enzyme have been identified. These results establish the molecular basis of this disease and open the way for future gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lei, K J -- Shelly, L L -- Pan, C J -- Sidbury, J B -- Chou, J Y -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genetics Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA, Complementary/genetics ; Exons ; Glucose-6-Phosphatase/*genetics/metabolism ; Glycogen Storage Disease Type I/enzymology/*genetics ; Glycosylation ; Humans ; Liver/enzymology ; Mice ; Molecular Sequence Data ; *Mutation ; Protein Conformation ; Transfection
    Print ISSN: 0036-8075
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  • 4
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    Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in inherited smooth muscle tumors (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-27
    Description: The gene encoding alpha 6(IV) collagen, COL4A6, was identified on the human X chromosome in a head-to-head arrangement and within 452 base pairs of the alpha 5(IV) collagen gene, COL4A5. In earlier studies, intragenic deletions of COL4A5 were detected in a subset of patients with Alport syndrome (AS), a hereditary defect of basement membranes. In some families, AS cosegregates with diffuse leiomyomatosis (DL), a benign smooth muscle tumor diathesis. Here it is shown that patients with AS-DL harbor deletions that disrupt both COL4A5 and COL4A6. Thus, type IV collagen may regulate smooth muscle differentiation and morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, J -- Mochizuki, T -- Smeets, H -- Antignac, C -- Laurila, P -- de Paepe, A -- Tryggvason, K -- Reeders, S T -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1167-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06536-0812.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356449" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Differentiation ; Collagen/chemistry/*genetics ; Exons ; Female ; Fetus/metabolism ; *Gene Deletion ; Genetic Linkage ; Humans ; Leiomyoma/*genetics ; Male ; Molecular Sequence Data ; Morphogenesis ; Muscle, Smooth/cytology ; Mutation ; Nephritis, Hereditary/*genetics ; RNA, Messenger/genetics/metabolism
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  • 5
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    Inhibition of Rev-mediated HIV-1 expression by an RNA binding protein encoded by the interferon-inducible 9-27 gene (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-26
    Description: Interferon inhibits expression of human immunodeficiency virus type-1 (HIV-1) through unknown mechanisms. A gene inducible by interferon-alpha (IFN-alpha) and interferon-gamma (IFN-gamma) was isolated by screening of a human complementary DNA library for proteins binding to the Rev-responsive element (RRE) of HIV-1. The product of this gene, RBP9-27, was shown to bind RNA in vitro and to inhibit HIV-1 expression after transfection into human cells. RBP9-27 primarily inhibited Rev-dependent posttranscriptional steps of viral gene expression. Thus, RBP9-27 is a cellular factor that antagonizes Rev function. These results suggest an interferon-induced antiviral mechanism operating through the induction of RNA binding proteins such as RBP9-27. Elucidation of RBP9-27 function may lead to a better understanding of the mechanism of interferon action during HIV-1 infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Constantoulakis, P -- Campbell, M -- Felber, B K -- Nasioulas, G -- Afonina, E -- Pavlakis, G N -- N0-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1314-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Retrovirus Section, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7680491" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; *Gene Expression Regulation, Viral ; Genes, env ; *Genes, rev ; HIV-1/*genetics ; Humans ; Interferons/pharmacology ; *Membrane Proteins ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; RNA-Binding Proteins/*genetics ; Regulatory Sequences, Nucleic Acid
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  • 6
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    Disappearance of the lymphoid system in Bcl-2 homozygous mutant chimeric mice (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-17
    Description: The bcl-2 proto-oncogene can prevent the death of many cell types. Mice were generated that were chimeric for the homozygous inactivation of bcl-2. Lymphocytes without Bcl-2 differentiated into phenotypically mature cells. However, in vitro, the mature T cells that lacked Bcl-2 had shorter life-spans and increased sensitivity to glucocorticoids and gamma-irradiation. In contrast, stimulation of CD3 inhibited the death of these cells. T and B cells with no Bcl-2 disappeared from the bone marrow, thymus, and periphery by 4 weeks of age. Thus, Bcl-2 was dispensable for lymphocyte maturation, but was required for a stable immune system after birth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakayama, K -- Negishi, I -- Kuida, K -- Shinkai, Y -- Louie, M C -- Fields, L E -- Lucas, P J -- Stewart, V -- Alt, F W -- AI 15322/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1584-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372353" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD3/immunology ; Apoptosis ; B-Lymphocytes/cytology/*immunology ; Base Sequence ; Bone Marrow/immunology ; Bone Marrow Cells ; Cell Line ; Chimera ; Homozygote ; Humans ; Lymphoid Tissue/cytology/immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins c-bcl-2 ; Proto-Oncogenes ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/cytology/*immunology
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  • 7
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    Induction of G alpha i2-specific antisense RNA in vivo inhibits neonatal growth (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: Guanosine triphosphate-binding regulatory proteins (G proteins) are key elements in transmembrane signaling and have been implicated as regulators of more complex biological processes such as differentiation and development. The G protein G alpha i2 is capable of mediating the inhibitory control of adenylylcyclase and regulates stem cell differentiation to primitive endoderm. Here an antisense RNA to G alpha i2 was expressed in a hybrid RNA construct whose expression was both tissue-specific and induced at birth. Transgenic mice in which the antisense construct was expressed displayed a lack of normal development in targeted organs that correlated with the absence of G alpha i2. The loss of G alpha i2 expression in adipose tissue of the transgenic mice was correlated with a rise in basal levels of adenosine 3',5'-monophosphate (cAMP) and the loss of receptor-mediated inhibition of adenylylcyclase. These data expand our understanding of G protein function in vivo and demonstrate the necessity for G alpha i2 in the development of liver and fat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moxham, C M -- Hod, Y -- Malbon, C C -- New York, N.Y. -- Science. 1993 May 14;260(5110):991-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, State University of New York (SUNY)/Stony Brook 11794-8651.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493537" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*growth & development/metabolism ; Animals ; Animals, Newborn/growth & development ; Base Sequence ; Body Weight ; GTP-Binding Proteins/biosynthesis/genetics/*physiology ; Growth/drug effects/*physiology ; Kidney/growth & development/metabolism ; Liver/*growth & development/metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Phosphoenolpyruvate Carboxykinase (GTP)/genetics ; RNA, Antisense/*genetics ; Transfection
    Print ISSN: 0036-8075
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  • 8
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    Shutdown of class switch recombination by deletion of a switch region control element (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-12
    Description: Upon activation, B lymphocytes can change the class of the antibody they express by immunoglobulin class switch recombination. Cytokines can direct this recombination to distinct classes by the specific activation of repetitive recombinogenic DNA sequences, the switch regions. Recombination to a particular switch region (s gamma 1) was abolished in mice that were altered to lack sequences that are 5' to the s gamma 1 region. This result directly implicates the functional importance of 5' switch region flanking sequences in the control of class switch recombination. Mutant mice exhibit a selective agammaglobulinemia and may be useful in the assessment of the biological importance of immunoglobulin G1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jung, S -- Rajewsky, K -- Radbruch, A -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):984-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438159" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Cell Line ; Chimera ; Drug Resistance/genetics ; Embryo, Mammalian ; *Gene Deletion ; Immunoglobulin G/genetics ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Switch Region/*genetics ; Interleukin-4/pharmacology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutagenesis ; Neomycin ; *Recombination, Genetic ; Stem Cells
    Print ISSN: 0036-8075
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  • 9
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    Uncovering of functional alternative CTLA-4 counter-receptor in B7-deficient mice (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-05
    Description: B7 delivers a costimulatory signal through CD28, resulting in interleukin-2 secretion and T cell proliferation. Blockade of this pathway results in T cell anergy. The in vivo role of B7 was evaluated with B7-deficient mice. These mice had a 70 percent decrease in costimulation of the response to alloantigen. Despite lacking B7 expression, activated B cells from these mice bound CTLA-4 and GL1 monoclonal antibody, demonstrating that alternative CTLA-4 ligand or ligands exist. These receptors are functionally important because the residual allogenic mixed lymphocyte responses were blocked by CTLA4Ig. Characterization of these CTLA-4 ligands should lead to strategies for manipulating the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeman, G J -- Borriello, F -- Hodes, R J -- Reiser, H -- Hathcock, K S -- Laszlo, G -- McKnight, A J -- Kim, J -- Du, L -- Lombard, D B -- CA 40216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):907-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematologic Malignancies, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694362" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD ; Antigens, CD80/genetics/*immunology/metabolism ; Antigens, Differentiation/immunology/*metabolism ; B-Lymphocytes/*immunology ; Base Sequence ; CTLA-4 Antigen ; Cell Line ; *Immunoconjugates ; Interleukin-2/secretion ; Isoantigens/immunology ; Lymphocyte Activation ; Lymphocyte Culture Test, Mixed ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; T-Lymphocytes/*immunology ; Transfection
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  • 10
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    Isolation of new ribozymes from a large pool of random sequences [see comment] (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-10
    Description: An iterative in vitro selection procedure was used to isolate a new class of catalytic RNAs (ribozymes) from a large pool of random-sequence RNA molecules. These ribozymes ligate two RNA molecules that are aligned on a template by catalyzing the attack of a 3'-hydroxyl on an adjacent 5'-triphosphate--a reaction similar to that employed by the familiar protein enzymes that synthesize RNA. The corresponding uncatalyzed reaction also yields a 3',5'-phosphodiester bond. In vitro evolution of the population of new ribozymes led to improvement of the average ligation activity and the emergence of ribozymes with reaction rates 7 million times faster than the uncatalyzed reaction rate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartel, D P -- Szostak, J W -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1411-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690155" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biological Evolution ; Catalysis ; Kinetics ; Magnesium/metabolism ; Molecular Sequence Data ; Mutation ; Oligoribonucleotides/metabolism ; RNA/*metabolism ; RNA Ligase (ATP)/chemistry/isolation & purification/metabolism ; RNA, Catalytic/chemistry/*isolation & purification/metabolism ; Temperature ; Templates, Genetic
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  • 11
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    AI helps researchers find meaning in molecules (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freedman, D -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):844-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8346437" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Artificial Intelligence ; Base Sequence ; Collagen/chemistry/genetics/physiology ; DNA/chemistry/genetics ; Humans ; Molecular Sequence Data ; Mutation ; *Protein Structure, Secondary ; *Protein Structure, Tertiary ; *Sequence Analysis, DNA ; Software
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  • 12
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    Nucleosome disruption by transcription factor binding in yeast (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-03
    Description: Studies in vivo and in vitro have shown that the packaging of DNA into chromatin can affect gene expression. Here, binding of the yeast transcriptional activator GAL4 to DNA in chromatin has been investigated in vivo with a yeast episome. A positioned nucleosome that is present in cells grown in glucose and contains a single GAL4 binding site is disrupted by GAL4 binding in galactose. GAL4 can also bind to DNA in chromatin when the carboxyl-terminal activation domain of GAL4 is either masked by GAL80 or is absent. These results show that a transcription factor can bind to its site in vivo in what would appear to be a repressive chromatin structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morse, R H -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1563-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Developmental Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248805" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/*metabolism ; Galactose/metabolism ; Glucose/metabolism ; Molecular Sequence Data ; Nucleosomes/*metabolism ; Plasmids ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*metabolism
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  • 13
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    Long-range photoinduced electron transfer through a DNA helix (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-12
    Description: Rapid photoinduced electron transfer is demonstrated over a distance of greater than 40 angstroms between metallointercalators that are tethered to the 5' termini of a 15-base pair DNA duplex. An oligomeric assembly was synthesized in which the donor is Ru(phen)2dppz2+ (phen, phenanthroline, and dppz, dipyridophenazine) and the acceptor is Rh(phi)2phen3+ (phi, phenanthrenequinone diimine). These metal complexes are intercalated either one or two base steps in from the helix termini. Although the ruthenium-modified oligonucleotide hybridized to an unmodified complement luminesces intensely, the ruthenium-modified oligomer hybridized to the rhodium-modified oligomer shows no detectable luminescence. Time-resolved studies point to a lower limit of 10(9) per second for the quenching rate. No quenching was observed upon metallation of two complementary octamers by Ru(phen)3(2+) and Rh(phen)3(3+) under conditions where the phen complexes do not intercalate. The stacked aromatic heterocycles of the DNA duplex therefore serve as an efficient medium for coupling electron donors and acceptors over very long distances.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, C J -- Arkin, M R -- Jenkins, Y -- Ghatlia, N D -- Bossmann, S H -- Turro, N J -- Barton, J K -- GM49216/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1025-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beckman Institute, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7802858" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; *Electrons ; Intercalating Agents/*chemistry ; Lasers ; Luminescence ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemistry ; Organometallic Compounds/chemistry ; Phenanthrenes/chemistry ; Phenanthrolines/chemistry ; Photochemistry
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  • 14
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    A detailed genetic map for the X chromosome of the malaria vector, Anopheles gambiae (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-30
    Description: Anopheles gambiae, the primary vector of human malaria in Africa, is responsible for approximately a million deaths per year, mostly of children. Despite its significance in disease transmission, this mosquito has not been studied extensively by genetic or molecular techniques. To facilitate studies on this vector, a genetic map has been developed that covers the X chromosome at an average resolution of 2 centimorgans. This map has been integrated with the chromosome banding pattern and used to localize a recessive, sex-linked mutation (white eye) to within 1 centimorgan of flanking markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, L -- Collins, F H -- Kumar, V -- Kafatos, F C -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):605-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342025" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Anopheles/*genetics ; Base Sequence ; Chromosome Banding ; *Chromosome Mapping ; Crosses, Genetic ; DNA, Satellite/genetics ; Female ; *Genes, Insect ; Genes, Recessive ; Genetic Markers ; Insect Vectors/*genetics ; Malaria/transmission ; Male ; Molecular Sequence Data ; Mutation ; Recombination, Genetic ; *X Chromosome
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  • 15
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    Generation of allospecific natural killer cells by stimulation across a polymorphism of HLA-C (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: The cytotoxicity of human natural killer (NK) cells is modulated by the major histocompatibility complex human leukocyte antigen (HLA)-C molecules on the surface of the target cell. Alloreactive NK cells specific for the NK-1 alloantigen could be reproducibly generated from individuals that were homozygous for HLA-C with asparagine at residue 77 and lysine at residue 80 [HLA-C(Asn77,Lys80)] by stimulation with target cells that were homozygous for HLA-C(Ser77,Asn80); the reciprocal stimulation yielded NK cells specific for the NK-2 alloantigen. However, neither homozygous target cell stimulated the generation of alloreactive NK cells from heterozygous individuals. Thus, these data reveal an unanticipated difference between human NK alloreactivity defined by this system and murine "hybrid resistance."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colonna, M -- Brooks, E G -- Falco, M -- Ferrara, G B -- Strominger, J L -- CA 47554/CA/NCI NIH HHS/ -- KO8 AI01064/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 May 21;260(5111):1121-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunogenetics, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493555" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Cell Line ; *Cytotoxicity, Immunologic ; Genotype ; HLA-C Antigens/genetics/*immunology ; Heterozygote ; Homozygote ; Humans ; Isoantigens/*immunology ; Killer Cells, Natural/*immunology ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymorphism, Genetic
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  • 16
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    Systemic gene expression after intravenous DNA delivery into adult mice (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-07-09
    Description: Direct gene transfer into adult animals resulting in generalized or tissue-specific expression would facilitate rapid analysis of transgene effects and allow precise in vivo manipulation of biologic processes at the molecular level. A single intravenous injection of expression plasmid:cationic liposome complexes into adult mice efficiently transfected virtually all tissues. In addition to vascular endothelial cells, most of the extravascular parenchymal cells present in many tissues including the lung, spleen, lymph nodes, and bone marrow expressed the transgene without any apparent treatment-related toxicity. The transgene was still expressed in large numbers of cells in multiple tissues for at least 9 weeks after a single injection. Expression could be targeted to specific tissues and cell types, depending on the promoter element used.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, N -- Liggitt, D -- Liu, Y -- Debs, R -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):209-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Institute, University of California, San Francisco 94143-0128.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7687073" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bone Marrow/metabolism ; Chloramphenicol O-Acetyltransferase/genetics ; Cystic Fibrosis/genetics ; Cystic Fibrosis Transmembrane Conductance Regulator ; Cytomegalovirus/genetics ; Female ; *Gene Expression ; Injections, Intravenous ; Liposomes ; Liver/metabolism ; Lung/metabolism ; Lung Neoplasms/genetics ; Lymphoid Tissue/metabolism ; Membrane Proteins/genetics ; Mice ; Mice, Inbred ICR ; Mice, Transgenic ; Molecular Sequence Data ; Myocardium/metabolism ; Oligodeoxyribonucleotides ; Phosphatidylethanolamines/chemistry ; Plasmids ; Quaternary Ammonium Compounds ; *Transfection
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  • 17
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    Altered fluid transport across airway epithelium in cystic fibrosis (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-10-15
    Description: In cystic fibrosis (CF), absence or dysfunction of a phosphorylation-regulated chloride channel [CF transmembrane conductance regulator (CFTR)] leads to the loss or reduction of chloride secretion into the airways. Active sodium absorption is also increased in CF, and both of these ion transport changes could alter fluid transport across the airways. Under baseline conditions, cultured human airway epithelia from normal individuals absorbed fluid, and this absorption was increased in epithelia from patients with CF. In normal and CF epithelial cultures fluid absorption was inhibited by amiloride. Adenosine 3',5'-monophosphate stimulated fluid secretion in normal epithelial cultures but not in cultures from individuals with CF. In contrast, fluid secretion induced by nucleotide triphosphates (uridine triphosphate or adenosine triphosphate) was unaltered in cultures of epithelia from patients with CF, suggesting an approach to the treatment of CF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jiang, C -- Finkbeiner, W E -- Widdicombe, J H -- McCray, P B Jr -- Miller, S S -- HL 42368/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):424-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211164" target="_blank"〉PubMed〈/a〉
    Keywords: Absorption ; Adenosine Triphosphate/pharmacology ; Adolescent ; Adult ; Amiloride/pharmacology ; Body Fluids/*metabolism ; Cells, Cultured ; Cyclic AMP/pharmacology ; Cystic Fibrosis/*metabolism ; Epithelial Cells ; Epithelium/metabolism ; Female ; Humans ; Male ; Middle Aged ; Nasal Mucosa/cytology/*metabolism ; Sodium/metabolism ; Sodium Channels/metabolism ; Trachea/cytology/*metabolism ; Uridine Triphosphate/pharmacology
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    Mineralocorticoids, glucocorticoids, receptors and response elements (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Funder, J W -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1132-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Baker Medical Research Institute, Prahran, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382375" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation ; Glucocorticoids/*physiology ; Mineralocorticoids/*physiology ; Models, Biological ; Molecular Sequence Data ; Receptors, Glucocorticoid/*metabolism ; Receptors, Mineralocorticoid ; Receptors, Steroid/*metabolism ; *Transcription, Genetic
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    Structure of DNA polymerase I Klenow fragment bound to duplex DNA (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-16
    Description: Klenow fragment of Escherichia coli DNA polymerase I, which was cocrystallized with duplex DNA, positioned 11 base pairs of DNA in a groove that lies at right angles to the cleft that contains the polymerase active site and is adjacent to the 3' to 5' exonuclease domain. When the fragment bound DNA, a region previously referred to as the "disordered domain" became more ordered and moved along with two helices toward the 3' to 5' exonuclease domain to form the binding groove. A single-stranded, 3' extension of three nucleotides bound to the 3' to 5' exonuclease active site. Although this cocrystal structure appears to be an editing complex, it suggests that the primer strand approaches the catalytic site of the polymerase from the direction of the 3' to 5' exonuclease domain and that the duplex DNA product may bend to enter the cleft that contains the polymerase catalytic site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beese, L S -- Derbyshire, V -- Steitz, T A -- GM28550/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):352-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469987" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallization ; DNA/chemistry/*metabolism ; DNA Polymerase I/*chemistry/metabolism ; DNA Replication ; DNA, Single-Stranded/chemistry/metabolism ; Escherichia coli/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Templates, Genetic
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    Cloning the differences between two complex genomes (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-12
    Description: The analysis of the differences between two complex genomes holds promise for the discovery of infectious agents and probes useful for genetic studies. A system was developed in which subtractive and kinetic enrichment was used to purify restriction endonuclease fragments present in one population of DNA fragments but not in another. Application of this method to DNA populations of reduced complexity ("representations") resulted in the isolation of probes to viral genomes present as single copies in human DNA, and probes that detect polymorphisms between two individuals. In principle, this system, called representational difference analysis (RDA), may also be used for isolating probes linked to sites of genomic rearrangements, whether occurring spontaneously and resulting in genetic disorders or cancer, or programmed during differentiation and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lisitsyn, N -- Wigler, M -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):946-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438152" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Bacteriophage lambda/genetics ; Base Sequence ; *Cloning, Molecular ; DNA/*chemistry ; DNA Probes ; DNA, Viral ; Female ; Gene Deletion ; Genetic Diseases, Inborn/genetics ; Humans ; Male ; Molecular Sequence Data ; Neoplasms/genetics ; Nucleic Acid Hybridization/methods ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sequence Homology, Nucleic Acid
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    Fusion between transcription factor CBF beta/PEBP2 beta and a myosin heavy chain in acute myeloid leukemia (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-08-20
    Description: The pericentric inversion of chromosome 16 [inv(16)(p13q22)] is a characteristic karyotypic abnormality associated with acute myeloid leukemia, most commonly of the M4Eo subtype. The 16p and 16q breakpoints were pinpointed by yeast artificial chromosome and cosmid cloning, and the two genes involved in this inversion were identified. On 16q the inversion occurred near the end of the coding region for CBF beta, also known as PEBP2 beta, a subunit of a heterodimeric transcription factor regulating genes expressed in T cells; on 16p a smooth muscle myosin heavy chain (SMMHC) gene (MYH11) was interrupted. In six of six inv(16) patient samples tested, an in-frame fusion messenger RNA was demonstrated that connected the first 165 amino acids of CBF beta with the tail region of SMMHC. The repeated coiled coil of SMMHC may result in dimerization of the CBF beta fusion protein, which in turn would lead to alterations in transcriptional regulation and contribute to leukemic transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, P -- Tarle, S A -- Hajra, A -- Claxton, D F -- Marlton, P -- Freedman, M -- Siciliano, M J -- Collins, F S -- CA55164/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1041-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Internal Medicine, University of Michigan Medical Center, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351518" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Chromosome Inversion ; *Chromosomes, Human, Pair 16 ; Cloning, Molecular ; Core Binding Factor Alpha 1 Subunit ; Core Binding Factor beta Subunit ; Core Binding Factors ; Cosmids ; DNA-Binding Proteins/*genetics ; Humans ; In Situ Hybridization, Fluorescence ; Leukemia, Myelomonocytic, Acute/*genetics ; Molecular Sequence Data ; Muscle, Smooth/chemistry ; Myosins/*genetics ; *Neoplasm Proteins ; Polymerase Chain Reaction ; Protein Multimerization ; Restriction Mapping ; Transcription Factor AP-2 ; Transcription Factors/*genetics
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  • 22
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    Isolation of ORC6, a component of the yeast origin recognition complex by a one-hybrid system (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-12-17
    Description: Here a method is described to identify genes encoding proteins that recognize a specific DNA sequence. A bank of random protein segments tagged with a transcriptional activation domain is screened for proteins that can activate a reporter gene containing the sequence in its promoter. This strategy was used to identify an essential protein that interacts in vivo with the yeast origin of DNA replication. Matches between its predicted amino acid sequence and peptide sequence obtained from the 50-kilodalton subunit of the yeast origin recognition complex (ORC) established that the gene isolated here, ORC6, encodes this subunit. These observations provide evidence that ORC recognizes yeast replication origins in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J J -- Herskowitz, I -- AI18738/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266075" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Cycle ; *DNA Replication ; DNA, Fungal/metabolism ; DNA-Binding Proteins/chemistry/*genetics/metabolism ; Fungal Proteins/chemistry/*genetics/metabolism ; *Genes, Fungal ; Genes, Reporter ; Molecular Sequence Data ; Open Reading Frames ; Origin Recognition Complex ; Promoter Regions, Genetic ; *Replicon ; Repressor Proteins/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; Saccharomyces cerevisiae Proteins
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    Genetic identification of a hantavirus associated with an outbreak of acute respiratory illness (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-05
    Description: A mysterious respiratory illness with high mortality was recently reported in the southwestern United States. Serologic studies implicated the hantaviruses, rodent-borne RNA viruses usually associated elsewhere in the world with hemorrhagic fever with renal syndrome. A genetic detection assay amplified hantavirus-specific DNA fragments from RNA extracted from the tissues of patients and deer mice (Peromyscus maniculatus) caught at or near patient residences. Nucleotide sequence analysis revealed the associated virus to be a new hantavirus and provided a direct genetic link between infection in patients and rodents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nichol, S T -- Spiropoulou, C F -- Morzunov, S -- Rollin, P E -- Ksiazek, T G -- Feldmann, H -- Sanchez, A -- Childs, J -- Zaki, S -- Peters, C J -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):914-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Viral and Rickettsial Diseases, Centers for Disease Control and Prevention, Atlanta, GA 30333.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235615" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bunyaviridae Infections/epidemiology/*microbiology/veterinary ; DNA Primers ; *Disease Outbreaks ; *Disease Reservoirs ; *Genome, Viral ; Hantavirus/classification/*genetics/isolation & purification ; Humans ; Lung Diseases/epidemiology/*microbiology ; Molecular Sequence Data ; Peromyscus/*microbiology ; Phylogeny ; Polymerase Chain Reaction ; Rodent Diseases/epidemiology/microbiology ; Sequence Homology, Nucleic Acid ; Southwestern United States/epidemiology
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  • 24
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    A third recognition element in bacterial promoters: DNA binding by the alpha subunit of RNA polymerase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-26
    Description: A DNA sequence rich in (A+T), located upstream of the -10, -35 region of the Escherichia coli ribosomal RNA promoter rrnB P1 and called the UP element, stimulates transcription by a factor of 30 in vivo, as well as in vitro in the absence of protein factors other than RNA polymerase (RNAP). When fused to other promoters, such as lacUV5, the UP element also stimulates transcription, indicating that it is a separate promoter module. Mutations in the carboxyl-terminal region of the alpha subunit of RNAP prevent stimulation of these promoters by the UP element although the mutant enzymes are effective in transcribing the "core" promoters (those lacking the UP element). Protection of UP element DNA by the mutant RNAPs is severely reduced in footprinting experiments, suggesting that the selective decrease in transcription might result from defective interactions between alpha and the UP element. Purified alpha binds specifically to the UP element, confirming that alpha acts directly in promoter recognition. Transcription of three other promoters was also reduced by the COOH-terminal alpha mutations. These results suggest that UP elements comprise a third promoter recognition region (in addition to the -10, -35 recognition hexamers, which interact with the sigma subunit) and may account for the presence of (A+T)-rich DNA upstream of many prokaryotic promoters. Since the same alpha mutations also block activation by some transcription factors, mechanisms of promoter stimulation by upstream DNA elements and positive control by certain transcription factors may be related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, W -- Gosink, K K -- Salomon, J -- Igarashi, K -- Zou, C -- Ishihama, A -- Severinov, K -- Gourse, R L -- AI90035/AI/NIAID NIH HHS/ -- GM49242/GM/NIGMS NIH HHS/ -- R01 GM37048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1407-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248780" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Carrier Proteins/metabolism ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology/*genetics ; *Escherichia coli Proteins ; Integration Host Factors ; Molecular Sequence Data ; *Promoter Regions, Genetic ; Transcription Factors/metabolism ; Transcription, Genetic ; *rRNA Operon
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    Identification of the von Hippel-Lindau disease tumor suppressor gene (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-05-28
    Description: A gene discovered by positional cloning has been identified as the von Hippel-Lindau (VHL) disease tumor suppressor gene. A restriction fragment encompassing the gene showed rearrangements in 28 of 221 VHL kindreds. Eighteen of these rearrangements were due to deletions in the candidate gene, including three large nonoverlapping deletions. Intragenic mutations were detected in cell lines derived from VHL patients and from sporadic renal cell carcinomas. The VHL gene is evolutionarily conserved and encodes two widely expressed transcripts of approximately 6 and 6.5 kilobases. The partial sequence of the inferred gene product shows no homology to other proteins, except for an acidic repeat domain found in the procyclic surface membrane glycoprotein of Trypanosoma brucei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Latif, F -- Tory, K -- Gnarra, J -- Yao, M -- Duh, F M -- Orcutt, M L -- Stackhouse, T -- Kuzmin, I -- Modi, W -- Geil, L -- New York, N.Y. -- Science. 1993 May 28;260(5112):1317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunobiology, National Cancer Institute-Frederick Cancer Research and Development Center (NCI-FCRDC), Frederick, MD 21702-1201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carcinoma, Renal Cell/genetics ; Chromosomes, Human, Pair 3 ; Cloning, Molecular ; Gene Deletion ; *Genes, Tumor Suppressor ; Humans ; Kidney Neoplasms/genetics ; Membrane Glycoproteins/chemistry/*genetics ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Pedigree ; Polymorphism, Genetic ; Tumor Cells, Cultured ; von Hippel-Lindau Disease/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Induction by EGF and interferon-gamma of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-24
    Description: Intraperitoneal injection of epidermal growth factor (EGF) into mice resulted in the appearance in liver nuclei of three tyrosine phosphorylated proteins (84, 91, and 92 kilodaltons) within minutes after administration of EGF. Administration of interferon-gamma (IFN-gamma) resulted in the appearance in liver nuclei of two tyrosine phosphorylated proteins (84 and 91 kilodaltons). The 84- and 91-kilodalton proteins detected after either EGF or IFN-gamma administration were identified as the IFN-gamma activation factors (GAF). Furthermore, gel shift analysis revealed that these GAF proteins, detected after either EGF or IFN-gamma administration, specifically bound to the sis-inducible element of the c-fos promoter. Thus, GAF proteins participate in nuclear signaling in both IFN-gamma and EGF pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruff-Jamison, S -- Chen, K -- Cohen, S -- HD-00700/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1733-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8378774" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/drug effects/*metabolism ; DNA-Binding Proteins/*metabolism ; Epidermal Growth Factor/*pharmacology ; Genes, fos ; Interferon-Stimulated Gene Factor 3 ; Interferon-gamma/*pharmacology ; Liver/drug effects/metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Promoter Regions, Genetic ; STAT1 Transcription Factor ; *Trans-Activators ; Transcription Factors/*metabolism ; Tyrosine/*metabolism
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    Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor alpha (RXR alpha) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5'-AGGTCA-3') arranged as tandem repeats.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, M S -- Kliewer, S A -- Provencal, J -- Wright, P E -- Evans, R M -- New York, N.Y. -- Science. 1993 May 21;260(5111):1117-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388124" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/*metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*chemistry/metabolism ; Oligodeoxyribonucleotides ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Cell Surface/*chemistry/metabolism ; *Receptors, Retinoic Acid ; Repetitive Sequences, Nucleic Acid ; Retinoid X Receptors ; *Transcription Factors ; Zinc Fingers
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    Ribozymes: killing the messenger (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1993 Dec 3;262(5139):1512-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248799" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Genetic Therapy/*methods ; HIV/genetics ; HIV Infections/*therapy ; Humans ; Molecular Sequence Data ; RNA, Catalytic/*genetics/metabolism/therapeutic use ; RNA, Viral/metabolism
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    GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: A potent neurotrophic factor that enhances survival of midbrain dopaminergic neurons was purified and cloned. Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-beta superfamily. In embryonic midbrain cultures, recombinant human GDNF promoted the survival and morphological differentiation of dopaminergic neurons and increased their high-affinity dopamine uptake. These effects were relatively specific; GDNF did not increase total neuron or astrocyte numbers nor did it increase transmitter uptake by gamma-aminobutyric-containing and serotonergic neurons. GDNF may have utility in the treatment of Parkinson's disease, which is marked by progressive degeneration of midbrain dopaminergic neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, L F -- Doherty, D H -- Lile, J D -- Bektesh, S -- Collins, F -- New York, N.Y. -- Science. 1993 May 21;260(5111):1130-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Synergen, Inc., Boulder, CO 80301.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493557" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Astrocytes/cytology/drug effects ; Base Sequence ; Cell Differentiation/drug effects ; Cell Line ; Cell Survival/drug effects ; Cells, Cultured ; Cloning, Molecular ; Dopamine/*biosynthesis ; Glial Cell Line-Derived Neurotrophic Factor ; Humans ; Mesencephalon/cytology/*drug effects/metabolism ; Molecular Sequence Data ; Molecular Weight ; *Nerve Growth Factors ; Nerve Tissue Proteins/chemistry/genetics/isolation & purification/*pharmacology ; Neuroglia/*metabolism ; Neurons/cytology/*drug effects/metabolism ; Parkinson Disease/drug therapy ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Cells in stress: transcriptional activation of heat shock genes (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morimoto, R I -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1409-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular and Cell Biology, Northwestern University, Evanston, IL 60201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8451637" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics/metabolism ; DNA-Binding Proteins/metabolism ; *Gene Expression Regulation ; Heat-Shock Proteins/*genetics ; Hot Temperature ; Humans ; Models, Genetic ; Molecular Sequence Data ; Transcription Factors/*metabolism ; *Transcription, Genetic
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    Genotypic and phenotypic characterization of HIV-1 patients with primary infection (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-08-27
    Description: Better characterization of human immunodeficiency virus-type 1 (HIV-1) in patients with primary infection has important implications for the development of an acquired immunodeficiency syndrome (AIDS) vaccine because vaccine strategies should target viral isolates with the properties of transmitted viruses. In five HIV-1 seroconverters, the viral phenotype was found to be uniformly macrophage-tropic and non-syncytium-inducing. Furthermore, the viruses were genotypically homogeneous within each patient, but a common signature sequence was not discernible among transmitted viruses. In the two cases where the sexual partners were also studied, the sequences of the transmitted viruses matched best with minor variants in the blood of the transmitters. There was also a stronger pressure to conserve sequences in gp120 than in gp41, nef, and p17, suggesting that a selective mechanism is involved in transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, T -- Mo, H -- Wang, N -- Nam, D S -- Cao, Y -- Koup, R A -- Ho, D D -- AI24030/AI/NIAID NIH HHS/ -- AI25541/AI/NIAID NIH HHS/ -- AI27742/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, New York University School of Medicine, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356453" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Female ; Gene Products, gag/chemistry/genetics ; Genes, Viral ; Genotype ; Giant Cells/physiology ; HIV Antigens/chemistry/genetics ; HIV Envelope Protein gp120/chemistry/*genetics ; HIV Envelope Protein gp41/chemistry/genetics ; HIV Infections/*microbiology/transmission ; HIV Seropositivity/microbiology ; HIV-1/chemistry/*genetics/*physiology ; Humans ; Macrophages ; Male ; Molecular Sequence Data ; Phenotype ; Sequence Alignment ; Sexual Partners ; *Viral Proteins ; Virus Replication ; gag Gene Products, Human Immunodeficiency Virus
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    Molecular cloning of an apolipoprotein B messenger RNA editing protein (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: Mammalian apolipoprotein B (apo B) exists in two forms, each the product of a single gene. The shorter form, apo B48, arises by posttranscriptional RNA editing whereby cytidine deamination produces a UAA termination codon. A full-length complementary DNA clone encoding an apo B messenger RNA editing protein (REPR) was isolated from rat small intestine. The 229-residue protein contains consensus phosphorylation sites and leucine zipper domains. HepG2 cell extracts acquire editing activity when mixed with REPR from oocyte extracts. REPR is essential for apo B messenger RNA editing, and the isolation and characterization of REPR may lead to the identification of other eukaryotic RNA editing proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teng, B -- Burant, C F -- Davidson, N O -- DK-42086/DK/NIDDK NIH HHS/ -- HL-38180/HL/NHLBI NIH HHS/ -- KO-4 HL-02166/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511591" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoproteins B/*genetics ; Base Sequence ; Cell Line ; *Cloning, Molecular ; Cytidine Deaminase/chemistry/*genetics ; Humans ; Intestine, Small/chemistry ; Leucine Zippers ; Molecular Sequence Data ; Molecular Weight ; Open Reading Frames ; Phosphorylation ; *RNA Editing ; Rats ; Tumor Cells, Cultured
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    Progression to diabetes in nonobese diabetic (NOD) mice with transgenic T cell receptors (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-19
    Description: The T cell receptor (TCR) requirements in the pathogenesis of insulin-dependent diabetes were examined with transgenic NOD mice bearing nondisease-related TCR alpha and beta chains. In both TCR beta and TCR alpha beta transgenic NOD mice the beta chain transgene was expressed by 〉 98% of peripheral T cells. The alpha chain transgene was also highly expressed. Insulitis developed in both sets of transgenic animals with most of the lymphocytes in the lesion expressing the transgenic beta chain and with depletion of the endogenous TCR V beta genes. Nonetheless, NOD animals transgenic for TCR beta and TCR alpha beta developed diabetes similar to controls. Thus, skewing the TCR repertoire did not diminish autoimmune susceptibility in NOD mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipes, M A -- Rosenzweig, A -- Tan, K N -- Tanigawa, G -- Ladd, D -- Seidman, J G -- Eisenbarth, G S -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1165-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joslin Diabetes Center, Harvard Medical School, Brigham and Women's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8267690" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/physiology ; Animals ; Base Sequence ; Crosses, Genetic ; Diabetes Mellitus, Type 2/genetics/immunology/*physiopathology ; Female ; Gene Rearrangement, T-Lymphocyte ; Islets of Langerhans/immunology/pathology ; Male ; Mice ; Mice, Inbred NOD/*physiology ; Mice, Transgenic ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Pancreatic Diseases/genetics/immunology/pathology ; Polymerase Chain Reaction/methods ; Receptors, Antigen, T-Cell, alpha-beta/genetics/*physiology ; T-Lymphocytes/*immunology/pathology
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    Death gives birth to the nervous system. But how? (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):762-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430328" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis/physiology ; Caenorhabditis elegans/embryology/genetics ; Cell Death/*physiology ; Cells, Cultured ; Embryo, Nonmammalian/physiology ; Nerve Growth Factors/physiology ; Nervous System/cytology/*embryology ; Neurons/cytology/*physiology ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-bcl-2 ; Proto-Oncogenes
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    Mutations in U6 snRNA that alter splice site specificity: implications for the active site (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-12-24
    Description: What determines the precise sites of cleavage in the two transesterification reactions of messenger RNA (mRNA) splicing is a major unsolved question. Mutation of the invariant G (guanosine) at position 5 of 5' splice sites in Saccharomyces cerevisiae introns activates cleavage at nearby aberrant sites. A genetic approach was used to test the hypothesis that a base-pairing interaction between the 5' splice site and the invariant ACAGAG sequence of U6 is a determinant of 5' splice site choice. Mutations in U6 or the intron (or both) that were predicted to stabilize the interaction suppressed aberrant cleavage and increased normal cleavage. In addition, a mutation in the ACAGAG sequence suppressed mutations of the 3' splice site dinucleotide. These data can fit a model for the spliceosomal active site comprised of a set of RNA-RNA interactions between the intron, U2 and U6.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lesser, C F -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):1982-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Scientist Training Program, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266093" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites/genetics ; Genes, Reporter ; Introns/genetics ; Models, Genetic ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Conformation ; RNA Splicing/*genetics ; RNA, Small Nuclear/*genetics ; Saccharomyces cerevisiae/genetics ; Suppression, Genetic
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    Two jobs for the origin replication complex (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newlon, C S -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1830-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of Medicine and Dentistry-New Jersey Medical School, Newark 07103.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266070" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA Replication ; DNA, Fungal/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics ; Fungal Proteins/chemistry/*genetics/metabolism ; *Gene Expression Regulation, Fungal ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Origin Recognition Complex ; *Replicon ; Repressor Proteins/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics ; Transcription, Genetic
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    Primers for mitochondrial DNA replication generated by endonuclease G (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-06
    Description: Endonuclease G (Endo G) is widely distributed among animals and cleaves DNA at double-stranded (dG)n.(dC)n and at single-stranded (dC)n tracts. Endo G is synthesized as a propeptide with an amino-terminal presequence that targets the nuclease to mitochondria. Endo G can also be detected in extranucleolar chromatin. In addition to deoxyribonuclease activities, Endo G also has ribonuclease (RNase) and RNase H activities and specifically cleaves mouse mitochondrial RNA and DNA-RNA substrates containing the origin of heavy-strand DNA replication (OH). The cleavage sites match those found in vivo, indicating that Endo G is capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cote, J -- Ruiz-Carrillo, A -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):765-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, Medical School of Laval University, L'Hotel-Dieu de Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/enzymology ; DNA/genetics ; *DNA Replication ; DNA, Mitochondrial/*metabolism ; Endodeoxyribonucleases/chemistry/genetics/*metabolism ; Genetic Vectors ; Mitochondria/enzymology ; Molecular Sequence Data ; RNA/*metabolism ; Ribonuclease H/metabolism ; Ribonucleases/metabolism ; Transfection
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    Enhancement by histamine of NMDA-mediated synaptic transmission in the hippocampus (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-07-02
    Description: Histamine is a neuromodulator in the brain, and the hippocampus is one of the regions of the brain that is innervated by histaminergic neurons. When applied to cultured hippocampal neurons, histamine selectively increased by up to tenfold the amplitude of the component of synaptic transmission that was mediated by N-methyl-D-aspartate (NMDA) receptors. Spontaneous miniature synaptic currents and the current elicited by applied NMDA also were enhanced, indicating that the histamine effect was expressed primarily postsynaptically. These results suggest that histamine may modulate processes involving NMDA receptors, such as the induction of long-term potentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bekkers, J M -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):104-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, John Curtin School of Medical Research, Australian National Univresity, Canberra, ACT.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8391168" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Cells, Cultured ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Hippocampus/cytology/drug effects/*physiology ; Histamine/*pharmacology ; Ion Channel Gating/drug effects ; N-Methylaspartate/*metabolism/pharmacology ; Rats ; Receptors, Histamine/physiology ; Receptors, N-Methyl-D-Aspartate/metabolism ; Synapses/*physiology ; Synaptic Transmission/*drug effects ; Virulence Factors, Bordetella/pharmacology
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    Helper T cells without CD4: control of leishmaniasis in CD4-deficient mice (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-10
    Description: Expression of either the CD4 or CD8 glycoproteins discriminates two functionally distinct lineages of T lymphocytes. A null mutation in the gene encoding CD4 impairs the development of the helper cell lineage that is normally defined by CD4 expression. Infection of CD4-null mice with Leishmania has revealed a population of functional helper T cells that develops despite the absence of CD4. These CD8- alpha beta T cell receptor+ T cells are major histocompatibility complex class II-restricted and produce interferon-gamma when challenged with parasite antigens. These results indicate that T lymphocyte lineage commitment and peripheral function need not depend on the function of CD4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locksley, R M -- Reiner, S L -- Hatam, F -- Littman, D R -- Killeen, N -- AI30663/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8367726" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/genetics/*immunology ; Antigens, CD8/immunology ; Antigens, Protozoan/immunology ; B-Lymphocytes/immunology ; Base Sequence ; CD4-CD8 Ratio ; Histocompatibility Antigens Class II/immunology ; Hypersensitivity, Delayed ; Interferon-gamma/biosynthesis/immunology ; Leishmania tropica/*immunology ; Leishmaniasis, Cutaneous/*immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides ; Receptors, Antigen, T-Cell, alpha-beta/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Helper-Inducer/*immunology
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    Group II intron RNA catalysis of progressive nucleotide insertion: a model for RNA editing (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-20
    Description: The self-splicing bl1 intron lariat from mitochondria of Saccharomyces cerevisiae catalyzed the insertion of nucleotidyl monomers derived from the 3' end of a donor RNA into an acceptor RNA in a 3' to 5' direction in vitro. In this catalyzed reaction, the site specificity provided by intermolecular base pair interactions, the formation of chimeric intermediates, the polarity of the nucleotidyl insertion, and its reversibility all resemble such properties in previously proposed models of RNA editing in kinetoplastid mitochondria. These results suggest that RNA editing occurs by way of a concerted, two-step transesterification mechanism and that RNA splicing and RNA editing might be prebiotically related mechanisms; possibly, both evolved from a primordial demand for self-replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueller, M W -- Hetzer, M -- Schweyen, R J -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1035-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vienna Biocenter, Institute for Microbiology and Genetics, University of Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351516" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*metabolism ; Base Sequence ; Esterification ; *Introns ; Mitochondria/metabolism ; Molecular Sequence Data ; *RNA Editing ; RNA Splicing ; RNA, Catalytic/*metabolism ; RNA, Fungal/*metabolism ; RNA, Guide/*metabolism ; Saccharomyces cerevisiae/genetics/metabolism
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  • 41
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    Cooperative interactions between the Caenorhabditis elegans homeoproteins UNC-86 and MEC-3 (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-03
    Description: The POU-type homeodomain protein UNC-86 and the LIM-type homeodomain protein MEC-3, which specify neuronal cell fate in the nematode Caenorhabditis elegans, bind cooperatively as a heterodimer to the mec-3 promoter. Heterodimer formation increases DNA binding stability and, therefore, increases DNA binding specificity. The in vivo significance of this heterodimer formation in neuronal differentiation is suggested by (i) a loss-of-function mec-3 mutation whose product in vitro binds DNA well but forms heterodimers with UNC-86 poorly and (ii) a mec-3 mutation with wild-type function whose product binds DNA poorly but forms heterodimers well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xue, D -- Tu, Y -- Chalfie, M -- GM30997/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 3;261(5126):1324-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8103239" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cell Differentiation ; DNA/*metabolism ; Genes, Helminth ; *Genes, Homeobox ; Helminth Proteins/chemistry/genetics/*metabolism ; *Homeodomain Proteins ; LIM-Homeodomain Proteins ; Molecular Sequence Data ; Neurons/cytology ; Oligodeoxyribonucleotides/metabolism ; POU Domain Factors ; Promoter Regions, Genetic ; Transcription Factors/chemistry/genetics/*metabolism
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    Interleukin-2 receptor gamma chain: a functional component of the interleukin-4 receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: The interleukin-2 (IL-2) receptor gamma chain (IL-2R gamma) is an essential component of high- and intermediate-affinity IL-2 receptors. IL-2R gamma was demonstrated to be a component of the IL-4 receptor on the basis of chemical cross-linking data, the ability of IL-2R gamma to augment IL-4 binding affinity, and the requirement for IL-2R gamma in IL-4-mediated phosphorylation of insulin receptor substrate-1. The observation that IL-2R gamma is a functional component of the IL-4 receptor, together with the finding that IL-2R gamma associates with the IL-7 receptor, begins to elucidate why deficiency of this common gamma chain (gamma c) has a profound effect on lymphoid function and development, as seen in X-linked severe combined immunodeficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, S M -- Keegan, A D -- Harada, N -- Nakamura, Y -- Noguchi, M -- Leland, P -- Friedmann, M C -- Miyajima, A -- Puri, R K -- Paul, W E -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1880-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Pulmonary and Molecular Immunology, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266078" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Cell Line, Transformed ; Genetic Linkage ; Humans ; Insulin Receptor Substrate Proteins ; Interleukin-4/metabolism ; L Cells (Cell Line) ; Mice ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Phosphorylation ; Receptors, Interleukin-2/chemistry/genetics/*metabolism ; Receptors, Interleukin-4 ; Receptors, Mitogen/chemistry/genetics/*metabolism ; Severe Combined Immunodeficiency/genetics/immunology ; Signal Transduction ; Transfection ; X Chromosome
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    A common nuclear signal transduction pathway activated by growth factor and cytokine receptors (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-24
    Description: Growth factors and cytokines act through cell surface receptors with different biochemical properties. Yet each type of receptor can elicit similar as well as distinct biological responses in target cells, suggesting that distinct classes of receptors activate common gene sets. Epidermal growth factor, interferon-gamma, and interleukin-6 all activated, through direct tyrosine phosphorylation, latent cytoplasmic transcription factors that recognized similar DNA elements. However, different ligands activated different patterns of factors with distinct DNA-binding specificities in the same and different cells. Thus, unrelated receptors may activate a common nuclear signal transduction pathway that, through differential use of latent cytoplasmic proteins, permits these receptors to regulate both common and unique sets of genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sadowski, H B -- Shuai, K -- Darnell, J E Jr -- Gilman, M Z -- AI32489/AI/NIAID NIH HHS/ -- CA09311/CA/NCI NIH HHS/ -- CA45642/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1739-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8397445" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Nucleus/metabolism ; Cytokines/metabolism/*pharmacology ; DNA-Binding Proteins/*metabolism ; Epidermal Growth Factor/pharmacology ; Growth Substances/metabolism/pharmacology ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-gamma/pharmacology ; Interleukin-6/pharmacology ; Molecular Sequence Data ; Phosphorylation ; Receptors, Cell Surface/*metabolism ; *Signal Transduction ; Transcription Factors/*metabolism ; Tumor Cells, Cultured ; Tyrosine/metabolism
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    Decreased expression of myotonin-protein kinase messenger RNA and protein in adult form of myotonic dystrophy (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-09
    Description: The myotonic dystrophy mutation has recently been identified; however, the molecular mechanism of the disease is still unknown. The sequence of the myotonin-protein kinase gene was determined, and messenger RNA spliced forms were identified in various tissues. Antisera were developed for analytical studies. Quantitative reverse transcription-polymerase chain reaction and radioimmunoassay were used to demonstrate that decreased levels of the messenger RNA and protein expression are associated with the adult form of myotonic dystrophy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, Y H -- Friedman, D L -- Richards, S -- Pearlman, J A -- Gibbs, R A -- Pizzuti, A -- Ashizawa, T -- Perryman, M B -- Scarlato, G -- Fenwick, R G Jr -- P30-HG00210/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):235-8.〈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/8469976" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Alternative Splicing ; Amino Acid Sequence ; Base Sequence ; Gene Expression ; Humans ; Molecular Sequence Data ; Molecular Weight ; Muscles/chemistry/*metabolism ; Myotonic Dystrophy/*genetics/metabolism ; Myotonin-Protein Kinase ; Polymerase Chain Reaction ; Protein Kinases/biosynthesis/chemistry/*genetics ; *Protein-Serine-Threonine Kinases ; RNA, Messenger/*genetics
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    Contamination of cDNA sequences in databases (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savakis, C -- Doelz, R -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1677-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456288" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; Databases, Factual/*standards ; Humans
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  • 46
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    Presentation of a viral T cell epitope expressed in the CDR3 region of a self immunoglobulin molecule (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-08
    Description: Synthetic peptides corresponding to microbial epitopes stimulate T cell immunity but their immunogenicity is poor and their half-lives are short. A viral epitope inserted into the complementarity-determining region 3 (CDR3) loop of the heavy chain of a self immunoglobulin (Ig) molecule was generated from the Ig context and was presented by I-Ed class II molecules to virus-specific, CD4+ T cells. Chimeric Ig-peptide was presented 100 to 1000 times more efficiently than free synthetic peptide and was able to prime virus-specific T cells in vivo. These features suggest that antigenized Ig can provide an improved and safe vaccine for the presentation of microbial and other peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaghouani, H -- Steinman, R -- Nonacs, R -- Shah, H -- Gerhard, W -- Bona, C -- AI13013/AI/NIAID NIH HHS/ -- AI18316/AI/NIAID NIH HHS/ -- AI24460/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7678469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/*immunology ; Antigens, Viral/*immunology ; Arsenic/immunology ; *Arsenicals ; Base Sequence ; CD4-Positive T-Lymphocytes/immunology ; DNA/genetics ; Epitopes/*immunology ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral/genetics/immunology ; Histocompatibility Antigens Class II/immunology ; Immunoglobulin Heavy Chains/genetics/immunology ; Immunoglobulin Variable Region/genetics/immunology ; Immunoglobulins/genetics/*immunology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutagenesis ; Receptors, Fc/immunology ; Recombinant Fusion Proteins/immunology ; Transfection
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    Generation of a mouse strain that produces immunoglobulin kappa chains with human constant regions (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-19
    Description: Humanized antibodies are highly efficient as immunotherapeutic reagents and have many advantages over rodent antibodies. A mouse strain was generated by gene targeting to replace the mouse kappa light chain constant (C) region gene with the human C kappa gene. Mice homozygous for the replacement mutation (C kappa R) produced normal concentrations of serum antibodies, most of which carry chimeric kappa light chains, and mounted normal immune responses to hapten-protein conjugates. This technology provides a feasible option for the generation of high-affinity humanized antibodies by means of the powerful somatic hypermutation-selection mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, Y R -- Gu, H -- Rajewsky, K -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1271-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235658" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Gene Rearrangement ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Constant Regions/*biosynthesis/genetics ; Immunoglobulin Isotypes/biosynthesis ; Immunoglobulin kappa-Chains/*biosynthesis/genetics ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Mutation ; Polymerase Chain Reaction ; Recombinant Fusion Proteins/biosynthesis ; Stem Cells ; Transfection
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  • 48
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    Requirement for Cdk2 in cytostatic factor-mediated metaphase II arrest (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: The unfertilized eggs of vertebrates are arrested in metaphase of meiosis II because of the activity of cytostatic factor (CSF). Xenopus CSF is thought to contain the product of the Mos proto-oncogene, but other proteins synthesized during meiosis II are also required for arrest induced by CSF. In Xenopus oocytes, ablation of synthesis of cyclin-dependent kinase 2 (Cdk2) during meiosis resulted in absence of the metaphase II block, even though the Mosxe protein kinase was fully active at metaphase. Introduction of purified Cdk2 restored metaphase II arrest, and increasing the amount of Cdk2 during meiosis I (when Mosxe is present) led to metaphase arrest at meiosis I. These data indicate that metaphase arrest is a result of cooperation between a proto-oncogene kinase and a cyclin-dependent kinase and illustrate the interaction of a cell growth regulator with a cell cycle control element.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrielli, B G -- Roy, L M -- Maller, J L -- F32 CA0981/CA/NCI NIH HHS/ -- GM26743/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1766-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado School of Medicine, Denver 80262.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456304" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *CDC2-CDC28 Kinases ; Cyclin-Dependent Kinase 2 ; *Cyclin-Dependent Kinases ; Female ; Meiosis/*physiology ; Metaphase/*physiology ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Oocytes/*cytology/drug effects/metabolism ; Phosphorylation ; Poly A/metabolism ; Progesterone/pharmacology ; Protein Kinases/genetics/*physiology ; *Protein-Serine-Threonine Kinases ; *Proto-Oncogene Proteins c-mos/metabolism/*physiology ; RNA, Messenger/metabolism ; Xenopus ; Xenopus Proteins
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    Regulation of lymphoid-specific immunoglobulin mu heavy chain gene enhancer by ETS-domain proteins (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-02
    Description: The enhancer for the immunoglobulin mu heavy chain gene (IgH) activates a heterologous gene at the pre-B cell stage of B lymphocyte differentiation. A lymphoid-specific element, microB, is necessary for enhancer function in pre-B cells. A microB binding protein is encoded by the PU.1/Spi-1 proto-oncogene. Another sequence element, microA, was identified in the mu enhancer that binds the product of the ets-1 proto-oncogene. The microA motif was required for microB-dependent enhancer activity, which suggests that a minimal B cell-specific enhancer is composed of both the PU.1 and Ets-1 binding sites. Co-expression of both PU.1 and Ets-1 in nonlymphoid cells trans-activated reporter plasmids that contained the minimal mu enhancer. These results implicate two members of the Ets family in the activation of IgH gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelsen, B -- Tian, G -- Erman, B -- Gregoire, J -- Maki, R -- Graves, B -- Sen, R -- 1K04GM00563/GM/NIGMS NIH HHS/ -- GM38663/GM/NIGMS NIH HHS/ -- GM38925/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):82-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Research Center, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8316859" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/cytology/*metabolism ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA-Binding Proteins/*genetics/metabolism ; *Enhancer Elements, Genetic ; Female ; Genes, Immunoglobulin ; Humans ; Immunoglobulin mu-Chains/*genetics ; Molecular Sequence Data ; Mutation ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/*genetics/metabolism ; Proto-Oncogene Proteins c-ets ; Retroviridae Proteins, Oncogenic ; Transcription Factors/*genetics/metabolism
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    Regional codon randomization: defining a TATA-binding protein surface required for RNA polymerase III transcription (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-08
    Description: The TATA-binding protein (TBP) is required for transcription by all three nuclear RNA polymerases. TBP was subjected to regional codon randomization, a codon-based mutagenesis method that generates complex yet compact protein libraries. Analysis of 186 temperature-sensitive TBP mutants yielded 65 specifically defective in transcription by RNA polymerase III (Pol III). These mutants map to a limited TBP surface that may interact with Tds4, a component of the Pol III transcription factor TFIIIB. Strains that contain the Pol III-defective derivatives have increased amounts of messenger RNA, which suggests that competition among TBP-interacting factors for limiting quantities of TBP determines the ratio of Pol II and Pol III transcription in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cormack, B P -- Struhl, K -- GM 30186/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 8;262(5131):244-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Base Sequence ; *Codon ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Mutagenesis ; RNA Polymerase III/*metabolism ; RNA, Messenger/genetics ; RNA, Ribosomal/genetics ; RNA, Transfer/genetics ; Random Allocation ; Saccharomyces cerevisiae/genetics ; *TATA Box ; TATA-Box Binding Protein ; Temperature ; Transcription Factor TFIIIB ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic
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    Interleukin-7: a cofactor for V(D)J rearrangement of the T cell receptor beta gene (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-02
    Description: The diversity of the T cell receptor repertoire is generated by rearrangement of gene elements in immature thymocytes. To identify a thymic signal that induces this rearrangement, a variety of agents were tested for their ability to induce rearrangement of the T cell receptor beta gene in suspensions of thymocytes from mouse embryos at day 14 of gestation. Of 16 agents tested, only interleukin-7 (IL-7) induced V(D)J gene rearrangement and sustained expression of the RAG-1 and RAG-2 genes, which are known to control rearrangement. These data implicate IL-7, a cytokine that is abundantly expressed in embryonic thymus, in driving gene rearrangement during early T cell development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muegge, K -- Vila, M P -- Durum, S K -- New York, N.Y. -- Science. 1993 Jul 2;261(5117):93-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Carcinogenesis and Development Program, Program Resources Inc./Dyncorp, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7686307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Cell Survival/drug effects ; Cells, Cultured ; *DNA-Binding Proteins ; Gene Expression ; *Gene Rearrangement, beta-Chain T-Cell Antigen Receptor ; Genes, RAG-1 ; Hematopoietic Cell Growth Factors/pharmacology ; Interleukin-7/*pharmacology ; Ionomycin/pharmacology ; Mice ; Molecular Sequence Data ; Organ Culture Techniques ; Proteins/genetics ; Stem Cell Factor ; T-Lymphocytes/cytology/*immunology ; Tetradecanoylphorbol Acetate/pharmacology ; Thymus Gland/embryology/immunology ; Tumor Cells, Cultured
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    Neuroprotective effects of glutamate antagonists and extracellular acidity (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Glutamate antagonists protect neurons from hypoxic injury both in vivo and in vitro, but in vitro studies have not been done under the acidic conditions typical of hypoxia-ischemia in vivo. Consistent with glutamate receptor antagonism, extracellular acidity reduced neuronal death in murine cortical cultures that were deprived of oxygen and glucose. Under these acid conditions, N-methyl-D-aspartate and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate-kainate antagonists further reduced neuronal death, such that some neurons tolerated prolonged oxygen and glucose deprivation almost as well as did astrocytes. Neuroprotection induced by this combination exceeded that induced by glutamate antagonists alone, suggesting that extracellular acidity has beneficial effects beyond the attenuation of ionotropic glutamate receptor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaku, D A -- Giffard, R G -- Choi, D W -- NS 01425/NS/NINDS NIH HHS/ -- NS 26907/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1516-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Neurological 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/8389056" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Death/drug effects ; Cell Hypoxia/physiology ; Cells, Cultured ; Cerebral Cortex/cytology ; *Excitatory Amino Acid Antagonists ; Extracellular Space/*metabolism ; Glucose/deficiency ; *Hydrogen-Ion Concentration ; L-Lactate Dehydrogenase/metabolism ; Mice ; Nerve Degeneration/drug effects ; Neurons/*drug effects/enzymology ; Receptors, AMPA ; Receptors, Kainic Acid ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors
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    Protein design by binary patterning of polar and nonpolar amino acids (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-10
    Description: A general strategy is described for the de novo design of proteins. In this strategy the sequence locations of hydrophobic and hydrophilic residues were specified explicitly, but the precise identities of the side chains were not constrained and varied extensively. This strategy was tested by constructing a large collection of synthetic genes whose protein products were designed to fold into four-helix bundle proteins. Each gene encoded a different amino acid sequence, but all sequences shared the same pattern of polar and nonpolar residues. Characterization of the expressed proteins indicated that most of the designed sequences folded into compact alpha-helical structures. Thus, a simple binary code of polar and nonpolar residues arranged in the appropriate order can drive polypeptide chains to collapse into globular alpha-helical folds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamtekar, S -- Schiffer, J M -- Xiong, H -- Babik, J M -- Hecht, M H -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1680-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8259512" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Codon ; Gene Library ; Genes, Synthetic ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Proteins/*chemistry/genetics/isolation & purification
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    Interaction between transcription regulatory regions of prolactin chromatin (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-09
    Description: The regulation of transcription requires complex interactions between proteins bound to DNA sequences that are often separated by hundreds of base pairs. As demonstrated by a nuclear ligation assay, the distal enhancer and the proximal promoter regions of the rat prolactin gene were found to be juxtaposed. By acting through its receptor bound to the distal enhancer, estrogen stimulated the interaction between the distal and proximal regulatory regions two- to threefold compared to control values. Thus, the chromatin structure of the prolactin gene may facilitate the occurrence of protein-protein interactions between transcription factors bound to widely separated regulatory elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cullen, K E -- Kladde, M P -- Seyfred, M A -- DK42731/DK/NIDDK NIH HHS/ -- T32HD07048/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 9;261(5118):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8327891" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Chromatin/*chemistry/metabolism ; DNA/chemistry/metabolism ; Deoxyribonucleases, Type II Site-Specific ; *Enhancer Elements, Genetic ; Estrogens/metabolism ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Prolactin/*genetics ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Rats ; Receptors, Estrogen/metabolism ; Regulatory Sequences, Nucleic Acid ; *Transcription, Genetic
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    Molecular mechanism of transcription-repair coupling (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-02
    Description: Lesions in the transcribed strand block transcription and are repaired more rapidly than lesions in the nontranscribed (coding) strand which do not block RNA polymerase (RNAP). It has been shown previously that in Escherichia coli the mfd (mutation frequency decline) gene is necessary for strand-specific repair. The mfd gene was cloned and sequenced and the Mfd protein was purified and used to reconstitute strand-specific repair in a completely defined system. The mfd gene encodes a protein of 130 kilodaltons and contains the so-called "helicase motifs," a leucine zipper motif, and regions of sequence similarity to UvrB and RecG proteins. The Mfd protein was shown to (i) displace RNAP stalled at a lesion in an adenosine triphosphate-dependent reaction, (ii) bind to the damage recognition subunit (UvrA) of the excision nuclease, and (iii) stimulate the repair of the transcribed strand only when transcription is taking place. Thus, Mfd appears to target the transcribed strand for repair by recognizing a stalled RNAP and actively recruiting the repair enzyme to the transcription blocking lesion as it dissociates the stalled RNAP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selby, C P -- Sancar, A -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):53-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465200" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*genetics/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; *DNA Helicases ; DNA Repair/*genetics ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Endodeoxyribonucleases/metabolism ; Escherichia coli/*genetics ; *Escherichia coli Proteins ; Leucine Zippers ; Molecular Sequence Data ; Multienzyme Complexes/chemistry/genetics ; Mutation/genetics ; Transcription Factors/chemistry/*genetics/metabolism ; *Transcription, Genetic
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    Dense nonsymmetrical DNA methylation resulting from repeat-induced point mutation in Neurospora (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-10
    Description: Cytosine methylation has been implicated in epigenetic control of gene expression in animals, plants, and fungi. It has been assumed that all methylation in eukaryotes is at symmetrical sequences such as CpG/GpC, because this can explain perpetuation of methylation states. Here the bisulfite genomic sequencing method was used to examine methylation in DNA from a Neurospora gene exposed to repeat-induced point mutation. 5-Methylcytosine was not limited to symmetrical sites and individual molecules showed different patterns and amounts of modification. The methylation extended beyond the mutated region and even beyond the edge of the duplicated segment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selker, E U -- Fritz, D Y -- Singer, M J -- GM 35690/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1724-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8259516" target="_blank"〉PubMed〈/a〉
    Keywords: 5-Methylcytosine ; Base Sequence ; Blotting, Southern ; Cytosine/*analogs & derivatives/analysis ; DNA Restriction Enzymes ; DNA, Fungal/chemistry/*metabolism ; DNA-Binding Proteins/genetics ; Fungal Proteins/genetics ; Genes, Fungal ; Glutamate Dehydrogenase/*genetics ; Methylation ; Molecular Sequence Data ; Neurospora crassa/enzymology/*genetics ; Point Mutation
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    DNA conformation-induced activation of an enediyne for site-specific cleavage (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-03
    Description: Neocarzinostatin chromophore (NCS chrom) was found to induce site-specific cleavage at the 3' side of a bulge in single-stranded DNA in the absence of thiol. This reaction involved the oxidative formation of a DNA fragment with a nucleoside 5'-aldehyde at its 5' terminus and generated an ultraviolet light-absorbing and fluorescent species of post-activated drug containing tritium abstracted from the carbon at the 5' position of the target nucleotide. The DNAs containing point mutations that disrupt the bulge were not cleavage substrates and did not generate this drug product. Thus, DNA is an active participant in its own destruction, and NCS chrom may be useful as a probe for bulged structures in nucleic acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kappen, L S -- Goldberg, I H -- CA44257/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 3;261(5126):1319-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8362243" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biotransformation ; *DNA Damage ; DNA, Single-Stranded/chemistry/*drug effects/genetics/metabolism ; Enediynes ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oxidation-Reduction ; Piperidines/pharmacology ; Point Mutation ; Sulfhydryl Compounds/pharmacology ; Zinostatin/*analogs & derivatives/chemistry/metabolism/pharmacology
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    Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-05
    Description: The actions of many hormones and neurotransmitters are mediated by the members of a superfamily of receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins). These receptors are characterized by a highly conserved topographical arrangement in which seven transmembrane domains are connected by intracellular and extracellular loops. The interaction between these receptors and G proteins is mediated in large part by the third intracellular loop of the receptor. Coexpression of the third intracellular loop of the alpha 1B-adrenergic receptor with its parent receptor inhibited receptor-mediated activation of phospholipase C. The inhibition extended to the closely related alpha 1C-adrenergic receptor subtype, but not the phospholipase C-coupled M1 muscarinic acetylcholine receptor nor the adenylate cyclase-coupled D1A dopamine receptor. These results suggest that the receptor-G protein interface may represent a target for receptor antagonist drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luttrell, L M -- Ostrowski, J -- Cotecchia, S -- Kendall, H -- Lefkowitz, R J -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1453-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/8383880" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cyclic AMP/metabolism ; Cytoplasm/metabolism ; GTP-Binding Proteins/*metabolism ; Globins/genetics ; Glutathione Transferase/genetics/metabolism ; Humans ; Inositol Phosphates/metabolism ; Kinetics ; Molecular Sequence Data ; Muscarinic Antagonists ; Oligodeoxyribonucleotides ; Plasmids ; Protein Structure, Secondary ; Receptors, Adrenergic, alpha/genetics/*metabolism ; Receptors, Dopamine D1/antagonists & inhibitors/genetics/*metabolism ; Receptors, Muscarinic/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transfection ; Type C Phospholipases/metabolism
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    Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-07
    Description: Previously known 5' exonucleases of several eubacterial DNA polymerases have now been shown to be structure-specific endonucleases that cleave single-stranded DNA or RNA at the bifurcated end of a base-paired duplex. Cleavage was not coupled to synthesis, although primers accelerated the rate of cleavage considerably. The enzyme appeared to gain access to the cleavage site by moving from the free end of a 5' extension to the bifurcation of the duplex, where cleavage took place. Single-stranded 5' arms up to 200 nucleotides long were cleaved from such a duplex. Essentially any linear single-stranded nucleic acid can be targeted for specific cleavage by the 5' nuclease of DNA polymerase through hybridization with an oligonucleotide that converts the desired cleavage site into a substrate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyamichev, V -- Brow, M A -- Dahlberg, J E -- 30220/PHS HHS/ -- New York, N.Y. -- Science. 1993 May 7;260(5109):778-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomolecular Chemistry, University of Wisconsin School of Medicine, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7683443" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Single-Stranded/*metabolism ; DNA-Directed DNA Polymerase/*metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*metabolism ; RNA/*metabolism ; Taq Polymerase ; Templates, Genetic
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    Inhibition of viral replication by interferon-gamma-induced nitric oxide synthase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-10
    Description: Interferons (IFNs) induce antiviral activity in many cell types. The ability of IFN-gamma to inhibit replication of ectromelia, vaccinia, and herpes simplex-1 viruses in mouse macrophages correlated with the cells' production of nitric oxide (NO). Viral replication was restored in IFN-gamma-treated macrophages exposed to inhibitors of NO synthase. Conversely, epithelial cells with no detectable NO synthesis restricted viral replication when transfected with a complementary DNA encoding inducible NO synthase or treated with organic compounds that generate NO. In mice, an inhibitor of NO synthase converted resolving ectromelia virus infection into fulminant mousepox. Thus, induction of NO synthase can be necessary and sufficient for a substantial antiviral effect of IFN-gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karupiah, G -- Xie, Q W -- Buller, R M -- Nathan, C -- Duarte, C -- MacMicking, J D -- CA43610/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1445-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7690156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/*biosynthesis/metabolism ; Animals ; Arginine/analogs & derivatives/pharmacology ; Cell Line ; Cells, Cultured ; Ectromelia virus/drug effects/*physiology ; Ectromelia, Infectious/microbiology ; Enzyme Induction ; Female ; Humans ; Interferon-gamma/*pharmacology ; Macrophages/*microbiology ; Mice ; Mice, Inbred C57BL ; Nitric Oxide/metabolism/pharmacology ; Nitric Oxide Synthase ; Simplexvirus/drug effects/physiology ; Transfection ; Vaccinia virus/drug effects/physiology ; *Virus Replication/drug effects ; omega-N-Methylarginine
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    Developmental regulation of neural response to FGF-1 and FGF-2 by heparan sulfate proteoglycan (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-02
    Description: Murine neural precursor cells and cell lines derived from them are stimulated by members of the heparin-binding fibroblast growth factor (FGF) family. The activity of FGF is regulated by heparan sulfate proteoglycans (HSPGs), and this interaction is an essential prerequisite for the binding of growth factor to the signal transducing receptors. Messenger RNA for FGF-2 was detectable in the neuroepithelium at embryonic day 9, and the HSPGs produced by these cells at this time preferentially bound FGF-2. However, at embryonic day 11, when messenger RNA for FGF-1 was first detectable, there was a switch in the binding specificity of the HSPG to FGF-1. Thus, a single species of HSPG undergoes a rapid, tightly controlled change in growth factor-binding specificity concomitant with the temporal expression of the FGFs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nurcombe, V -- Ford, M D -- Wildschut, J A -- Bartlett, P F -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, University of Melbourne, Parkville, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682010" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cells, Cultured ; Culture Media, Conditioned ; Epithelium/chemistry/embryology ; Fibroblast Growth Factor 1/genetics/*pharmacology ; Fibroblast Growth Factor 2/genetics/*pharmacology ; Gene Expression ; Gestational Age ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate/*pharmacology ; Mice ; Molecular Weight ; Nervous System/chemistry/*embryology/metabolism ; Neurons/cytology ; Polysaccharide-Lyases/metabolism ; Proteoglycans/*pharmacology ; RNA, Messenger/analysis ; Signal Transduction/physiology ; Stem Cells/cytology
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    AIDS theories (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curtis, T -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418488" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Acquired Immunodeficiency Syndrome/immunology/*transmission ; Animals ; Cells, Cultured ; *Hiv-1 ; Haplorhini ; Humans ; Kidney ; Male
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    Mice lacking TdT: mature animals with an immature lymphocyte repertoire (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-27
    Description: In adult animals, template-independent (or N) nucleotides are frequently added during the rearrangement of variable (V), diversity (D), and joining (J) segments of lymphocyte receptor genes, greatly enhancing junctional diversity. Receptor genes from adult mice carrying a mutation in the terminal deoxynucleotidyl transferase (TdT) gene have few N nucleotides, providing proof that this enzyme is essential for creating diversity. Unlike those from normal adults, receptor genes from adult mutant mice show extensive evidence of homology-directed recombination, suggesting that TdT blocks this process. Thus, switch-on of the TdT gene during the first week after birth provokes an even greater expansion of lymphocyte receptor diversity than had previously been thought.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilfillan, S -- Dierich, A -- Lemeur, M -- Benoist, C -- Mathis, D -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1175-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, Institut de Chimie Biologique, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356452" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Nucleotidylexotransferase/genetics/*metabolism ; Gene Rearrangement, B-Lymphocyte ; Gene Rearrangement, T-Lymphocyte ; *Genes, Immunoglobulin ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Variable Region/genetics ; Lymphocytes/*immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Nucleotides/*metabolism ; Receptors, Antigen, T-Cell/*genetics ; Recombination, Genetic
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    Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-15
    Description: Unlike most serine proteases of the chymotrypsin family, tissue-type plasminogen activator (tPA) is secreted from cells as an active, single-chain enzyme with a catalytic efficiency only slightly lower than that of the proteolytically cleaved form. A zymogenic mutant of tPA has been engineered that displays a reduction in catalytic efficiency by a factor of 141 in the single-chain form while retaining full activity in the cleaved form. The residues introduced in the mutant, serine 292 and histidine 305, are proposed to form a hydrogen-bonded network with aspartate 477, similar to the aspartate 194-histidine 40-serine 32 network found to stabilize the zymogen chymotrypsinogen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madison, E L -- Kobe, A -- Gething, M J -- Sambrook, J F -- Goldsmith, E J -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):419-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, 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/8211162" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/chemistry ; Base Sequence ; Catalysis ; Chymotrypsin/chemistry/metabolism ; Enzyme Precursors/chemistry/*metabolism ; Histidine/chemistry ; Hydrogen Bonding ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Plasminogen/metabolism ; Plasminogen Activator Inhibitor 1/metabolism ; Serine/chemistry ; Tissue Plasminogen Activator/chemistry/genetics/*metabolism
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    Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-20
    Description: Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation Ala4 to Val in exon 1 was the most frequent one; mutations were identified in exons 2, 4, and 5 but not in the active site region formed by exon 3. The 2.4 A crystal structure of human SOD, along with two other SOD structures, established that all 12 observed FALS mutant sites alter conserved interactions critical to the beta-barrel fold and dimer contact, rather than catalysis. Red cells from heterozygotes had less than 50 percent normal SOD activity, consistent with a structurally defective SOD dimer. Thus, defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of FALS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deng, H X -- Hentati, A -- Tainer, J A -- Iqbal, Z -- Cayabyab, A -- Hung, W Y -- Getzoff, E D -- Hu, P -- Herzfeldt, B -- Roos, R P -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1047-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amyotrophic Lateral Sclerosis/enzymology/*genetics ; Base Sequence ; Binding Sites ; Erythrocytes/enzymology ; Exons ; Free Radicals/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Folding ; Protein Structure, Tertiary ; Superoxide Dismutase/blood/chemistry/*genetics/metabolism ; X-Ray Diffraction
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    A yeast protein similar to bacterial two-component regulators (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-10-22
    Description: Many bacterial signaling pathways involve a two-component design. In these pathways, a sensor kinase, when activated by a signal, phosphorylates its own histidine, which then serves as a phosphoryl donor to an aspartate in a response regulator protein. The Sln1 protein of the yeast Saccharomyces cerevisiae has sequence similarities to both the histidine kinase and the response regulator proteins of bacteria. A missense mutation in SLN1 is lethal in the absence but not in the presence of the N-end rule pathway, a ubiquitin-dependent proteolytic system. The finding of SLN1 demonstrates that a mode of signal transduction similar to the bacterial two-component design operates in eukaryotes as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ota, I M -- Varshavsky, A -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):566-9.〈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/8211183" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/metabolism ; Base Sequence ; Fungal Proteins/chemistry/*genetics/metabolism ; Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; *Ligases ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics/growth & development/metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; *Signal Transduction ; *Ubiquitin-Protein Ligases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Heterologous protection against influenza by injection of DNA encoding a viral protein (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-19
    Description: Cytotoxic T lymphocytes (CTLs) specific for conserved viral antigens can respond to different strains of virus, in contrast to antibodies, which are generally strain-specific. The generation of such CTLs in vivo usually requires endogenous expression of the antigen, as occurs in the case of virus infection. To generate a viral antigen for presentation to the immune system without the limitations of direct peptide delivery or viral vectors, plasmid DNA encoding influenza A nucleoprotein was injected into the quadriceps of BALB/c mice. This resulted in the generation of nucleoprotein-specific CTLs and protection from a subsequent challenge with a heterologous strain of influenza A virus, as measured by decreased viral lung titers, inhibition of mass loss, and increased survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, J B -- Donnelly, J J -- Parker, S E -- Rhodes, G H -- Felgner, P L -- Dwarki, V J -- Gromkowski, S H -- Deck, R R -- DeWitt, C M -- Friedman, A -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1745-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Research, Merck Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456302" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA, Viral/*genetics/therapeutic use ; Gene Expression ; Genetic Vectors ; Histocompatibility Antigens Class I/immunology ; Immunization ; Influenza A virus/*genetics/immunology/isolation & purification ; Lung/microbiology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Muscles/metabolism ; Nucleoproteins/*genetics/*immunology ; Orthomyxoviridae Infections/microbiology/*prevention & control ; Plasmids ; *RNA-Binding Proteins ; T-Lymphocytes, Cytotoxic/immunology ; Transfection ; Viral Core Proteins/*genetics/*immunology ; Viral Vaccines/*genetics
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    Expression of two T cell receptor alpha chains: dual receptor T cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-15
    Description: Although many T cells carry two in-frame V alpha rearrangements, the products of both V alpha rearrangements have never been shown simultaneously on the surface of normal cells. With the use of monoclonal antibodies to V alpha 2, V alpha 12, and V alpha 24, up to one-third of mature T cells expressed two V alpha chains as part of two functional and independent T cell receptors (TCRs). Thus, the "one cell, one receptor" rule does not apply to a large subset of alpha beta T cells. Cells that belong to this dual TCR subset may be specific for a broader range of antigens than cells with a single receptor, which may be important for autoimmunity and alloreactivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Padovan, E -- Casorati, G -- Dellabona, P -- Meyer, S -- Brockhaus, M -- Lanzavecchia, A -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):422-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211163" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Antigens, CD3/analysis ; Base Sequence ; Gene Rearrangement, alpha-Chain T-Cell Antigen Receptor ; Humans ; Molecular Sequence Data ; Receptors, Antigen, T-Cell, alpha-beta/*analysis/genetics/immunology ; T-Lymphocytes/*immunology
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    A functional recombinant myosin II lacking a regulatory light chain-binding site (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs). Dictyostelium myosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uyeda, T Q -- Spudich, J A -- GM46551/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1867-70.〈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/8266074" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Ca(2+) Mg(2+)-ATPase/metabolism ; Calcium-Transporting ATPases/metabolism ; Cell Division ; Dictyostelium/cytology/genetics/*metabolism ; Genes, Fungal ; Molecular Sequence Data ; Myosin-Light-Chain Kinase/metabolism ; Myosins/chemistry/genetics/*metabolism ; Phosphorylation ; Recombinant Proteins/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular biology. New EMBL director reaches out to southern Europe (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1740-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511576" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes ; Base Sequence ; Europe ; Genome ; Human Genome Project ; *Molecular Biology
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    Knotting of a DNA chain during ring closure (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-23
    Description: The formation of knotted species on random ring closure of two DNAs that are 5.6 kilobase pairs (kbp) and 8.6 kbp in length was measured, and these data were used to calculate the effective DNA helix diameter as a function of sodium ion and magnesium ion concentration. In the presence of more than 50 mM magnesium ion, interactions between DNA segments appear to be attractive rather than repulsive. The free energy of formation of relaxed trefoil and figure-eight DNA knots and of supercoiled trefoil DNA knots was also evaluated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, S Y -- Wang, J C -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):533-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harvard University, Department of Biochemistry and Molecular Biology, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8475384" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry/metabolism ; DNA, Circular/*chemistry/metabolism ; DNA, Single-Stranded/chemistry ; DNA, Superhelical/*chemistry/metabolism ; Magnesium/pharmacology ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Probability ; Sodium Chloride/pharmacology ; Thermodynamics
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    Surface expression of two distinct functional antigen receptors on human gamma delta T cells (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-06-18
    Description: Lymphocytes recognize antigens with highly variable heterodimeric surface receptors. Although four distinct antigen receptors could in principle be produced by any lymphocyte, only one functional combination of receptor chains has thus far been found expressed on their surface. Examination of human gamma delta T cells revealed a population that violated this rule by expressing on their surface two distinct functional gamma delta T cell receptors (TCRs) that used different TCR gamma gene alleles. Thus, current models for T cell clonal selection may need modification, and a possible escape mechanism for autoreactive TCRs is suggested.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davodeau, F -- Peyrat, M A -- Houde, I -- Hallet, M M -- De Libero, G -- Vie, H -- Bonneville, M -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1800-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U211, Institut de Biologie, Nantes, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8390096" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Cell Line ; Cytotoxicity, Immunologic ; *Gene Expression ; Gene Rearrangement, gamma-Chain T-Cell Antigen Receptor ; Humans ; Molecular Sequence Data ; Receptors, Antigen, T-Cell, gamma-delta/analysis/*genetics/immunology ; T-Lymphocytes/*immunology ; T-Lymphocytes, Cytotoxic/*immunology
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    Beta-adrenergic receptor kinase-2 and beta-arrestin-2 as mediators of odorant-induced desensitization (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-05
    Description: beta-Adrenergic receptor kinase (beta ARK) and beta-arrestin function in the homologous or agonist-activated desensitization of G protein-coupled receptors. The isoforms beta ARK-2 and beta-arrestin-2 are highly enriched in and localized to the dendritic knobs and cilia of the olfactory receptor neurons where the initial events of olfactory signal transduction occur. Odorants induce a rapid and transient elevation of adenosine 3',5'-monophosphate (cAMP), which activates a nonspecific cation channel and produces membrane depolarization. Preincubation of rat olfactory cilia with antibodies raised against beta ARK-2 and beta-arrestin-2 increased the odorant-induced elevation of cAMP and attenuated desensitization. These results suggest that beta ARK-2 and beta-arrestin-2 mediate agonist-dependent desensitization in olfaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dawson, T M -- Arriza, J L -- Jaworsky, D E -- Borisy, F F -- Attramadal, H -- Lefkowitz, R J -- Ronnett, G V -- NS 01578-01/NS/NINDS NIH HHS/ -- NS-02131/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):825-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins Medical Institutions, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8381559" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/*metabolism ; *Arrestins ; Cells, Cultured ; Cyclic AMP/metabolism ; *Cyclic AMP-Dependent Protein Kinases ; Cytosol/metabolism ; Dendrites/physiology ; Eye Proteins/*metabolism ; G-Protein-Coupled Receptor Kinase 2 ; GTP-Binding Proteins/*metabolism ; Isoenzymes/metabolism ; Male ; Mechanoreceptors/*physiology ; Neurons/*physiology ; *Odors ; Olfactory Bulb/*physiology ; Protein Kinases/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Adrenergic, beta/*physiology ; Signal Transduction ; *Smell ; Testis/physiology ; Turbinates/*physiology ; beta-Adrenergic Receptor Kinases
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    Proliferation of human smooth muscle cells promoted by lipoprotein(a) (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-06-11
    Description: Elevated blood concentrations of lipoprotein(a) [Lp(a)] and its constituent, apolipoprotein(a) [apo(a)], constitute a major risk factor for atherosclerosis, but their physiological activities remain obscure. Lp(a) and purified apo(a) stimulated the growth of human smooth muscle cells in culture. This effect resulted from inhibition of plasminogen activation, and consequently the activation by plasmin of latent transforming growth factor-beta, which is an inhibitor of smooth muscle cell growth. Because smooth muscle proliferation is one of the hallmarks of atherosclerotic lesions, these results point to a plausible mechanism for the atherogenic activity of Lp(a).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grainger, D J -- Kirschenlohr, H L -- Metcalfe, J C -- Weissberg, P L -- Wade, D P -- Lawn, R M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1655-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoproteins/physiology ; Apoprotein(a) ; Cell Division/drug effects/physiology ; Cells, Cultured ; Fibrinolysin/physiology ; Humans ; Lipoprotein(a)/*physiology ; Muscle, Smooth, Vascular/*cytology/metabolism ; Plasminogen Activators/metabolism ; Rats ; Tamoxifen/pharmacology ; Transforming Growth Factor beta/physiology
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    Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-09-24
    Description: Zinc finger proteins, of the type first discovered in transcription factor IIIA (TFIIIA), are one of the largest and most important families of DNA-binding proteins. The crystal structure of a complex containing the five Zn fingers from the human GLI oncogene and a high-affinity DNA binding site has been determined at 2.6 A resolution. Finger one does not contact the DNA. Fingers two through five bind in the major groove and wrap around the DNA, but lack the simple, strictly periodic arrangement observed in the Zif268 complex. Fingers four and five of GLI make extensive base contacts in a conserved nine base-pair region, and this section of the DNA has a conformation intermediate between B-DNA and A-DNA. Analyzing the GLI complex and comparing it with Zif268 offers new perspectives on Zn finger-DNA recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pavletich, N P -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1701-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8378770" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Computer Graphics ; DNA/*chemistry/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oncogene Proteins/*chemistry/genetics/metabolism ; Oncogenes ; Protein Conformation ; Trans-Activators ; Transcription Factors/*chemistry/genetics/metabolism ; X-Ray Diffraction ; *Zinc Fingers
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    DNA sequence determination by hybridization: a strategy for efficient large-scale sequencing (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-06-11
    Description: The concept of sequencing by hybridization (SBH) makes use of an array of all possible n-nucleotide oligomers (n-mers) to identify n-mers present in an unknown DNA sequence. Computational approaches can then be used to assemble the complete sequence. As a validation of this concept, the sequences of three DNA fragments, 343 base pairs in length, were determined with octamer oligonucleotides. Possible applications of SBH include physical mapping (ordering) of overlapping DNA clones, sequence checking, DNA fingerprinting comparisons of normal and disease-causing genes, and the identification of DNA fragments with particular sequence motifs in complementary DNA and genomic libraries. The SBH techniques may accelerate the mapping and sequencing phases of the human genome project.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drmanac, R -- Drmanac, S -- Strezoska, Z -- Paunesku, T -- Labat, I -- Zeremski, M -- Snoddy, J -- Funkhouser, W K -- Koop, B -- Hood, L -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1649-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological and Medical Research Division, Argonne National Laboratory, IL 60439.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; Humans ; Macaca mulatta ; Molecular Sequence Data ; *Nucleic Acid Hybridization ; Oligonucleotide Probes ; Sequence Analysis, DNA/*methods
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    Identification of a whitefly species by genomic and behavioral studies (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-01
    Description: An introduced whitefly species, responsible for over a half billion dollars in damage to U.S. agricultural production in 1991, is morphologically indistinguishable from Bemisia tabaci (Gennadius). However, with the use of polymerase chain reaction-based DNA differentiation tests, allozymic frequency analyses, crossing experiments, and mating behavior studies, the introduced whitefly is found to be a distinct species. Recognition of this new species, the silverleaf whitefly, is critical in the search for management options.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perring, T M -- Cooper, A D -- Rodriguez, R J -- Farrar, C A -- Bellows, T S Jr -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):74-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of California, Riverside 92521.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418497" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Crosses, Genetic ; DNA/genetics ; Diptera/*classification/genetics/*physiology ; Enzymes/genetics ; Female ; Genetic Linkage ; Male ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Sexual Behavior, Animal ; United States
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    WT1-mediated growth suppression of Wilms tumor cells expressing a WT1 splicing variant (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-24
    Description: A human Wilms tumor cell line (RM1) was developed to test the tumor suppressor activity of WT1, a zinc finger transcription factor that is expressed in the developing human kidney and is mutationally inactivated in a subset of Wilms tumors. Transfection of each of four wild-type WT1 isoforms suppressed the growth of RM1 cells. The endogenous WT1 transcript in these cells was devoid of exon 2 sequences, a splicing alteration that was also detected in varying amounts in all Wilms tumors tested but not in normal kidney. Production of this abnormal transcript, which encodes a functionally altered protein, may represent a distinct mechanism for inactivating WT1 in Wilms tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haber, D A -- Park, S -- Maheswaran, S -- Englert, C -- Re, G G -- Hazen-Martin, D J -- Sens, D A -- Garvin, A J -- CA37887/CA/NCI NIH HHS/ -- CA58596/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2057-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Massachusetts General Hospital Cancer Center, Boston 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266105" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division/genetics ; DNA-Binding Proteins/biosynthesis/*genetics/physiology ; Genes, Wilms Tumor/genetics/*physiology ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasm Transplantation ; RNA, Messenger/genetics ; Tumor Cells, Cultured ; WT1 Proteins ; Wilms Tumor/*genetics/*pathology
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    Protein-induced bending as a transcriptional switch (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-07
    Description: The question of whether protein-induced DNA bending can act as a switch factor when placed upstream of an array of promoters located in tandem was investigated in vivo. The catabolite activating protein binding site of the fur operon was replaced by the binding site of the RepA repressor protein, which is able to bend DNA immediately after binding. Appropriately phased induced bending could act as a transcriptional switch factor in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perez-Martin, J -- Espinosa, M -- New York, N.Y. -- Science. 1993 May 7;260(5109):805-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centro de Investigaciones Biologicas, Consejo Superior de Investigaciones Cientificas, Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8387228" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Base Sequence ; Cyclic AMP Receptor Protein/*metabolism ; *DNA Helicases ; DNA, Bacterial/chemistry/*genetics/metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/genetics ; Gene Expression Regulation, Bacterial ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Operon ; *Promoter Regions, Genetic ; *Proteins ; Repressor Proteins/genetics ; *Trans-Activators ; *Transcription, Genetic
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  • 80
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    Relation of phenotype evolution of HIV-1 to envelope V2 configuration (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Biological variability of human immunodeficiency virus type-1 (HIV-1) is involved in the pathogenesis of acquired immunodeficiency syndrome (AIDS). Syncytium-inducing (SI) HIV-1 variants emerge in 50 percent of infected individuals during infection, preceding accelerated CD4+ T cell loss and rapid progression to AIDS. The V1 to V2 and V3 region of the viral envelope glycoprotein gp120 contained the major determinants of SI capacity. The configuration of a hypervariable locus in the V2 domain appeared to be predictive for non-SI to SI phenotype conversion. Early prediction of HIV-1 phenotype evolution may be useful for clinical monitoring and treatment of asymptomatic infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Groenink, M -- Fouchier, R A -- Broersen, S -- Baker, C H -- Koot, M -- van't Wout, A B -- Huisman, H G -- Miedema, F -- Tersmette, M -- Schuitemaker, H -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Clinical Viro-Immunology, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502996" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Consensus Sequence ; Genetic Variation ; Giant Cells/microbiology ; HIV Envelope Protein gp120/*chemistry ; HIV Seropositivity/microbiology ; HIV-1/*chemistry/*genetics/pathogenicity ; Humans ; Male ; Molecular Sequence Data ; Phenotype ; Protein Conformation ; Recombination, Genetic
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  • 81
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    Antisense gene inhibition by oligonucleotides containing C-5 propyne pyrimidines (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Phosphorothioate oligodeoxynucleotides containing the C-5 propyne analogs of uridine and cytidine bind RNA with high affinity and are potent antisense inhibitors of gene expression. In a cellular assay, gene-specific antisense inhibition occurred at nanomolar concentrations of oligonucleotide, was dose-dependent and exquisitely sensitive to sequence mismatches, and was correlated with the melting temperature and length of oligonucleotide. Activity was independent of RNA target site and cell type but was detectable only when the oligonucleotides were microinjected or delivered with cell-permeabilizing agents. These oligonucleotides may have important applications in therapy and in studies of gene function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, R W -- Matteucci, M D -- Lewis, J G -- Gutierrez, A J -- Moulds, C -- Froehler, B C -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1510-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gilead Sciences, Inc., Foster City, CA 94404.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7684856" target="_blank"〉PubMed〈/a〉
    Keywords: Alkynes/pharmacology ; Animals ; Base Sequence ; Cell Line ; Cercopithecus aethiops ; Humans ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacokinetics/*pharmacology ; Pyrimidine Nucleotides/pharmacokinetics/*pharmacology ; RNA/*drug effects ; Rats ; Thionucleotides/pharmacokinetics/*pharmacology
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  • 82
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    Determination of type I receptor specificity by the type II receptors for TGF-beta or activin (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-05
    Description: Transforming growth factor-beta (TGF-beta) and activin signal primarily through interaction with type I and type II receptors, which are transmembrane serine-threonine kinases. Tsk 7L is a type I receptor for TGF-beta and requires coexpression of the type II TGF-beta receptor for ligand binding. Tsk 7L also specifically bound activin, when coexpressed with the type IIA activin receptor. Tsk 7L could associate with either type II receptor and the ligand binding specificity of Tsk 7L was conferred by the type II receptor. Tsk 7L can therefore act as type I receptor for both activin and TGF-beta, and possibly other ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebner, R -- Chen, R H -- Lawler, S -- Zioncheck, T -- Derynck, R -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):900-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Growth and Development, and Anatomy, University of California at San Francisco 94143-0640.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235612" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; Activins ; Base Sequence ; DNA Primers ; Growth Substances/metabolism ; Humans ; Inhibins/*metabolism ; Molecular Sequence Data ; Precipitin Tests ; Protein-Serine-Threonine Kinases/*metabolism ; Receptors, Growth Factor/*metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; Transforming Growth Factor beta/*metabolism
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  • 83
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    Reconstitution of T cell receptor zeta-mediated calcium mobilization in nonlymphoid cells (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-08-13
    Description: T cell antigen receptor (TCR) activation involves interactions between receptor subunits and nonreceptor protein tyrosine kinases (PTKs). Early steps in signaling through the zeta chain of the TCR were examined in transfected COS-1 cells. Coexpression of the PTK p59fynT, but not p56lck, with zeta or with a homodimeric TCR beta-zeta fusion protein produced tyrosine phosphorylation of both zeta and phospholipase C (PLC)-gamma 1, as well as calcium ion mobilization in response to receptor cross-linking. CD45 coexpression enhanced these effects. No requirement for the PTKZAP-70 was observed. Thus, p59fynT may link zeta directly to the PLC-gamma 1 activation pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, C G -- Sancho, J -- Terhorst, C -- AI 15066/AI/NIAID NIH HHS/ -- CA 01486/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 13;261(5123):915-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, Beth Israel Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8346442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD45/analysis ; Base Sequence ; Calcium/*metabolism ; Cell Line ; Cercopithecus aethiops ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism/physiology ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-fyn ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; Type C Phospholipases/metabolism ; Tyrosine/metabolism ; ZAP-70 Protein-Tyrosine Kinase
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  • 84
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    How to drive nucleic acids up a tree (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amato, I -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):491.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682725" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Molecular Sequence Data ; *Nucleic Acid Conformation ; RNA/chemical synthesis/*chemistry
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  • 85
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    A Ca-dependent early step in the release of catecholamines from adrenal chromaffin cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-12
    Description: Intense stimuli, such as trains of depolarizing pulses or the caffeine-induced release of calcium from intracellular stores, readily depress the secretory response in neuroendocrine cells. Secretory responses are restored by rest periods of minutes in duration. This recovery was accelerated when the concentration of cytosolic calcium was moderately increased and probably resulted from calcium-dependent replenishment of a pool of release-ready granules. Continuously increased concentrations of calcium led the over-filling of such a pool. Subsequently, secretory responses to stronger calcium stimuli were augmented. Hormone-induced calcium transients with a plateau phase of increased concentration of calcium may enhance the secretory response in this way.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Ruden, L -- Neher, E -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1061-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Membrane Biophysics, Max-Planck-Institut fur biophysikalische Chemie, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235626" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Medulla/cytology/drug effects/metabolism/*secretion ; Animals ; Bradykinin/pharmacology ; Caffeine/pharmacology ; Calcium/*metabolism ; Catecholamines/metabolism/*secretion ; Cattle ; Cells, Cultured ; Chromaffin Granules/drug effects/*secretion ; Electric Conductivity ; Histamine ; Membrane Potentials ; Models, Biological ; Nystatin/pharmacology
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  • 86
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    Controlling signal transduction with synthetic ligands (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-12
    Description: Dimerization and oligomerization are general biological control mechanisms contributing to the activation of cell membrane receptors, transcription factors, vesicle fusion proteins, and other classes of intra- and extracellular proteins. Cell permeable, synthetic ligands were devised that can be used to control the intracellular oligomerization of specific proteins. To demonstrate their utility, these ligands were used to induce intracellular oligomerization of cell surface receptors that lacked their transmembrane and extracellular regions but contained intracellular signaling domains. Addition of these ligands to cells in culture resulted in signal transmission and specific target gene activation. Monomeric forms of the ligands blocked the pathway. This method of ligand-regulated activation and termination of signaling pathways has the potential to be applied wherever precise control of a signal transduction pathway is desired.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spencer, D M -- Wandless, T J -- Schreiber, S L -- Crabtree, G R -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1019-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7694365" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Carrier Proteins/*metabolism ; Cross-Linking Reagents ; Gene Expression Regulation ; Heat-Shock Proteins/*metabolism ; Ligands ; Membrane Proteins/*metabolism ; Models, Biological ; Molecular Sequence Data ; Polymers ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/*metabolism ; Tacrolimus/*analogs & derivatives/chemical synthesis/chemistry/metabolism ; Tacrolimus Binding Proteins ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
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  • 87
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    Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: PU.1 recruits the binding of a second B cell-restricted nuclear factor, NF-EM5, to a DNA site in the immunoglobulin kappa 3' enhancer. DNA binding by NF-EM5 requires a protein-protein interaction with PU.1 and specific DNA contacts. Dephosphorylated PU.1 bound to DNA but did not interact with NF-EM5. Analysis of serine-to-alanine mutations in PU.1 indicated that serine 148 (Ser148) is required for protein-protein interaction. PU.1 produced in bacteria did not interact with NF-EM5. Phosphorylation of bacterially produced PU.1 by purified casein kinase II modified it to a form that interacted with NF-EM5 and that recruited NF-EM5 to bind to DNA. Phosphopeptide analysis of bacterially produced PU.1 suggested that Ser148 is phosphorylated by casein kinase II. This site is also phosphorylated in vivo. Expression of wild-type PU.1 increased expression of a reporter construct containing the PU.1 and NF-EM5 binding sites nearly sixfold, whereas the Ser148 mutant form only weakly activated transcription. These results demonstrate that phosphorylation of PU.1 at Ser148 is necessary for interaction with NF-EM5 and suggest that this phosphorylation can regulate transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pongubala, J M -- Van Beveren, C -- Nagulapalli, S -- Klemsz, M J -- McKercher, S R -- Maki, R A -- Atchison, M L -- AI 30656/AI/NIAID NIH HHS/ -- CA 42909/CA/NCI NIH HHS/ -- GM 42415/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1622-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Biology, University of Pennsylvania, School of Veterinary Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456286" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; DNA-Binding Proteins/genetics/isolation & purification/*metabolism ; Enhancer Elements, Genetic ; Immunoglobulin kappa-Chains/genetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Phosphorylation ; Plasmacytoma ; Recombinant Proteins/isolation & purification/metabolism ; Retroviridae Proteins, Oncogenic ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured
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  • 88
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    Translocation of repetitive RNA sequences with the germ plasm in Xenopus oocytes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-10
    Description: Xlsirts are a family of interspersed repeat RNAs from Xenopus laevis that contain from 3 to 13 repeat units (each 79 to 81 nucleotides long) flanked by unique sequences. They are homologous to the mammalian Xist gene that is involved in X chromosome inactivation. Xlsirt RNA appears first in the mitochondrial cloud (Balbiani body) in stage 2 oocytes and is then translocated as island-like structures to the vegetal cortex at early stage 3 coincident with the localization of the germ plasm. Exogenous Xlsirt RNA injected into oocytes translocates to the location of the endogenous RNA at that particular stage. The Xlsirt RNA repeat sequences are required for translocation and can cause the translocation of heterologous unique RNAs to the vegetal cortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kloc, M -- Spohr, G -- Etkin, L D -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1712-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas, M.D. Anderson Cancer Center, Houston 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7505061" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary ; Female ; In Situ Hybridization ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oocytes/*metabolism ; Oogenesis ; RNA/chemistry/*metabolism ; *Repetitive Sequences, Nucleic Acid ; Xenopus laevis
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  • 89
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    Movement of the guide sequence during RNA catalysis by a group I ribozyme (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-23
    Description: Ribozymes derived from the self-splicing pre-ribosomal RNA of Tetrahymena act as sequence-specific endonucleases. The reaction involves binding an RNA or DNA substrate by base pairing to the internal guide sequence (IGS) to form helix P1. Site-specific photo-crosslinking localized the 5' end of the IGS in helix P1 to the vicinity of conserved bases between helices P4 and P5, supporting a major feature of the Michel-Westhof three-dimensional structure model. The crosslinked ribozyme retained catalytic activity. When not base-paired, the IGS was still specifically crosslinked, but the major site was 37 A distant from the reactive site in the experimentally supported three-dimensional model. The data indicate that a substantial induced-fit conformational change accompanies P1 formation, and they provide a physical basis for understanding the transport of oligonucleotides to the catalytic core of the ribozyme. The ability of RNA to orchestrate large-scale conformational changes may help explain why the ribosome and the spliceosome are RNA-based machines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J F -- Downs, W D -- Cech, T R -- New York, N.Y. -- Science. 1993 Apr 23;260(5107):504-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682726" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; DNA/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/metabolism ; RNA/chemistry/*metabolism ; RNA, Catalytic/chemistry/*metabolism ; RNA, Guide/chemistry/*metabolism ; RNA, Protozoan/chemistry/metabolism ; Tetrahymena/enzymology
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  • 90
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    Sequences and structures required for recombination between virus-associated RNAs (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-05-07
    Description: RNA recombination has been described for a number of viruses in the plant and animal kingdoms, but the mechanisms of selection of recombination sites are poorly understood. The nonrandom recombination between two subviral RNAs associated with turnip crinkle virus was used to study the requirement for specific sequences and structures in the generation of recombinant molecules. Single-base mutations that disrupted either the stem or the loop of one of the two computer-predicted stem-loop structures eliminated detectable recombinant molecules. However, recombinants were detected if compensatory mutations were generated that re-formed a stable hairpin structure. These results provide evidence for the necessity of specific structures in the formation of recombinant molecules in this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cascone, P J -- Haydar, T F -- Simon, A E -- New York, N.Y. -- Science. 1993 May 7;260(5109):801-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cellular Biology, University of Massachusetts, Amherst 01003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8484119" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Plant Viruses/*genetics/physiology ; Plants/microbiology ; RNA Viruses/*genetics/physiology ; RNA, Viral/chemistry/*genetics ; *Recombination, Genetic
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  • 91
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    Switch of CD8 T cells to noncytolytic CD8-CD4- cells that make TH2 cytokines and help B cells (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-18
    Description: CD8+ T cells are a major defense against viral infections and intracellular parasites. Their production of interferon-gamma (IFN-gamma) and their cytolytic activity are key elements in the immune response to these pathogens. Mature mouse CD8+ T cells that were activated in the presence of interleukin-4 (IL-4) developed into a CD8-CD4- population that was not cytolytic and did not produce IFN-gamma. However, these CD8- cells produced large amounts of IL-4, IL-5, and IL-10 and helped activate resting B cells. Thus, CD8 effector functions are potentially diverse and could be exploited by infectious agents that switch off host protective cytolytic responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erard, F -- Wild, M T -- Garcia-Sanz, J A -- Le Gros, G -- New York, N.Y. -- Science. 1993 Jun 18;260(5115):1802-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Allergy/Immunology, Ciba-Geigy Ltd., Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8511588" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/analysis ; Antigens, CD8/*analysis ; B-Lymphocytes/*immunology ; Cell Line ; Cells, Cultured ; Cytotoxicity, Immunologic ; Immunophenotyping ; Interleukin-10/biosynthesis ; Interleukin-2/pharmacology ; Interleukin-4/biosynthesis/pharmacology ; Interleukin-5/biosynthesis ; Interleukins/*biosynthesis ; Ionomycin/pharmacology ; *Lymphocyte Activation ; Membrane Glycoproteins/genetics ; Mice ; Perforin ; Pore Forming Cytotoxic Proteins ; T-Lymphocyte Subsets/*immunology ; T-Lymphocytes, Cytotoxic/immunology ; Tetradecanoylphorbol Acetate/pharmacology
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  • 92
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    Ribozymes: a distinct class of metalloenzymes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-06
    Description: Ribozymes are an important new class of metalloenzymes that have an unlikely feature: they are made entirely of ribonucleic acid (RNA). Metal ions are essential for efficient chemical catalysis by ribozymes and are often required for the stabilization of ribozyme structure. Most ribozymes catalyze reactions at phosphorus centers through one of two major mechanistic pathways, and reaction has been observed at carbon centers. Creative experiments have revealed the position of metal ions in the active site of two ribozymes. The exploitation of variable metal geometry and reactivity has expanded ribozyme chemistry and has facilitated the application of in vitro selection for the creation of novel ribozymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pyle, A M -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):709-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7688142" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Catalysis ; *Cations, Divalent/chemistry/metabolism ; *Metals/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oxidation-Reduction ; Phosphorus/metabolism ; RNA/*metabolism ; RNA Splicing ; *RNA, Catalytic/chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Tumor suppression in Xiphophorus by an accidentally acquired promoter (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-05
    Description: Melanoma formation in the teleost Xiphophorus is caused by a dominant genetic locus, Tu. This locus includes the Xmrk oncogene, which encodes a receptor tyrosine kinase. Tumor induction is suppressed in wild-type fish by a tumor suppressor locus, R. Molecular genetic analyses revealed that the Tu locus emerged by nonhomologous recombination of the Xmrk proto-oncogene with a previously uncharacterized sequence, D. This event generated an additional copy of Xmrk with a new promoter. Suppression of the new Xmrk promoter by R in parental fish and its deregulation in hybrids explain the genetics of melanoma formation in Xiphophorus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adam, D -- Dimitrijevic, N -- Schartl, M -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genzentrum, Max-Planck-Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430335" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cyprinodontiformes/*genetics ; Embryo, Nonmammalian ; Fish Diseases/*genetics ; *Fish Proteins ; Gene Library ; *Genes, Tumor Suppressor ; Melanoma/genetics/*veterinary ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; *Oncogenes ; Polymerase Chain Reaction/methods ; *Promoter Regions, Genetic ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogenes ; *Receptor Protein-Tyrosine Kinases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-16
    Description: Mice that bear the X-linked immunodeficiency (xid) mutation have a B lymphocyte-specific defect resulting in an inability to make antibody responses to polysaccharide antigens. A backcross of 1114 progeny revealed the colocalization of xid with Bruton's agammaglobulinemia tyrosine kinase (btk) gene, which is implicated in the human immune deficiency, X-linked agammaglobulinemia. Mice that carry xid have a missense mutation that alters a highly conserved arginine near the amino-terminus of the btk protein, Btk. Because this region of Btk lies outside any obvious kinase domain, the xid mutation may define another aspect of tyrosine kinase function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, J D -- Sideras, P -- Smith, C I -- Vorechovsky, I -- Chapman, V -- Paul, W E -- GM33160/GM/NIGMS NIH HHS/ -- HG00277/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 16;261(5119):355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332900" target="_blank"〉PubMed〈/a〉
    Keywords: Agammaglobulinemia/enzymology/*genetics/immunology ; Amino Acid Sequence ; Animals ; B-Lymphocytes/enzymology/immunology ; Base Sequence ; Chromosome Mapping ; Crosses, Genetic ; Female ; *Genes ; Genetic Linkage ; Immunologic Deficiency Syndromes/enzymology/*genetics/immunology ; Male ; Mice ; Mice, Inbred CBA ; Mice, Mutant Strains ; Molecular Sequence Data ; Muridae ; Mutation ; Protein-Tyrosine Kinases/chemistry/*genetics/metabolism ; *X Chromosome
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  • 95
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    Editing of transfer RNAs in Acanthamoeba castellanii mitochondria (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-05
    Description: With the discovery of RNA editing, a process whereby the primary sequence of RNA is altered after transcription, traditional concepts of genetic information transfer had to be revised. The known RNA editing systems act mainly on messenger RNAs, introducing sequence changes that alter their coding properties. An editing system that acts on transfer RNAs is described here. In the mitochondria of Acanthamoeba castellanii, an amoeboid protozoan, certain transfer RNAs differ in sequence from the genes that encode them. The changes consist of single-nucleotide conversions (U to A, U to G, and A to G) that appear to arise posttranscriptionally, are localized in the acceptor stem, and have the effect of correcting mismatched base pairs. Editing thus restores the base pairing expected of a normal transfer RNA in this region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lonergan, K M -- Gray, M W -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):812-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Dalhousie University, Halifax, Nova Scotia, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430334" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthamoeba/*genetics ; Animals ; Base Sequence ; Blotting, Southern ; DNA, Mitochondrial/*genetics ; Mitochondria/physiology ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; RNA, Transfer/chemistry/*genetics ; RNA, Transfer, Ala/chemistry/genetics ; RNA, Transfer, Asp/chemistry/genetics ; RNA, Transfer, Met/chemistry/genetics ; RNA, Transfer, Pro/chemistry/genetics
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  • 96
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    Natural selection and the origin of jingwei, a chimeric processed functional gene in Drosophila (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-02
    Description: The origin of new genes includes both the initial molecular events and subsequent population dynamics. A processed Drosophila alcohol dehydrogenase (Adh) gene, previously thought to be a pseudogene, provided an opportunity to examine the two phases of the origin of a new gene. The sequence of the processed Adh messenger RNA became part of a new functional gene by capturing several upstream exons and introns of an unrelated gene. This novel chimeric gene, jingwei, differs from its parent Adh gene in both its pattern of expression and rate of molecular evolution. Natural selection participated in the origin and subsequent evolution of this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, M -- Langley, C H -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):91-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Genetics, University of California, Davis 95616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682012" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Dehydrogenase/*genetics ; Animals ; Base Composition ; Base Sequence ; Biological Evolution ; Blotting, Northern ; *Chimera ; Drosophila/*genetics ; Introns ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA/analysis/chemistry ; RNA, Messenger/analysis/chemistry ; *Selection, Genetic ; Species Specificity
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  • 97
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    Regulation of the human hsp70 promoter by p53 (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: The tumor suppressor p53 is a nuclear phosphoprotein with characteristics of a transcription factor. It displays sequence-specific DNA binding, contains a potent transactivation domain, and has been implicated as both a transcriptional activator and a repressor. Transcription of the human hsp70 gene is stimulated by adenovirus E1a protein. This E1a transactivation of the hsp70 promoter is mediated by CCAAT binding factor (CBF). It is demonstrated here that p53 both represses transcription from the human hsp70 promoter and also interacts with CBF. Thus, the repression of the hsp70 promoter by p53 may be mediated by direct protein-protein interaction with CBF. These results suggest that protein-protein interaction between p53 and specific transcription factors may be an additional mechanism by which p53 regulates gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agoff, S N -- Hou, J -- Linzer, D I -- Wu, B -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):84-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418500" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Base Sequence ; CCAAT-Enhancer-Binding Proteins ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Cloning, Molecular ; DNA-Binding Proteins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/genetics ; *Gene Expression Regulation ; Heat-Shock Proteins/biosynthesis/*genetics/isolation & purification ; Humans ; *Promoter Regions, Genetic ; Recombinant Fusion Proteins/isolation & purification/metabolism ; TATA Box ; Transcription Factors/metabolism ; *Transcription, Genetic ; Tumor Suppressor Protein p53/genetics/isolation & purification/*metabolism
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  • 98
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    CNTF protection of oligodendrocytes against natural and tumor necrosis factor-induced death (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: A proportion of developing oligodendrocytes undergo natural cell death by apoptosis, and mature oligodendrocytes die, either by apoptosis or necrosis, in response to injurious signals such as cytotoxic cytokines and complement. Ciliary neurotrophic factor (CNTF), a trophic factor found in astrocytes in the central nervous system (CNS), promoted the survival and maturation of cultured oligodendrocytes. This trophic factor also protected oligodendrocytes from death induced by tumor necrosis factors (apoptosis) but not against complement (necrosis). These results suggest that CNTF functions in the survival of oligodendrocytes during development and may lead to therapeutic approaches for degenerative diseases of the CNS that involve oligodendrocyte destruction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Louis, J C -- Magal, E -- Takayama, S -- Varon, S -- NS16349/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):689-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430320" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/physiology ; Cell Death/*drug effects ; Cell Survival/drug effects ; Cells, Cultured ; Central Nervous System/physiology ; Ciliary Neurotrophic Factor ; Dose-Response Relationship, Drug ; Humans ; Kinetics ; Lymphotoxin-alpha/*pharmacology ; Nerve Growth Factors/*pharmacology ; Nerve Tissue Proteins/*pharmacology ; Oligodendroglia/cytology/drug effects/*physiology ; Recombinant Proteins/pharmacology ; Time Factors ; Tumor Necrosis Factor-alpha/*pharmacology
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  • 99
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    The conserved pre-mRNA splicing factor U2AF from Drosophila: requirement for viability (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-22
    Description: The large subunit of the human pre-messenger RNA splicing factor U2 small nuclear ribonucleoprotein auxiliary factor (hU2AF65) is required for spliceosome assembly in vitro. A complementary DNA clone encoding the large subunit of Drosophila U2AF (dU2AF50) has been isolated. The dU2AF50 protein is closely related to its mammalian counterpart and contains three carboxyl-terminal ribonucleoprotein consensus sequence RNA binding domains and an amino-terminal arginine- and serine-rich (R/S) domain. Recombinant dU2AF50 protein complements mammalian splicing extracts depleted of U2AF activity. Germline transformation of Drosophila with the dU2AF50 complementary DNA rescues a lethal mutation, establishing that the dU2AF50 gene is essential for viability. R/S domains have been found in numerous metazoan splicing factors, but their function is unknown. The mutation in Drosophila U2AF will allow in vivo analysis of a conserved R/S domain-containing general splicing factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanaar, R -- Roche, S E -- Beall, E L -- Green, M R -- Rio, D C -- R01-HD28063/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):569-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7692602" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Conserved Sequence ; DNA, Complementary ; Drosophila melanogaster/*genetics/growth & development ; Female ; Gene Transfer Techniques ; Genes, Insect ; Genes, Lethal ; In Situ Hybridization ; Male ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; RNA/metabolism ; RNA Precursors/*metabolism ; *RNA Splicing ; Recombinant Proteins/metabolism ; Ribonucleoproteins/chemistry/*genetics/metabolism ; Sequence Alignment
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  • 100
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    Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-15
    Description: Rab geranylgeranyl transferase (GG transferase) is a two-component enzyme that attaches 20-carbon isoprenoid groups to cysteine residues in Rab proteins, a family of guanosine triphosphate-binding proteins that regulate vesicular traffic. The mutant gene in human choroideremia, an X-linked form of retinal degeneration, encodes a protein that resembles component A of rat Rab GG transferase. Lymphoblasts from choroideremia subjects showed a marked deficiency in the activity of component A, but not component B, of Rab GG transferase. The deficiency was more pronounced when the substrate was Rab3A, a synaptic vesicle protein, than it was when the substrate was Rab1A, a protein of the endoplasmic reticulum. The data imply the existence of multiple component A proteins, one of which is missing in choroideremia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seabra, M C -- Brown, M S -- Goldstein, J L -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):377-81.〈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/8380507" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; *Alkyl and Aryl Transferases ; Cell Line, Transformed ; Cells, Cultured ; Choroid/chemistry ; Choroideremia/*genetics ; Female ; GTP-Binding Proteins/analysis/*metabolism ; Gene Expression Regulation, Enzymologic ; Humans ; Lymphocyte Activation ; Male ; Middle Aged ; Mutation ; Nerve Tissue Proteins/analysis/*metabolism ; Photoreceptor Cells/chemistry ; Pigment Epithelium of Eye/chemistry ; Protein Prenylation ; Retina/chemistry ; Substrate Specificity ; Transferases/*deficiency/genetics ; rab1 GTP-Binding Proteins ; rab3 GTP-Binding Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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