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  • Base Sequence  (7)
  • American Association for the Advancement of Science (AAAS)  (7)
  • American Physical Society
  • 2010-2014
  • 1980-1984  (7)
  • 1983  (7)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (7)
  • American Physical Society
Years
  • 2010-2014
  • 1980-1984  (7)
Year
  • 1
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    Separation of signal transduction and adaptation functions of the aspartate receptor in bacterial sensing (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-06-03
    Description: In order to investigate the functions of stimulus recognition, signal transduction, and adaptation, the aspartate receptor gene for bacterial chemotaxis in Salmonella typhimurium has been sequenced and modified. A carboxyl-terminal truncated receptor was shown to bind aspartate and to transmit a signal to change motility behavior. However, the truncated receptor showed greatly reduced methyl-accepting capacity, and did not allow adaptation to the sensory stimulation. The separation of receptor functions by alteration of primary structure emphasizes that the receptor is directly involved in adaptation and is not solely a device for transmitting a signal across a membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russo, A F -- Koshland, D E Jr -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1016-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Aspartic Acid ; *Bacterial Physiological Phenomena ; Base Sequence ; *Chemotaxis ; Escherichia coli/physiology ; Methylation ; *Receptors, Amino Acid ; Receptors, Cell Surface/genetics/*physiology ; Salmonella typhimurium/physiology ; Serine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Insertion sequence duplication in transpositional recombination (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: Insertion sequences (IS) are discrete segments of DNA that can transpose from one genomic site to another and promote genetic rearrangements. A question that is central to understanding the mechanism of transpositional recombination is whether genetic rearrangements are accompanied by duplication of the IS that promotes them. Analysis of adjacent deletions mediated by IS903 provides the strongest evidence to date than any IS-mediated transpositional recombination can occur by an efficient replicative mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinert, T A -- Schaus, N A -- Grindley, N D -- GM28470/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):755-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314502" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; *DNA Transposable Elements ; DNA, Bacterial/*genetics ; Plasmids ; *Recombination, Genetic ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    An inverted repeat borders a fivefold amplification in satellite DNA (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-08-26
    Description: One variant of a complex satellite DNA of the Bermuda land crab is significantly longer than the average repeat unit of the satellite. The extra DNA in the variant is accounted for by a fivefold tandem amplification of a 0.142-kilobase sequence. The amplified sequence is bounded by a tetranucleotide inverted repeat; the upstream arm of the inverted repeat is missing from two other variants of the satellite. The latter variants contain only one copy of a sequence that is closely related to the amplified sequence. By contrast, in several satellite DNA's of other organisms, extra DNA is inserted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonnewell, V -- Fowler, R F -- Skinner, D M -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):862-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brachyura/genetics ; Chromosome Inversion ; DNA, Satellite/*genetics ; *Gene Amplification ; Nucleic Acid Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Detection of antibodies to herpes simplex virus with a continuous cell line expressing cloned glycoprotein D (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-04
    Description: The gene for glycoprotein D of herpes simplex virus type 1 (HSV-1) was expressed in stable mammalian cell lines. Glycoprotein D produced in these cells has a number of antigenic determinants in common with the native glycoprotein. Cell lines expressing glycoprotein D were used in an enzyme-linked immunosorbent assay to detect human antibodies to glycoprotein D. This strategy should prove useful in determining the extent to which the immune response to HSV-1 is directed toward glycoprotein D.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berman, P W -- Dowbenko, D -- Lasky, L A -- Simonsen, C C -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):524-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6312563" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Viral/*analysis ; Base Sequence ; Cell Line ; Clone Cells ; DNA Restriction Enzymes ; DNA, Viral/genetics ; Enzyme-Linked Immunosorbent Assay ; *Genes ; *Genes, Viral ; Humans ; Plasmids ; Simplexvirus/genetics/*immunology ; Tetrahydrofolate Dehydrogenase/genetics ; *Viral Envelope Proteins ; Viral Proteins/*genetics/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Ectopic pro-opiolipomelanocortin: sequence of cDNA coding for beta-melanocyte-stimulating hormone and beta-endorphin (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-13
    Description: A recombinant bacterial plasmid, pMS1, was constructed that contains 318 nucleotides complementary to a portion of pro-opiolipomelanocortin (proOLMC) messenger RNA from an ectopic adrenocorticotropin-producing tumor. The cloned complementary DNA insert, which contains the sequence that codes for all of the beta-melanocyte-stimulating hormone and beta-endorphin portions of proOLMC, as well as the 3' nontranslated section, is identical to the genomic sequence. Hybridization of tumor proOLMC complementary DNA to RNA subjected to electrophoresis and transferred to a nitrocellulose filter revealed two proOLMC messenger RNA species in the tumor polyadenylated RNA, but only one in pituitary polyadenylated RNA. At least one of the tumor proOLMC messenger RNA's is similar, if not identical, to human pituitary proOLMC messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeBold, C R -- Schworer, M E -- Connor, T B -- Bird, R E -- Orth, D N -- 2-R01-GM25526/GM/NIGMS NIH HHS/ -- 5-R01-CA11685/CA/NCI NIH HHS/ -- 5-R25-CA19429/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 May 13;220(4598):721-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carcinoid Tumor/physiopathology ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA, Recombinant/*metabolism ; Endorphins/*genetics ; Hormones, Ectopic/*genetics ; Humans ; Male ; Melanocyte-Stimulating Hormones/*genetics ; Middle Aged ; Pancreatic Neoplasms/physiopathology ; Pituitary Hormones, Anterior/*genetics ; Pro-Opiomelanocortin ; Protein Precursors/*genetics ; RNA, Messenger/genetics ; beta-Endorphin
    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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  • 6
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    Isolation of human C-reactive protein complementary DNA and localization of the gene to chromosome 1 (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-07-01
    Description: With a synthetic oligonucleotide mixture as probe, complementary DNA clones of C-reactive protein were isolated from an adult human liver complementary DNA library. The clones ranged in size from 700 to 1100 base pairs and were identified by partial DNA sequence analysis. One complementary DNA clone was used as a probe for hybridization with human-rodent DNA's isolated from somatic cell hybrids and bound to nitrocellulose filters (Southern blot analysis) to assign the human C-reactive protein gene to chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitehead, A S -- Bruns, G A -- Markham, A F -- Colten, H R -- Woods, D E -- AI15033/AI/NIAID NIH HHS/ -- HD4807/HD/NICHD NIH HHS/ -- HL22487/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):69-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; C-Reactive Protein/*genetics ; *Chromosome Mapping ; *Chromosomes, Human, 1-3 ; Cloning, Molecular ; Cricetinae ; DNA/*genetics/isolation & purification ; Genes ; Humans ; Hybrid Cells/metabolism ; Mice
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Directed mutagenesis of dihydrofolate reductase (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations--at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine--were designed to answer questions about the relations between molecular structure and function that were raised by the x-ray crystal structures. Properties of the mutant proteins show that Asp-27 is important for catalysis and that perturbation of the local structure at a conserved cis peptide bond following Gly-95 abolishes activity. Substitution of cysteine for proline at residue 39 results in the appearance of new forms of the enzyme that correspond to various oxidation states of the cysteine. One of these forms probably represents a species cross-linked by an intrachain disulfide bridge between the cysteine at position 85 and the new cysteine at position 39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Villafranca, J E -- Howell, E E -- Voet, D H -- Strobel, M S -- Ogden, R C -- Abelson, J N -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):782-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Disulfides ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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