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  • Base Sequence  (43)
  • American Association for the Advancement of Science (AAAS)  (43)
  • 1980-1984  (43)
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Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (43)
Years
Year
  • 1
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    Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-04
    Description: A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system. When Escherichia coli transformed with this plasmid was grown in tryptophan-depleted media, approximately 17 percent of the total cellular protein was found to be an insoluble and stable chimeric protein. The purified chimeric protein competed equally on a molar basis with VP3 for specific antibodies to foot-and-mouth disease virus. When inoculated into six cattle and two swine, this protein elicited high levels of neutralizing antibody and protection against challenge with foot-and-mouth disease virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleid, D G -- Yansura, D -- Small, B -- Dowbenko, D -- Moore, D M -- Grubman, M J -- McKercher, P D -- Morgan, D O -- Robertson, B H -- Bachrach, H L -- New York, N.Y. -- Science. 1981 Dec 4;214(4525):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6272395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Base Sequence ; Cattle ; Cattle Diseases/*prevention & control ; *Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; Foot-and-Mouth Disease/*prevention & control ; Immunity, Cellular ; Protein Biosynthesis ; Swine ; Swine Diseases/*prevention & control ; Transcription, Genetic ; *Vaccines ; Viral Proteins/genetics/*therapeutic use
    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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    Genes for growth hormone, chorionic somatommammotropin, and growth hormones-like gene on chromosome 17 in humans (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-11
    Description: The human genes for growth hormone (GH), chorionic somatomammotropin (CSH), and a third growth hormone-like gene (GHL) have been located on chromosome 17 in humans. DNA fragments of 2.6, 2.8, and 9.5 kilobase pairs containing GH, CSH, and GHL, respectively, were identified in human genomic DNA, and a 7.5-kilobase DNA fragment related to growth hormone DNA sequences was found in mouse cells. In somatic hybrids of human and mouse cells containing reduced numbers of human chromosomes, but a normal complement of mouse chromosomes, the mouse, 7.5-kolobase DNA fragment was always present, whereas the 2.6-, 2.8-, and 9.5-kilobase human fragments were present only when human chromosome 17 was also present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owerbach, D -- Rutter, W J -- Martial, J A -- Baxter, J D -- Shows, T B -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):289-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384802" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; *Chromosomes, Human, 16-18 ; *DNA/metabolism ; *Genes ; Growth Hormone/*biosynthesis ; Humans ; Hybrid Cells/metabolism ; Mice ; Placental Lactogen/*biosynthesis ; Translocation, Genetic
    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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    Structure of the gene encoding the immunodominant surface antigen on the sporozoite of the human malaria parasite Plasmodium falciparum (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-10
    Description: The gene for the circumsporozoite (CS) protein of Plasmodium falciparum has been cloned and its nucleotide sequence determined. The gene encodes a protein of 412 amino acids as deduced from the nucleotide sequence. The protein contains 41 tandem repeats of a tetrapeptide, 37 of which are Asn-Ala-Asn-Pro and four of which are Asn-Val-Asp-Pro. Monoclonal antibodies against the CS protein of Plasmodium falciparum were inhibited from binding to the protein by synthetic peptides of the repeat sequence. The CS protein of Plasmodium falciparum and the CS protein of a simian malaria parasite, Plasmodium knowlesi, have two regions of homology, one of which is present on either side of the repeat. One region contains 12 of 13 identical amino acids. Within the nucleotide sequence of this region, 25 of 27 nucleotides are conserved. The conservation of these regions in parasites widely separated in evolution suggests that they may have a function such as binding to liver cells and may represent an invariant target for immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dame, J B -- Williams, J L -- McCutchan, T F -- Weber, J L -- Wirtz, R A -- Hockmeyer, W T -- Maloy, W L -- Haynes, J D -- Schneider, I -- Roberts, D -- New York, N.Y. -- Science. 1984 Aug 10;225(4662):593-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Base Sequence ; Epitopes/genetics ; *Genes ; Humans ; Liver/parasitology ; Malaria/*immunology ; Plasmodium/genetics ; Plasmodium falciparum/*genetics/immunology ; *Protozoan Proteins
    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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  • 4
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    Interferon-beta-related DNA is dispersed in the human genome (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-23
    Description: Interferon-beta 1 (IFN-beta 1) complementary DNA was used as a hybridization probe to isolate human genomic DNA clones lambda B3 and lambda B4 from a human genomic DNA library. Blot-hybridization procedures and partial nucleotide sequencing revealed that lambda B3 is related to IFN-beta 1 (and more distantly to IFN-alpha 1). Analyses of DNA obtained from a panel of human-rodent somatic cell hybrids that were probed with DNA derived from lambda B3 showed that lambda B3 is on human chromosome 2. Similar experiments indicated that lambda B4 is not on human chromosomes 2, 5, or 9. The finding that DNA related to the IFN-beta 1 gene (and IFN-alpha 1 gene) is dispersed in the human genome raises new questions about the origins of the interferon genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sagar, A D -- Sehgal, P B -- May, L T -- Inouye, M -- Slate, D L -- Shulman, L -- Ruddle, F H -- AI-16262/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 23;223(4642):1312-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6546621" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human/*analysis ; Chromosomes, Human, 1-3 ; Chromosomes, Human, 4-5 ; Chromosomes, Human, 6-12 and X ; Cloning, Molecular ; Cricetinae ; DNA/*analysis ; *Genes ; Humans ; Hybrid Cells ; Interferon Type I/*genetics ; Mice ; Nucleic Acid Hybridization
    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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    A replication cycle for viroids and other small infectious RNA's (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-02-03
    Description: Experimental data concerning viroid-specific nucleic acids accumulating in tomato plants establish, together with earlier studies, the major features of a replication cycle for viroid RNA in plant cells. Many features of this pathway, which involves multimeric strands of both polarities, may be shared by other small infectious RNA's including certain satellite RNA's and "virusoid" RNA's which replicate in conjunction with conventional plant viruses. The presence, in host plans, of an elaborate machinery for replicating these disease agents suggests a role for endogenous small RNA's in cellular development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Branch, A D -- Robertson, H D -- New York, N.Y. -- Science. 1984 Feb 3;223(4635):450-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6197756" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Base Sequence ; Models, Biological ; Nucleic Acid Hybridization ; Nucleic Acid Precursors/metabolism ; Phosphates/metabolism ; Plants/enzymology/microbiology ; RNA/*biosynthesis/metabolism ; RNA Ligase (ATP)/metabolism ; RNA Precursors ; RNA Splicing ; RNA, Double-Stranded/metabolism ; RNA, Viral/*biosynthesis ; Viroids/*physiology ; *Virus Replication
    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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    Structure of 3' terminal region of type II human T lymphotropic virus: evidence for new coding region (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-07-27
    Description: The sequence of the 3' terminus of the human T lymphotropic virus type II (HTLV-II) was determined and compared to the corresponding sequence of HTLV-I. The 1557-nucleotide-long sequence can be divided into a 5' region that is not conserved between the two viruses, and a 3', 1011-nucleotide-long region that is highly conserved and that corresponds precisely with a long open reading frame for both HTLV-I and -II. The proteins that could be encoded by these open reading frames have a molecular weight of about 38,000 and are closely related in primary amino acid sequence. The genomic structure in the 3' region of HTLV was found to be similar to that of bovine leukemia virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haseltine, W A -- Sodroski, J -- Patarca, R -- Briggs, D -- Perkins, D -- Wong-Staal, F -- CA07094/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jul 27;225(4660):419-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6330894" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Deltaretrovirus/*genetics ; Genes, Viral ; Humans ; Leukemia/microbiology ; Leukemia Virus, Bovine/genetics ; Retroviridae Infections/microbiology ; Transcription, Genetic
    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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    Site-specific mutagenesis of the human interleukin-2 gene: structure-function analysis of the cysteine residues (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-29
    Description: The gene encoding human interleukin-2 (IL-2) has been cloned from human spleen cells, peripheral blood lymphocytes, and the Jurkat cell line. Nucleotide sequence analysis of the gene revealed that the encoded IL-2 protein has three cysteines located at amino acid residues 58, 105, and 125 of the mature protein. Site-specific mutagenesis procedures were used to modify the IL-2 gene by changing each of the cysteine codons individually to serine codons. Substitution of serine for cysteine residues at either position 58 or 105 of the IL-2 protein substantially reduced biological activity, indicating that the cysteines at these positions are necessary for maintenance of the biologically active conformation and may therefore be linked by a disulfide bridge. The modified IL-2 protein containing a substitution at position 125 retained full biological activity, suggesting that the cysteine at this position is not involved in a disulfide bond and that a free sulfhydryl group at that position is not necessary for receptor binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A -- Lu, S D -- Mark, D F -- New York, N.Y. -- Science. 1984 Jun 29;224(4656):1431-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6427925" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cysteine/metabolism ; DNA, Recombinant/metabolism ; Escherichia coli/genetics ; Genes ; Humans ; Interleukin-2/*genetics ; *Mutation ; Receptors, Immunologic/metabolism ; Receptors, Interleukin-2 ; Serine/metabolism ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Sequence of the envelope glycoprotein gene of type II human T lymphotropic virus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-07-27
    Description: The sequence of the envelope glycoprotein gene of type II human T lymphotropic virus (HTLV) is presented. The predicted amino acid sequence is similar to that of the corresponding protein of HTLV type I, in that the proteins share the same amino acids at 336 of 488 residues, and 68 of the 152 differences are of a conservative nature. The overall structural similarity of these proteins provides an explanation for the antigenic cross-reactivity observed among diverse members of the HTLV retrovirus family by procedures that assay for the viral envelope glycoprotein, for example, membrane immunofluorescence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodroski, J -- Patarca, R -- Perkins, D -- Briggs, D -- Lee, T H -- Essex, M -- Coligan, J -- Wong-Staal, F -- Gallo, R C -- Haseltine, W A -- CA-18216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jul 27;225(4660):421-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204380" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Base Sequence ; Cross Reactions ; Cysteine/metabolism ; Deltaretrovirus/*genetics ; Epitopes/immunology ; *Genes, Viral ; Glycoproteins/*genetics ; Humans ; Viral Envelope 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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  • 9
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    Distribution of active gene sequences: a subset associated with tightly bound chromosomal proteins (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-08
    Description: The distribution of active polyadenylate-messenger RNA sequences in fractionated chicken liver chromatin was examined. A portion of these active gene sequences is concentrated in a DNA fraction retained by tightly bound nonhistone chromosomal proteins, while the nonretained DNA fraction is substantially depleted of a portion of these sequences. These findings suggest that the tightly bound nonhistones are physically associated with a subset of active gene sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gates, D M -- Bekhor, I -- New York, N.Y. -- Science. 1980 Feb 8;207(4431):661-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Chromatin/ultrastructure ; Chromosomal Proteins, Non-Histone/*metabolism ; DNA/*metabolism ; *Genes ; Liver/*metabolism ; Nucleic Acid Hybridization ; Protein Binding ; RNA, Messenger/genetics ; Sodium Chloride
    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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  • 10
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    The phylogeny of prokaryotes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, G E -- Stackebrandt, E -- Hespell, R B -- Gibson, J -- Maniloff, J -- Dyer, T A -- Wolfe, R S -- Balch, W E -- Tanner, R S -- Magrum, L J -- Zablen, L B -- Blakemore, R -- Gupta, R -- Bonen, L -- Lewis, B J -- Stahl, D A -- Luehrsen, K R -- Chen, K N -- Woese, C R -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):457-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6771870" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*classification ; Base Sequence ; Biological Evolution ; Chloroplasts/analysis ; Clostridium/classification ; Cyanobacteria/classification ; DNA/analysis ; *Phylogeny ; RNA, Ribosomal/*analysis ; Species Specificity
    Print ISSN: 0036-8075
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