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  • Articles  (13)
  • Genes
  • American Association for the Advancement of Science (AAAS)  (13)
  • American Chemical Society
  • Oxford University Press
  • 1980-1984  (13)
  • 1925-1929
  • 1984  (13)
  • 1
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    Homology of genome of AIDS-associated virus with genomes of human T-cell leukemia viruses (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-31
    Description: A T lymphotropic virus found in patients with the acquired immune deficiency syndrome (AIDS) or lymphadenopathy syndrome has been postulated to be the cause of AIDS. Immunological analysis of this retrovirus and its biological properties suggest that it is a member of the family of human T-lymphotropic retroviruses known as HTLV. Accordingly, it has been named HTLV-III. In the present report it is shown by nucleic acid hybridization that sequences of the genome of HTLV-III are homologous to the structural genes (gag, pol, and env) of both HTLV-I and HTLV-II and to a potential coding region called pX located between the env gene and the long terminal repeating sequence that is unique to the HTLV family of retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Gallo, R C -- Hahn, B H -- Shaw, G M -- Popovic, M -- Salahuddin, S Z -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):927-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089333" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; Cloning, Molecular ; Dna ; DNA, Viral ; Deltaretrovirus/classification/*genetics ; Genes ; *Genes, Viral ; Humans ; *Nucleic Acid Hybridization ; RNA, Viral ; 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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  • 2
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    A major human histone gene cluster on the long arm of chromosome 1 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: A human histone gene cluster was assigned to chromosome 1 by Southern blot analysis of DNA's from a series of mouse-human somatic cell hybrids with 32P-labeled cloned human H4 and H3 histone DNA as probes. Localization of this histone gene cluster on the long arm of chromosome 1 was confirmed by in situ hybridization of this DNA probe to metaphase chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, L -- Van Antwerpen, R -- Stein, J -- Stein, G -- Tripputi, P -- Emanuel, B -- Selden, J -- Croce, C -- GM20138/GM/NIGMS NIH HHS/ -- GM20700/GM/NIGMS NIH HHS/ -- GM32010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):838-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494913" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Chromosome Mapping ; *Chromosomes, Human, 1-3 ; Chromosomes, Human, 6-12 and X ; DNA/metabolism ; Genes ; Histones/*genetics ; Humans ; Hybrid Cells/metabolism ; Mice ; Nucleic Acid Hybridization
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Repression of rearranged mu gene and translocated c-myc in mouse 3T3 cells X Burkitt lymphoma cell hybrids (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: The productively rearranged immunoglobulin mu chain gene and the translocated cellular oncogene c-myc are transcribed at high levels both in human Burkitt lymphoma cells carrying the t(8;14) chromosome translocation and in mouse plasmacytoma X Burkitt lymphoma cell hybrids. In the experiments reported here these genes were found to be repressed in mouse 3T3 fibroblast X Burkitt lymphoma cell hybrids. Such repression probably occurs at the transcriptional level since no human mu- and c-myc messenger RNA's are detectable in hybrid clones carrying the corresponding genes. It is therefore concluded that the ability to express these genes requires a differential B cell environment. The results suggest that the 3T3 cell assay may not be suitable to detect oncogenes directly involved in human B cell oncogenesis, since 3T3 cells apparently are incapable of transcribing an oncogene that is highly active in malignant B cells with specific chromosomal translocations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishikura, K -- ar-Rushdi, A -- Erikson, J -- DeJesus, E -- Dugan, D -- Croce, C M -- CA 09171/CA/NCI NIH HHS/ -- CA 10815/CA/NCI NIH HHS/ -- GM 31060/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):399-402.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6424234" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Burkitt Lymphoma/*genetics ; Fibroblasts ; *Gene Expression Regulation ; Genes ; Humans ; Hybrid Cells/*metabolism ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin mu-Chains/*genetics ; Mice ; *Oncogenes ; RNA, Messenger/genetics ; Transcription, Genetic ; *Translocation, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Nucleotide sequences of the human and mouse atrial natriuretic factor genes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-07
    Description: Mouse and human atrial natriuretic factor (ANF) genes have been cloned and their nucleotide sequences determined. Each ANF gene consists of three coding blocks separated by two intervening sequences. The 5' flanking sequences and those encoding proANF are highly conserved between the two species, while the intervening sequences and 3' untranslated regions are not. The conserved sequences 5' of the gene may play an important role in the regulation of ANF gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seidman, C E -- Bloch, K D -- Klein, K A -- Smith, J A -- Seidman, J G -- AI-18436/AI/NIAID NIH HHS/ -- HL-070208/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 7;226(4679):1206-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6542248" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atrial Natriuretic Factor ; Base Sequence ; Cloning, Molecular ; Gene Expression Regulation ; Genes ; Heart Atria/metabolism ; Humans ; Mice ; Natriuretic Agents ; Protein Precursors/genetics ; Proteins/*genetics ; Receptors, Glucocorticoid/metabolism
    Print ISSN: 0036-8075
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  • 5
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    Neuropeptides: mediators of behavior in Aplysia (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The Aplysia neuroendocrine system is a particularly advantageous model for cellular and molecular studies because of the relatively small number and large size of its component neurons. Recombinant DNA techniques have been used to isolate the genes that encode the precursors of peptides expressed in identified neurons of known function. The organization and developmental expression of these genes have been examined in detail. Several of the genes encode precursors of multiple biologically active peptides that are expressed in cells which also contain classical transmitters. These studies, as well as immunohistochemical studies and the use of intracellular recording and voltage clamp techniques are the first steps toward revealing the mechanisms by which neuropeptides govern simple behaviors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheller, R H -- Kaldany, R R -- Kreiner, T -- Mahon, A C -- Nambu, J R -- Schaefer, M -- Taussig, R -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1300-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/*physiology ; Behavior, Animal ; Cloning, Molecular ; DNA, Recombinant/metabolism ; Female ; Ganglia/physiology ; Genes ; Male ; Nerve Tissue Proteins/genetics/*physiology ; *Nervous System Physiological Phenomena ; Neurons/physiology ; Protein Biosynthesis ; Reproduction
    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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    Plasmodium knowlesi sporozoite antigen: expression by infectious recombinant vaccinia virus (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: The gene coding for the circumsporozoite antigen of the malaria parasite Plasmodium knowlesi was inserted into the vaccinia virus genome under the control of a defined vaccinia virus promoter. Cells infected with the recombinant virus synthesized polypeptides of 53,000 to 56,000 daltons that reacted with monoclonal antibody against the repeating epitope of the malaria protein. Furthermore, rabbits vaccinated with the recombinant virus produced antibodies that bound specifically to sporozoites. These data provide evidence for expression of a cloned malaria gene in mammalian cells and illustrate the potential of vaccinia virus recombinants as live malaria vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, G L -- Godson, G N -- Nussenzweig, V -- Nussenzweig, R S -- Barnwell, J -- Moss, B -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):397-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Formation ; Antigens, Surface/analysis/*genetics/immunology ; *Cloning, Molecular ; *DNA, Recombinant ; Epitopes/immunology ; Genes ; Genes, Viral ; Genetic Vectors ; Operon ; Plasmodium/*genetics/immunology ; Rabbits ; Vaccination ; Vaccinia virus/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Hemoglobin I mutation encoded at both alpha-globin loci on the same chromosome: concerted evolution in the human genome (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-21
    Description: Genetic analysis of an individual expressing an unexpectedly high level of hemoglobin I, an alpha-globin structural mutant, reveals that the mutation is present at both the alpha 1- and the alpha 2-globin gene loci. Kindred analysis confirms that the two affected genes are located in cis. The most likely explanation for this finding is that a recent conversion event occurred within the human alpha-globin gene cluster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liebhaber, S A -- Rappaport, E F -- Cash, F E -- Ballas, S K -- Schwartz, E -- Surrey, S -- AM 16691/AM/NIADDK NIH HHS/ -- AM 33975/AM/NIADDK NIH HHS/ -- HL 28157/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Dec 21;226(4681):1449-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505702" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Genes ; Globins/*genetics ; *Hemoglobins ; Hemoglobins, Abnormal/*genetics ; Humans ; *Mutation ; Nucleic Acid Hybridization ; Recombination, Genetic
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  • 8
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    More on the T-cell receptor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1065.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494924" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; Genes ; Humans ; Receptors, Antigen, T-Cell/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Evolution of proteolytic enzymes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
    Print ISSN: 0036-8075
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  • 10
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    Duchenne muscular dystrophy involving translocation of the dmd gene next to ribosomal RNA genes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-29
    Description: Duchenne muscular dystrophy (DMD) is a severe X-linked disorder leading to early death of affected males. Females with the disease are rare, but seven are known to be affected because of a chromosomal rearrangement involving a site at or near the dmd gene on the X chromosome. One of the seven has a translocation between the X and chromosome 21. The translocation-derived chromosomes from this patient have been isolated, and the translocation is shown to have split the block of genes encoding ribosomal RNA on the short arm of chromosome 21. Thus ribosomal RNA gene probes may be used to identify a junction fragment from the translocation site, allowing access to cloned segments of the X at or near the dmd gene and presenting a new approach to the study of this disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worton, R G -- Duff, C -- Sylvester, J E -- Schmickel, R D -- Willard, H F -- New York, N.Y. -- Science. 1984 Jun 29;224(4656):1447-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6729462" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Child ; DNA/genetics ; Female ; Genes ; Humans ; Hybrid Cells ; Male ; Mice ; Muscular Dystrophies/*genetics ; RNA, Ribosomal/*genetics ; *Translocation, Genetic ; X Chromosome
    Print ISSN: 0036-8075
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  • 11
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 12
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    Sequence of the human somatostatin I gene (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-13
    Description: Two human genomic DNA fragments containing alleles for the gene coding for somatostatin I were isolated and sequenced. This gene contains a single intron that interrupts the coding sequence in the propeptide portion of the somatostatin moiety. The site of initiation of transcription of the gene was located by transcription experiments in HeLa cell extracts, and the putative regions for controlling the initiation of transcription were identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shen, L P -- Rutter, W J -- AM 21344/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 13;224(4645):168-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6142531" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; Genes ; Humans ; Nucleic Acid Hybridization ; Somatostatin/*genetics ; Transcription, Genetic
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  • 13
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    Multiple mutations produce delta beta 0 thalassemia in Sardinia (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-03-02
    Description: In Sardinia the common form of beta thalassemia is a beta 0 thalassemia due to a nonsense mutation at codon 39. delta beta 0 Thalassemia is rare in Sardinia and is associated with increased production of hemoglobin F of the A gamma type. In this study we used a synthetic oligomer assay and detected the beta 39 nonsense mutation on the delta beta 0 thalassemia chromosome. Hence at least two different mutations have occurred on this chromosome; one that increases A gamma globin synthesis and another that silences the beta globin gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pirastu, M -- Kan, Y W -- Galanello, R -- Cao, A -- AM16666/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 2;223(4639):929-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6198720" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosomes, Human ; Fetal Hemoglobin/genetics ; Genes ; Genotype ; Globins/*genetics ; Humans ; Italy ; *Mutation ; Pedigree ; Thalassemia/*genetics
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