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  • Articles  (35)
  • Genes
  • 1980-1984  (35)
  • 1945-1949
  • 1925-1929
  • 1984  (13)
  • 1980  (22)
  • 1928
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  • Articles  (35)
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  • 1980-1984  (35)
  • 1945-1949
  • 1925-1929
Year
Journal
Topic
  • 1
    Electronic Resource
    Electronic Resource
    Evolutionary analysis ofα andβ hemoglobin genes by reh theory under the assumption of the equiprobability of genetic events (1980)
    Springer
    Journal of molecular evolution 15 (1980), S. 149-159 
    Details
    ISSN: 1432-1432
    Keywords: Genes ; REH theory ; Genetic distance ; Evolution ; mRNA ; Nucleic acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary It is shown how REH theory in conjunction with mRNA or gene sequence data can be used to obtain estimates of the fixation intensity, the number of varions, and the total mutations fixed between homologous pairs of nucleic acids. These estimates are more accurate than those that can be derived from amino acid sequence data. The method is illustrated forα andβ hemoglobin genes and these improved estimates are compared with those made from the amino acid sequences for which those genes code. Significant differences are found between the estimates made by these two methods. For theβ hemoglobin gene sequences examined here, the fixation intensity is some-what less than the protein data had suggested, and the number of rations is considerably greater. Depending on the gene sequences examined, between 62 and 83% of the codons appear able to fix mutations during the divergences considered. This reflects the constraints of natural selection on acceptable mutations. The total number of base replacements separating the genes for human, mouse, and rabbitβ hemoglobin varies from 61 to 105 depending on the pair examined. Rabbitα andβ hemoglobin are separated by at least 290 fixed mutations. For such distantly related sequences estimates made from protein and mRNA data differ less, reflecting the higher quality of information from the many observed changes in primary structure. The effects of nonrandom gene structure on these evolutionary estimates and the fact that various genetic events are not equiprobable are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01732667
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  • 2
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    Allele increasing susceptibility to human breast cancer may be linked to the glutamate-pyruvate transaminase locus (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-04-25
    Description: The patterns of the occurrence of breast cancer in 11 high-risk families were evaluated by segregation and linkage analysis. These patterns were consistent with the hypothesis that increased susceptibility to breast cancer was inherited as an autosomal dominant allele with high penetrance in women. The postulated susceptibility allele in these families may be chromosomally linked to the glutamate-pyruvate transaminase (E.C. 2.6.1.2, alanine aminotransferase) locus. Confirmation of this linkage in other families would establish the existence of a gene increasing susceptibility to breast cancer. Since there is no association in the general population between a woman's glutamate-pyruvate transaminase genotype and her cancer risk, the glutamate-pyruvate transaminase linkage cannot be used as a screening test for breast cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, M C -- Go, R C -- Elston, R C -- Lynch, H T -- Petrakis, N L -- New York, N.Y. -- Science. 1980 Apr 25;208(4442):406-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367867" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine Transaminase/*genetics ; Alleles ; Breast Neoplasms/*genetics/transmission ; Female ; Genes ; Genetic Linkage ; Humans ; Pedigree ; X Chromosome
    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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    Tooth induction in chick epithelium: expression of quiescent genes for enamel synthesis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-29
    Description: Intraocular grafts of chick epithelium combined with mouse molar mesenchyme produced a variety of dental structures including perfectly formed crowns with differentiated ameloblasts depositing enamel matrix. The results suggest that the loss of teeth in Aves did not result from a loss of genetic coding for enamel synthesis in the oral epithelium but from an alteration in the tissue interactions requisite for odontogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kollar, E J -- Fisher, C -- New York, N.Y. -- Science. 1980 Feb 29;207(4434):993-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352302" target="_blank"〉PubMed〈/a〉
    Keywords: *Amelogenesis ; Animals ; Chick Embryo/*cytology ; Culture Techniques ; Dental Enamel Proteins/*biosynthesis/genetics ; Embryonic Induction ; Epithelial Cells ; Genes ; Mandible/cytology ; Mesoderm/cytology ; Mice ; *Odontogenesis
    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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    Immunoglobulin gene rearrangement in immature B cells (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Two types of immature B cells, namely fetal liver hybridomas and the leukemic cell line 70Z/3, both of which have cytoplasmic mu chains but no light chains, were examined for DNA rearrangements of their light chain and heavy chain immunoglobulin genes. In the fetal liver hybridomas, which were constructed from fetal liver cells and a tumor cell, no light chain gene rearrangement was observed, whereas in the 70Z/3 cell line a kappa light chain rearrangement probably occurred. The results suggest that, although the lack of light chain synthesis can be due to a lack of gene rearrangement, there may also be transcriptional regulation, which may also be important for the expression of light chain immunoglobulins in immature B cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maki, R -- Kearney, J -- Paige, C -- Tonegawa, S -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1366-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6774416" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Genes ; Hybrid Cells/immunology ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin kappa-Chains/*genetics ; Immunoglobulin mu-Chains/*genetics ; Leukemia, Experimental/*immunology ; Liver/*embryology ; Mice ; Recombination, Genetic ; Transcription, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    J genes for heavy chain immunoglobulins of mouse (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-05
    Description: A 15,8-kilobase pair fragment of BALB/c mouse liver DNA, cloned in the Charon 4A lambda phage vector system, was shown to contain the mu heavy chain constant region (CHmu) gene for the mouse immunoglobulin M. In addition, this fragment of DNA contains at least two J genes, used to code for the carboxyl terminal portion of heavy chain variable regions. These genes are located in genomic DNA about eight kilobase pairs to the 5' side of the CHmu gene. The complete nucleotide sequence of a 1120-base pair stretch of DNA that includes the two J genes has been determined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newell, N -- Richards, J E -- Tucker, P W -- Blattner, F R -- New York, N.Y. -- Science. 1980 Sep 5;209(4461):1128-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6250219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites, Antibody/*genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; Genes ; Genetic Linkage ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulin mu-Chains/*genetics ; 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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  • 6
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    Gene affecting superoxide dismutase activity linked to the histocompatibility complex in H-2 congenic mice (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-01-04
    Description: The activity of cyanide-sensitive, Cu-Zn superoxide dismutase (SOD) was studied in liver sytosols from H-2 congenic strains of mice. Higher SOD activity was found in livers of mice having H-2b/A.BY, B10, and C3H.SW/haplotypes than in those of H-2a, H-2k and H-2d haplotypes. Segregation studies supported these correlations. In H-2 recombinant strains of mice, the genes influencing the liver SOD activity occur, as ascertained by mapping techniques, at or near the H-2d region of the major histocompatibility complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Novak, R -- Bosze, Z -- Matkovics, B -- Fachet, J -- New York, N.Y. -- Science. 1980 Jan 4;207(4426):86-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7350646" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Genes ; Genes, Regulator ; Genetic Linkage ; H-2 Antigens/*genetics ; Liver/enzymology ; *Major Histocompatibility Complex ; Mice ; Superoxide Dismutase/*genetics
    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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  • 7
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    Altering genotype and phenotype by DNA-mediated gene transfer (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Transformation, or DNA-mediated gene transfer, permits the introduction of new genetic information into a cell and frequently results in a change in phenotype. The transforming DNA is ultimately integrated into a recipient cell chromosome. No unique chromosomal locations are apparent, different lines contain the transforming DNA on different chromosomes. Expression of transformed genes frequently results in the synthesis of new polypeptide products which restore appropriate mutant cells to the wild-type phenotype. Thus transformation provides an in vivo assay for the functional role of DNA sequence organization about specific genes. Transforming genes coding for selectable functions, such as adenine phosphoribosyltransferase or thymidine kinase, have now been isolated by utilizing transformation in concert with molecular cloning. Finally, transformation may provide a general approach to the analysis of complex heritable phenotypes by permitting the distinction between phenotypic changes without concomitant changes in DNA and functional genetic rearrangements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellicer, A -- Robins, D -- Wold, B -- Sweet, R -- Jackson, J -- Lowy, I -- Roberts, J M -- Sim, G K -- Silverstein, S -- Axel, R -- CA 16346/CA/NCI NIH HHS/ -- CA 17477/CA/NCI NIH HHS/ -- CA 23767/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1414-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414320" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Phosphoribosyltransferase/*genetics ; Cloning, Molecular/methods ; DNA/*genetics ; *DNA, Recombinant ; Genes ; Genotype ; Mutation ; Pentosyltransferases/*genetics ; Phenotype ; Recombination, Genetic ; Selection, Genetic ; Thymidine Kinase/*genetics ; *Transformation, 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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  • 8
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    Regional assignment of genes for human esterase D and retinoblastoma to chromosome band 13q14 (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-30
    Description: The expression of human esterase D was evaluated quantitatively and qualitatively in five persons with partial deletions or duplications of chromosome 13. The results showed that the locus of this enzyme is at band 13q14. Deletion of this same band in other subjects has been found previously to indicate a predisposition to the development of retinoblastoma, which was present in the four individuals in this study who had partial deletions of chromosome 13. Because of this close synteny, esterase D evaluation should aid in the diagnosis and genetic counseling of retinoblastoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sparkes, R S -- Sparkes, M C -- Wilson, M G -- Towner, J W -- Benedict, W -- Murphree, A L -- Yunis, J J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1042-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375916" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Deletion ; Chromosome Mapping ; *Chromosomes, Human, 13-15 ; Esterases/*genetics ; Female ; Genes ; Humans ; Intellectual Disability/enzymology/genetics ; Male ; Retinoblastoma/enzymology/*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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  • 9
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    Directed deletion of a yeast transfer RNA intervening sequence (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Many eukaryotic genes contain intevening sequences, segments of DNA that interrupt the continuity of the gene. They are removed from RNA transcripts of the gene by a process known as splicing. The intervening sequence in a yeast tyrosine transfer RNA (tRNA Tyr) suppressor gene was deleted in order to test its role in the expression of the gene. The altered gene and its parent were introduced into yeast by transformation. Both genes exhibited suppressor function, showing that the intervening sequence is not absolutely essential for the expression of this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, R B -- Johnson, P F -- Tanaka, S -- Schold, M -- Itakura, K -- Abelson, J -- CA10984/CA/NCI NIH HHS/ -- GM 26391/GM/NIGMS NIH HHS/ -- GM 35658/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1396-400.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6997991" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; DNA, Recombinant ; Genes ; Mutation ; Nucleic Acid Precursors/genetics ; Plasmids ; RNA, Fungal/*genetics ; RNA, Transfer/*genetics ; Saccharomyces cerevisiae/genetics ; Suppression, Genetic ; Tyrosine
    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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  • 10
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
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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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  • 12
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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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  • 13
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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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  • 14
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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
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  • 15
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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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    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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    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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  • 18
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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
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  • 19
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    A revolution in biology (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, J -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1319-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251541" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular/methods ; DNA Transposable Elements ; *DNA, Recombinant ; Drug Industry ; Eukaryotic Cells/physiology ; Forecasting ; Genes ; Immunoglobulins/genetics ; Molecular Biology/*trends ; Mutation ; Transformation, Genetic
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  • 20
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    Disorders of human hemoglobin (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-01
    Description: Studies of the human hemoglobin system have provided new insights into the regulation of expression of a group of linked human genes, the gamma-delta-beta-globin gene complex in man. In particular, the thalassemia syndromes and related disorders of man are inherited anemias that provide mutations for the study of the regulation of globin gene expression. New methods, including restriction enzyme analysis and cloning of cellular DNA, have made it feasible to define more precisely the structure and organization of the globin genes in cellular DNA. Deletions of specific globin gene fragments have already been found in certain of these disorders and have been applied in prenatal diagnosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bank, A -- Mears, J G -- Ramirez, F -- New York, N.Y. -- Science. 1980 Feb 1;207(4430):486-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352255" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Aberrations/genetics ; Chromosome Deletion ; Chromosome Disorders ; Fetal Hemoglobin/genetics ; Genes ; Genetic Linkage ; Globins/*genetics ; Hemoglobins/*biosynthesis ; Hemoglobins, Abnormal/*genetics ; Humans ; Nucleic Acid Precursors/genetics ; Polymorphism, Genetic ; RNA, Messenger/genetics ; Thalassemia/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Tissue specificity of enzyme expression regulated by diffusible factors: evidence in Drosophila hybrids (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-29
    Description: Pairs of hybridizable species of Hawaiian picture-winged Drosophila differ qualitatively in the distributions of specific enzymes in their tissues. An examination of the patterns of enzyme expression in the hybrids showed that, in three instances, absence of an enzyme from a specific tissue was dominant to presence. Since other developmental features indicated that both parental genomes were functioning, these results suggest that, in these cases, the pattern differences in the parental species were due to diffusible factors that affected expression of the relevant structural genes rather than to differences in the genes themselves or in cis-acting regulatory sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickinson, W J -- New York, N.Y. -- Science. 1980 Feb 29;207(4434):995-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352303" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/enzymology ; Alcohol Oxidoreductases/genetics ; Aldehyde Oxidoreductases/genetics ; Animals ; Drosophila/embryology/*enzymology/genetics ; Genes ; *Genes, Regulator ; Hybridization, Genetic ; Malpighian Tubules/enzymology ; Octanols ; Tissue Distribution
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    DNA gyrase and the supercoiling of DNA (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-29
    Description: Negative supercoiling of bacterial DNA by DNA gyrase influences all metabolic processes involving DNA and is essential for replication. Gyrase supercoils DNA by a mechanism called sign inversion, whereby a positive supercoil is directly inverted to a negative one by passing a DNA segment through a transient double-strand break. Reversal of this scheme relaxes DNA, and this mechanism also accounts for the ability of gyrase to catenate and uncatenate DNA rings. Each round of supercoiling is driven by a conformational change induced by adenosine triphosphate (ATP) binding: ATP hydrolysis permits fresh cycles. The inhibition of gyrase by two classes of antimicrobials reflects its composition from two reversibly associated subunits. The A subunit is particularly associated with the concerted breakage-and-rejoining of DNA and the B subunit mediates energy transduction. Gyrase is a prototype for a growing class of prokaryotic and eukaryotic topoisomerases that interconvert complex forms by way of transient double-strand breaks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cozzarelli, N R -- New York, N.Y. -- Science. 1980 Feb 29;207(4434):953-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6243420" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Animals ; DNA Topoisomerases, Type I/metabolism ; DNA Topoisomerases, Type II/genetics/*metabolism ; DNA, Superhelical/*metabolism ; Escherichia coli/enzymology ; Eukaryotic Cells/enzymology ; Genes ; Macromolecular Substances ; Nalidixic Acid/pharmacology ; Novobiocin/pharmacology ; Oxolinic Acid/pharmacology ; Substrate Specificity ; Topoisomerase II Inhibitors
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    Phase variation: evolution of a controlling element (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Phase variation in bacteria is regulated by homologous recombination at a specific DNA site. This recombinational event causes the inversion of a 970-base-pair DNA sequence that includes the promoter necessary for transcription of a flagellar gene. The invertible segment is flanked by two sites that are necessary for the inversion and contains a gene (hin) whose product mediates the inversion event. The hin gene shows extensive homology with the TnpR gene carried on the Tn3 transposon. It is also homologous with the gin gene carried on bacteriophage mu. These relationships suggest that the phase variation system may have evolved by the association of a transposon with a resident gene and the subsequent specialization of these elements to regulate flagellar antigen expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, M -- Zieg, J -- Silverman, M -- Mandel, G -- Doolittle, R -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1370-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251543" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Base Sequence ; *DNA Transposable Elements ; DNA, Bacterial/genetics ; Flagellin/*genetics ; Genes ; Recombination, Genetic ; Salmonella/*genetics
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    Recombinant DNA revisited (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singer, M -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1317.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414317" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *DNA, Recombinant ; Genes ; Humans ; Molecular Biology/trends
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    Human gene treatment stirs new debate (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-10-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G B -- Wade, N -- New York, N.Y. -- Science. 1980 Oct;210(4468):407.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6933693" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/therapy ; Bone Marrow Cells ; Ethics Committees, Research ; Genes ; Genetic Engineering/*methods ; Globins/genetics ; Humans ; Thalassemia/genetics/*therapy ; Thymidine Kinase/genetics
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    Interferon congress highlights (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-11-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1980 Nov 28;210(4473):998.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6159687" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents ; Congresses as Topic ; DNA, Recombinant ; Genes ; Humans ; *Interferons/genetics/therapeutic use
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    At least three human type alpha interferons: structure of alpha 2 (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: The sequence of a human leukocyte-derived complementary DNA (cDNA), Hif-2h, which directs the formation in Escherichia coli of a polypeptide, IFN-alpha 1, with interferon (IFN) activity has been described. A second IFN cDNA, Hif-SN206, which also elicits synthesis of a biologically active IFN, IFN-alpha 2, is described in this article. Whereas IFN-alpha 2 is twice as active on human as on bovine cells, IFN-alpha 1 is 10 to 20 times more active on bovine than on human cells. As deduced from the cDNA's, the messenger RNA's for the two IFN's differ in length and in 20 percent of the nucleotides; the mature IFN polypeptides differ in 17 percent of the amino acids. Both IFN-alpha 1 and IFN-alpha 2 differ from the lymphoblastoid IFN described by others. Therefore, at least three different IFN-alpha genes are expressed in man; studies on genomic DNA reveal the presence of at least eight IFN-related genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Streuli, M -- Nagata, S -- Weissmann, C -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1343-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6158094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA, Recombinant ; Escherichia coli/genetics ; Genes ; Humans ; *Interferons/genetics ; Leukocytes ; Lymphocytes ; Mice ; RNA, Messenger/genetics ; Structure-Activity Relationship
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    Steps toward computer analysis of nucleotide sequences (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Advances in recombinant DNA technology have allowed the isolation of large numbers of biologically interesting fragments of DNA. Concomitant improvements in methods for nucleic acid sequencing have led many investigators to characterize their clones by sequencing them. This has resulted in the accumulation of such large amounts of sequence data that computer-assisted methods, with programs directed toward the manipulation of nucleic acid sequences, have become indispensable during the collection and analysis of that data.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gingeras, T R -- Roberts, R J -- 1R01-CA27275-01/CA/NCI NIH HHS/ -- CA 13106/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1322-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251542" target="_blank"〉PubMed〈/a〉
    Keywords: Autoanalysis ; *Base Sequence ; *Computers ; DNA Restriction Enzymes ; DNA, Viral ; Genes ; Hydrogen Bonding ; Nucleic Acid Conformation ; Nucleic Acid Precursors/genetics ; *Nucleic Acids ; RNA, Transfer/genetics ; Substrate Specificity
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    Thalassemias: models of genetic diseases (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-10-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G B -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):300-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423190" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Deletion ; Gene Expression Regulation ; Genes ; Globins/*genetics ; Humans ; Models, Genetic ; Nucleic Acid Precursors/genetics ; RNA, Messenger/genetics ; Thalassemia/blood/*genetics ; Transcription, Genetic
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    Mouse globin system: a functional and evolutionary analysis (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Structural and functional analysis of the mouse alpha-globin and beta-globin genes reveals that the globin genes are encoded in discontinous bits of coding information and that each gene locus is much more complex than was originally supposed. Each seems to consist of an array of several authentic genes as well as several apparently inactive pseudogenes. Comparison of the sequences of some of these genes to one another indicates that chromosomal DNA is a dynamic structure. Flanking and intervening sequences change in two ways: quickly, by duplication and extensive insertions and deletions, and slowly, by point mutation. Active coding sequences are usually limited to the slower mode of evolution. In addition to identifying fast and slow modes of evolution, it has also been possible to test the function of several signals that surround these genes and to identify those that appear to play a role in gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leder, P -- Hansen, J N -- Konkel, D -- Leder, A -- Nishioka, Y -- Talkington, C -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1336-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Genes ; Globins/*genetics ; Mice ; Nucleic Acid Hybridization ; Nucleic Acid Precursors/genetics ; RNA, Messenger/genetics/metabolism
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    Lactate dehydrogenases of Atlantic hagfish: physiological and evolutionary implications of a primitive heart isozyme (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-02-15
    Description: Isozymes of lactate dehydrogenase from heart and muscle of Atlantic hagfish show less functional divergence than those from other fishes and higher vertebrates. The enzyme from hagfish heart (B4) displays a higher Michaelis constant for pyruvate and lower substrate inhibition at moderate pyruvate concentrations than heart isozymes from other species. These properties support the hypothesis that the ancestral vertebrate lactate dehydrogenase was a muscle (A4)-type enzyme and also suggest a role for the B4 enzyme in the unusual physiology of hagfish cardiac tissue which functions under sustained hypoxic conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidell, B D -- Beland, K F -- New York, N.Y. -- Science. 1980 Feb 15;207(4432):769-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352286" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; Animals ; *Biological Evolution ; Energy Metabolism ; Fishes/genetics/*physiology ; Genes ; Isoenzymes ; Kinetics ; L-Lactate Dehydrogenase/*genetics/metabolism ; Muscles/*enzymology ; Myocardium/enzymology ; Pyruvates/metabolism
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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)
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    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
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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)
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    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
    Published by American Association for the Advancement of Science (AAAS)
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  • 34
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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
    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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  • 35
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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
    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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