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  • Genes
  • American Association for the Advancement of Science (AAAS)  (110)
  • Annual Reviews
  • Nature Publishing Group
  • 2010-2014  (19)
  • 1980-1984  (91)
  • 1960-1964
  • 1955-1959
  • 1930-1934
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  • 101
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    Steps toward computer analysis of nucleotide sequences (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 102
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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
    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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  • 103
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    Mouse globin system: a functional and evolutionary analysis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 104
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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)
    Details
    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
    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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  • 105
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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
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 106
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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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  • 107
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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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    Electronic ISSN: 1095-9203
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  • 108
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    Isolation of human C-reactive protein complementary DNA and localization of the gene to chromosome 1 (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-07-01
    Description: With a synthetic oligonucleotide mixture as probe, complementary DNA clones of C-reactive protein were isolated from an adult human liver complementary DNA library. The clones ranged in size from 700 to 1100 base pairs and were identified by partial DNA sequence analysis. One complementary DNA clone was used as a probe for hybridization with human-rodent DNA's isolated from somatic cell hybrids and bound to nitrocellulose filters (Southern blot analysis) to assign the human C-reactive protein gene to chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitehead, A S -- Bruns, G A -- Markham, A F -- Colten, H R -- Woods, D E -- AI15033/AI/NIAID NIH HHS/ -- HD4807/HD/NICHD NIH HHS/ -- HL22487/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):69-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; C-Reactive Protein/*genetics ; *Chromosome Mapping ; *Chromosomes, Human, 1-3 ; Cloning, Molecular ; Cricetinae ; DNA/*genetics/isolation & purification ; Genes ; Humans ; Hybrid Cells/metabolism ; Mice
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 109
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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
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  • 110
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    Directed mutagenesis of dihydrofolate reductase (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations--at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine--were designed to answer questions about the relations between molecular structure and function that were raised by the x-ray crystal structures. Properties of the mutant proteins show that Asp-27 is important for catalysis and that perturbation of the local structure at a conserved cis peptide bond following Gly-95 abolishes activity. Substitution of cysteine for proline at residue 39 results in the appearance of new forms of the enzyme that correspond to various oxidation states of the cysteine. One of these forms probably represents a species cross-linked by an intrachain disulfide bridge between the cysteine at position 85 and the new cysteine at position 39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Villafranca, J E -- Howell, E E -- Voet, D H -- Strobel, M S -- Ogden, R C -- Abelson, J N -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):782-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Disulfides ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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