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  • 1
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    Removal of nonhomologous DNA ends in double-strand break recombination: the role of the yeast ultraviolet repair gene RAD1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-16
    Description: Double-strand breaks (DSBs) in Saccharomyces cerevisiae can be repaired by gene conversions or by deletions resulting from single-strand annealing between direct repeats of homologous sequences. Although rad1 mutants are resistant to x-rays and can complete DSB-mediated mating-type switching, they could not complete recombination when the ends of the break contained approximately 60 base pairs of nonhomology. Recombination was restored when the ends of the break were made homologous to donor sequences. Additionally, the absence of RAD1 led to the frequent appearance of a previously unobserved type of recombination product. These data suggest RAD1 is required to remove nonhomologous DNA from the 3' ends of recombining DNA, a process analogous to the excision of photodimers during repair of ultraviolet-damaged DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fishman-Lobell, J -- Haber, J E -- GM01722/GM/NIGMS NIH HHS/ -- GM20056/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):480-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411547" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; Deoxyribonucleases, Type II Site-Specific/*metabolism ; Gene Conversion ; Kinetics ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Ultraviolet Rays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Renin-specific antibody for study of cardiovascular homeostasis (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-07
    Description: Antiserum specific for purified canine renal renin was used to inhibit this enzyme in trained, conscious dogs. The antiserum did not affect blood pressure in sodium-replete dogs but decreased plasma renin activity and blood pressure in sodium-depleted animals. The antiserum also reduced blood pressure to control levels concomitant with suppression of plasma renin activity in uninephrectomized dogs with acute renovascular hypertension. These observations establish the role of the renin-angiotensin system in the maintenance of blood pressure in the sodium-depleted state as well as in the initiation of renovascular hypertension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dzau, V J -- Kopelman, R I -- Barger, A C -- Haber, E -- New York, N.Y. -- Science. 1980 Mar 7;207(4435):1091-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6986653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Specificity ; Antigen-Antibody Reactions ; *Blood Pressure ; Diet, Sodium-Restricted ; Dogs ; Homeostasis ; Hypertension, Renal/*enzymology ; Hypertension, Renovascular/*enzymology ; Immunologic Techniques ; Kidney/blood supply ; Renin/antagonists & inhibitors/blood/*immunology ; Vascular Resistance
    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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  • 3
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    Lethal disruption of the yeast actin gene by integrative DNA transformation (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-23
    Description: A mutant allele of the chromosomal locus corresponding to the cloned actin gene of the yeast Saccharomyces cerevisiae has been constructed by DNA transformation with a hybrid plasmid which integrates into, and thereby disrupts, the protein-encoding sequences of the gene. In a diploid strain of yeast, disruption of the actin gene on one chromosome results in a mutation that segregates as a recessive lethal tightly linked to a selectable genetic marker on the integrated plasmid. The actin gene, therefore, must encode an essential function for yeast cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shortle, D -- Haber, J E -- Botstein, D -- GM18973/GM/NIGMS NIH HHS/ -- GM20056/GM/NIGMS NIH HHS/ -- GM21253/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Jul 23;217(4557):371-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7046050" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*genetics/physiology ; Alleles ; Cloning, Molecular ; DNA, Fungal/genetics ; DNA, Recombinant ; Genes, Lethal ; Genes, Recessive ; Plasmids ; Recombination, Genetic ; Saccharomyces cerevisiae/*genetics ; Transformation, 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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  • 4
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    Myocardial infarct imaging of antibodies to canine cardiac myosin with indium-111-diethylenetriamine pentaacetic acid (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-11
    Description: Antibodies, by virtue of marked selectivity and affinity, may lend themselves to identification of structures of unique antigenic specificity in vivo. In experimental myocardial infarction in dogs, F(ab')2 fragments of antibodies to cardiac myosin that had been labeled with iodine-131 were shown to localize within the lesion. Because the energy characteristics of iodine isotopes are not ideal for imaging with a gamma camera, a new method for labeling antibody fragments with divalent or polyvalent radionuclides was developed. A bifunctional chelating agent, diethylenetriamine pentaacetic acid was covalently coupled, by an amide bond, to Fab fragments of antibodies to canine cardiac myosin. A stable chelate was then formed with indium-111, a nuclide that has appropriate half-life and energy characteristics for gamma imaging. Antibodies treated in this way retain their antigen-binding activity and are useful in locating myocardial infarcts in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khaw, B A -- Fallon, F T -- Strauss, H W -- Haber, E -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):295-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384803" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*analysis ; Dogs ; Immunoglobulin Fab Fragments/analysis ; Indium ; Myocardial Infarction/*metabolism ; Myocardium/*analysis ; Myosins/*analysis ; Radioisotopes
    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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