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  • 1
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    Identification of the DNA binding site for NGFI-B by genetic selection in yeast (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: An in vivo selection system for isolating targets of DNA binding proteins in yeast was developed and used to identify the DNA binding site for the NGFI-B protein, a member of the steroid-thyroid hormone receptor superfamily. The feasibility of the technique was verified by selecting DNA fragments that contained binding sites for GCN4, a well-characterized yeast transcriptional activator. The DNA binding domain of NGFI-B, expressed as part of a LexA-NGFI-B-GAL4 chimeric activator, was then used to isolate a rat genomic DNA fragment that contained an NGFI-B binding site. The NGFI-B response element (NBRE) is similar to but functionally distinct from elements recognized by the estrogen and thyroid hormone receptors and the hormone receptor-like proteins COUP-TF, CF1, and H-2RIIBP. Cotransfection experiments in mammalian cells demonstrated that NGFI-B can activate transcription from the NBRE with or without its putative ligand binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Fahrner, T J -- Johnston, M -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1296-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/*metabolism ; DNA-Binding Proteins/genetics/*metabolism/pharmacology ; Fungal Proteins/metabolism ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Plasmids ; *Protein Kinases ; Rats ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Repressor Proteins ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; *Serine Endopeptidases ; Transcription Factors/genetics/*metabolism/pharmacology ; Transcription, Genetic ; Transfection
    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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    Participation of non-zinc finger residues in DNA binding by two nuclear orphan receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/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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  • 3
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    Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-23
    Description: In mammalian cells, repair of DNA double-strand breaks (DSBs) by nonhomologous end-joining (NHEJ) is critical for genome stability. Although the end-bridging and ligation steps of NHEJ have been reconstituted in vitro, little is known about the end-processing reactions that occur before ligation. Recently, functionally homologous end-bridging and ligation activities have been identified in prokarya. Consistent with its homology to polymerases and nucleases, we demonstrate that DNA ligase D from Mycobacterium tuberculosis (Mt-Lig) possesses a unique variety of nucleotidyl transferase activities, including gap-filling polymerase, terminal transferase, and primase, and is also a 3' to 5' exonuclease. These enzyme activities allow the Mt-Ku and Mt-Lig proteins to join incompatible DSB ends in vitro, as well as to reconstitute NHEJ in vivo in yeast. These results demonstrate that prokaryotic Ku and ligase form a bona fide NHEJ system that encodes all the recognition, processing, and ligation activities required for DSB repair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Della, Marina -- Palmbos, Phillip L -- Tseng, Hui-Min -- Tonkin, Louise M -- Daley, James M -- Topper, Leana M -- Pitcher, Robert S -- Tomkinson, Alan E -- Wilson, Thomas E -- Doherty, Aidan J -- R01 CA102563/CA/NCI NIH HHS/ -- R01 CA102563-01A1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 22;306(5696):683-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Institute for Medical Research, University of Cambridge, Department of Haematology, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15499016" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/genetics/*metabolism ; DNA/*metabolism ; DNA Damage ; DNA Ligases/chemistry/genetics/*metabolism ; DNA Nucleotidyltransferases/chemistry/metabolism ; DNA Primase/chemistry/metabolism ; *DNA Repair ; DNA-Directed DNA Polymerase/chemistry/metabolism ; Exonucleases/chemistry/metabolism ; Mutation ; Mycobacterium tuberculosis/genetics/*metabolism ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Recombination, Genetic ; Saccharomyces cerevisiae/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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  • 4
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    Direct observation of native DNA structures with the scanning tunneling microscope (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-20
    Description: Uncoated double-stranded DNA dissolved in a salt solution was deposited on graphite and imaged in air with the scanning tunneling microscope (STM). The resolution was such that the major and minor grooves could be distinguished. The pitch of the helix varied between 27 and 63 angstroms in the images obtained. Thus the STM can be useful for structural studies of a variety of uncoated and isolated biomolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beebe, T P Jr -- Wilson, T E -- Ogletree, D F -- Katz, J E -- Balhorn, R -- Salmeron, M B -- Siekhaus, W J -- New York, N.Y. -- Science. 1989 Jan 20;243(4889):370-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lawrence Livermore National Laboratory, Department of Chemistry, Livermore, CA 94550.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911747" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; DNA/*ultrastructure ; Microscopy, Electron, Scanning/instrumentation/*methods ; *Nucleic Acid Conformation
    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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  • 5
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    Molecular biology: Breaks in the brain (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-03-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glover, Thomas W -- Wilson, Thomas E -- R21 ES022311/ES/NIEHS NIH HHS/ -- England -- Nature. 2016 Apr 7;532(7597):46-7. doi: 10.1038/nature17316. Epub 2016 Mar 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Human Genetics and Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27007850" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Optical turbulence characterization at the SAAO Sutherland site (2013)
    Oxford University Press
    Details
    Publication Date: 2013-10-29
    Description: We present results from the first year of a campaign to characterize and monitor the optical turbulence profile at the South African Astronomical Observatory's Sutherland observing station in South Africa. A Multi Aperture Scintillation Sensor Differential Image Motion Monitor (MASS-DIMM) was commissioned in 2010 March to provide continuous monitoring of the seeing conditions. Over the first month of the campaign, a Slope Detection And Ranging (SLODAR) from Durham University was also installed, allowing an independent verification of the performance of the MASS-DIMM device. After the first year of data collection, the overall median seeing value is found to be 1.32 arcsec as measured at ground level. The ground layer which includes all layers below 1 km accounts for 84 per cent of the turbulence, while the free atmosphere above 1 km accounts for 16 per cent with a median value of 0.41 arcsec. The median isoplanatic angle value is 1.92 arcsec, which is similar to other major astronomical sites. The median coherence time, calculated from corrected MASS measurements, is 2.85 ms. The seeing conditions at the site do show a strong correlation with wind direction, with bad seeing conditions being associated with winds from the south-east.
    Print ISSN: 0035-8711
    Electronic ISSN: 1365-2966
    Topics: Physics
    Published by Oxford University Press
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  • 7
    Electronic Resource
    Electronic Resource
    Novel approach to micro infrared sample preparation (1975)
    s.l. : American Chemical Society
    Analytical chemistry 47 (1975), S. 2482-2483 
    Details
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ac60364a033
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  • 8
    Electronic Resource
    Electronic Resource
    Simultaneous Synthesis of Two Inducible Enzymes in Staphylococcus aureus (1957)
    [s.l.] : Nature Publishing Group
    Nature 180 (1957), S. 761-761 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Studies conducted to date have been confined to single systems, and to our knowledge, little is known concerning the effect of one inducible system upon another under conditions favouring simultaneous induction of both. For this reason, we have compared the induction of nitrate reductase and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/180761a0
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  • 9
    Electronic Resource
    Electronic Resource
    Generation of high repetition rate far-infrared laser pulses (1994)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 64 (1994), S. 3383-3385 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We report the generation of pulsed optically pumped far-infrared (FIR) radiation with a repetition rate of 200 kHz. These pulses were obtained in a straightforward method by pumping a FIR resonator with a high repetition rate, rf-excited, waveguide CO2 laser. Pulses approximately 50 ns wide were generated both at 432.6 μm in HCOOH, and 117.7 μm in CH2F2. The pulse width of the FIR radiation was studied as a function of the CO2 pulse width, and the relative delay between the two was measured. Based on this data we conclude that the FIR radiation was gain switched and of a duration which was a function of either the gain bandwidth of the FIR transition, or more likely the FIR cavity parameters.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.111282
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  • 10
    Electronic Resource
    Electronic Resource
    Flotation of Dichromate Ion (1965)
    [s.l.] : Nature Publishing Group
    Nature 205 (1965), S. 1066-1068 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] ION flotation (foam separation) has been used by chemists and engineers for the removal of inorganic and organic anions and cations from aqueous solution. The process involves the addition of a surf ace-active ion of opposite charge to the ion to be separated. The resulting surface-active complex ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2051066a0
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