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  • 1985-1989  (342)
  • 1975-1979  (162)
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  • 1
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    U.s. Scientists and china (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J C -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1547.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17834400" target="_blank"〉PubMed〈/a〉
    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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    Action at a distance along a DNA (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: A number of ways are known by which an event at one location on a DNA molecule can affect an event at a distant location on the same molecule. Three classes of mechanisms are described for such distal actions: tracking or translocation of a protein along a DNA, the association of two proteins bound at separate sites to form a DNA loop in between, and distal interactions that are affected by the topology of the DNA. The basic characteristics of each type of mechanism are discussed in terms of the known physicochemical properties of DNA. The various modes of action at a distance are often interrelated. Examples include the formation of positively and negatively supercoiled DNA loops by tracking and the strong effects of DNA topology on looping.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J C -- Giaever, G N -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):300-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3281259" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA/genetics/metabolism ; DNA, Superhelical ; Deoxyribonucleoproteins/metabolism ; Models, Molecular ; *Nucleic Acid Conformation
    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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    Mount agung eruption provides test of a global climatic perturbation (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-10
    Description: The Mount Agung volcanic eruption in 1963 provides the best-documented global radiative perturbation to the earth's atmosphere currently available. Data on stratospheric aerosols produced by this eruption have been used as input to a model for the atmospheric thermal structure. The computed magnitude, sign, and phase lag of the temperature changes in both the stratosphere and the troposphere are in good agreement with observations, providing evidence that the climatic response to a global radiative perturbation is significant, as well as support for the use of theoretical models to predict climatic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hansen, J E -- Wang, W C -- Lacis, A A -- New York, N.Y. -- Science. 1978 Mar 10;199(4333):1065-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17844417" target="_blank"〉PubMed〈/a〉
    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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    Conformational changes in 16S ribosomal RNA induced by 30S ribosomal subunit proteins from Escherichia coli (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-12-01
    Description: Laser light scattering has been used to evaluate conformational differences between free 16S RNA and several specific protein-16S RNA complexes. Proteins that interact strongly with the 16S RNA early in subunit assembly stabilize the RNA chain against unfolding in 1 mM Mg2+ and actually promote the formation of a more compact teriary structure in 20 mM Mg2+. A vital function of these proteins may therfore consist in altering the configuration of the RNA so that further assembly reactions can take place.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bogdanov, A A -- Zimmermann, R A -- Wang, C C -- Ford, N C Jr -- New York, N.Y. -- Science. 1978 Dec 1;202(4371):999-1001.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/362531" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins ; Diffusion ; Escherichia coli ; Nucleic Acid Conformation ; Protein Binding ; RNA, Bacterial ; *RNA, Ribosomal ; Ribonucleoproteins ; *Ribosomal Proteins ; Ribosomes/*ultrastructure
    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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  • 5
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    Nonhistone proteins HMG1 and HMG2 change the DNA helical structure (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-24
    Description: Two chromatin nonhistone proteins (from calf thymus) of the high mobility group, HMG1 and HMG2, reduce the linking number (topological winding number) of a circular DNA if the covalent closure of the DNA is carried out in their presence. This indicates that these proteins can either unwind the double helix, or induce a supercoiling of the DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Javaherian, K -- Liu, J F -- Wang, J C -- New York, N.Y. -- Science. 1978 Mar 24;199(4335):1345-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/628842" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages ; Chromosomal Proteins, Non-Histone/*pharmacology ; *DNA, Circular ; DNA, Superhelical ; *DNA, Viral ; Nucleic Acid Conformation/drug effects ; Pseudomonas
    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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    Hv(1), a variable-region genetic marker of human immunoglobulin heavy chains (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-21
    Description: A new antigenic determinant was discovered with a hemagglutination-inhibition assay system. Designated Hv(1), it is located in the variable region of human immunoglobulin heavy chains of the G, M, and A classes. Pedigree and population analyses suggest that it has an autosomal dominant mode of inheritance. This represents the first description of an allotypic determinant in the variable region of human immunoglobulins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A C -- Mathur, S -- Pandey, J -- Siegel, F P -- Middaugh, C R -- Litman, G W -- New York, N.Y. -- Science. 1978 Apr 21;200(4339):327-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/416494" target="_blank"〉PubMed〈/a〉
    Keywords: *Binding Sites, Antibody ; Genes ; Hemagglutination Inhibition Tests ; Humans ; Immunoglobulin Fab Fragments/genetics ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Heavy Chains/*genetics ; *Immunoglobulin Variable Region ; Pedigree
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Crystallographic structure of the octameric histone core of the nucleosome at a resolution of 3.3 A (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-03
    Description: The structure of the (H2A-H2B-H3-H4)2 histone octamer has been determined by means of x-ray crystallographic techniques at a resolution of 3.3 angstroms. The octamer is a prolate ellipsoid 110 angstroms long and 65 to 70 angstroms in diameter, and its general shape is that of a rugby ball. The size and shape are radically different from those determined in earlier studies. The most striking feature of the histone octamer is its tripartite organization, that is, a central (H3-H4)2 tetramer flanked by two H2A-H2B dimers. The DNA helix, placed around the octamer in a path suggested by the features on the surface of the protein, appears like a spring holding the H2A-H2B dimers at either end of the (H3-H4)2 tetramer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burlingame, R W -- Love, W E -- Wang, B C -- Hamlin, R -- Nguyen, H X -- Moudrianakis, E N -- New York, N.Y. -- Science. 1985 May 3;228(4699):546-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3983639" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens ; Chromatin/ultrastructure ; DNA/metabolism ; *Histones/metabolism ; Models, Chemical ; Nucleosomes/*ultrastructure ; Protein Conformation ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-22
    Description: The x-ray structure of chicken skeletal muscle troponin C (TnC), the Ca2+-binding subunit of the troponin complex, shows that the protein is about 70 angstroms long with an unusual dumbbell shape. The carboxyl and amino domains are separated by a single long alpha helix of about nine turns. Only the two high-affinity Ca2+-Mg2+ sites of the COOH-domain are occupied by metal ions resulting in conformational differences between the COOH- and NH2-domains. These differences are probably important in the triggering of muscle contraction by TnC. Also the structure of TnC is relevant in understanding the function of other calcium-regulated proteins, in particular that of calmodulin because of its strong similarity in amino acid sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sundaralingam, M -- Bergstrom, R -- Strasburg, G -- Rao, S T -- Roychowdhury, P -- Greaser, M -- Wang, B C -- AM-34139/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 22;227(4689):945-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3969570" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calmodulin/physiology ; Chickens ; Muscle Contraction ; Muscles/physiology/ultrastructure ; Protein Conformation ; Troponin/*physiology ; Troponin C ; Turkeys ; X-Ray Diffraction
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  • 9
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    Tandem regions of yeast DNA topoisomerase II share homology with different subunits of bacterial gyrase (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-08
    Description: The nucleotide sequence for the Saccharomyces cerevisiae gene TOP2, which encodes DNA topoisomerase II, was compared with the sequence for bacterial DNA gyrase. The amino and carboxyl terminal halves of the single-subunit yeast enzyme showed homologies with the B and A subunits of bacterial gyrase, respectively, at corresponding positions along the polypeptide chains. Although the two enzymes differ in both quaternary structure and activity, the homology between the two proteins indicates mechanistic as well as structural similarities, and a probable evolutionary relationship.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lynn, R -- Giaever, G -- Swanberg, S L -- Wang, J C -- GM24544/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):647-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014661" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/enzymology/genetics ; DNA Topoisomerases, Type II/*genetics ; Escherichia coli/enzymology/genetics ; Genes, Fungal ; Saccharomyces cerevisiae/enzymology/*genetics ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
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  • 10
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    Structure of the DNA-Eco RI endonuclease recognition complex at 3 A resolution (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: The crystal structure of the complex between Eco RI endonuclease and the cognate oligonucleotide TCGCGAATTCGCG provides a detailed example of the structural basis of sequence-specific DNA-protein interactions. The structure was determined, to 3 A resolution, by the ISIR (iterative single isomorphous replacement) method with a platinum isomorphous derivative. The complex has twofold symmetry. Each subunit of the endonuclease is organized into an alpha/beta domain consisting a five-stranded beta sheet, alpha helices, and an extension, called the "arm," which wraps around the DNA. The large beta sheet consists of antiparallel and parallel motifs that form the foundations for the loops and alpha helices responsible for DNA strand scission and sequence-specific recognition, respectively. The DNA cleavage site is located in a cleft that binds the DNA backbone in the vicinity of the scissile bond. Sequence specificity is mediated by 12 hydrogen bonds originating from alpha helical recognition modules. Arg200 forms two hydrogen bonds with guanine while Glu144 and Arg145 form four hydrogen bonds to adjacent adenine residues. These interactions discriminate the Eco RI hexanucleotide GAATTC from all other hexanucleotides because any base substitution would require rupture of at least one of these hydrogen bonds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McClarin, J A -- Frederick, C A -- Wang, B C -- Greene, P -- Boyer, H W -- Grable, J -- Rosenberg, J M -- GM25671/GM/NIGMS NIH HHS/ -- GM33506/GM/NIGMS NIH HHS/ -- RR07084/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1526-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3024321" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Base Composition ; Binding Sites ; Chemistry, Physical ; Crystallization ; DNA/*metabolism ; DNA Restriction Enzymes/*metabolism ; Deoxyribonuclease EcoRI ; Hydrogen Bonding ; Macromolecular Substances ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Substrate Specificity
    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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