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  • 1
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    Zinc fingers in Caenorhabditis elegans: finding families and probing pathways (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-16
    Description: More than 3 percent of the protein sequences inferred from the Caenorhabditis elegans genome contain sequence motifs characteristic of zinc-binding structural domains, and of these more than half are believed to be sequence-specific DNA-binding proteins. The distribution of these zinc-binding domains among the genomes of various organisms offers insights into the role of zinc-binding proteins in evolution. In addition, the complete genome sequence of C. elegans provides an opportunity to analyze, and perhaps predict, pathways of transcriptional regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, N D -- Berg, J M -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2018-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Caenorhabditis elegans/*chemistry/genetics/metabolism ; *Caenorhabditis elegans Proteins ; DNA-Binding Proteins/chemistry/genetics/metabolism ; Evolution, Molecular ; GATA Transcription Factors ; Gene Expression Regulation ; Helminth Proteins/*chemistry/genetics/metabolism ; Membrane Proteins/chemistry/genetics/metabolism ; Receptors, Cell Surface/chemistry/genetics ; Trans-Activators/chemistry/genetics/metabolism ; Transcription Factors/chemistry/genetics/metabolism ; *Zinc Fingers
    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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    Mechanism of ribosomal peptide bond formation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, J M -- Lorsch, J R -- New York, N.Y. -- Science. 2001 Jan 12;291(5502):203.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, 725 North Wolfe Street, Baltimore, MD 21205, USA. jberg@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11406869" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/chemistry/*metabolism ; Catalysis ; Hydrogen-Ion Concentration ; Models, Chemical ; *Peptide Biosynthesis ; Protons ; RNA, Ribosomal/chemistry/*metabolism ; RNA, Transfer, Amino Acyl/chemistry/metabolism ; Ribosomes/chemistry/*metabolism
    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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    The problems of bonus pay (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Jeremy M -- New York, N.Y. -- Science. 2004 May 7;304(5672):824.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131290" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; *Employee Incentive Plans ; *Faculty, Medical ; *Research Personnel ; Research Support as Topic ; *Salaries and Fringe Benefits ; Schools, Medical ; United States
    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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    Science policy: Well-funded investigators should receive extra scrutiny (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Jeremy M -- England -- Nature. 2012 Sep 13;489(7415):203. doi: 10.1038/489203a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Pittsburgh, Pennsylvania 15260, USA. jberg@pitt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22972279" target="_blank"〉PubMed〈/a〉
    Keywords: Financing, Organized/*economics/*organization & administration ; Forecasting ; National Institutes of Health (U.S.)/*economics ; Peer Review, Research/*methods ; Research Personnel/*economics/standards ; Research Support as Topic/*economics/methods/*organization & administration ; United States
    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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  • 5
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    The galvanization of biology: a growing appreciation for the roles of zinc (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-23
    Description: Zinc ions are key structural components of a large number of proteins. The binding of zinc stabilizes the folded conformations of domains so that they may facilitate interactions between the proteins and other macromolecules such as DNA. The modular nature of some of these zinc-containing proteins has allowed the rational design of site-specific DNA binding proteins. The ability of zinc to be bound specifically within a range of tetrahedral sites appears to be responsible for the evolution of the side range of zinc-stabilized structural domains now known to exist. The lack of redox activity for the zinc ion and its binding and exchange kinetics also may be important in the use of zinc for specific functional roles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, J M -- Shi, Y -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1081-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Engineering ; Transcription Factors/chemistry/*metabolism ; Zinc/chemistry/metabolism/*physiology ; Zinc Fingers/*physiology
    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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  • 6
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    Specific DNA-RNA hybrid binding by zinc finger proteins (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: Zinc finger proteins of the Cys2His2 type represent a large class of proteins that have been assumed to function by means of specific interactions with DNA. Experiments motivated by structural characteristics of zinc finger protein-DNA complexes revealed that certain zinc finger proteins bound DNA-RNA hybrids with affinities comparable to or greater than those for DNA duplexes. The interactions between the zinc finger proteins and the DNA-RNA hybrids were dependent on which strand was RNA and were sequence-specific. Thus, interactions with DNA-RNA hybrids should be considered with regard to the biological roles of zinc finger proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, Y -- Berg, J M -- GM46257/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):282-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7536342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/chemistry/*metabolism ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA/chemistry/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Sp1 Transcription Factor/metabolism ; Zinc Fingers/*physiology
    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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  • 7
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    A Nobel lesson: the grant behind the prize (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Jeremy M -- New York, N.Y. -- Science. 2008 Feb 15;319(5865):900-1. doi: 10.1126/science.319.5865.900d.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18276870" target="_blank"〉PubMed〈/a〉
    Keywords: Financing, Government ; *National Institutes of Health (U.S.) ; *Nobel Prize ; *Peer Review, Research ; *Research Support as Topic ; United States
    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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  • 8
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    SCIENTIFIC COMMUNITY. Preprints for the life sciences (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Jeremy M -- Bhalla, Needhi -- Bourne, Philip E -- Chalfie, Martin -- Drubin, David G -- Fraser, James S -- Greider, Carol W -- Hendricks, Michael -- Jones, Chonnettia -- Kiley, Robert -- King, Susan -- Kirschner, Marc W -- Krumholz, Harlan M -- Lehmann, Ruth -- Leptin, Maria -- Pulverer, Bernd -- Rosenzweig, Brooke -- Spiro, John E -- Stebbins, Michael -- Strasser, Carly -- Swaminathan, Sowmya -- Turner, Paul -- Vale, Ronald D -- VijayRaghavan, K -- Wolberger, Cynthia -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2016 May 20;352(6288):899-901. doi: 10.1126/science.aaf9133.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Personalized Medicine, University of Pittsburgh School of Medicine. ; Department of Molecular, Cell and Developmental Biology, University of California, Santa Cruz. ; Office of the Director, National Institutes of Health. ; Department of Biological Sciences, Columbia University. ; Department of Molecular and Cell Biology, University of California, Berkeley. ; Department of Bioengineering and Therapeutic Sciences, University of California San Francisco. ; Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine. ; Department of Biology, McGill University. ; Wellcome Trust. ; Rockefeller University Press. ; Department of Systems Biology, Harvard Medical School. ; Yale School of Medicine, Yale University. ; Kimmel Center for Biology and Medicine of the Skirball Institute, Department of Cell Biology, New York University School of Medicine. ; European Molecular Biology Organization. ; The Leona M. and Harry B. Helmsley Charitable Trust. ; Simons Foundation. ; Laura and John Arnold Foundation. ; Gordon and Betty Moore Foundation. ; Nature Research Group. ; Department of Ecology and Evolutionary Biology, Yale University. ; Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California San Francisco. ron.vale@ucsf.edu. ; Department of Biotechnology, Ministry of Science and Technology, Government of India. ; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27199406" 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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  • 9
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    No myth: Benefits of breast screening (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-01-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Jeremy M -- Berg, Wendie A -- England -- Nature. 2016 Jan 21;529(7586):283. doi: 10.1038/529283b.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Pittsburgh, Pennsylvania, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26791708" 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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  • 10
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    Systematic variation in DNA length yields highly ordered repressor-operator cocrystals (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: Crystals have been grown that contain the operator-binding domain of the lambda repressor and the lambda operator site OL1. Crystallization conditions were tested with a set of DNA fragments, ranging in length from 17 to 23 base pairs. The best crystals were grown with a 20-base pair DNA fragment. These crystals have space-group symmetry P2I, with unit cell dimensions a = 37.1 A, b = 68.8 A, c = 56.8 A, and a beta angle of 91.5 degrees. They diffracted to at least 2.5 A resolution. High resolution data from these crystals should allow the direct determination of how a repressor recognizes its operator site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, S R -- Whitcombe, T V -- Berg, J M -- Pabo, C O -- GM 31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 20;230(4732):1383-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3906896" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromatography, High Pressure Liquid ; Crystallization ; DNA, Bacterial/*genetics ; Escherichia coli/genetics ; *Gene Expression Regulation ; Nucleic Acid Conformation ; Protein Conformation ; Repressor Proteins/*genetics/isolation & purification ; Structure-Activity Relationship ; Transcription Factors/*genetics ; X-Ray Diffraction
    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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