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  • 1
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    Proposed changes for NIH's Center for Scientific Review. Panel on Scientific Boundaries for Review. Center for Scientific Review Advisory Committee, National Institutes of Health (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alberts, B M -- Ayala, F J -- Botstein, D -- Frank, E -- Holmes, E W -- Lee, R D -- Macagno, E R -- Marrack, P -- Oparil, S -- Orkin, S H -- Rubenstein, A H -- Slayman, C W -- Sparling, P F -- Squire, L R -- von Hippel, P H -- Yamamoto, K R -- New York, N.Y. -- Science. 1999 Jul 30;285(5428):666-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10454921" target="_blank"〉PubMed〈/a〉
    Keywords: National Institutes of Health (U.S.)/*organization & administration ; *Peer Review, Research ; Public Policy ; Research ; United States
    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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  • 2
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    Mammalian glucocorticoid receptor derivatives enhance transcription in yeast (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: In mammalian cells, the glucocorticoid receptor binds specifically to glucocorticoid response element (GRE) DNA sequences and enhances transcription from linked promoters. It is shown here that derivatives of the glucocorticoid receptor also enhance transcription when expressed in yeast. Receptor-mediated enhancement in yeast was observed in fusions of GRE sequences to the yeast cytochrome c1 (CYC1) promoter; the CYC1 upstream activator sequences were not essential, since enhancement was observed in fusions of GREs to mutant CYC1 promoters retaining only the TATA region and transcription startpoints. It is concluded that the receptor operates by a common, highly conserved mechanism in yeast and mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schena, M -- Yamamoto, K R -- CA20535-12/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):965-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3043665" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/metabolism ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Immunoassay ; Plasmids ; Promoter Regions, Genetic ; Rats ; Receptors, Glucocorticoid/*genetics ; Saccharomyces cerevisiae/*genetics ; *Transcription, Genetic
    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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    In vitro transcription enhancement by purified derivatives of the glucocorticoid receptor (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-07-21
    Description: Mammalian glucocorticoid receptors enhance transcription from linked promoters by binding to glucocorticoid response element (GRE) DNA sequences. Understanding the mechanism of receptor action will require biochemical studies with purified components. Enhancement was observed in vitro with derivatives of the receptor that were expressed in Escherichia coli, purified, and added to a cell-free extract from Drosophila embryo nuclei. Transcription from promoters linked to one or multiple GREs was selectively enhanced by as much as six times. The effect was weaker with only one GRE, and enhancement was abolished by a point mutation that inactivates the GRE in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freedman, L P -- Yoshinaga, S K -- Vanderbilt, J N -- Yamamoto, K R -- New York, N.Y. -- Science. 1989 Jul 21;245(4915):298-301.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2473529" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics/metabolism ; Drosophila melanogaster ; Mutation ; Promoter Regions, Genetic ; RNA/biosynthesis ; Rats ; Receptors, Glucocorticoid/*genetics/isolation & purification/metabolism ; Templates, Genetic ; *Transcription, Genetic
    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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  • 4
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    Transcription factor interactions: selectors of positive or negative regulation from a single DNA element (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-14
    Description: The mechanism by which a single factor evokes opposite regulatory effects from a specific DNA sequence is not well understood. In this study, a 25-base pair element that resides upstream of the mouse proliferin gene was examined; it conferred on linked promoters either positive or negative glucocorticoid regulation, depending upon physiological context. This sequence, denoted a "composite" glucocorticoid response element (GRE), was bound selectively in vitro both by the glucocorticoid receptor and by c-Jun and c-Fos, components of the phorbol ester-activated AP-1 transcription factor. Indeed, c-Jun and c-Fos served as selectors of hormone responsiveness: the composite GRE was inactive in the absence of c-Jun, whereas it conferred a positive glucocorticoid effect in the presence of c-Jun, and a negative glucocorticoid effect in the presence of c-Jun and relatively high levels of c-Fos. The receptor also interacted selectively with c-Jun in vitro. A general model for composite GRE action is proposed that invokes both DNA binding and protein-protein interactions by receptor and nonreceptor factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, M I -- Miner, J N -- Yoshinaga, S K -- Yamamoto, K R -- New York, N.Y. -- Science. 1990 Sep 14;249(4974):1266-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2119054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cross-Linking Reagents ; DNA-Binding Proteins/physiology ; Gene Expression Regulation/genetics/*physiology ; Glucocorticoids/physiology ; Glycoproteins/*genetics ; HeLa Cells ; Humans ; Intercellular Signaling Peptides and Proteins ; Mice ; Molecular Sequence Data ; Proto-Oncogene Proteins/physiology ; Proto-Oncogene Proteins c-fos ; Proto-Oncogene Proteins c-jun ; Receptors, Glucocorticoid/metabolism ; Regulatory Sequences, Nucleic Acid/genetics ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/*physiology ; Transcription, Genetic/drug effects
    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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    Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-04
    Description: The SWI1, SWI2, and SWI3 proteins, which are required for regulated transcription of numerous yeast genes, were found also to be essential for rat glucocorticoid receptor function in yeast; the receptor failed to activate transcription in strains with mutations in the SWI1, SWI2, or SWI3 genes. Certain mutations in genes encoding components of chromatin, identified as suppressors of swi mutations, partially relieved the SWI- requirement for receptor function. Immunoprecipitation of glucocorticoid receptor derivatives from wild-type (SWI+) yeast extracts coprecipitated the SWI3 protein; such receptor-SWI3 complexes were not detected in swi1- or swi2- mutant strains, implying that a complex of multiple SWI proteins may associate with the receptor. Prior incubation of a Drosophila embryo transcription extract with the yeast SWI3-specific antibody inhibited receptor function in vitro whereas the antibody had no effect if added after initiation complex formation. Thus, positive regulation by the glucocorticoid receptor in vivo and in vitro appears to require its interaction, at an early step, with one or more SWI proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshinaga, S K -- Peterson, C L -- Herskowitz, I -- Yamamoto, K R -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1598-604.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1360703" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Animals ; Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; DNA-Binding Proteins/genetics/*metabolism ; Fungal Proteins/genetics/*metabolism ; Gene Deletion ; *Gene Expression Regulation, Fungal ; Glucosephosphate Dehydrogenase/genetics/metabolism ; Nuclear Proteins/genetics/*metabolism ; Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Rats ; Receptors, Glucocorticoid/*genetics/metabolism ; Receptors, Steroid/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; TATA Box ; *Trans-Activators ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Tyrosine Transaminase/genetics/metabolism ; beta-Galactosidase/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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  • 6
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    Solution structure of the glucocorticoid receptor DNA-binding domain (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-13
    Description: The three-dimensional structure of the DNA-binding domain (DBD) of the glucocorticoid receptor has been determined by nuclear magnetic resonance spectroscopy and distance geometry. The structure of a 71-residue protein fragment containing two "zinc finger" domains is based on a large set of proton-proton distances derived from nuclear Overhauser enhancement spectra, hydrogen bonds in previously identified secondary structure elements, and coordination of two zinc atoms by conserved cysteine residues. The DBD is found to consist of a globular body from which the finger regions extend. A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed. The model is consistent with previous results indicating that specific amino acid residues of the DBD are involved in protein-DNA and protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hard, T -- Kellenbach, E -- Boelens, R -- Maler, B A -- Dahlman, K -- Freedman, L P -- Carlstedt-Duke, J -- Yamamoto, K R -- Gustafsson, J A -- Kaptein, R -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):157-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Utrecht, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115209" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/*metabolism ; DNA-Binding Proteins/analysis/*metabolism ; Humans ; Magnetic Resonance Spectroscopy ; Metalloproteins/analysis ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments/analysis/metabolism ; Protein Conformation ; Rats ; Receptors, Glucocorticoid/*analysis/metabolism ; Regulatory Sequences, Nucleic Acid ; Zinc/analysis
    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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    DNA binding site sequence directs glucocorticoid receptor structure and activity (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-18
    Description: Genes are not simply turned on or off, but instead their expression is fine-tuned to meet the needs of a cell. How genes are modulated so precisely is not well understood. The glucocorticoid receptor (GR) regulates target genes by associating with specific DNA binding sites, the sequences of which differ between genes. Traditionally, these binding sites have been viewed only as docking sites. Using structural, biochemical, and cell-based assays, we show that GR binding sequences, differing by as little as a single base pair, differentially affect GR conformation and regulatory activity. We therefore propose that DNA is a sequence-specific allosteric ligand of GR that tailors the activity of the receptor toward specific target genes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777810/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777810/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meijsing, Sebastiaan H -- Pufall, Miles A -- So, Alex Y -- Bates, Darren L -- Chen, Lin -- Yamamoto, Keith R -- GM08537/GM/NIGMS NIH HHS/ -- R01 CA020535/CA/NCI NIH HHS/ -- R01 CA020535-31/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2009 Apr 17;324(5925):407-10. doi: 10.1126/science.1164265.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19372434" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Line, Tumor ; Crystallography, X-Ray ; DNA/*chemistry/*metabolism ; Humans ; Ligands ; Models, Molecular ; Mutation ; Protein Conformation ; Protein Isoforms/chemistry/metabolism ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Receptors, Glucocorticoid/chemistry/genetics/*metabolism ; Transcriptional Activation
    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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  • 8
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    Medicine. Consent from donors for embryo and stem cell research (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-16
    Description: As research with human embryos and embryonic stem cells proceeds, the authors of this Policy Forum argue that all donors of biological materials should give informed consent, including oocyte and sperm donors. Informed consent is particularly important because of the diverse opinions and strong emotions that surround such research. Some gamete donors who are willing to help women and couples bear children may object to the use of their genetic materials for certain types of research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lo, Bernard -- Chou, Vicki -- Cedars, Marcelle I -- Gates, Elena -- Taylor, Robert N -- Wagner, Richard M -- Wolf, Leslie -- Yamamoto, Keith R -- New York, N.Y. -- Science. 2003 Aug 15;301(5635):921.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Medical Ethics, School of Medicine at the University of California, San Francisco, CA 94143, USA. bernie@medicine.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12920284" target="_blank"〉PubMed〈/a〉
    Keywords: *Embryo Research ; Embryo, Mammalian/*cytology ; Female ; Humans ; *Informed Consent ; Male ; Oocytes ; Reproductive Techniques, Assisted ; Spermatozoa ; *Stem Cells ; *Tissue Donors
    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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  • 9
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    Disassembly of transcriptional regulatory complexes by molecular chaperones (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Many biological processes are initiated by cooperative assembly of large multicomponent complexes; however, mechanisms for modulating or terminating the actions of these complexes are not well understood. For example, hormone-bound intracellular receptors (IRs) nucleate formation of transcriptional regulatory complexes whose actions cease promptly upon hormone withdrawal. Here, we show that the p23 molecular chaperone localizes in vivo to genomic response elements in a hormone-dependent manner, disrupting receptor-mediated transcriptional activation in vivo and in vitro; Hsp90 weakly displayed similar activities. Indeed, p23 and Hsp90 also disrupted the activities of some non-IR-containing transcriptional regulatory complexes. We suggest that molecular chaperones promote disassembly of transcriptional regulatory complexes, thus enabling regulatory machineries to detect and respond to signaling changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeman, Brian C -- Yamamoto, Keith R -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2232-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Structural Biology, University of Illinois, Urbana-Champaign, 601 South Goodwin Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/metabolism ; Dexamethasone/metabolism/pharmacology ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/*metabolism ; HeLa Cells ; Humans ; Molecular Chaperones/*metabolism ; Nuclear Receptor Coactivator 2 ; Phosphoproteins/*metabolism ; Promoter Regions, Genetic ; Rats ; Receptors, Cytoplasmic and Nuclear/*metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Retinoic Acid/metabolism ; Receptors, Thyroid Hormone/metabolism ; Recombinant Fusion Proteins/metabolism ; *Response Elements ; Retinoid X Receptors ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Tryptophan Oxygenase/genetics ; Tumor Cells, Cultured ; Tyrosine Transaminase/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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  • 10
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    Hold 'em and fold 'em: chaperones and signal transduction (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohen, S P -- Kralli, A -- Yamamoto, K R -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1303-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4255, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761850" target="_blank"〉PubMed〈/a〉
    Keywords: Fungal Proteins/genetics/*physiology ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins/physiology ; HSP90 Heat-Shock Proteins/physiology ; *Heat-Shock Proteins ; Molecular Chaperones/*physiology ; Mutation ; Oncogene Protein pp60(v-src)/metabolism ; Protein Folding ; Receptors, Estrogen/metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Steroid/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
    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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