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  • Base Sequence  (4)
  • Immunoblotting  (2)
  • Promoter Regions, Genetic  (2)
  • 1
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    A single amino acid that determines the sensitivity of progesterone receptors to RU486 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-10
    Description: The progesterone analog RU486, an abortifacient, inhibits the action of progestins in humans but not in chickens or hamsters. Substitution of cysteine at position 575 by glycine in the hormone binding domain (HBD) of the chicken progesterone receptor (cPR) generated a cPR that binds RU486 and whose activity is antagonized by that compound. In fact, all receptors that bind RU486 have a glycine at the corresponding position. The hamster PR, like cPR, has a cysteine. Only glycine--not methionine or leucine--at position 575 allowed binding of RU486 to cPR. Substitution of this glycine by cysteine in the human PR (hPR) abrogated binding of RU486 but not that of an agonist. The corresponding mutation in the human glucocorticoid receptor resulted in a loss of binding of both dexamethasone and RU486. Examination of a series of 11 beta-substituted steroids showed that antagonism is not an intrinsic property of an antihormone, because one hPR antagonist acted as an agonist for a mutated hPR. The positioning of an aromatic 11 beta-substitution in the PR HBD appears to be critical for generating agonistic or antagonistic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benhamou, B -- Garcia, T -- Lerouge, T -- Vergezac, A -- Gofflo, D -- Bigogne, C -- Chambon, P -- Gronemeyer, H -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):206-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department Endocrinologie, Centre de Recherche Roussel-Uclaf, Romainville, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1372753" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; Female ; Humans ; Mifepristone/*pharmacology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Progesterone/analogs & derivatives/metabolism ; RNA/genetics/isolation & purification ; Receptors, Mineralocorticoid ; Receptors, Progesterone/*drug effects/genetics/metabolism ; Receptors, Steroid/drug effects/genetics/metabolism ; Recombinant Proteins/drug effects/metabolism ; Restriction Mapping ; Uterus/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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  • 2
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    Cloning of the 62-kilodalton component of basic transcription factor BTF2 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-04
    Description: Cloning of the mammalian basic transcription factors serves as a major step in understanding the mechanism of transcription initiation. The 62-kilodalton component (p62) of one of these transcription factors, BTF2 was cloned and overexpressed. A monoclonal antibody to this polypeptide inhibited transcription in vitro. Immunoaffinity experiments demonstrated that the 62-kilodalton component is closely associated with the other polypeptides present in the BTF2 factor. Sequence similarity suggests that BTF2 may be the human counterpart of RNA polymerase II initiation factor b from yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischer, L -- Gerard, M -- Chalut, C -- Lutz, Y -- Humbert, S -- Kanno, M -- Chambon, P -- Egly, J M -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes, Centre National de la Recherche Scientifique, Unite 184, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529339" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cloning, Molecular ; Escherichia coli/genetics ; Gene Expression ; HeLa Cells ; Humans ; Immunoblotting ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Recombinant Proteins/chemistry ; Sequence Homology, Nucleic Acid ; Transcription Factor TFIIH ; Transcription Factors/chemistry/*genetics ; *Transcription Factors, TFII ; 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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    Retinoic acid signaling affects cortical synchrony during sleep (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-08
    Description: Delta oscillations, characteristic of the electroencephalogram (EEG) of slow wave sleep, estimate sleep depth and need and are thought to be closely linked to the recovery function of sleep. The cellular mechanisms underlying the generation of delta waves at the cortical and thalamic levels are well documented, but the molecular regulatory mechanisms remain elusive. Here we demonstrate in the mouse that the gene encoding the retinoic acid receptor beta determines the contribution of delta oscillations to the sleep EEG. Thus, retinoic acid signaling, which is involved in the patterning of the brain and dopaminergic pathways, regulates cortical synchrony in the adult.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maret, Stephanie -- Franken, Paul -- Dauvilliers, Yves -- Ghyselinck, Norbert B -- Chambon, Pierre -- Tafti, Mehdi -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):111-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Integrative Genomics, University of Lausanne, Genopode, 1015 Lausanne-Dorigny, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cerebral Cortex/*physiology ; *Delta Rhythm ; Gene Deletion ; Gene Expression ; Mice ; Mice, Inbred Strains ; Polymorphism, Genetic ; Promoter Regions, Genetic ; Receptors, Retinoic Acid/biosynthesis/*genetics ; Reverse Transcriptase Polymerase Chain Reaction ; *Signal Transduction ; Sleep/*physiology ; Transcription, Genetic ; Tretinoin/*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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  • 4
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    DNA repair helicase: a component of BTF2 (TFIIH) basic transcription factor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-02
    Description: The human BTF2 basic transcription factor (also called TFIIH), which is similar to the delta factor in rat and factor b in yeast, is required for class II gene transcription. A strand displacement assay was used to show that highly purified preparation of BTF2 had an adenosine triphosphate-dependent DNA helicase activity, in addition to the previously characterized carboxyl-terminal domain kinase activity. Amino acid sequence analysis of the tryptic digest generated from the 89-kilodalton subunit of BTF2 indicated that this polypeptide corresponded to the ERCC-3 gene product, a presumed helicase implicated in the human DNA excision repair disorders xeroderma pigmentosum and Cockayne's syndrome. These findings suggest that transcription and nucleotide excision repair may share common factors and hence may be considered to be functionally related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaeffer, L -- Roy, R -- Humbert, S -- Moncollin, V -- Vermeulen, W -- Hoeijmakers, J H -- Chambon, P -- Egly, J M -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):58-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UPR 6520 (CNRS), Unite 184 (INSERM), Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465201" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Binding Sites ; Cockayne Syndrome/enzymology/genetics ; DNA/metabolism ; DNA Helicases/metabolism ; *DNA Repair ; Humans ; Immunoblotting ; Peptide Fragments ; Promoter Regions, Genetic ; Protein Kinases/metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Sequence Analysis ; Transcription Factor TFIIH ; Transcription Factors/*metabolism ; *Transcription Factors, TFII ; Transcription, Genetic ; Trypsin/metabolism ; Xeroderma Pigmentosum/enzymology/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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  • 5
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    Gastric mucosa abnormalities and tumorigenesis in mice lacking the pS2 trefoil protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: To determine the function of the pS2 trefoil protein, which is normally expressed in the gastric mucosa, the mouse pS2 (mpS2) gene was inactivated. The antral and pyloric gastric mucosa of mpS2-null mice was dysfunctional and exhibited severe hyperplasia and dysplasia. All homozygous mutant mice developed antropyloric adenoma, and 30 percent developed multifocal intraepithelial or intramucosal carcinomas. The small intestine was characterized by enlarged villi and an abnormal infiltrate of lymphoid cells. These results indicate that mpS2 is essential for normal differentiation of the antral and pyloric gastric mucosa and may function as a gastric-specific tumor suppressor gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lefebvre, O -- Chenard, M P -- Masson, R -- Linares, J -- Dierich, A -- LeMeur, M -- Wendling, C -- Tomasetto, C -- Chambon, P -- Rio, M C -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):259-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/Universite Louis Pasteur/College de France, Communaute Urbaine de Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824193" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/etiology/pathology ; Animals ; Base Sequence ; Cell Differentiation ; Cloning, Molecular ; Female ; Gastric Mucosa/cytology/*pathology ; Gene Targeting ; Genes, Tumor Suppressor ; Intestinal Mucosa/cytology/*pathology ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Neoplasm Proteins/genetics/*physiology ; Phenotype ; *Proteins ; Pyloric Antrum ; Stomach Neoplasms/*etiology/pathology ; Tumor Suppressor Proteins
    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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    Promoter sequences of eukaryotic protein-coding genes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: In vitro genetic techniques were used to study the sequence requirements for the initiation of specific transcription. Deletion mutants were constructed around the putative promoter of the adenovirus-2 major late and chicken conalbumin genes. Specific transcription in vitro by RNA polymerase B together with a HeLa cell cytoplasmic extract was used as the test for promoter function. With this approach sequences which are essential for the initiation of specific transcription in vitro, were shown to be located between 12 and 32 base pairs upstream from the 5' end of these genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corden, J -- Wasylyk, B -- Buchwalder, A -- Sassone-Corsi, P -- Kedinger, C -- Chambon, P -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1406-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251548" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; *Cell Physiological Phenomena ; DNA/genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; DNA-Directed RNA Polymerases/*metabolism ; Eukaryotic Cells/*physiology ; *Operon ; RNA Polymerase II/*metabolism ; RNA, Messenger/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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  • 7
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    Bidirectional SV40 transcription mediated by tandem Sp1 binding interactions (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: The 21-base pair repeat elements of the SV40 promoter contain six tandem copies of the GGGCGG hexanucleotide (GC-box), each of which can bind, with varying affinity, to the cellular transcription factor, Sp1. In vitro SV40 early RNA synthesis is mediated by interaction of Sp1 with GC-boxes I, II, and III, whereas transcription in the late direction is mediated by binding to GC-boxes III, V, and VI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gidoni, D -- Kadonaga, J T -- Barrera-Saldana, H -- Takahashi, K -- Chambon, P -- Tjian, R -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):511-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996137" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Mutation ; Pregnancy Proteins/*metabolism ; RNA, Messenger/analysis ; RNA, Viral/biosynthesis ; Simian virus 40/*genetics ; Sp1 Transcription Factor ; Templates, Genetic ; Transcription Factors/*metabolism ; *Transcription, 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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