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  • Amino Acid Sequence  (17)
  • Tumor Cells, Cultured  (9)
  • 1995-1999  (23)
  • 1
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    Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-20
    Description: A vertebrate securin (vSecurin) was identified on the basis of its biochemical analogy to the Pds1p protein of budding yeast and the Cut2p protein of fission yeast. The vSecurin protein bound to a vertebrate homolog of yeast separins Esp1p and Cut1p and was degraded by proteolysis mediated by an anaphase-promoting complex in a manner dependent on a destruction motif. Furthermore, expression of a stable Xenopus securin mutant protein blocked sister-chromatid separation but did not block the embryonic cell cycle. The vSecurin proteins share extensive sequence similarity with each other but show no sequence similarity to either of their yeast counterparts. Human securin is identical to the product of the gene called pituitary tumor-transforming gene (PTTG), which is overexpressed in some tumors and exhibits transforming activity in NIH 3T3 cells. The oncogenic nature of increased expression of vSecurin may result from chromosome gain or loss, produced by errors in chromatid separation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zou, H -- McGarry, T J -- Bernal, T -- Kirschner, M W -- GM26875/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 16;285(5426):418-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10411507" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; *Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/metabolism ; *Cell Transformation, Neoplastic ; Chromatids/*physiology ; Conserved Sequence ; Cyclin B/metabolism ; Cyclin B1 ; *Endopeptidases ; Fungal Proteins/chemistry/metabolism ; HeLa Cells ; Humans ; Ligases/metabolism ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Neoplasm Proteins/chemistry/genetics/*metabolism ; Neoplasms/etiology ; Nuclear Proteins/chemistry/metabolism ; Oncogene Proteins/chemistry/genetics/*metabolism ; Oncogenes ; *Saccharomyces cerevisiae Proteins ; *Schizosaccharomyces pombe Proteins ; Securin ; Separase ; Spindle Apparatus/metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Xenopus
    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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    Implication of tubby proteins as transcription factors by structure-based functional analysis (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-11
    Description: Tubby-like proteins (TULPs) are found in a broad range of multicellular organisms. In mammals, genetic mutation of tubby or other TULPs can result in one or more of three disease phenotypes: obesity (from which the name "tubby" is derived), retinal degeneration, and hearing loss. These disease phenotypes indicate a vital role for tubby proteins; however, no biochemical function has yet been ascribed to any member of this protein family. A structure-directed approach was employed to investigate the biological function of these proteins. The crystal structure of the core domain from mouse tubby was determined at a resolution of 1.9 angstroms. From primarily structural clues, experiments were devised, the results of which suggest that TULPs are a unique family of bipartite transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boggon, T J -- Shan, W S -- Santagata, S -- Myers, S C -- Shapiro, L -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2119-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Program, Department of Physiology and Biophysics, Ruttenberg Cancer Center, Mount Sinai School of Medicine of New York University, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10591637" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Nucleus/chemistry ; Crystallography, X-Ray ; DNA/metabolism ; Eye Proteins/*chemistry/genetics/*metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry/genetics/*metabolism ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment ; Transcription Factors/*chemistry/genetics/*metabolism ; Transcriptional Activation
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  • 3
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    Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-05
    Description: Small molecules that perturb specific protein functions are valuable tools for dissecting complex processes in mammalian cells. A combination of two phenotype-based screens, one based on a specific posttranslational modification, the other visualizing microtubules and chromatin, was used to identify compounds that affect mitosis. One compound, here named monastrol, arrested mammalian cells in mitosis with monopolar spindles. In vitro, monastrol specifically inhibited the motility of the mitotic kinesin Eg5, a motor protein required for spindle bipolarity. All previously known small molecules that specifically affect the mitotic machinery target tubulin. Monastrol will therefore be a particularly useful tool for studying mitotic mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayer, T U -- Kapoor, T M -- Haggarty, S J -- King, R W -- Schreiber, S L -- Mitchison, T J -- CA78048/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 29;286(5441):971-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, and Institute of Chemistry and Cell Biology, Harvard Medical School, Boston, MA 02115, USA. Thomas_Mayer@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10542155" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/drug effects ; Animals ; Cattle ; Cell Line ; Cytoskeleton/drug effects ; Golgi Apparatus/drug effects ; Kinesin/*drug effects ; Microtubules/drug effects ; Mitosis/*drug effects ; Molecular Motor Proteins/drug effects ; Phenotype ; Phosphoproteins/metabolism ; Protein Processing, Post-Translational ; Pyrimidines/*pharmacology ; RNA-Binding Proteins/metabolism ; Spindle Apparatus/*drug effects ; Thiones/*pharmacology ; Tumor Cells, Cultured ; Xenopus ; *Xenopus Proteins
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  • 4
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    Identification of a conserved receptor-binding site on the fiber proteins of CAR-recognizing adenoviridae (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-24
    Description: The human adenovirus serotype 5 (Ad5) is used widely for applications in human gene therapy. Cellular attachment of Ad5 is mediated by binding of the carboxyl-terminal knob of its fiber coat protein to the Coxsackie adenovirus receptor (CAR) protein. However, Ad5 binding to CAR hampers the development of adenovirus vectors capable of specifically targeting (diseased) tissues or organs. Through sequence analysis and mutagenesis, a conserved receptor-binding region was identified on the side of three divergent CAR-binding knobs. The feasibility of simultaneous CAR ablation and redirection of an adenovirus to a new receptor is demonstrated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roelvink, P W -- Mi Lee, G -- Einfeld, D A -- Kovesdi, I -- Wickham, T J -- New York, N.Y. -- Science. 1999 Nov 19;286(5444):1568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research and Development, GenVec Inc., 65 West Watkins Mill Road, Gaithersburg, MD 20879, USA. genecloner@genvec.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10567265" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*chemistry/metabolism ; Amino Acid Sequence ; Binding Sites ; Capsid/*chemistry/genetics/*metabolism ; *Capsid Proteins ; Cell Line ; Conserved Sequence ; Coxsackie and Adenovirus Receptor-Like Membrane Protein ; Genetic Vectors ; Humans ; Models, Molecular ; Mutagenesis, Site-Directed ; Point Mutation ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Virus/*metabolism ; Sequence Deletion ; Transfection ; Tumor Cells, Cultured
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  • 5
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    Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: Angiogenesis is thought to depend on a precise balance of positive and negative regulation. Angiopoietin-1 (Ang1) is an angiogenic factor that signals through the endothelial cell-specific Tie2 receptor tyrosine kinase. Like vascular endothelial growth factor, Ang1 is essential for normal vascular development in the mouse. An Ang1 relative, termed angiopoietin-2 (Ang2), was identified by homology screening and shown to be a naturally occurring antagonist for Ang1 and Tie2. Transgenic overexpression of Ang2 disrupts blood vessel formation in the mouse embryo. In adult mice and humans, Ang2 is expressed only at sites of vascular remodeling. Natural antagonists for vertebrate receptor tyrosine kinases are atypical; thus, the discovery of a negative regulator acting on Tie2 emphasizes the need for exquisite regulation of this angiogenic receptor system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maisonpierre, P C -- Suri, C -- Jones, P F -- Bartunkova, S -- Wiegand, S J -- Radziejewski, C -- Compton, D -- McClain, J -- Aldrich, T H -- Papadopoulos, N -- Daly, T J -- Davis, S -- Sato, T N -- Yancopoulos, G D -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):55-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals Inc., 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204896" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiopoietin-1 ; Angiopoietin-2 ; Animals ; Blood Vessels/embryology/*metabolism ; Cells, Cultured ; Cloning, Molecular ; Embryo, Mammalian/metabolism ; Endothelial Growth Factors/genetics/metabolism ; Endothelium, Vascular/*cytology/metabolism ; Female ; Humans ; Ligands ; Lymphokines/genetics/metabolism ; Membrane Glycoproteins/antagonists & inhibitors/metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Neovascularization, Physiologic ; Phosphorylation ; Proteins/chemistry/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptor Protein-Tyrosine Kinases/*antagonists & inhibitors/metabolism ; Receptor, TIE-2 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors
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  • 6
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    Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-10
    Description: The caspase-3 (CPP32, apopain, YAMA) family of cysteinyl proteases has been implicated as key mediators of apoptosis in mammalian cells. Gelsolin was identified as a substrate for caspase-3 by screening the translation products of small complementary DNA pools for sensitivity to cleavage by caspase-3. Gelsolin was cleaved in vivo in a caspase-dependent manner in cells stimulated by Fas. Caspase-cleaved gelsolin severed actin filaments in vitro in a Ca2+-independent manner. Expression of the gelsolin cleavage product in multiple cell types caused the cells to round up, detach from the plate, and undergo nuclear fragmentation. Neutrophils isolated from mice lacking gelsolin had delayed onset of both blebbing and DNA fragmentation, following apoptosis induction, compared with wild-type neutrophils. Thus, cleaved gelsolin may be one physiological effector of morphologic change during apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kothakota, S -- Azuma, T -- Reinhard, C -- Klippel, A -- Tang, J -- Chu, K -- McGarry, T J -- Kirschner, M W -- Koths, K -- Kwiatkowski, D J -- Williams, L T -- P01 HL48743/HL/NHLBI NIH HHS/ -- R01 HL54188/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 10;278(5336):294-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chiron Corporation, Emeryville, CA 94608, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9323209" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Antigens, CD95/physiology ; *Apoptosis ; Caspase 3 ; *Caspases ; Cell Line ; *Cell Size ; Cycloheximide/pharmacology ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Cytoskeleton/metabolism ; DNA Fragmentation ; Gelsolin/*metabolism ; Humans ; Mice ; Neutrophils/cytology/metabolism ; Recombinant Proteins/metabolism ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/pharmacology
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  • 7
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    A potassium channel mutation in neonatal human epilepsy (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: Benign familial neonatal convulsions (BFNC) is an autosomal dominant epilepsy of infancy, with loci mapped to human chromosomes 20q13.3 and 8q24. By positional cloning, a potassium channel gene (KCNQ2) located on 20q13.3 was isolated and found to be expressed in brain. Expression of KCNQ2 in frog (Xenopus laevis) oocytes led to potassium-selective currents that activated slowly with depolarization. In a large pedigree with BFNC, a five-base pair insertion would delete more than 300 amino acids from the KCNQ2 carboxyl terminus. Expression of the mutant channel did not yield measurable currents. Thus, impairment of potassium-dependent repolarization is likely to cause this age-specific epileptic syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biervert, C -- Schroeder, B C -- Kubisch, C -- Berkovic, S F -- Propping, P -- Jentsch, T J -- Steinlein, O K -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):403-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Human Genetics, University of Bonn, Bonn, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430594" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; Brain/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 20 ; Cloning, Molecular ; Epilepsy/*genetics/metabolism ; Female ; Frameshift Mutation ; Humans ; Infant, Newborn ; KCNQ2 Potassium Channel ; Male ; Molecular Sequence Data ; Mutagenesis, Insertional ; Oocytes/metabolism ; Open Reading Frames ; Pedigree ; Potassium/metabolism ; Potassium Channels/chemistry/*genetics/metabolism ; *Potassium Channels, Voltage-Gated ; Xenopus laevis
    Print ISSN: 0036-8075
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  • 8
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    An MTP inhibitor that normalizes atherogenic lipoprotein levels in WHHL rabbits (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-23
    Description: Patients with abetalipoproteinemia, a disease caused by defects in the microsomal triglyceride transfer protein (MTP), do not produce apolipoprotein B-containing lipoproteins. It was hypothesized that small molecule inhibitors of MTP would prevent the assembly and secretion of these atherogenic lipoproteins. To test this hypothesis, two compounds identified in a high-throughput screen for MTP inhibitors were used to direct the synthesis of a highly potent MTP inhibitor. This molecule (compound 9) inhibited the production of lipoprotein particles in rodent models and normalized plasma lipoprotein levels in Watanabe-heritable hyperlipidemic (WHHL) rabbits, which are a model for human homozygous familial hypercholesterolemia. These results suggest that compound 9, or derivatives thereof, has potential applications for the therapeutic lowering of atherogenic lipoprotein levels in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wetterau, J R -- Gregg, R E -- Harrity, T W -- Arbeeny, C -- Cap, M -- Connolly, F -- Chu, C H -- George, R J -- Gordon, D A -- Jamil, H -- Jolibois, K G -- Kunselman, L K -- Lan, S J -- Maccagnan, T J -- Ricci, B -- Yan, M -- Young, D -- Chen, Y -- Fryszman, O M -- Logan, J V -- Musial, C L -- Poss, M A -- Robl, J A -- Simpkins, L M -- Slusarchyk, W A -- Sulsky, R -- Taunk, P -- Magnin, D R -- Tino, J A -- Lawrence, R M -- Dickson, J K Jr -- Biller, S A -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):751-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Metabolic Diseases, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000, USA. Wetterau_John_R@msmail.bms.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784135" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine Transaminase/blood ; Animals ; Apolipoproteins B/*blood ; Aspartate Aminotransferases/blood ; Carrier Proteins/*antagonists & inhibitors ; Cholesterol/*blood ; Cricetinae ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Drug Design ; Drug Evaluation, Preclinical ; Fluorenes/chemistry/pharmacokinetics/*pharmacology ; Humans ; Hyperlipidemias/blood/drug therapy ; Hyperlipoproteinemia Type II/*blood/drug therapy ; Lipids/blood ; Lipoproteins/blood ; Liver/metabolism ; Mice ; Piperidines/chemistry/pharmacokinetics/*pharmacology ; Rabbits ; Rats ; Triglycerides/*blood/metabolism ; Tumor Cells, Cultured
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  • 9
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    Angiogenic and HIV-inhibitory functions of KSHV-encoded chemokines (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-10
    Description: Unique among known human herpesviruses, Kaposi's sarcoma-associated herpesvirus (KSHV or HHV-8) encodes chemokine-like proteins (vMIP-I and vMIP-II). vMIP-II was shown to block infection of human immunodeficiency virus-type 1 (HIV-1) on a CD4-positive cell line expressing CCR3 and to a lesser extent on one expressing CCR5, whereas both vMIP-I and vMIP-II partially inhibited HIV infection of peripheral blood mononuclear cells. Like eotaxin, vMIP-II activated and chemoattracted human eosinophils by way of CCR3. vMIP-I and vMIP-II, but not cellular MIP-1alpha or RANTES, were highly angiogenic in the chorioallantoic assay, suggesting a possible pathogenic role in Kaposi's sarcoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boshoff, C -- Endo, Y -- Collins, P D -- Takeuchi, Y -- Reeves, J D -- Schweickart, V L -- Siani, M A -- Sasaki, T -- Williams, T J -- Gray, P W -- Moore, P S -- Chang, Y -- Weiss, R A -- CA 67391/CA/NCI NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Oct 10;278(5336):290-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9323208" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/virology ; Chemokines/genetics/metabolism/pharmacology/*physiology ; Chemotaxis, Leukocyte ; Chick Embryo ; Eosinophils/physiology ; HIV-1/*physiology ; Herpesvirus 8, Human/*genetics/physiology ; Humans ; Leukocytes, Mononuclear/virology ; Macrophage Inflammatory Proteins/genetics/metabolism/pharmacology/*physiology ; Neovascularization, Pathologic/*etiology ; Neutrophils/physiology ; Receptors, CCR3 ; *Receptors, Chemokine ; Receptors, Cytokine/agonists/metabolism ; Receptors, HIV/metabolism ; Tumor Cells, Cultured ; *Viral Proteins ; Virus Replication
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  • 10
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    ARF1, a transcription factor that binds to auxin response elements (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: The plant hormone auxin regulates plant physiology by modulating the interaction of transcription factors with auxin response elements (AuxREs) of the affected genes. A transcription factor, Auxin Response Factor 1 (ARF1), that binds to the sequence TGTCTC in AuxREs was cloned from Arabidopsis by using a yeast one-hybrid system. ARF1 has an amino-terminal DNA-binding domain related to the carboxyl terminus of the maize transactivator Viviparous-1. Sequence requirements for ARF1 binding in vitro are identical to those that confer auxin responsiveness in vivo. The carboxyl terminus of ARF1 contains two motifs found in the Aux/IAA class of proteins and appears to mediate protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmasov, T -- Hagen, G -- Guilfoyle, T J -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1865-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188533" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Arabidopsis Proteins ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Plant/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Genes, Plant ; Indoleacetic Acids/*pharmacology ; Molecular Sequence Data ; Mutation ; Plant Proteins ; *Promoter Regions, Genetic ; *Repetitive Sequences, Nucleic Acid ; Transcription Factors/chemistry/genetics/*metabolism
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