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  • 1995-1999  (10,317)
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  • Articles  (10,317)
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  • 1
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    Structural basis of Smad2 recognition by the Smad anchor for receptor activation (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-30
    Description: The Smad proteins mediate transforming growth factor-beta (TGFbeta) signaling from the transmembrane serine-threonine receptor kinases to the nucleus. The Smad anchor for receptor activation (SARA) recruits Smad2 to the TGFbeta receptors for phosphorylation. The crystal structure of a Smad2 MH2 domain in complex with the Smad-binding domain (SBD) of SARA has been determined at 2.2 angstrom resolution. SARA SBD, in an extended conformation comprising a rigid coil, an alpha helix, and a beta strand, interacts with the beta sheet and the three-helix bundle of Smad2. Recognition between the SARA rigid coil and the Smad2 beta sheet is essential for specificity, whereas interactions between the SARA beta strand and the Smad2 three-helix bundle contribute significantly to binding affinity. Comparison of the structures between Smad2 and a comediator Smad suggests a model for how receptor-regulated Smads are recognized by the type I receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, G -- Chen, Y G -- Ozdamar, B -- Gyuricza, C A -- Chong, P A -- Wrana, J L -- Massague, J -- Shi, Y -- CA85171/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):92-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10615055" target="_blank"〉PubMed〈/a〉
    Keywords: *Activin Receptors, Type I ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Point Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/genetics/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction ; Smad2 Protein ; Trans-Activators/*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
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  • 2
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    Modulation of brain reward circuitry by leptin (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-30
    Description: Leptin, a hormone secreted by fat cells, suppresses food intake and promotes weight loss. To assess the action of this hormone on brain reward circuitry, changes in the rewarding effect of lateral hypothalamic stimulation were measured after leptin administration. At five stimulation sites near the fornix, the effectiveness of the rewarding electrical stimulation was enhanced by chronic food restriction and attenuated by intracerebroventricular infusion of leptin. In contrast, the rewarding effect of stimulating neighboring sites was insensitive to chronic food restriction and was enhanced by leptin in three of four cases. These opposing effects of leptin may mirror complementary changes in the rewarding effects of feeding and of competing behaviors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fulton, S -- Woodside, B -- Shizgal, P -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):125-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Studies in Behavioural Neurobiology, Concordia University, Montreal, QC, H3G 1M8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10615045" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Stimulation ; Energy Metabolism ; Feeding Behavior ; Food Deprivation/*physiology ; Hypothalamic Area, Lateral/drug effects/*physiology ; Injections, Intraventricular ; Leptin/administration & dosage/*pharmacology ; Male ; Neurons/physiology ; Neuropeptides/physiology ; Rats ; Rats, Long-Evans ; Recombinant Proteins/administration & dosage/pharmacology ; *Reward ; Self Stimulation/physiology ; Time Factors
    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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    A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-30
    Description: Voltage-gated proton (H+) channels are found in many human and animal tissues and play an important role in cellular defense against acidic stress. However, a molecular identification of these unique ion conductances has so far not been achieved. A 191-amino acid protein is described that, upon heterologous expression, has properties indistinguishable from those of native H+ channels. This protein is generated through alternative splicing of messenger RNA derived from the gene NOH-1 (NADPH oxidase homolog 1, where NADPH is the reduced form of nicotinamide adenine dinucleotide phosphate).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banfi, B -- Maturana, A -- Jaconi, S -- Arnaudeau, S -- Laforge, T -- Sinha, B -- Ligeti, E -- Demaurex, N -- Krause, K H -- New York, N.Y. -- Science. 2000 Jan 7;287(5450):138-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology of Aging Laboratory, Department of Geriatrics, Geneva University Hospitals, Geneva Medical School, CH-1211 Geneva 4, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10615049" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Cell Line ; Cytosol/metabolism ; Electric Conductivity ; Electron Transport ; Expressed Sequence Tags ; Humans ; Hydrogen/*metabolism ; Hydrogen-Ion Concentration ; Ion Channel Gating ; Ion Channels/chemistry/*genetics/metabolism ; Membrane Glycoproteins/chemistry/*genetics ; Molecular Sequence Data ; NADPH Oxidase/chemistry/*genetics ; Patch-Clamp Techniques ; Protons ; Transfection ; Tumor Cells, Cultured ; Zinc/pharmacology
    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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    Stem cells. Rat spinal cord function partially restored (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1826-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610569" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/cytology ; Cell Differentiation ; Cell Survival ; Embryo, Mammalian ; Mice ; Neurons/cytology ; Oligodendroglia/cytology ; Rats ; Spinal Cord/cytology/*physiology ; Spinal Cord Injuries/*therapy ; *Stem Cell Transplantation ; Stem Cells/cytology
    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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    Key brain receptor gets an unusual regulator (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1999 Nov 12;286(5443):1265-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610528" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/*enzymology ; Brain/*enzymology ; Cloning, Molecular ; Glutamic Acid/metabolism ; Neurons/metabolism ; Racemases and Epimerases/*genetics/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/metabolism ; Serine/*biosynthesis/metabolism ; Stereoisomerism ; Synapses/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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    Cholesterol-lowering drugs may boost bones (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1825-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610568" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anticholesteremic Agents/*pharmacology ; Bone Density/*drug effects ; Bone Morphogenetic Protein 2 ; Bone Morphogenetic Proteins/biosynthesis ; Clinical Trials as Topic ; Female ; Humans ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/*pharmacology ; Lovastatin/*pharmacology ; Mice ; Osteogenesis/*drug effects ; Osteoporosis/drug therapy ; Rats ; Simvastatin/pharmacology ; *Transforming Growth Factor beta
    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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    Learning visualised, on the double (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1661.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/physiology/*ultrastructure ; Calcium/metabolism ; Image Processing, Computer-Assisted ; In Vitro Techniques ; Learning/*physiology ; *Long-Term Potentiation ; Microscopy, Electron ; Rats ; Synapses/*ultrastructure ; Synaptic Transmission
    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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    Cutting back the calories (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerhard, G S -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1679-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610562" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Cerebral Cortex/metabolism ; *Energy Intake ; Gene Expression ; *Gene Expression Profiling ; Mice ; Mice, Inbred C57BL ; Muscle, Skeletal/*metabolism ; Oligonucleotide Array Sequence Analysis ; Rats ; Research Design
    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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    Posttranscriptional gene silencing in Neurospora by a RecQ DNA helicase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: The phenomenon of posttranscriptional gene silencing (PTGS), which occurs when a transgene is introduced into a cell, is poorly understood. Here, the qde-3 gene, which is required for the activation and maintenance of gene silencing in the fungus Neurospora crassa, was isolated. Sequence analysis revealed that the qde-3 gene belongs to the RecQ DNA helicase family. The QDE3 protein may function in the DNA-DNA interaction between introduced transgenes or with an endogenous gene required for gene-silencing activation. In animals, genes that are homologous to RecQ protein, such as the human genes for Bloom's syndrome and Werner's syndrome, may also function in PTGS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cogoni, C -- Macino, G -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2342-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dipartimento di Biotecnologie Cellulari ed Ematologia, Sezione di Genetica Molecolare, Universita di Roma La Sapienza, Viale Regina Elena, 324, 00161 Roma, Italy. carlo@bce.med.uniroma1.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600745" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry/genetics/*metabolism ; Amino Acid Sequence ; Bloom Syndrome/genetics ; Camptothecin/pharmacology ; DNA Helicases/chemistry/genetics/*metabolism ; DNA, Fungal/metabolism ; Enzyme Inhibitors/pharmacology ; Etoposide/pharmacology ; *Fungal Proteins ; *Gene Silencing ; Genes, Fungal ; Genetic Complementation Test ; Humans ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Insertional ; Neurospora crassa/drug effects/enzymology/*genetics ; RecQ Helicases ; Sequence Alignment ; Transcription, Genetic ; Transgenes ; Werner Syndrome/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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    Binding of transcription termination protein nun to nascent RNA and template DNA (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: The amino-terminal arginine-rich motif of coliphage HK022 Nun binds phage lambda nascent transcript, whereas the carboxyl-terminal domain interacts with RNA polymerase (RNAP) and blocks transcription elongation. RNA binding is inhibited by zinc (Zn2+) and stimulated by Escherichia coli NusA. To study these interactions, the Nun carboxyl terminus was extended by a cysteine residue conjugated to a photochemical cross-linker. The carboxyl terminus contacted NusA and made Zn2+-dependent intramolecular contacts. When Nun was added to a paused transcription elongation complex, it cross-linked to the DNA template. Nun may arrest transcription by anchoring RNAP to DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watnick, R S -- Gottesman, M E -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2337-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics and Institute of Cancer Research, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600743" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Azides ; Bacterial Proteins/metabolism ; Bacteriophage lambda/genetics/physiology ; Cross-Linking Reagents ; DNA, Viral/*metabolism ; DNA-Directed RNA Polymerases/metabolism ; Dithiothreitol/pharmacology ; Escherichia coli/enzymology/virology ; Escherichia coli Proteins ; Molecular Sequence Data ; *Peptide Elongation Factors ; Phenanthrolines/metabolism ; Protein Binding ; Pyridines ; RNA, Messenger/*metabolism ; RNA, Viral/metabolism ; Templates, Genetic ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; Transcriptional Elongation Factors ; Viral Plaque Assay ; Viral Proteins/chemistry/*metabolism ; Zinc/pharmacology
    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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