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  • 1
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    A mutation in the C. elegans EXP-2 potassium channel that alters feeding behavior (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: The nematode pharynx has a potassium channel with unusual properties, which allows the muscles to repolarize quickly and with the proper delay. Here, the Caenorhabditis elegans exp-2 gene is shown to encode this channel. EXP-2 is a Kv-type (voltage-activated) potassium channel that has inward-rectifying properties resembling those of the structurally dissimilar human ether-a-go-go-related gene (HERG) channel. Null and gain-of-function mutations affect pharyngeal muscle excitability in ways that are consistent with the electrophysiological behavior of the channel, and thereby demonstrate a direct link between the kinetics of this unusual channel and behavior.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791429/" 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/PMC3791429/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M W -- Fleischhauer, R -- Dent, J A -- Joho, R H -- Avery, L -- HL46154/HL/NHLBI NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- R01 HL046154/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2501-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA. wdavis@biology.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617464" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Feeding Behavior ; Genes, Helminth ; Genes, Reporter ; Ion Channel Gating ; Kinetics ; Membrane Potentials ; Models, Molecular ; Muscles/metabolism ; Mutation ; Neurons/metabolism ; Oocytes/metabolism ; Pharyngeal Muscles/physiology ; Potassium Channels/chemistry/genetics/*physiology ; Protein Conformation ; RNA, Complementary/genetics ; Recombinant Fusion Proteins/biosynthesis ; Xenopus laevis
    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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    Bacteriophytochromes: phytochrome-like photoreceptors from nonphotosynthetic eubacteria (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: Phytochromes are a family of photoreceptors used by green plants to entrain their development to the light environment. The distribution of these chromoproteins has been expanded beyond photoautotrophs with the discovery of phytochrome-like proteins in the nonphotosynthetic eubacteria Deinococcus radiodurans and Pseudomonas aeruginosa. Like plant phytochromes, the D. radiodurans receptor covalently binds linear tetrapyrroles autocatalytically to generate a photochromic holoprotein. However, the attachment site is distinct, using a histidine to potentially form a Schiff base linkage. Sequence homology and mutational analysis suggest that D. radiodurans bacteriophytochrome functions as a light-regulated histidine kinase, which helps protect the bacterium from visible light.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S J -- Vener, A V -- Vierstra, R D -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2517-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, Cellular and Molecular Biology Program and Department of Horticulture, University of Wisconsin-Madison, 1575 Linden Drive, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Bacterial Proteins/chemistry/genetics/*metabolism ; Biliverdine/analogs & derivatives/metabolism ; Binding Sites ; Gram-Positive Cocci/genetics/*metabolism ; Histidine/metabolism ; Light ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Photoreceptors, Microbial/chemistry/genetics/*metabolism ; Phytochrome/metabolism ; Protein Kinases/chemistry/genetics/*metabolism ; Pseudomonas aeruginosa/*metabolism ; Signal Transduction
    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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    On the origin of internal structure of word forms (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-25
    Description: This study shows that a corpus of proto-word forms shares four sequential sound patterns with words of modern languages and the first words of infants. Three of the patterns involve intrasyllabic consonant-vowel (CV) co-occurrence: labial (lip) consonants with central vowels, coronal (tongue front) consonants with front vowels, and dorsal (tongue back) consonants with back vowels. The fourth pattern is an intersyllabic preference for initiating words with a labial consonant-vowel-coronal consonant sequence (LC). The CV effects may be primarily biomechanically motivated. The LC effect may be self-organizational, with multivariate causality. The findings support the hypothesis that these four patterns were basic to the origin of words.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacNeilage, P F -- Davis, B L -- R01 HD 27733-07/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):527-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, Department of Communication Sciences and Disorders, University of Texas, Austin, TX 78712, USA. macneilage@psy.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775113" target="_blank"〉PubMed〈/a〉
    Keywords: Biomechanical Phenomena ; Humans ; Infant ; *Language Development ; Lip/physiology ; Mandible/physiology ; Movement ; *Phonetics ; *Speech ; Tongue/physiology
    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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    Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-08
    Description: The c-Jun NH2-terminal kinase (JNK) is activated when cells are exposed to ultraviolet (UV) radiation. However, the functional consequence of JNK activation in UV-irradiated cells has not been established. It is shown here that JNK is required for UV-induced apoptosis in primary murine embryonic fibroblasts. Fibroblasts with simultaneous targeted disruptions of all the functional Jnk genes were protected against UV-stimulated apoptosis. The absence of JNK caused a defect in the mitochondrial death signaling pathway, including the failure to release cytochrome c. These data indicate that mitochondria are influenced by proapoptotic signal transduction through the JNK pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tournier, C -- Hess, P -- Yang, D D -- Xu, J -- Turner, T K -- Nimnual, A -- Bar-Sagi, D -- Jones, S N -- Flavell, R A -- Davis, R J -- New York, N.Y. -- Science. 2000 May 5;288(5467):870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry & Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10797012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptotic Protease-Activating Factor 1 ; Caspase 3 ; Caspase 9 ; Caspases/metabolism ; Cell Count ; Cell Division ; Cells, Cultured ; Cytochrome c Group/*metabolism ; DNA Fragmentation ; Enzyme Activation ; Fibroblasts ; Gene Targeting ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Methyl Methanesulfonate/pharmacology ; Mice ; Mitochondria/metabolism ; Mitogen-Activated Protein Kinases/genetics/*metabolism ; NF-kappa B/metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Tumor Suppressor Protein p53/metabolism ; Ultraviolet Rays
    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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    Northridge earthquake damage caused by geologic focusing of seismic waves (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-08
    Description: Despite being located 21 kilometers from the epicenter of the 1994 Northridge earthquake (magnitude 6.7), the city of Santa Monica experienced anomalously concentrated damage with Mercalli intensity IX, an intensity as large as that experienced in the vicinity of the epicenter. Seismic records from aftershocks suggest that the damage resulted from the focusing of seismic waves by several underground acoustic lenses at depths of about 3 kilometers, formed by the faults that bound the northwestern edge of the Los Angeles basin. The amplification was greatest for high-frequency waves and was less powerful at lower frequencies, which is consistent with focusing theory and finite-difference simulations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis -- Rubinstein -- Liu -- Gao -- Knopoff -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1746-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth and Space Sciences, University of California, Los Angeles, CA 90095-1567, USA. Department of Geology, Kansas State University, Manhattan, KS 66506-3201, USA. Institute of Geophysics and Planetary Physics and Department of Physic.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10976067" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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  • 6
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    Convergence of the secretory pathways for cholera toxin and the filamentous phage, CTXphi (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-15
    Description: Virulence of Vibrio cholerae depends on secretion of cholera toxin (CT), which is encoded within the genome of a filamentous phage, CTXphi. Release of CT is mediated by the extracellular protein secretion (eps) type II secretion system. Here, the outer membrane component of this system, EpsD, was shown to be required for secretion of the phage as well. Thus, EpsD plays a role both in pathogenicity and in horizontal transfer of a key virulence gene. Genomic analysis suggests that additional filamentous phages also exploit chromosome-encoded outer membrane channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, B M -- Lawson, E H -- Sandkvist, M -- Ali, A -- Sozhamannan, S -- Waldor, M K -- AI-42347/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 14;288(5464):333-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geographic Medicine and Infectious Diseases, Tufts University School of Medicine, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10764646" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/genetics/*metabolism ; Bacteriophages/genetics/growth & development/*metabolism ; Cholera Toxin/*metabolism ; Genes, Bacterial ; Genetic Complementation Test ; Metalloendopeptidases/metabolism ; Mutagenesis, Insertional ; Plasmids ; Transduction, Genetic ; Vibrio cholerae/genetics/*metabolism/pathogenicity ; Virulence
    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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    "Restoration"--a misnomer? (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M A -- New York, N.Y. -- Science. 2000 Feb 18;287(5456):1203.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10712150" target="_blank"〉PubMed〈/a〉
    Keywords: *Conservation of Natural Resources ; *Ecosystem ; North America ; Terminology as Topic ; *Trees
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    Differential clustering of CD4 and CD3zeta during T cell recognition (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-26
    Description: Whereas T helper cells recognize peptide-major histocompatibility complex (MHC) class II complexes through their T cell receptors (TCRs), CD4 binds to an antigen-independent region of the MHC. Using green fluorescent protein-tagged chimeras and three-dimensional video microscopy, we show that CD4 and TCR-associated CD3zeta cluster in the interface coincident with increases in intracellular calcium. Signaling-, costimulation-, and cytoskeleton-dependent processes then stabilize CD3zeta in a single cluster at the center of the interface, while CD4 moves to the periphery. Thus, the CD4 coreceptor may serve primarily to "boost" recognition of ligand by the TCR and may not be required once activation has been initiated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krummel, M F -- Sjaastad, M D -- Wulfing, C -- Davis, M M -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, and the Howard Hughes Medical Institute, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958781" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/immunology ; Antigens, CD3/*metabolism ; Antigens, CD4/*metabolism ; Calcium Signaling ; Cell Line ; Cytoskeleton/physiology ; Histocompatibility Antigens Class II/immunology/metabolism ; Ligands ; *Lymphocyte Activation ; Microscopy, Video ; Phosphorylation ; Receptors, Antigen, T-Cell/immunology/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes, Helper-Inducer/*immunology/metabolism ; Transfection
    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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    Role of the guanosine triphosphatase Rac2 in T helper 1 cell differentiation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-24
    Description: T helper 1 (TH1) cells mediate cellular immunity, whereas TH2 cells potentiate antiparasite and humoral immunity. We used a complementary DNA subtraction method, representational display analysis, to show that the small guanosine triphosphatase Rac2 is expressed selectively in murine TH1 cells. Rac induces the interferon-gamma (IFN-gamma) promoter through cooperative activation of the nuclear factor kappa B and p38 mitogen-activated protein kinase pathways. Tetracycline-regulated transgenic mice expressing constitutively active Rac2 in T cells exhibited enhanced IFN-gamma production. Dominant-negative Rac inhibited IFN-gamma production in murine T cells. Moreover, T cells from Rac2-/- mice showed decreased IFN-gamma production under TH1 conditions in vitro. Thus, Rac2 activates TH1-specific signaling and IFN-gamma gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, B -- Yu, H -- Zheng, W -- Voll, R -- Na, S -- Roberts, A W -- Williams, D A -- Davis, R J -- Ghosh, S -- Flavell, R A -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Howard Hughes Medical Institute, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06520-8011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10864872" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cells, Cultured ; Cytokines/biosynthesis/genetics ; Gene Expression Regulation ; Humans ; Interferon-gamma/biosynthesis/*genetics ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Mitogen-Activated Protein Kinases/metabolism ; NF-kappa B/metabolism ; Promoter Regions, Genetic ; Signal Transduction ; Th1 Cells/cytology/*immunology/*metabolism ; Transfection ; p38 Mitogen-Activated Protein Kinases ; rac GTP-Binding Proteins/genetics/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Mode-specific energy disposal in the four-atom reaction OH + D2 --〉 HOD + D (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-04
    Description: Experiments, employing crossed molecular beams, with vibrational state resolution have been performed on the simplest four-atom reaction, OH + D2 --〉 HOD + D. In good agreement with the most recent quantum scattering predictions, mode-specific reaction dynamics is observed, with vibration in the newly formed oxygen-deuterium bond preferentially excited to v = 2. This demonstrates that quantum theoretical calculations, which in the past decade have achieved remarkable accuracy for three-atom reactions involving three dimensions, have progressed to the point where it is now possible to accurately predict energy disposal in four-atom reactions involving six dimensions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strazisar, B R -- Lin, C -- Davis, H F -- New York, N.Y. -- Science. 2000 Nov 3;290(5493):958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11062122" target="_blank"〉PubMed〈/a〉
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