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  • Articles  (75)
  • Signal Transduction  (75)
  • American Association for the Advancement of Science (AAAS)  (75)
  • EMBO Press
  • Essen : Verl. Glückauf
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • 2005-2009  (75)
  • 2005  (75)
Collection
  • Articles  (75)
Publisher
  • American Association for the Advancement of Science (AAAS)  (75)
  • EMBO Press
  • Essen : Verl. Glückauf
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
Years
  • 2005-2009  (75)
Year
  • 1
    Publication Date: 2005-02-01
    Description: Pollen tube guidance precedes the double fertilization of flowering plants. Here, we report the identification of a small maize protein of 94 amino acids involved in short-range signaling required for pollen tube attraction by the female gametophyte. ZmEA1 is exclusively expressed in the egg apparatus, consisting of the egg cell and two synergids. Chimeric ZmEA1 fused to green fluorescent protein (ZmEA1:GFP) was first visible within the filiform apparatus and later was localized to nucellar cell walls below the micropylar opening of the ovule. Transgenic down-regulation of the ZmEA1 gene led to ovule sterility caused by loss of close-range pollen tube guidance to the micropyle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marton, Mihaela L -- Cordts, Simone -- Broadhvest, Jean -- Dresselhaus, Thomas -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biocenter Klein Flottbek, Developmental Biology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, D-22609 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antisense Elements (Genetics) ; Crosses, Genetic ; DNA, Complementary ; Flowers/growth & development/*physiology ; Genes, Plant ; Green Fluorescent Proteins/metabolism ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/*physiology ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Reproduction ; Seeds/physiology ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Zea mays/*genetics/*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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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-11-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sawa, Akira -- Snyder, Solomon H -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1128-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA. asawa1@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293746" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/*genetics/physiology ; Affective Disorders, Psychotic/enzymology/*genetics ; Carrier Proteins/physiology ; Cyclic AMP/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Enzyme Activation ; Humans ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Protein Binding ; Schizophrenia/*genetics ; Signal Transduction ; Translocation, Genetic
    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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  • 3
    Publication Date: 2005-10-01
    Description: Monocular deprivation normally alters ocular dominance in the visual cortex only during a postnatal critical period (20 to 32 days postnatal in mice). We find that mutations in the Nogo-66 receptor (NgR) affect cessation of ocular dominance plasticity. In NgR-/- mice, plasticity during the critical period is normal, but it continues abnormally such that ocular dominance at 45 or 120 days postnatal is subject to the same plasticity as at juvenile ages. Thus, physiological NgR signaling from myelin-derived Nogo, MAG, and OMgp consolidates the neural circuitry established during experience-dependent plasticity. After pathological trauma, similar NgR signaling limits functional recovery and axonal regeneration.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856689/" 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/PMC2856689/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGee, Aaron W -- Yang, Yupeng -- Fischer, Quentin S -- Daw, Nigel W -- Strittmatter, Stephen M -- R01 NS039962/NS/NINDS NIH HHS/ -- R01 NS039962-10/NS/NINDS NIH HHS/ -- R01 NS042304/NS/NINDS NIH HHS/ -- R01 NS042304-08/NS/NINDS NIH HHS/ -- R01 NS056485/NS/NINDS NIH HHS/ -- R01 NS056485-04/NS/NINDS NIH HHS/ -- R37 NS033020/NS/NINDS NIH HHS/ -- R37 NS033020-15/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2222-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Yale University School of Medicine, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195464" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chondroitin Sulfate Proteoglycans/metabolism ; Darkness ; Dominance, Ocular/*physiology ; Electrophysiology ; GPI-Linked Proteins ; Gene Targeting ; Mice ; Mice, Inbred C57BL ; Mutation ; Myelin Basic Protein/metabolism ; Myelin Proteins/genetics/metabolism/*physiology ; Myelin Sheath/*physiology ; Myelin-Associated Glycoprotein/metabolism ; Neurites/physiology ; Neuronal Plasticity/*physiology ; Neurons/*physiology ; Photic Stimulation ; Receptors, Cell Surface/genetics/*physiology ; Signal Transduction ; Visual Cortex/cytology/growth & development/*physiology ; gamma-Aminobutyric Acid/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
    Publication Date: 2005-02-05
    Description: The gene encoding the Nod2 protein is frequently mutated in Crohn's disease (CD) patients, although the physiological function of Nod2 in the intestine remains elusive. Here we show that protective immunity mediated by Nod2 recognition of bacterial muramyl dipeptide is abolished in Nod2-deficient mice. These animals are susceptible to bacterial infection via the oral route but not through intravenous or peritoneal delivery. Nod2 is required for the expression of a subgroup of intestinal anti-microbial peptides, known as cryptdins. The Nod2 protein is thus a critical regulator of bacterial immunity within the intestine, providing a possible mechanism for Nod2 mutations in CD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobayashi, Koichi S -- Chamaillard, Mathias -- Ogura, Yasunori -- Henegariu, Octavian -- Inohara, Naohiro -- Nunez, Gabriel -- Flavell, Richard A -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692051" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylmuramyl-Alanyl-Isoglutamine/*immunology ; Animals ; *Antibody Formation ; Female ; Gene Expression ; Gene Targeting ; Ileum/*immunology/microbiology ; *Immunity, Innate ; Immunity, Mucosal ; Immunoglobulins/biosynthesis ; Interleukins/biosynthesis ; Intestinal Diseases/immunology/microbiology ; Intestinal Mucosa/immunology/microbiology ; Intracellular Signaling Peptides and Proteins/*physiology ; Ligands ; Lipopolysaccharides/toxicity ; Listeria monocytogenes/growth & development/immunology/isolation & purification ; Listeriosis/*immunology/microbiology ; Liver/microbiology ; Macrophages/immunology ; Male ; Membrane Glycoproteins/physiology ; Mice ; Nod2 Signaling Adaptor Protein ; Oligonucleotide Array Sequence Analysis ; Protein Precursors/biosynthesis/genetics ; Receptors, Cell Surface/physiology ; Serum Albumin/immunology ; Signal Transduction ; Spleen/microbiology ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/biosynthesis ; alpha-Defensins/*biosynthesis/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1310-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123271" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Blood Glucose/analysis ; Female ; Glucuronidase ; Insulin/blood/metabolism ; Insulin Resistance ; Insulin-Like Growth Factor I/metabolism ; Longevity/*genetics ; Male ; Membrane Proteins/blood/*genetics/*physiology ; Mice ; Mutation ; Signal Transduction
    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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  • 6
    Publication Date: 2005-09-17
    Description: The activation dynamics of the transcription factor NF-kappaB exhibit damped oscillatory behavior when cells are stimulated by tumor necrosis factor-alpha (TNFalpha) but stable behavior when stimulated by lipopolysaccharide (LPS). LPS binding to Toll-like receptor 4 (TLR4) causes activation of NF-kappaB that requires two downstream pathways, each of which when isolated exhibits damped oscillatory behavior. Computational modeling of the two TLR4-dependent signaling pathways suggests that one pathway requires a time delay to establish early anti-phase activation of NF-kappaB by the two pathways. The MyD88-independent pathway required Inferon regulatory factor 3-dependent expression of TNFalpha to activate NF-kappaB, and the time required for TNFalpha synthesis established the delay.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Covert, Markus W -- Leung, Thomas H -- Gaston, Jahlionais E -- Baltimore, David -- GM039458-21/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166516" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport/deficiency/physiology ; Animals ; Antigens, Differentiation/physiology ; Cell Line ; Cells, Cultured ; Computer Simulation ; Cycloheximide/pharmacology ; DNA-Binding Proteins/genetics/physiology ; Gene Expression Profiling ; Gene Expression Regulation ; I-kappa B Kinase ; I-kappa B Proteins/biosynthesis/genetics/metabolism ; Interferon Regulatory Factor-3 ; Kinetics ; Lipopolysaccharides/*immunology/metabolism ; Mice ; Models, Biological ; Myeloid Differentiation Factor 88 ; NF-kappa B/*metabolism ; Oligonucleotide Array Sequence Analysis ; Protein Synthesis Inhibitors/pharmacology ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Immunologic/deficiency/metabolism/physiology ; Signal Transduction ; Time Factors ; Toll-Like Receptor 4 ; Transcription Factors/genetics/physiology ; Tumor Necrosis Factor-alpha/biosynthesis/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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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-07-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):551-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16040685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/physiology ; Circadian Rhythm ; Female ; Gonadotropin-Releasing Hormone/physiology/secretion ; Humans ; Hypogonadism/genetics ; Kisspeptins ; Leptin/genetics/physiology ; Male ; Mutation ; Neurons/physiology ; Proteins/genetics/*physiology ; Puberty/*physiology ; Receptors, Cell Surface/genetics/metabolism ; Receptors, G-Protein-Coupled ; Receptors, Leptin ; Receptors, Neuropeptide/genetics/*physiology ; Reproduction ; Signal Transduction ; Tumor Suppressor Proteins
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  • 8
    Publication Date: 2005-09-17
    Description: A small number of mammalian signaling pathways mediate a myriad of distinct physiological responses to diverse cellular stimuli. Temporal control of the signaling module that contains IkappaB kinase (IKK), its substrate inhibitor of NF-kappaB (IkappaB), and the key inflammatory transcription factor NF-kappaB can allow for selective gene activation. We have demonstrated that different inflammatory stimuli induce distinct IKK profiles, and we examined the underlying molecular mechanisms. Although tumor necrosis factor-alpha (TNFalpha)-induced IKK activity was rapidly attenuated by negative feedback, lipopolysaccharide (LPS) signaling and LPS-specific gene expression programs were dependent on a cytokine-mediated positive feedback mechanism. Thus, the distinct biological responses to LPS and TNFalpha depend on signaling pathway-specific mechanisms that regulate the temporal profile of IKK activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werner, Shannon L -- Barken, Derren -- Hoffmann, Alexander -- GM071573/GM/NIGMS NIH HHS/ -- GM72024/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1857-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Signaling Systems Laboratory, Department of Chemistry and Biochemistry, 9500 Gilman Drive, Mailcode 0375, La Jolla, CA 92093-0375, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166517" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Autocrine Communication ; Cell Line ; Cells, Cultured ; Computer Simulation ; Cytokines/genetics ; Feedback, Physiological ; Gene Expression Profiling ; *Gene Expression Regulation ; I-kappa B Kinase ; I-kappa B Proteins/metabolism ; Lipopolysaccharides/immunology/metabolism/pharmacology ; Mice ; Models, Biological ; NF-kappa B/deficiency/metabolism ; Oligonucleotide Array Sequence Analysis ; Protein-Serine-Threonine Kinases/*metabolism ; Receptors, Immunologic/metabolism ; Signal Transduction ; Toll-Like Receptor 4 ; Transcriptional Activation ; Tumor Necrosis Factor-alpha/deficiency/immunology/metabolism/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-12-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Antebi, Adam -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1911-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373563" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/*physiology ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/genetics/*physiology ; Forkhead Transcription Factors ; Longevity/genetics/physiology ; MicroRNAs/*physiology ; Nuclear Proteins/genetics/*physiology ; RNA, Helminth/*physiology ; Repressor Proteins/genetics/*physiology ; Signal Transduction ; Transcription Factors/physiology
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  • 10
    Publication Date: 2005-08-16
    Description: Flowering of Arabidopsis is regulated by several environmental and endogenous signals. An important integrator of these inputs is the FLOWERING LOCUS T (FT) gene, which encodes a small, possibly mobile protein. A primary response to floral induction is the activation of FT RNA expression in leaves. Because flowers form at a distant site, the shoot apex, these data suggest that FT primarily controls the timing of flowering. Integration of temporal and spatial information is mediated in part by the bZIP transcription factor FD, which is already expressed at the shoot apex before floral induction. A complex of FT and FD proteins in turn can activate floral identity genes such as APETALA1 (AP1).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wigge, Philip A -- Kim, Min Chul -- Jaeger, Katja E -- Busch, Wolfgang -- Schmid, Markus -- Lohmann, Jan U -- Weigel, Detlef -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1056-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany. philip.wigge@bbsrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099980" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Chromatin Immunoprecipitation ; DNA-Binding Proteins/genetics/metabolism ; Flowers/*growth & development ; Gene Expression Regulation, Plant ; Homeodomain Proteins/genetics/metabolism ; MADS Domain Proteins ; Models, Biological ; Mutation ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Plant Leaves/metabolism ; Plant Proteins/genetics/metabolism ; Plant Shoots/metabolism ; Protein Interaction Mapping ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Time Factors ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic ; Two-Hybrid System Techniques
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-26
    Description: The function of an organ is dependent on its cellular constituents as well as on their assembly into a cohesive unit. The developing gut faces unique challenges as one of the longest and largest organs in the body and also because it is constantly interfacing with external factors through the diet. Its location deep within the body has until recently hampered investigation into its formation. The patterning of the gut along its longitudinal, dorsoventral, left-right, and radial axes is one of the fascinating issues that pertain to the development, function, and homeostasis of this understudied organ.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stainier, Didier Y R -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1902-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Programs in Developmental Biology, Genetics and Human Genetics, University of California, San Francisco, San Francisco, CA 94143-2711, USA. didier_stainier@biochem.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790841" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Body Patterning ; Diet ; Digestive System/*embryology/microbiology ; Digestive System Abnormalities ; Digestive System Physiological Phenomena ; Endoderm/physiology ; Epigenesis, Genetic ; Gene Expression Regulation, Developmental ; Genes, Homeobox ; Humans ; Intestinal Mucosa/cytology/embryology ; Intestines/abnormalities/*embryology/microbiology/physiology ; Mesoderm/physiology ; Morphogenesis ; Signal Transduction ; Stem Cells/physiology
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-26
    Description: The intestinal epithelium follows the paradigms of stem cell biology established for other self-renewing tissues. With a unique topology, it constitutes a two-dimensional structure folded into valleys and hills: the proliferative crypts and the differentiated villi. Its unprecedented self-renewal rate appears reflected in a high susceptibility to malignant transformation. The molecular mechanisms that control homeostatic self-renewal and those that underlie colorectal cancer are remarkably symmetrical. Here, we discuss the biology of the intestinal epithelium, emphasizing the roles played by Wnt, bone morphogenic protein, and Notch signaling cascades in epithelial self-renewal and cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radtke, Freddy -- Clevers, Hans -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1904-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, Chemin de Boveresses 155, CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790842" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/genetics/metabolism/pathology ; Animals ; Bone Morphogenetic Proteins/metabolism ; Cell Transformation, Neoplastic ; Colorectal Neoplasms/*etiology/genetics/pathology/physiopathology ; Colorectal Neoplasms, Hereditary Nonpolyposis/genetics/metabolism/pathology ; Helix-Loop-Helix Motifs ; Humans ; Intercellular Signaling Peptides and Proteins/metabolism ; Intestinal Mucosa/*cytology/embryology/*physiology ; Membrane Proteins/metabolism ; Mutation ; Receptors, Notch ; Signal Transduction ; Stem Cells/cytology/physiology ; Wnt Proteins
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  • 13
    Publication Date: 2005-07-16
    Description: Whole-genome sequencing of the protozoan pathogen Trypanosoma cruzi revealed that the diploid genome contains a predicted 22,570 proteins encoded by genes, of which 12,570 represent allelic pairs. Over 50% of the genome consists of repeated sequences, such as retrotransposons and genes for large families of surface molecules, which include trans-sialidases, mucins, gp63s, and a large novel family (〉1300 copies) of mucin-associated surface protein (MASP) genes. Analyses of the T. cruzi, T. brucei, and Leishmania major (Tritryp) genomes imply differences from other eukaryotes in DNA repair and initiation of replication and reflect their unusual mitochondrial DNA. Although the Tritryp lack several classes of signaling molecules, their kinomes contain a large and diverse set of protein kinases and phosphatases; their size and diversity imply previously unknown interactions and regulatory processes, which may be targets for intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉El-Sayed, Najib M -- Myler, Peter J -- Bartholomeu, Daniella C -- Nilsson, Daniel -- Aggarwal, Gautam -- Tran, Anh-Nhi -- Ghedin, Elodie -- Worthey, Elizabeth A -- Delcher, Arthur L -- Blandin, Gaelle -- Westenberger, Scott J -- Caler, Elisabet -- Cerqueira, Gustavo C -- Branche, Carole -- Haas, Brian -- Anupama, Atashi -- Arner, Erik -- Aslund, Lena -- Attipoe, Philip -- Bontempi, Esteban -- Bringaud, Frederic -- Burton, Peter -- Cadag, Eithon -- Campbell, David A -- Carrington, Mark -- Crabtree, Jonathan -- Darban, Hamid -- da Silveira, Jose Franco -- de Jong, Pieter -- Edwards, Kimberly -- Englund, Paul T -- Fazelina, Gholam -- Feldblyum, Tamara -- Ferella, Marcela -- Frasch, Alberto Carlos -- Gull, Keith -- Horn, David -- Hou, Lihua -- Huang, Yiting -- Kindlund, Ellen -- Klingbeil, Michele -- Kluge, Sindy -- Koo, Hean -- Lacerda, Daniela -- Levin, Mariano J -- Lorenzi, Hernan -- Louie, Tin -- Machado, Carlos Renato -- McCulloch, Richard -- McKenna, Alan -- Mizuno, Yumi -- Mottram, Jeremy C -- Nelson, Siri -- Ochaya, Stephen -- Osoegawa, Kazutoyo -- Pai, Grace -- Parsons, Marilyn -- Pentony, Martin -- Pettersson, Ulf -- Pop, Mihai -- Ramirez, Jose Luis -- Rinta, Joel -- Robertson, Laura -- Salzberg, Steven L -- Sanchez, Daniel O -- Seyler, Amber -- Sharma, Reuben -- Shetty, Jyoti -- Simpson, Anjana J -- Sisk, Ellen -- Tammi, Martti T -- Tarleton, Rick -- Teixeira, Santuza -- Van Aken, Susan -- Vogt, Christy -- Ward, Pauline N -- Wickstead, Bill -- Wortman, Jennifer -- White, Owen -- Fraser, Claire M -- Stuart, Kenneth D -- Andersson, Bjorn -- AI045039/AI/NIAID NIH HHS/ -- AI45038/AI/NIAID NIH HHS/ -- AI45061/AI/NIAID NIH HHS/ -- R01 AI031077/AI/NIAID NIH HHS/ -- R01 AI031077-11/AI/NIAID NIH HHS/ -- U01 AI045038/AI/NIAID NIH HHS/ -- U01 AI045039/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):409-15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Parasite Genomics, Institute for Genomic Research, Rockville, MD 20850, USA. nelsayed@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020725" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chagas Disease/drug therapy/parasitology ; DNA Repair ; DNA Replication ; DNA, Mitochondrial/genetics ; DNA, Protozoan/genetics ; Genes, Protozoan ; *Genome, Protozoan ; Humans ; Meiosis ; Membrane Proteins/chemistry/genetics/physiology ; Multigene Family ; Protozoan Proteins/chemistry/*genetics/physiology ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroelements ; *Sequence Analysis, DNA ; Signal Transduction ; Telomere/genetics ; Trypanocidal Agents/pharmacology/therapeutic use ; Trypanosoma cruzi/chemistry/*genetics/physiology
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  • 14
    Publication Date: 2005-02-05
    Description: Mitochondrial DNA (mtDNA) is essential for cells to maintain respiratory competency and is inherited as a protein-DNA complex called the nucleoid. We have identified 22 mtDNA-associated proteins in yeast, among which is mitochondrial aconitase (Aco1p). We show that this Krebs-cycle enzyme is essential for mtDNA maintenance independent of its catalytic activity. Regulation of ACO1 expression by the HAP and retrograde metabolic signaling pathways directly affects mtDNA maintenance. When constitutively expressed, Aco1p can replace the mtDNA packaging function of the high-mobility-group protein Abf2p. Thus, Aco1p may integrate metabolic signals and mtDNA maintenance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Xin Jie -- Wang, Xiaowen -- Kaufman, Brett A -- Butow, Ronald A -- GM22525/GM/NIGMS NIH HHS/ -- GM33510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):714-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390-9148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692048" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Substitution ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; CCAAT-Binding Factor/genetics/metabolism ; DNA, Fungal/*metabolism ; DNA, Mitochondrial/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Glucose/metabolism ; Iron Regulatory Protein 1/genetics/*metabolism ; Mutation ; Repressor Proteins/genetics/metabolism ; Saccharomyces cerevisiae/enzymology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Signal Transduction ; Spores, Fungal/physiology ; Transcription Factors/genetics/metabolism ; Transformation, Genetic
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  • 15
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, John B -- 1P01CA71932/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1570-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor, MI 48109-2216, USA. johnlowe@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Cell Membrane/*metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/genetics/*metabolism ; Endoplasmic Reticulum/enzymology/metabolism ; Fucose/metabolism ; Fucosyltransferases/chemistry/genetics/*metabolism ; Guanosine Diphosphate Fucose/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Mutation ; Protein Folding ; Protein Transport ; RNA Interference ; Receptors, Cell Surface/*metabolism ; Receptors, Notch ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 16
    Publication Date: 2005-04-30
    Description: Mammalian Toll-like receptors (TLRs) play an important role in the innate recognition of pathogens by dendritic cells (DCs). Although TLRs are clearly involved in the detection of bacteria and viruses, relatively little is known about their function in the innate response to eukaryotic microorganisms. Here we identify a profilin-like molecule from the protozoan parasite Toxoplasma gondii that generates a potent interleukin-12 (IL-12) response in murine DCs that is dependent on myeloid differentiation factor 88. T. gondii profilin activates DCs through TLR11 and is the first chemically defined ligand for this TLR. Moreover, TLR11 is required in vivo for parasite-induced IL-12 production and optimal resistance to infection, thereby establishing a role for the receptor in host recognition of protozoan pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarovinsky, Felix -- Zhang, Dekai -- Andersen, John F -- Bannenberg, Gerard L -- Serhan, Charles N -- Hayden, Matthew S -- Hieny, Sara -- Sutterwala, Fayyaz S -- Flavell, Richard A -- Ghosh, Sankar -- Sher, Alan -- 1R01AI045806-01A1/AI/NIAID NIH HHS/ -- AI05093/AI/NIAID NIH HHS/ -- R01-AI59440/AI/NIAID NIH HHS/ -- R01-GM38765/GM/NIGMS NIH HHS/ -- Intramural NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1626-9. Epub 2005 Apr 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunobiology Section, Laboratory of Parasitic Diseases; National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA. fyarovinsky@niaid.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15860593" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antigens, Differentiation/genetics/metabolism ; Contractile Proteins/chemistry/*immunology/isolation & purification/metabolism ; Dendritic Cells/*immunology ; Genes, Protozoan ; Immunity, Innate ; Interleukin-12/biosynthesis/blood ; Ligands ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Inbred C57BL ; Microfilament Proteins/chemistry/*immunology/isolation & purification/metabolism ; Molecular Sequence Data ; Myeloid Differentiation Factor 88 ; NF-kappa B/metabolism ; Profilins ; Protozoan Proteins/chemistry/*immunology/isolation & purification/metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Immunologic/genetics/metabolism ; Recombinant Proteins/immunology ; Signal Transduction ; Toll-Like Receptors ; Toxoplasma/genetics/*immunology ; Toxoplasmosis, Animal/*immunology ; Transfection
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  • 17
    Publication Date: 2005-10-22
    Description: Cell-cell interactions and cross-talk between signaling pathways specify Caenorhabditis elegans vulval precursor cells (VPCs) to adopt a spatial pattern: a central "1 degrees " VPC, in which epidermal growth factor receptor (EGFR)-mitogen-activated protein kinase (MAPK) activity is high and LIN-12/Notch activity is low, flanked by two "2 degrees " VPCs, in which LIN-12/Notch activity is high and EGFR-MAPK activity is low. Here, we identify a microRNA gene, mir-61, as a direct transcriptional target of LIN-12 and show that expression of mir-61 promotes the 2 degrees fate. We also identify vav-1, the ortholog of the Vav oncogene, as a target of mir-61, and show that down-regulation of VAV-1 promotes lin-12 activity in specifying the 2 degrees fate. Our results suggest that lin-12, mir-61, and vav-1 form a feedback loop that helps maximize lin-12 activity in the presumptive 2 degrees VPCs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3010395/" 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/PMC3010395/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoo, Andrew S -- Greenwald, Iva -- CA095389/CA/NCI NIH HHS/ -- R01 CA095389/CA/NCI NIH HHS/ -- R01 CA095389-01A1/CA/NCI NIH HHS/ -- R01 CA095389-02/CA/NCI NIH HHS/ -- R01 CA095389-03/CA/NCI NIH HHS/ -- R01 CA095389-04/CA/NCI NIH HHS/ -- R01 CA095389-05/CA/NCI NIH HHS/ -- R01 CA095389-06A1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1330-3. Epub 2005 Oct 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrated Program in Cellular, Molecular, and Biophysical Studies, Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, 701 West 168th Street, Room 720, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239437" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/*cytology/*genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins/*genetics/*metabolism ; Computational Biology ; Down-Regulation ; Feedback, Physiological ; Female ; Gene Expression Regulation, Developmental ; Genes, Helminth ; Membrane Proteins/genetics/*metabolism ; MicroRNAs/*genetics/*metabolism ; Proto-Oncogene Proteins c-vav/*genetics/metabolism ; Receptors, Notch ; Regulatory Sequences, Nucleic Acid ; Signal Transduction ; Stem Cells/*cytology/metabolism ; Transcription, Genetic ; Vulva/cytology/growth & development
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  • 18
    Publication Date: 2005-06-18
    Description: Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choe, Jungwoo -- Kelker, Matthew S -- Wilson, Ian A -- AI-42266/AI/NIAID NIH HHS/ -- CA-58896/CA/NCI NIH HHS/ -- T32 AI077606/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 22;309(5734):581-5. Epub 2005 Jun 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute (TSRI), 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961631" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Glycosylation ; Humans ; Hydrogen Bonding ; Leucine/chemistry ; Ligands ; Membrane Glycoproteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Double-Stranded/metabolism ; Receptors, Cell Surface/*chemistry/metabolism ; Repetitive Sequences, Amino Acid ; Signal Transduction ; Static Electricity ; Surface Properties ; Toll-Like Receptor 3 ; Toll-Like Receptors
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  • 19
    Publication Date: 2005-06-25
    Description: Pathogen recognition by the plant immune system is governed by structurally related, polymorphic products of disease resistance (R) genes. RAR1 and/or SGT1b mediate the function of many R proteins. RAR1 controls preactivation R protein accumulation by an unknown mechanism. We demonstrate that Arabidopsis SGT1b has two distinct, genetically separable functions in the plant immune system: SGT1b antagonizes RAR1 to negatively regulate R protein accumulation before infection, and SGT1b has a RAR1-independent function that regulates programmed cell death during infection. The balanced activities of RAR1 and SGT1, in concert with cytosolic HSP90, modulate preactivation R protein accumulation and signaling competence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holt, Ben F 3rd -- Belkhadir, Youssef -- Dangl, Jeffery L -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):929-32. Epub 2005 Jun 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976272" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis ; Arabidopsis/*immunology/microbiology ; Arabidopsis Proteins/genetics/immunology/*physiology ; Carrier Proteins/antagonists & inhibitors/immunology/*physiology ; Cell Cycle Proteins/immunology/*physiology ; Genes, Plant ; HSP90 Heat-Shock Proteins/immunology/physiology ; Mutation ; Peronospora/physiology ; Plant Diseases/microbiology ; Plant Proteins/antagonists & inhibitors/immunology/*physiology ; Plants, Genetically Modified ; Signal Transduction
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  • 20
    Publication Date: 2005-03-26
    Description: Major phenotypic changes evolve in parallel in nature by molecular mechanisms that are largely unknown. Here, we use positional cloning methods to identify the major chromosome locus controlling armor plate patterning in wild threespine sticklebacks. Mapping, sequencing, and transgenic studies show that the Ectodysplasin (EDA) signaling pathway plays a key role in evolutionary change in natural populations and that parallel evolution of stickleback low-plated phenotypes at most freshwater locations around the world has occurred by repeated selection of Eda alleles derived from an ancestral low-plated haplotype that first appeared more than two million years ago. Members of this clade of low-plated alleles are present at low frequencies in marine fish, which suggests that standing genetic variation can provide a molecular basis for rapid, parallel evolution of dramatic phenotypic change in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colosimo, Pamela F -- Hosemann, Kim E -- Balabhadra, Sarita -- Villarreal, Guadalupe Jr -- Dickson, Mark -- Grimwood, Jane -- Schmutz, Jeremy -- Myers, Richard M -- Schluter, Dolph -- Kingsley, David M -- 1P50HG02568/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1928-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305-5329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790847" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; *Biological Evolution ; Body Patterning ; Chromosome Walking ; Cloning, Molecular ; Ectodysplasins ; Fresh Water ; Gene Frequency ; Genetic Variation ; Haplotypes ; Linkage Disequilibrium ; Membrane Proteins/*genetics/physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Polymorphism, Single Nucleotide ; Seawater ; Selection, Genetic ; Sequence Analysis, DNA ; Signal Transduction ; Smegmamorpha/*anatomy & histology/classification/*genetics/growth & development
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  • 21
    Publication Date: 2005-03-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isaacs, Farren J -- Blake, William J -- Collins, James J -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1886-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lipper Center for Computational Genetics and Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790834" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/biosynthesis/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Escherichia coli/*genetics ; Escherichia coli Proteins/*metabolism ; Feedback, Physiological ; *Gene Expression Regulation, Bacterial ; Green Fluorescent Proteins/biosynthesis ; Lac Repressors ; Luminescent Proteins/biosynthesis ; *Models, Genetic ; Repressor Proteins/genetics/metabolism ; Signal Transduction ; Stochastic Processes ; Transcription Factors/*metabolism ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 22
    Publication Date: 2005-06-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Udvardi, Michael K -- Scheible, Wolf-Rudiger -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1749-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institute of Molecular Plant Physiology, Am Muhlenberg 1, 14476 Golm, Germany. udvardi@mpimp-golm.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961658" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/metabolism ; Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Nucleus/metabolism ; Fabaceae/*genetics/metabolism/*microbiology ; Gene Expression Regulation, Plant ; *Genes, Plant ; Lipopolysaccharides/metabolism ; Medicago/genetics/metabolism/microbiology ; Mycorrhizae/physiology ; *Nitrogen Fixation ; Plant Proteins/metabolism ; Plant Roots/metabolism ; Rhizobiaceae/*physiology ; Signal Transduction ; *Symbiosis ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 23
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-01-22
    Description: Recent evidence suggests a key role for the brain in the control of both body fat content and glucose metabolism. Neuronal systems that regulate energy intake, energy expenditure, and endogenous glucose production sense and respond to input from hormonal and nutrient-related signals that convey information regarding both body energy stores and current energy availability. In response to this input, adaptive changes occur that promote energy homeostasis and the maintenance of blood glucose levels in the normal range. Defects in this control system are implicated in the link between obesity and type 2 diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, Michael W -- Porte, Daniel Jr -- DK52989/DK/NIDDK NIH HHS/ -- DK683840/DK/NIDDK NIH HHS/ -- NS32273/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):375-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Metabolism, Endocrinology and Nutrition, University of Washington, Seattle, WA 98110, USA. mschwart@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662002" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Brain/*metabolism ; Diabetes Mellitus, Type 2/etiology/metabolism/*physiopathology ; Eating ; Energy Metabolism ; Fatty Acids, Nonesterified/metabolism ; Glucose/metabolism ; Homeostasis ; Humans ; Hypothalamus/metabolism ; Insulin/metabolism ; Insulin Resistance ; Leptin/genetics/metabolism ; Lipodystrophy/physiopathology ; Models, Biological ; Neurons/physiology ; Obesity/etiology/metabolism/*physiopathology ; Receptor, Insulin/metabolism ; Signal Transduction
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  • 24
    Publication Date: 2005-06-04
    Description: Closely related signals often lead to very different cellular outcomes. We found that the differentiation of human mesenchymal stem cells into bone-forming cells is stimulated by epidermal growth factor (EGF) but not platelet-derived growth factor (PDGF). We used mass spectrometry-based proteomics to comprehensively compare proteins that were tyrosine phosphorylated in response to EGF and PDGF and their associated partners. More than 90% of these signaling proteins were used by both ligands, whereas the phosphatidylinositol 3-kinase (PI3K) pathway was exclusively activated by PDGF, implicating it as a possible control point. Indeed, chemical inhibition of PI3K in PDGF-stimulated cells removed the differential effect of the two growth factors, bestowing full differentiation effect onto PDGF. Thus, quantitative proteomics can directly compare entire signaling networks and discover critical differences capable of changing cell fate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kratchmarova, Irina -- Blagoev, Blagoy -- Haack-Sorensen, Mandana -- Kassem, Moustapha -- Mann, Matthias -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1472-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Experimental BioInformatics (CEBI), Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933201" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Differentiation ; Cell Line ; Epidermal Growth Factor/*physiology ; Fibroblast Growth Factors/physiology ; Humans ; MAP Kinase Signaling System ; Mesoderm/*cytology ; Nerve Growth Factor/physiology ; Osteoblasts/cytology ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/*physiology ; Proteins/metabolism ; Proteomics ; Signal Transduction ; Stem Cells/*cytology ; Tyrosine/metabolism
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  • 25
    Publication Date: 2005-08-27
    Description: A defect in Klotho gene expression in mice accelerates the degeneration of multiple age-sensitive traits. Here, we show that overexpression of Klotho in mice extends life span. Klotho protein functions as a circulating hormone that binds to a cell-surface receptor and represses intracellular signals of insulin and insulin-like growth factor 1 (IGF1), an evolutionarily conserved mechanism for extending life span. Alleviation of aging-like phenotypes in Klotho-deficient mice was observed by perturbing insulin and IGF1 signaling, suggesting that Klotho-mediated inhibition of insulin and IGF1 signaling contributes to its anti-aging properties. Klotho protein may function as an anti-aging hormone in mammals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2536606/" 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/PMC2536606/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kurosu, Hiroshi -- Yamamoto, Masaya -- Clark, Jeremy D -- Pastor, Johanne V -- Nandi, Animesh -- Gurnani, Prem -- McGuinness, Owen P -- Chikuda, Hirotaka -- Yamaguchi, Masayuki -- Kawaguchi, Hiroshi -- Shimomura, Iichiro -- Takayama, Yoshiharu -- Herz, Joachim -- Kahn, C Ronald -- Rosenblatt, Kevin P -- Kuro-o, Makoto -- R01 AG019712/AG/NIA NIH HHS/ -- R01 AG019712-05/AG/NIA NIH HHS/ -- R01 AG025326/AG/NIA NIH HHS/ -- R01 AG025326-03/AG/NIA NIH HHS/ -- R01AG19712/AG/NIA NIH HHS/ -- R01AG25326/AG/NIA NIH HHS/ -- R37 HL063762/HL/NHLBI NIH HHS/ -- U24 DK059637/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1829-33. Epub 2005 Aug 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Texas (UT) Southwestern Medical Center at Dallas, 5323 Harry Hines Bouleuvard, Dallas, TX 75390-9072, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123266" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/*physiology ; Animals ; Blood Glucose/analysis ; Cell Line ; Cell Line, Tumor ; Eating ; Female ; Glucuronidase ; Insulin/blood/metabolism ; Insulin Resistance ; Insulin-Like Growth Factor I/metabolism/pharmacology ; Ligands ; Longevity/genetics/*physiology ; Male ; Membrane Proteins/chemistry/*genetics/pharmacology/*physiology ; Mice ; Mice, Transgenic ; Myoblasts/metabolism ; Oxygen Consumption ; Peptide Fragments/chemistry/pharmacology ; Phosphorylation ; Receptor, IGF Type 1/metabolism ; Receptor, Insulin/metabolism ; Receptors, Cell Surface/metabolism ; Recombinant Proteins/chemistry/isolation & purification/metabolism ; Signal Transduction
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowerman, Bruce -- New York, N.Y. -- Science. 2005 May 20;308(5725):1119-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA. bbowerman@molbio.uoregon.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905385" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/genetics/*metabolism/physiology ; Caenorhabditis elegans Proteins/*metabolism ; Cell Cycle ; Cell Line, Tumor ; Cell Proliferation ; Cell Survival ; Cytoskeletal Proteins/*metabolism ; Forkhead Transcription Factors ; Gene Expression Regulation ; Humans ; Longevity ; Neoplasms/metabolism/therapy ; *Oxidative Stress ; Receptor, Insulin/metabolism ; Signal Transduction ; Superoxide Dismutase/metabolism ; Trans-Activators/*metabolism ; Transcription Factors/*metabolism ; beta Catenin
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  • 27
    Publication Date: 2005-11-08
    Description: Local catabolism of the amino acid tryptophan (Trp) by indoleamine 2,3-dioxygenase (IDO) is considered an important mechanism of regulating T cell immunity. We show that IDO transcription was increased when myelin-specific T cells were stimulated with tolerogenic altered self-peptides. Catabolites of Trp suppressed proliferation of myelin-specific T cells and inhibited production of proinflammatory T helper-1 (T(H)1) cytokines. N-(3,4,-Dimethoxycinnamoyl) anthranilic acid (3,4-DAA), an orally active synthetic derivative of the Trp metabolite anthranilic acid, reversed paralysis in mice with experimental autoimmune encephalomyelitis, a model of multiple sclerosis (MS). Trp catabolites and their derivatives offer a new strategy for treating T(H)1-mediated autoimmune diseases such as MS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Platten, Michael -- Ho, Peggy P -- Youssef, Sawsan -- Fontoura, Paulo -- Garren, Hideki -- Hur, Eun Mi -- Gupta, Rohit -- Lee, Lowen Y -- Kidd, Brian A -- Robinson, William H -- Sobel, Raymond A -- Selley, Michael L -- Steinman, Lawrence -- New York, N.Y. -- Science. 2005 Nov 4;310(5749):850-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Neurological Sciences, Beckman Center for Molecular Medicine, Stanford University, Stanford, CA 94305, USA. michael.platten@uni-tuebingen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16272121" target="_blank"〉PubMed〈/a〉
    Keywords: Adoptive Transfer ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/administration & ; dosage/pharmacology/*therapeutic use ; Antigen-Presenting Cells/drug effects/immunology ; Brain/pathology ; Cell Line ; Cytokines/biosynthesis ; Disease Models, Animal ; Encephalomyelitis, Autoimmune, Experimental/*drug therapy/immunology ; Female ; Histocompatibility Antigens Class II/immunology/metabolism ; Immune Tolerance ; Immunosuppressive Agents/pharmacology/therapeutic use ; Indoleamine-Pyrrole 2,3,-Dioxygenase/genetics/metabolism ; Interferon-gamma/immunology ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Microglia/drug effects/immunology ; Multiple Sclerosis/drug therapy/immunology/pathology ; Myelin Proteins/immunology ; Signal Transduction ; Spinal Cord/pathology ; T-Lymphocytes/immunology ; Th1 Cells/immunology ; Th2 Cells/immunology ; Tryptophan/*metabolism ; ortho-Aminobenzoates/administration & dosage/pharmacology/*therapeutic use
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  • 28
    Publication Date: 2005-06-18
    Description: Rhizobial Nod factors induce in their legume hosts the expression of many genes and set in motion developmental processes leading to root nodule formation. Here we report the identification of the Medicago GRAS-type protein Nodulation signaling pathway 1 (NSP1), which is essential for all known Nod factor-induced changes in gene expression. NSP1 is constitutively expressed, and so it acts as a primary transcriptional regulator mediating all known Nod factor-induced transcriptional responses, and therefore, we named it a Nod factor response factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smit, Patrick -- Raedts, John -- Portyanko, Vladimir -- Debelle, Frederic -- Gough, Clare -- Bisseling, Ton -- Geurts, Rene -- New York, N.Y. -- Science. 2005 Jun 17;308(5729):1789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Science, Laboratory of Molecular Biology, Wageningen University, Wageningen 6703 HA, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15961669" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/metabolism ; Cell Nucleus/metabolism ; Cloning, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; Lipopolysaccharides/*metabolism ; Medicago/*genetics/metabolism/*microbiology ; Molecular Sequence Data ; Mutation ; Plant Proteins/chemistry/genetics/*metabolism ; Plant Roots/metabolism/microbiology ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; Signal Transduction ; Sinorhizobium meliloti/*physiology ; Symbiosis ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic
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  • 29
    Publication Date: 2005-10-08
    Description: The transport of auxin controls developmental events in plants. Here, we report that in addition to maintaining vacuolar pH, the H+-pyrophosphatase, AVP1, controls auxin transport and consequently auxin-dependent development. AVP1 overexpression results in increased cell division at the onset of organ formation, hyperplasia, and increased auxin transport. In contrast, avp1-1 null mutants have severely disrupted root and shoot development and reduced auxin transport. Changes in the expression of AVP1 affect the distribution and abundance of the P-adenosine triphosphatase and Pinformed 1 auxin efflux facilitator, two proteins implicated in auxin distribution. Thus, AVP1 facilitates the auxin fluxes that regulate organogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Jisheng -- Yang, Haibing -- Peer, Wendy Ann -- Richter, Gregory -- Blakeslee, Joshua -- Bandyopadhyay, Anindita -- Titapiwantakun, Boosaree -- Undurraga, Soledad -- Khodakovskaya, Mariya -- Richards, Elizabeth L -- Krizek, Beth -- Murphy, Angus S -- Gilroy, Simon -- Gaxiola, Roberto -- New York, N.Y. -- Science. 2005 Oct 7;310(5745):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Science, University of Connecticut, Storrs, CT 06268, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210544" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Arabidopsis/cytology/genetics/*growth & development/*metabolism ; Arabidopsis Proteins/metabolism ; Biological Transport ; Cell Count ; Cell Proliferation ; Cell Shape ; Cell Wall/metabolism ; Hydrogen-Ion Concentration ; In Situ Hybridization ; Indoleacetic Acids/*metabolism/pharmacology ; Inorganic Pyrophosphatase/genetics/*metabolism ; Membrane Transport Proteins/metabolism ; Meristem/metabolism ; Microsomes/metabolism ; Mutation ; Plant Leaves/cytology/growth & development/metabolism ; Plant Roots/cytology/growth & development/metabolism ; Proton Pumps/genetics/*metabolism ; RNA Interference ; Signal Transduction ; Transformation, Genetic
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woof, Jenny M -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1442-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Pathology and Neuroscience, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK. j.m.woof@dundee.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322444" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*immunology/therapeutic use ; Antibodies, Monoclonal/immunology/therapeutic use ; Antigen-Antibody Reactions ; Antigens, Neoplasm/immunology ; Blood Platelets/immunology ; Humans ; Immunoglobulin G/immunology/*therapeutic use ; Lung Neoplasms/immunology/prevention & control ; Mice ; Models, Immunological ; Receptors, IgG/immunology ; Signal Transduction
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-26
    Description: In addition to digesting and assimilating nutrients, the intestine and associated visceral organs play a key sensing and signaling role in the physiology of energy homeostasis. The gut, the pancreatic islets of Langerhans, elements in the portal vasculature, and even visceral adipose tissue communicate with the controllers of energy balance in the brain by means of neural and endocrine pathways. Signals reflecting energy stores, recent nutritional state, and other parameters are integrated in the central nervous system, particularly in the hypothalamus, to coordinate energy intake and expenditure. Our understanding of regulatory neural circuits and the signaling molecules that influence them has progressed rapidly, particularly after the discovery of the adipocyte hormone leptin. These discoveries have led to exploration of novel routes for obesity control, some of which involve gut-derived pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Badman, Michael K -- Flier, Jeffrey S -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1909-14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Endocrinology, Diabetes, and Metabolism, Beth Israel Deaconess Medical Center, Finard 202, 330 Brookline Avenue, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790843" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/physiology ; Animals ; Brain/*physiology ; *Energy Intake ; *Energy Metabolism ; Enteric Nervous System/physiology ; Gastrointestinal Tract/innervation/*physiology ; Humans ; Hunger ; Islets of Langerhans/physiology ; Neural Pathways ; Obesity/*physiopathology/surgery/therapy ; Peptide Hormones/*physiology ; Satiation ; Signal Transduction
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  • 32
    Publication Date: 2005-07-30
    Description: It is generally reasoned that lethal infections caused by opportunistic pathogens develop permissively by invading a host that is both physiologically stressed and immunologically compromised. However, an alternative hypothesis might be that opportunistic pathogens actively sense alterations in host immune function and respond by enhancing their virulence phenotype. We demonstrate that interferon-gamma binds to an outer membrane protein in Pseudomonas aeruginosa, OprF, resulting in the expression of a quorum-sensing dependent virulence determinant, the PA-I lectin. These observations provide details of the mechanisms by which prokaryotic organisms are directly signaled by immune activation in their eukaryotic host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Licheng -- Estrada, Oscar -- Zaborina, Olga -- Bains, Manjeet -- Shen, Le -- Kohler, Jonathan E -- Patel, Nachiket -- Musch, Mark W -- Chang, Eugene B -- Fu, Yang-Xin -- Jacobs, Michael A -- Nishimura, Michael I -- Hancock, Robert E W -- Turner, Jerrold R -- Alverdy, John C -- 2-RO1 GM062344-05/GM/NIGMS NIH HHS/ -- DK-38510/DK/NIDDK NIH HHS/ -- DK-47722/DK/NIDDK NIH HHS/ -- R01DK61931/DK/NIDDK NIH HHS/ -- R01DK68271/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 29;309(5735):774-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, University of Chicago, Pritzker School of Medicine, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16051797" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/*biosynthesis ; Animals ; Cell Line ; Cell Line, Tumor ; Cells, Cultured ; Cytokines/immunology/metabolism/pharmacology ; Humans ; Interferon-gamma/immunology/*metabolism/pharmacology ; Lectins/*biosynthesis ; Lymphocyte Activation ; Porins/isolation & purification/*metabolism ; Protein Binding ; Pseudomonas aeruginosa/growth & development/*immunology/metabolism/*pathogenicity ; Pyocyanine/biosynthesis ; Recombinant Proteins/pharmacology ; Signal Transduction ; T-Lymphocytes/*immunology ; Up-Regulation ; Virulence
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  • 33
    Publication Date: 2005-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nogueiras, Ruben -- Tschop, Matthias -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):985-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of Cincinnati, Cincinnati, OH 45237, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284170" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Appetite/drug effects ; Computational Biology ; *Eating/drug effects ; Energy Metabolism ; Fasting ; Gastric Emptying/drug effects ; Gastrointestinal Motility/drug effects ; Ghrelin ; Humans ; Mice ; Peptide Hormones/genetics/metabolism/pharmacology/*physiology ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Rats ; Receptors, G-Protein-Coupled/genetics/metabolism ; Signal Transduction ; Stomach/metabolism ; Weight Gain/drug effects
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  • 34
    Publication Date: 2005-02-05
    Description: Variants of NOD2, an intracellular sensor of bacteria-derived muramyl dipeptide (MDP), increase susceptibility to Crohn's disease (CD). These variants are thought to be defective in activation of nuclear factor kappaB (NF-kappaB) and antibacterial defenses, but CD clinical specimens display elevated NF-kappaB activity. To illuminate the pathophysiological function of NOD2, we introduced such a variant to the mouse Nod2 locus. Mutant mice exhibited elevated NF-kappaB activation in response to MDP and more efficient processing and secretion of the cytokine interleukin-1beta (IL-1beta). These effects are linked to increased susceptibility to bacterial-induced intestinal inflammation and identify NOD2 as a positive regulator of NF-kappaB activation and IL-1beta secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maeda, Shin -- Hsu, Li-Chung -- Liu, Hongjun -- Bankston, Laurie A -- Iimura, Mitsutoshi -- Kagnoff, Martin F -- Eckmann, Lars -- Karin, Michael -- AI43477/AI/NIAID NIH HHS/ -- AI56075/AI/NIAID NIH HHS/ -- DK07202/DK/NIDDK NIH HHS/ -- DK35108/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 4;307(5710):734-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0723, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692052" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylmuramyl-Alanyl-Isoglutamine/immunology ; Animals ; Anti-Bacterial Agents/pharmacology ; Apoptosis ; Bacteria/immunology ; Cells, Cultured ; Colitis/immunology/pathology ; Colon/*immunology/microbiology ; Crohn Disease/genetics/*immunology ; Cytokines/biosynthesis/genetics ; Dextran Sulfate/pharmacology ; Interleukin-1/*metabolism ; Intestinal Mucosa/immunology ; Intracellular Signaling Peptides and Proteins/*genetics/*physiology ; Lipopolysaccharides/immunology ; Macrophage Activation ; Macrophages/*immunology/metabolism ; Mice ; Mutation ; NF-kappa B/*metabolism ; Nod2 Signaling Adaptor Protein ; Peptidoglycan/immunology ; Signal Transduction
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  • 35
    Publication Date: 2005-11-15
    Description: Ghrelin, a circulating appetite-inducing hormone, is derived from a prohormone by posttranslational processing. On the basis of the bioinformatic prediction that another peptide also derived from proghrelin exists, we isolated a hormone from rat stomach and named it obestatin-a contraction of obese, from the Latin "obedere," meaning to devour, and "statin," denoting suppression. Contrary to the appetite-stimulating effects of ghrelin, treatment of rats with obestatin suppressed food intake, inhibited jejunal contraction, and decreased body-weight gain. Obestatin bound to the orphan G protein-coupled receptor GPR39. Thus, two peptide hormones with opposing action in weight regulation are derived from the same ghrelin gene. After differential modification, these hormones activate distinct receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Jian V -- Ren, Pei-Gen -- Avsian-Kretchmer, Orna -- Luo, Ching-Wei -- Rauch, Rami -- Klein, Cynthia -- Hsueh, Aaron J W -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):996-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Reproductive Biology, Department of Obstetrics and Gynecology, Stanford University School of Medicine, Stanford, CA 94305-5317, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284174" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Computational Biology ; Conserved Sequence ; Cricetinae ; *Eating/drug effects ; Fasting ; Gastric Emptying/drug effects ; Gastrointestinal Motility/drug effects ; Ghrelin ; Humans ; In Vitro Techniques ; Ligands ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptide Hormones/blood/chemistry/*genetics/metabolism/pharmacology/*physiology ; Protein Binding ; Protein Precursors/*genetics ; Radioimmunoassay ; Rats ; Rats, Sprague-Dawley ; Receptors, G-Protein-Coupled/metabolism ; Receptors, Ghrelin ; Signal Transduction ; Weight Gain/drug effects
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  • 36
    Publication Date: 2005-03-26
    Description: The quantitative relation between transcription factor concentrations and the rate of protein production from downstream genes is central to the function of genetic networks. Here we show that this relation, which we call the gene regulation function (GRF), fluctuates dynamically in individual living cells, thereby limiting the accuracy with which transcriptional genetic circuits can transfer signals. Using fluorescent reporter genes and fusion proteins, we characterized the bacteriophage lambda promoter P(R) in Escherichia coli. A novel technique based on binomial errors in protein partitioning enabled calibration of in vivo biochemical parameters in molecular units. We found that protein production rates fluctuate over a time scale of about one cell cycle, while intrinsic noise decays rapidly. Thus, biochemical parameters, noise, and slowly varying cellular states together determine the effective single-cell GRF. These results can form a basis for quantitative modeling of natural gene circuits and for design of synthetic ones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenfeld, Nitzan -- Young, Jonathan W -- Alon, Uri -- Swain, Peter S -- Elowitz, Michael B -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1962-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Molecular Cell Biology and Physics of Complex Systems, Weizmann Institute of Science, Rehovot, 76100, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790856" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/biosynthesis ; Bacteriophage lambda/genetics ; Cell Cycle ; DNA-Binding Proteins/*metabolism ; Escherichia coli/*genetics/growth & development/metabolism ; Escherichia coli Proteins/biosynthesis/*metabolism ; Fluorescence ; *Gene Expression Regulation, Bacterial ; Green Fluorescent Proteins/biosynthesis ; Image Processing, Computer-Assisted ; Luminescent Proteins/biosynthesis ; Mathematics ; Microscopy, Fluorescence ; *Models, Genetic ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/*metabolism ; Signal Transduction ; Transcription Factors/*metabolism ; Transcription, Genetic ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, Paul R -- BB/C007778/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2005 Aug 26;309(5739):1334-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomedical Research Centre, Ninewells Hospital and Medical School, University of Dundee, Dundee DD1 9SY, Scotland, UK. paul.clarke@cancer.org.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16123292" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle Proteins/metabolism ; Chromosomes/*metabolism ; Diffusion ; GTPase-Activating Proteins/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Guanosine Triphosphate/*metabolism ; Mathematics ; Microtubules/*metabolism ; *Mitosis ; Models, Biological ; Oocytes/metabolism ; Signal Transduction ; Spindle Apparatus/*metabolism ; Xenopus ; Xenopus Proteins ; beta Karyopherins/metabolism ; ran GTP-Binding Protein/*metabolism
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  • 38
    Publication Date: 2005-08-16
    Description: Day length controls flowering time in many plants. The day-length signal is perceived in the leaf, but how this signal is transduced to the shoot apex, where floral initiation occurs, is not known. In Arabidopsis, the day-length response depends on the induction of the FLOWERING LOCUS T (FT) gene. We show here that local induction of FT in a single Arabidopsis leaf is sufficient to trigger flowering. The FT messenger RNA is transported to the shoot apex, where downstream genes are activated. These data suggest that the FT mRNA is an important component of the elusive "florigen" signal that moves from leaf to shoot apex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Tao -- Bohlenius, Henrik -- Eriksson, Sven -- Parcy, Francois -- Nilsson, Ove -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1694-6. Epub 2005 Aug 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Umea Plant Science Centre, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, S-90183, Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099949" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/growth & development/metabolism ; Arabidopsis Proteins/*genetics/metabolism/physiology ; DNA-Binding Proteins/genetics/metabolism ; Flowers/*growth & development ; *Gene Expression Regulation, Plant ; Homeodomain Proteins/genetics ; Hot Temperature ; MADS Domain Proteins ; Plant Leaves/*genetics/metabolism ; Plant Proteins/genetics ; Plant Shoots/genetics/metabolism ; Plants, Genetically Modified ; Promoter Regions, Genetic ; RNA, Messenger/*genetics/*metabolism ; RNA, Plant/genetics/metabolism ; Signal Transduction ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-05-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferber, Dan -- New York, N.Y. -- Science. 2005 May 27;308(5726):1240.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919964" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; DNA-Binding Proteins/metabolism ; F-Box Proteins/genetics/*metabolism ; Gene Expression Regulation, Plant ; Genes, Plant ; Indoleacetic Acids/*metabolism ; Nuclear Proteins/metabolism ; Plant Proteins/genetics/*metabolism ; Protein Binding ; Receptors, Cell Surface/genetics/*metabolism ; Signal Transduction
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  • 40
    Publication Date: 2005-02-19
    Description: Apoptosis is important in controlling hematopoietic stem cell (HSC) numbers. However, the specific BCL-2 family member(s) that regulate HSC homeostasis are not precisely defined. We tested myeloid leukemia-1 (MCL-1) as an attractive candidate that is highly expressed in HSCs and regulated by growth factor signals. Inducible deletion of Mcl-1 in mice resulted in ablation of bone marrow. This resulted in the loss of early bone marrow progenitor populations, including HSCs. Moreover, growth factors including stem cell factor increased transcription of the Mcl-1 gene and required MCL-1 to augment survival of purified bone marrow progenitors. Deletion of Mcl-1 in other tissues, including liver, did not impair survival. Thus, MCL-1 is a critical and specific regulator essential for ensuring the homeostasis of early hematopoietic progenitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Opferman, Joseph T -- Iwasaki, Hiromi -- Ong, Christy C -- Suh, Heikyung -- Mizuno, Shin-ichi -- Akashi, Koichi -- Korsmeyer, Stanley J -- CA072009/CA/NCI NIH HHS/ -- DK061320/DK/NIDDK NIH HHS/ -- R37CA50239/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 18;307(5712):1101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Cancer Immunology and AIDS, Pathology and Medicine, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15718471" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Bone Marrow Cells/cytology/physiology ; Cell Count ; Cell Lineage ; Cell Shape ; Cell Survival ; Cells, Cultured ; Colony-Forming Units Assay ; Gene Deletion ; Gene Expression ; Hematopoietic Stem Cells/cytology/*physiology ; Homeostasis ; Interleukin-6/pharmacology ; Liver/cytology/physiology ; Mice ; Myeloid Cell Leukemia Sequence 1 Protein ; Neoplasm Proteins/genetics/*physiology ; Poly I-C/pharmacology ; Polymerase Chain Reaction ; Proto-Oncogene Proteins c-bcl-2/genetics/*physiology ; RNA, Messenger/genetics/metabolism ; Signal Transduction ; Stem Cell Factor/pharmacology ; Transduction, Genetic
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  • 41
    Publication Date: 2005-09-24
    Description: All animals coordinate growth and maturation to reach their final size and shape. In insects, insulin family molecules control growth and metabolism, whereas pulses of the steroid 20-hydroxyecdysone (20E) initiate major developmental transitions. We show that 20E signaling also negatively controls animal growth rates by impeding general insulin signaling involving localization of the transcription factor dFOXO and transcription of the translation inhibitor 4E-BP. We also demonstrate that the larval fat body, equivalent to the vertebrate liver, is a key relay element for ecdysone-dependent growth inhibition. Hence, ecdysone counteracts the growth-promoting action of insulins, thus forming a humoral regulatory loop that determines organismal size.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colombani, Julien -- Bianchini, Laurence -- Layalle, Sophie -- Pondeville, Emilie -- Dauphin-Villemant, Chantal -- Antoniewski, Christophe -- Carre, Clement -- Noselli, Stephane -- Leopold, Pierre -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):667-70. Epub 2005 Sep 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS/University of Nice-Sophia Antipolis, UMR6543, Parc Valrose, 06108 Nice Cedex 2, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16179433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Size ; Crosses, Genetic ; DNA-Binding Proteins/genetics/metabolism ; Drosophila melanogaster/*growth & development/metabolism ; Ecdysterone/*physiology ; Fat Body/physiology ; Insect Proteins/physiology ; Insulin/*physiology ; *Insulin Antagonists ; Larva/growth & development ; Phosphatidylinositol 3-Kinases/genetics/metabolism ; Signal Transduction ; Transcription Factors/genetics/metabolism
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  • 42
    Publication Date: 2005-05-10
    Description: To determine the role of reactive oxygen species in mammalian longevity, we generated transgenic mice that overexpress human catalase localized to the peroxisome, the nucleus, or mitochondria (MCAT). Median and maximum life spans were maximally increased (averages of 5 months and 5.5 months, respectively) in MCAT animals. Cardiac pathology and cataract development were delayed, oxidative damage was reduced, H2O2 production and H2O2-induced aconitase inactivation were attenuated, and the development of mitochondrial deletions was reduced. These results support the free radical theory of aging and reinforce the importance of mitochondria as a source of these radicals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schriner, Samuel E -- Linford, Nancy J -- Martin, George M -- Treuting, Piper -- Ogburn, Charles E -- Emond, Mary -- Coskun, Pinar E -- Ladiges, Warren -- Wolf, Norman -- Van Remmen, Holly -- Wallace, Douglas C -- Rabinovitch, Peter S -- AG001751/AG/NIA NIH HHS/ -- AG13280/AG/NIA NIH HHS/ -- ES07033/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1909-11. Epub 2005 May 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genome Sciences, University of Washington, Seattle, WA 91895, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879174" target="_blank"〉PubMed〈/a〉
    Keywords: Aconitate Hydratase/metabolism ; *Aging ; Animals ; Arteriosclerosis/pathology ; Catalase/genetics/*metabolism ; Cataract/pathology ; Cell Nucleus/enzymology/metabolism ; DNA/chemistry ; Deoxyguanosine/*analogs & derivatives/analysis ; Female ; Free Radicals ; Heart Diseases/pathology ; Humans ; Hydrogen Peroxide/*metabolism ; *Longevity ; Male ; Mice ; Mice, Transgenic ; Mitochondria/enzymology/*metabolism ; Mitochondria, Heart/enzymology/*metabolism ; Muscle, Skeletal/chemistry ; Myocardium/chemistry/pathology ; Oxidation-Reduction ; Oxidative Stress ; Peroxisomes/enzymology ; Reactive Oxygen Species/*metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Superoxide Dismutase/genetics/metabolism
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  • 43
    Publication Date: 2005-03-19
    Description: MicroRNAs (miRNAs) are small RNAs that regulate gene expression posttranscriptionally. To block all miRNA formation in zebrafish, we generated maternal-zygotic dicer (MZdicer) mutants that disrupt the Dicer ribonuclease III and double-stranded RNA-binding domains. Mutant embryos do not process precursor miRNAs into mature miRNAs, but injection of preprocessed miRNAs restores gene silencing, indicating that the disrupted domains are dispensable for later steps in silencing. MZdicer mutants undergo axis formation and differentiate multiple cell types but display abnormal morphogenesis during gastrulation, brain formation, somitogenesis, and heart development. Injection of miR-430 miRNAs rescues the brain defects in MZdicer mutants, revealing essential roles for miRNAs during morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giraldez, Antonio J -- Cinalli, Ryan M -- Glasner, Margaret E -- Enright, Anton J -- Thomson, J Michael -- Baskerville, Scott -- Hammond, Scott M -- Bartel, David P -- Schier, Alexander F -- New York, N.Y. -- Science. 2005 May 6;308(5723):833-8. Epub 2005 Mar 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Genetics Program, Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA. giraldez@saturn.med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774722" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; Brain/*embryology ; Cell Differentiation ; Central Nervous System/embryology ; Gastrula/physiology ; Gene Silencing ; Heart/embryology ; MicroRNAs/genetics/metabolism/*physiology ; *Morphogenesis ; Mutation ; Neurons/cytology ; Phenotype ; RNA Processing, Post-Transcriptional ; RNA, Double-Stranded/metabolism ; Ribonuclease III/genetics/metabolism ; Signal Transduction ; Somites/cytology/physiology ; Spinal Cord/embryology ; Zebrafish/*embryology/*genetics
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  • 44
    Publication Date: 2005-01-08
    Description: Solid tumors require blood vessels for growth, and many new cancer therapies are directed against the tumor vasculature. The widely held view is that these antiangiogenic therapies should destroy the tumor vasculature, thereby depriving the tumor of oxygen and nutrients. Here, I review emerging evidence supporting an alternative hypothesis-that certain antiangiogenic agents can also transiently "normalize" the abnormal structure and function of tumor vasculature to make it more efficient for oxygen and drug delivery. Drugs that induce vascular normalization can alleviate hypoxia and increase the efficacy of conventional therapies if both are carefully scheduled. A better understanding of the molecular and cellular underpinnings of vascular normalization may ultimately lead to more effective therapies not only for cancer but also for diseases with abnormal vasculature, as well as regenerative medicine, in which the goal is to create and maintain a functionally normal vasculature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jain, Rakesh K -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):58-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. L. Steele Lab for Tumor Biology, Department of Radiation Oncology, Massachusetts General Hospital, and Harvard Medical School, Cox-7, 100 Blossom Street, Boston, MA 02114, USA. jain@steele.mgh.harvard.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637262" target="_blank"〉PubMed〈/a〉
    Keywords: Angiogenesis Inhibitors/administration & dosage/*therapeutic use ; Animals ; Antineoplastic Agents/therapeutic use ; Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Cell Hypoxia ; Cell Proliferation ; Combined Modality Therapy ; Humans ; Neoplasms/*blood supply/*drug therapy/pathology/therapy ; Neovascularization, Pathologic ; Signal Transduction ; Vascular Endothelial Growth Factor A/antagonists & inhibitors/metabolism
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  • 45
    Publication Date: 2005-02-26
    Description: A striking characteristic of vertebrate embryos is their bilaterally symmetric body plan, which is particularly obvious at the level of the somites and their derivatives such as the vertebral column. Segmentation of the presomitic mesoderm must therefore be tightly coordinated along the left and right embryonic sides. We show that mutant mice defective for retinoic acid synthesis exhibit delayed somite formation on the right side. Asymmetric somite formation correlates with a left-right desynchronization of the segmentation clock oscillations. These data implicate retinoic acid as an endogenous signal that maintains the bilateral synchrony of mesoderm segmentation, and therefore controls bilateral symmetry, in vertebrate embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vermot, Julien -- Gallego Llamas, Jabier -- Fraulob, Valerie -- Niederreither, Karen -- Chambon, Pierre -- Dolle, Pascal -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):563-6. Epub 2005 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/ULP/College de France, BP 10142, 67404 Illkirch Cedex, Strasbourg, France. julien@igbmc.u-strasbg.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15731404" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/genetics/metabolism ; Animals ; *Body Patterning ; Embryo, Mammalian/*metabolism ; *Embryonic Development ; Fibroblast Growth Factor 8 ; Fibroblast Growth Factors/genetics/metabolism ; Gene Expression Profiling ; In Situ Hybridization ; Mesoderm/*physiology ; Mice ; Mice, Transgenic ; Morphogenesis ; Signal Transduction ; Somites/*physiology ; Tretinoin/*metabolism
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  • 46
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-06-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aguzzi, Adriano -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1420-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Neuropathology, University Hospital of Zurich, CH-8091 Zurich, Switzerland. adriano@pathol.unizh.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933188" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/pathology ; Cell Membrane/metabolism ; Glycosylphosphatidylinositols/*metabolism ; Mice ; Mice, Transgenic ; PrPC Proteins/physiology ; PrPSc Proteins/chemistry/*metabolism ; Prion Diseases/*etiology/pathology ; Protein Conformation ; Signal Transduction
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  • 47
    Publication Date: 2005-11-26
    Description: The Peutz-Jegher syndrome tumor-suppressor gene encodes a protein-threonine kinase, LKB1, which phosphorylates and activates AMPK [adenosine monophosphate (AMP)-activated protein kinase]. The deletion of LKB1 in the liver of adult mice resulted in a nearly complete loss of AMPK activity. Loss of LKB1 function resulted in hyperglycemia with increased gluconeogenic and lipogenic gene expression. In LKB1-deficient livers, TORC2, a transcriptional coactivator of CREB (cAMP response element-binding protein), was dephosphorylated and entered the nucleus, driving the expression of peroxisome proliferator-activated receptor-gamma coactivator 1alpha (PGC-1alpha), which in turn drives gluconeogenesis. Adenoviral small hairpin RNA (shRNA) for TORC2 reduced PGC-1alpha expression and normalized blood glucose levels in mice with deleted liver LKB1, indicating that TORC2 is a critical target of LKB1/AMPK signals in the regulation of gluconeogenesis. Finally, we show that metformin, one of the most widely prescribed type 2 diabetes therapeutics, requires LKB1 in the liver to lower blood glucose levels.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3074427/" 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/PMC3074427/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, Reuben J -- Lamia, Katja A -- Vasquez, Debbie -- Koo, Seung-Hoi -- Bardeesy, Nabeel -- Depinho, Ronald A -- Montminy, Marc -- Cantley, Lewis C -- CA84313/CA/NCI NIH HHS/ -- GM056203/GM/NIGMS NIH HHS/ -- GM37828/GM/NIGMS NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- R01 GM056203-09/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1642-6. Epub 2005 Nov 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA. shaw@salk.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16308421" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases ; Animals ; Blood Glucose/analysis ; Diabetes Mellitus, Type 2/drug therapy/metabolism ; Enzyme Activation ; Female ; Gene Expression Regulation ; Gluconeogenesis/genetics ; Glucose/*metabolism ; HeLa Cells ; Homeostasis ; Humans ; Hyperglycemia/drug therapy/metabolism ; Hypoglycemic Agents/*pharmacology/therapeutic use ; Lipogenesis/genetics ; Liver/enzymology/*metabolism ; Male ; Metformin/*pharmacology/therapeutic use ; Mice ; Mice, Obese ; Multienzyme Complexes/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Signal Transduction ; Trans-Activators/genetics/metabolism ; Transcription Factors
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  • 48
    Publication Date: 2005-07-09
    Description: Coordinated spacing and patterning of stomata allow efficient gas exchange between plants and the atmosphere. Here we report that three ERECTA (ER)-family leucine-rich repeat-receptor-like kinases (LRR-RLKs) together control stomatal patterning, with specific family members regulating the specification of stomatal stem cell fate and the differentiation of guard cells. Loss-of-function mutations in all three ER-family genes cause stomatal clustering. Genetic interactions with a known stomatal patterning mutant too many mouths (tmm) revealed stoichiometric epistasis and combination-specific neomorphism. Our findings suggest that the negative regulation of ER-family RLKs by TMM, which is an LRR receptor-like protein, is critical for proper stomatal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shpak, Elena D -- McAbee, Jessica Messmer -- Pillitteri, Lynn Jo -- Torii, Keiko U -- New York, N.Y. -- Science. 2005 Jul 8;309(5732):290-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16002616" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/*enzymology/genetics/growth & development ; Arabidopsis Proteins/genetics/*metabolism ; Cell Communication ; Cell Differentiation ; Cell Division ; Cell Lineage ; Epistasis, Genetic ; Gene Expression ; Genes, Plant ; Meristem/cytology ; Mutation ; Plant Epidermis/*cytology/enzymology/growth & development ; Plant Leaves/*cytology/enzymology/growth & development ; Promoter Regions, Genetic ; Protein Kinases/genetics/*metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Signal Transduction ; Stem Cells/cytology/physiology
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  • 49
    Publication Date: 2005-03-26
    Description: The ataxia-telangiectasia mutated (ATM) kinase signals the presence of DNA double-strand breaks in mammalian cells by phosphorylating proteins that initiate cell-cycle arrest, apoptosis, and DNA repair. We show that the Mre11-Rad50-Nbs1 (MRN) complex acts as a double-strand break sensor for ATM and recruits ATM to broken DNA molecules. Inactive ATM dimers were activated in vitro with DNA in the presence of MRN, leading to phosphorylation of the downstream cellular targets p53 and Chk2. ATM autophosphorylation was not required for monomerization of ATM by MRN. The unwinding of DNA ends by MRN was essential for ATM stimulation, which is consistent with the central role of single-stranded DNA as an evolutionarily conserved signal for DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Ji-Hoon -- Paull, Tanya T -- CA094008/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):551-4. Epub 2005 Mar 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, 1 University Station, A4800, Austin, TX 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790808" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Cell Line ; DNA/chemistry/*metabolism ; *DNA Damage ; DNA Repair ; DNA Repair Enzymes/genetics/*metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; Enzyme Activation ; Humans ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Nucleic Acid Conformation ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Recombinant Proteins/metabolism ; Serine ; Signal Transduction ; Transfection ; Tumor Suppressor Proteins/chemistry/*metabolism
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  • 50
    Publication Date: 2005-07-05
    Description: Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pufall, Miles A -- Lee, Gregory M -- Nelson, Mary L -- Kang, Hyun-Seo -- Velyvis, Algirdas -- Kay, Lewis E -- McIntosh, Lawrence P -- Graves, Barbara J -- GM08537/GM/NIGMS NIH HHS/ -- P01-CA24014/CA/NCI NIH HHS/ -- R01 GM38663/GM/NIGMS NIH HHS/ -- T32-CA93247/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):142-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Huntsman Cancer Institute, Department of Oncological Sciences, University of Utah, Salt Lake City, UT 84112-5550, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994560" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; DNA/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/*chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-ets ; Signal Transduction ; Transcription Factors/*chemistry/genetics/*metabolism
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  • 51
    Publication Date: 2005-10-01
    Description: During neural development, coordinate regulation of cell-cycle exit and differentiation is essential for cell-fate specification, cell survival, and proper wiring of neuronal circuits. However, the molecules that direct these events remain poorly defined. In the developing spinal cord, the differentiation of motor neuron progenitors into postmitotic motor neurons is regulated by retinoid signaling. Here, we identify a retinoid-inducible gene, GDE2 (glycerophosphodiester phosphodiesterase 2), encoding a six-transmembrane protein that is necessary and sufficient to drive spinal motor neuron differentiation in vivo. A single amino acid mutation in the extracellular catalytic domain abolishes protein function. This reveals a critical role for glycerophosphodiester metabolism in motor neuron differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rao, Meenakshi -- Sockanathan, Shanthini -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2212-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195461" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Catalytic Domain ; Cell Cycle ; *Cell Differentiation ; Chick Embryo ; Electroporation ; Gene Silencing ; Homeodomain Proteins/metabolism ; Immunohistochemistry ; Mitosis ; Molecular Sequence Data ; Motor Neurons/*cytology/*metabolism ; Nerve Tissue Proteins/metabolism ; Phosphoric Diester Hydrolases/chemistry/genetics/*metabolism ; RNA, Small Interfering ; Signal Transduction ; Spinal Cord/*cytology/embryology/metabolism ; Stem Cells/cytology/metabolism ; Transcription Factors/metabolism ; Transfection ; Tretinoin/metabolism ; Vitamin A/pharmacology
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  • 52
    Publication Date: 2005-02-05
    Description: We describe two male-specific olfactory receptors (ORs) in the silk moth, Bombyx mori, that are mutually exclusively expressed in a pair of adjacent pheromone-sensitive neurons of male antennae: One is specifically tuned to bombykol, the sex pheromone, and the other to bombykal, its oxidized form. Both pheromone ORs are coexpressed with an OR from the highly conserved insect OR subfamily. This coexpression promotes the functional expression of pheromone receptors and confers ligand-stimulated nonselective cation channel activity. The same effects were also observed for general ORs. Both odorant and pheromone signaling pathways are mediated by means of a common mechanism in insects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakagawa, Takao -- Sakurai, Takeshi -- Nishioka, Takaaki -- Touhara, Kazushige -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1638-42. Epub 2005 Feb 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrated Biosciences, Graduate School of Frontier Sciences, The University of Tokyo, Chiba 277-8562, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15692016" target="_blank"〉PubMed〈/a〉
    Keywords: Alkadienes/metabolism/*pharmacology ; Animals ; Bombyx/genetics/*physiology ; Cations/metabolism ; Dose-Response Relationship, Drug ; Fatty Alcohols/metabolism/*pharmacology ; Female ; Genes, Insect ; In Situ Hybridization ; Insect Proteins/genetics/*physiology ; Ion Channels/physiology ; Ligands ; Male ; Molecular Sequence Data ; Odors ; Olfactory Receptor Neurons/physiology ; Patch-Clamp Techniques ; Receptors, Odorant/genetics/*physiology ; Sense Organs/physiology ; Sex Attractants/*pharmacology/*physiology ; Signal Transduction ; Xenopus laevis
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  • 53
    Publication Date: 2005-11-19
    Description: Nonhost resistance describes the immunity of an entire plant species against nonadapted pathogen species. We report that Arabidopsis PEN2 restricts pathogen entry of two ascomycete powdery mildew fungi that in nature colonize grass and pea species. The PEN2 glycosyl hydrolase localizes to peroxisomes and acts as a component of an inducible preinvasion resistance mechanism. Postinvasion fungal growth is blocked by a separate resistance layer requiring the EDS1-PAD4-SAG101 signaling complex, which is known to function in basal and resistance (R) gene-triggered immunity. Concurrent impairment of pre- and postinvasion resistance renders Arabidopsis a host for both nonadapted fungi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lipka, Volker -- Dittgen, Jan -- Bednarek, Pawel -- Bhat, Riyaz -- Wiermer, Marcel -- Stein, Monica -- Landtag, Jorn -- Brandt, Wolfgang -- Rosahl, Sabine -- Scheel, Dierk -- Llorente, Francisco -- Molina, Antonio -- Parker, Jane -- Somerville, Shauna -- Schulze-Lefert, Paul -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1180-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl von Linne Weg 10, D-50829 Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293760" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/enzymology/genetics/*immunology/microbiology ; Arabidopsis Proteins/genetics/*physiology ; Ascomycota/physiology ; Carboxylic Ester Hydrolases/physiology ; DNA-Binding Proteins/physiology ; Mutation ; N-Glycosyl Hydrolases/*physiology ; Peroxisomes/physiology ; Phytophthora/physiology ; Plant Diseases/*microbiology ; Qa-SNARE Proteins/genetics/*physiology ; Signal Transduction
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-04-16
    Description: Cell-cell fusion is fundamental to the development and physiology of multicellular organisms, but little is known of its mechanistic underpinnings. Recent studies have revealed that many proteins involved in cell-cell fusion are also required for seemingly unrelated cellular processes such as phagocytosis, cell migration, axon growth, and synaptogenesis. We review advances in understanding cell-cell fusion by contrasting it with virus-cell and intracellular vesicle fusion. We also consider how proteins involved in general aspects of membrane dynamics have been co-opted to control fusion of diverse cell types by coupling with specialized proteins involved in cell-cell recognition, adhesion, and signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Elizabeth H -- Olson, Eric N -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):369-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. echen@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831748" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Fusion ; Cytoplasmic Vesicles/physiology ; Cytoskeleton/physiology ; Disease ; Humans ; Membrane Fusion ; Membrane Proteins/physiology ; Models, Biological ; Signal Transduction ; Therapeutics ; Viral Fusion Proteins/metabolism ; Virus Physiological Phenomena
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  • 55
    Publication Date: 2005-07-05
    Description: Technologies to assess the molecular targets of biomolecules in living cells are lacking. We have developed a technology called magnetism-based interaction capture (MAGIC) that identifies molecular targets on the basis of induced movement of superparamagnetic nanoparticles inside living cells. Efficient intracellular uptake of superparamagnetic nanoparticles (coated with a small molecule of interest) was mediated by a transducible fusogenic peptide. These nanoprobes captured the small molecule's labeled target protein and were translocated in a direction specified by the magnetic field. Use of MAGIC in genome-wide expression screening identified multiple protein targets of a drug. MAGIC was also used to monitor signal-dependent modification and multiple interactions of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Won, Jaejoon -- Kim, Mina -- Yi, Yong-Weon -- Kim, Young Ho -- Jung, Neoncheol -- Kim, Tae Kook -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994554" target="_blank"〉PubMed〈/a〉
    Keywords: Caspase 3 ; Caspases/metabolism ; Cell Line ; *Cell Physiological Phenomena ; Cell Survival ; Endocytosis ; Fluorescein-5-isothiocyanate ; Fluorescent Dyes ; HeLa Cells ; Humans ; I-kappa B Proteins/metabolism ; *Magnetics ; Microscopy, Confocal ; *Molecular Probe Techniques ; *Molecular Probes ; NF-kappa B/metabolism ; *Nanostructures ; Oligopeptides/metabolism ; Phosphorylation ; Protein Binding ; Proteins/*metabolism ; Quantum Dots ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Streptavidin ; Tacrolimus/metabolism ; Transcription Factor RelA ; Tumor Necrosis Factor-alpha/pharmacology ; beta-Transducin Repeat-Containing Proteins/metabolism
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  • 56
    Publication Date: 2005-10-08
    Description: The shoot apical meristem (SAM) is a collection of stem cells that resides at the tip of each shoot and provides the cells of the shoot. It is divided into functional regions. The central zone (CZ) at the tip of the meristem is the domain of expression of the CLAVATA3 (CLV3) gene, encoding a putative ligand for a transmembrane receptor kinase, CLAVATA1, active in cells of the rib meristem (RM), located just below the CZ. We show here that CLV3 restricts its own domain of expression (the CZ) by preventing differentiation of peripheral zone cells (PZ), which surround the CZ, into CZ cells and restricts overall SAM size by a separate, long-range effect on cell division rate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, G Venugopala -- Meyerowitz, Elliot M -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):663-7. Epub 2005 Oct 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Division of Biology, MC 156-29, 1200 East California Boulevard, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16210497" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/cytology/drug effects/*growth & development ; Arabidopsis Proteins/genetics/*physiology ; Cell Differentiation/physiology ; Cell Division/physiology ; Dexamethasone/pharmacology ; Gene Expression ; Gene Silencing ; Homeostasis ; Meristem/cytology/*growth & development ; Plants, Genetically Modified ; Signal Transduction ; Stem Cells/*physiology
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-01-22
    Description: In type 2 diabetes, the beta cells of the pancreas fail to produce enough insulin to meet the body's demand, in part because of an acquired decrease in beta-cell mass. In adults, pancreatic beta-cell mass is controlled by several mechanisms, including beta-cell replication, neogenesis, hypertrophy, and survival. Here, I discuss evidence supporting the notion that increased beta-cell apoptosis is an important factor contributing to beta-cell loss and the onset of type 2 diabetes. Interestingly, a key signaling molecule that promotes beta-cell growth and survival, insulin receptor substrate 2 (IRS-2), is a member of a family of proteins whose inhibition contributes to the development of insulin resistance in the liver and other insulin-responsive tissues. Thus, the IRS-2 pathway appears to be a crucial participant in the tenuous balance between effective pancreatic beta-cell mass and insulin resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhodes, Christopher J -- DK-55267/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):380-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pacific Northwest Research Institute, 720 Broadway, Seattle, WA 98122, USA. cjr@pnri.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15662003" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; *Apoptosis ; Cell Count ; Cell Division ; Cell Size ; Cell Survival ; Cytokines/metabolism ; Diabetes Mellitus, Type 2/*physiopathology ; Homeostasis ; Humans ; Hyperglycemia/physiopathology ; Hyperlipidemias/physiopathology ; Insulin/metabolism ; Insulin Receptor Substrate Proteins ; Insulin Resistance ; Intracellular Signaling Peptides and Proteins ; Islets of Langerhans/cytology/*physiology ; Lipid Metabolism ; Obesity/*physiopathology ; Phosphoproteins/metabolism ; Signal Transduction
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Adrian -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):191.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15821063" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallization ; DNA-Binding Proteins/physiology ; Diptera/anatomy & histology/*growth & development ; Eye/growth & development ; Larva/growth & development ; Models, Biological ; Nerve Tissue Proteins/physiology ; Signal Transduction ; Transcription Factors/physiology
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  • 59
    Publication Date: 2005-03-05
    Description: Caspase-8, a proapoptotic protease, has an essential role in lymphocyte activation and protective immunity. We show that caspase-8 deficiency (CED) in humans and mice specifically abolishes activation of the transcription factor nuclear factor kappaB (NF-kappaB) after stimulation through antigen receptors, Fc receptors, or Toll-like receptor 4 in T, B, and natural killer cells. Caspase-8 also causes the alphabeta complex of the inhibitor of NF-kappaB kinase (IKK) to associate with the upstream Bcl10-MALT1 (mucosa-associated lymphatic tissue) adapter complex. Recruitment of the IKKalpha, beta complex, its activation, and the nuclear translocation of NF-kappaB require enzyme activity of full-length caspase-8. These findings thus explain the paradoxical association of defective apoptosis and combined immunodeficiency in human CED.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Helen -- Bidere, Nicolas -- Zheng, Lixin -- Cubre, Alan -- Sakai, Keiko -- Dale, Janet -- Salmena, Leonardo -- Hakem, Razqallah -- Straus, Stephen -- Lenardo, Michael -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1465-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746428" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Apoptosis ; B-Lymphocytes/immunology/metabolism ; Caspase 8 ; Caspases/genetics/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Humans ; I-kappa B Kinase ; Immunity, Innate ; Immunologic Deficiency Syndromes/immunology/metabolism ; Isoenzymes/metabolism ; Killer Cells, Natural/immunology/metabolism ; Lipopolysaccharides/immunology ; Lymphocyte Activation ; Membrane Glycoproteins/metabolism ; Mice ; Mutation ; NF-kappa B/*metabolism ; Phosphorylation ; Protein Kinase C/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Antigen, T-Cell/*immunology ; Receptors, Cell Surface/metabolism ; Receptors, IgG/immunology ; Signal Transduction ; T-Lymphocytes/immunology/metabolism ; Toll-Like Receptor 4 ; Toll-Like Receptors ; Transcription Factor RelA ; Transfection
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartlett, Douglas H -- Azam, Farooq -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1775-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marine Biology Research Division, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093-0202, USA. dbartlett@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357249" target="_blank"〉PubMed〈/a〉
    Keywords: Biofilms/growth & development ; Chitin/metabolism/*physiology ; DNA, Bacterial/*genetics/*metabolism ; Fimbriae, Bacterial/metabolism ; Genes, Bacterial ; Genetic Variation ; Signal Transduction ; *Transformation, Bacterial ; Vibrio/genetics ; Vibrio cholerae/*genetics/pathogenicity/physiology ; Virulence ; Water Microbiology
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-04-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Feng-Quan -- Snider, William D -- New York, N.Y. -- Science. 2005 Apr 8;308(5719):211-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of North Carolina Neuroscience Center, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15825222" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein/metabolism ; Animals ; Axons/*physiology ; Glycogen Synthase Kinase 3/*physiology ; Intercellular Signaling Peptides and Proteins ; Microtubule-Associated Proteins/metabolism ; Microtubules/*physiology ; Nerve Tissue Proteins/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Signal Transduction
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  • 62
    Publication Date: 2005-12-13
    Description: G protein-coupled receptor kinase 2 (GRK2) plays a key role in the desensitization of G protein-coupled receptor signaling by phosphorylating activated heptahelical receptors and by sequestering heterotrimeric G proteins. We report the atomic structure of GRK2 in complex with Galphaq and Gbetagamma, in which the activated Galpha subunit of Gq is fully dissociated from Gbetagamma and dramatically reoriented from its position in the inactive Galphabetagamma heterotrimer. Galphaq forms an effector-like interaction with the GRK2 regulator of G protein signaling (RGS) homology domain that is distinct from and does not overlap with that used to bind RGS proteins such as RGS4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tesmer, Valerie M -- Kawano, Takeharu -- Shankaranarayanan, Aruna -- Kozasa, Tohru -- Tesmer, John J G -- AG006093/AG/NIA NIH HHS/ -- GM61454/GM/NIGMS NIH HHS/ -- HL071818/HL/NHLBI NIH HHS/ -- NS41441/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1686-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cellular and Molecular Biology, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339447" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cattle ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gq-G11/*chemistry/metabolism ; GTP-Binding Protein beta Subunits/*chemistry/metabolism ; GTP-Binding Protein gamma Subunits/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; RGS Proteins/metabolism ; Signal Transduction ; beta-Adrenergic Receptor Kinases/*chemistry/metabolism
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-10-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King-Jones, Kirst -- Thummel, Carl S -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):630-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112, USA. kirst@genetics.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16254176" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Size ; Drosophila melanogaster/*growth & development ; Ecdysone/*physiology ; Insulin/physiology ; Insulin Antagonists ; Larva/growth & development ; Models, Biological ; Phosphatidylinositol 3-Kinases/metabolism ; Signal Transduction
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  • 64
    Publication Date: 2005-06-25
    Description: Signaling by heterotrimeric GTP-binding proteins (G proteins) drives numerous cellular processes. The number of G protein molecules activated by a single membrane receptor is a determinant of signal amplification, although in most cases this parameter remains unknown. In retinal rod photoreceptors, a long-lived photoisomerized rhodopsin molecule activates many G protein molecules (transducins), yielding substantial amplification and a large elementary (single-photon) response, before rhodopsin activity is terminated. Here we report that the elementary response in olfactory transduction is extremely small. A ligand-bound odorant receptor has a low probability of activating even one G protein molecule because the odorant dwell-time is very brief. Thus, signal amplification in olfactory transduction appears fundamentally different from that of phototransduction.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2957801/" 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/PMC2957801/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhandawat, Vikas -- Reisert, Johannes -- Yau, King-Wai -- DC06904/DC/NIDCD NIH HHS/ -- R01 DC006904/DC/NIDCD NIH HHS/ -- R01 DC006904-01/DC/NIDCD NIH HHS/ -- R01 EY006837/EY/NEI NIH HHS/ -- R01 EY006837-16A1/EY/NEI NIH HHS/ -- R01 EY006837-17/EY/NEI NIH HHS/ -- R01 EY006837-18/EY/NEI NIH HHS/ -- R01 EY014596/EY/NEI NIH HHS/ -- R01 EY014596-01/EY/NEI NIH HHS/ -- R01 EY014596-02/EY/NEI NIH HHS/ -- R01 EY014596-03/EY/NEI NIH HHS/ -- R37 EY006837/EY/NEI NIH HHS/ -- R37 EY006837-15/EY/NEI NIH HHS/ -- R37 EY006837-15S1/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1931-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. vbhanda@mail.jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976304" target="_blank"〉PubMed〈/a〉
    Keywords: Acetophenones/*metabolism/pharmacology ; Action Potentials ; Adenylyl Cyclases/metabolism ; Animals ; Calcium/metabolism/pharmacology ; Cell Separation ; Cyclohexanols/*metabolism/pharmacology ; Dose-Response Relationship, Drug ; Heterotrimeric GTP-Binding Proteins/metabolism ; In Vitro Techniques ; Kinetics ; Ligands ; Monoterpenes/*metabolism/pharmacology ; *Odors ; Olfactory Receptor Neurons/cytology/*physiology ; Phosphorylation ; Rana pipiens ; Receptors, Odorant/*metabolism ; Signal Transduction ; Smell/physiology
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blazquez, Miguel A -- New York, N.Y. -- Science. 2005 Aug 12;309(5737):1024-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Biologia Molecular y Celular de Plantas (UPV-CSIC), Universidad Politecnica de Valencia, 46022 Valencia, Spain. mblazquez@ibmcp.upv.es〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16099968" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/metabolism ; Arabidopsis Proteins/genetics/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Flowers/*growth & development/metabolism ; Genes, Plant ; Homeodomain Proteins/genetics/metabolism ; MADS Domain Proteins ; Models, Biological ; Plant Leaves/metabolism ; Plant Proteins/genetics/metabolism ; Plant Shoots/metabolism ; RNA, Messenger/metabolism ; RNA, Plant/metabolism ; Signal Transduction ; Transcription Factors/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-26
    Description: Accurately predicting noise propagation in gene networks is crucial for understanding signal fidelity in natural networks and designing noise-tolerant gene circuits. To quantify how noise propagates through gene networks, we measured expression correlations between genes in single cells. We found that noise in a gene was determined by its intrinsic fluctuations, transmitted noise from upstream genes, and global noise affecting all genes. A model was developed that explains the complex behavior exhibited by the correlations and reveals the dominant noise sources. The model successfully predicts the correlations as the network is systematically perturbed. This approach provides a step toward understanding and manipulating noise propagation in more complex gene networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pedraza, Juan M -- van Oudenaarden, Alexander -- R01-GM068957/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1965-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790857" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/biosynthesis/genetics/metabolism ; DNA-Binding Proteins/genetics ; Escherichia coli/*genetics/metabolism ; Escherichia coli Proteins/biosynthesis/genetics ; Fluorescence ; *Gene Expression Regulation, Bacterial/drug effects ; *Genes, Bacterial ; Genes, Reporter ; Green Fluorescent Proteins/biosynthesis/genetics ; Isopropyl Thiogalactoside/pharmacology ; Lac Repressors ; Luminescent Proteins/biosynthesis/genetics ; Mathematics ; Microscopy, Fluorescence ; *Models, Genetic ; Promoter Regions, Genetic ; Repressor Proteins/genetics/metabolism ; Signal Transduction ; Stochastic Processes ; Tetracyclines/pharmacology ; Transcription, Genetic ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-06-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerard, Craig -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1560-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Children's Hospital, Harvard Medical School, Children's Hospital and Harvard Medical School, Boston, MA 02115 USA. craig.gerard@childrens.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947161" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/pharmacology ; Alcohol Dehydrogenase ; Animals ; Asthma/drug therapy/*physiopathology ; Bronchi/physiology/physiopathology ; Bronchial Hyperreactivity/physiopathology ; Glutathione Reductase/antagonists & inhibitors/genetics/*metabolism ; Humans ; Isoproterenol/pharmacology ; Lung/metabolism/*physiopathology ; Mice ; Mice, Knockout ; Muscle, Smooth/physiology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/metabolism ; Nitric Oxide Synthase Type II ; Receptors, G-Protein-Coupled/metabolism ; S-Nitrosoglutathione/metabolism ; S-Nitrosothiols/*metabolism ; Signal Transduction
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1711.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774738" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Antineoplastic Agents/*therapeutic use ; Benzamides ; Diabetes Mellitus, Type 2/*complications/*drug therapy ; Female ; Humans ; Imatinib Mesylate ; Insulin/metabolism ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/complications/*drug therapy ; Piperazines/*therapeutic use ; Platelet-Derived Growth Factor/antagonists & inhibitors ; Protein Kinase Inhibitors/*therapeutic use ; Pyrimidines/*therapeutic use ; Signal Transduction
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-06-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bix, Mark -- Kim, Sunhwa -- Rao, Anjana -- P01 HL67664/HL/NHLBI NIH HHS/ -- R01 AI44432/AI/NIAID NIH HHS/ -- R01 AI48636/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1563-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology,University of Washington School of Medicine, 1959 N.E. Pacific Street, HSC I6071, Seattle,WA 98195, USA. arao.cbr.med.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15947163" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/genetics/metabolism ; Animals ; CD4-Positive T-Lymphocytes/cytology/immunology/physiology ; Cell Differentiation ; Cell Nucleus/metabolism ; Chromosomes, Mammalian/genetics/metabolism ; DNA-Binding Proteins/metabolism ; GATA3 Transcription Factor ; *Gene Expression Regulation ; Genes, Regulator ; Interferon-gamma/*genetics/metabolism ; Interleukins/*genetics/immunology/metabolism ; Locus Control Region ; Mice ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/immunology ; *Regulatory Sequences, Nucleic Acid ; Signal Transduction ; T-Box Domain Proteins ; Th1 Cells/cytology/immunology/*physiology ; Th2 Cells/cytology/immunology/*physiology ; Trans-Activators/metabolism ; Transcription Factors/metabolism ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 70
    Publication Date: 2005-12-24
    Description: The microRNA lin-4 and its target, the putative transcription factor lin-14, control the timing of larval development in Caenorhabditis elegans. Here, we report that lin-4 and lin-14 also regulate life span in the adult. Reducing the activity of lin-4 shortened life span and accelerated tissue aging, whereas overexpressing lin-4 or reducing the activity of lin-14 extended life span. Lifespan extension conferred by a reduction in lin-14 was dependent on the DAF-16 and HSF-1 transcription factors, suggesting that the lin-4-lin-14 pair affects life span through the insulin/insulin-like growth factor-1 pathway. This work reveals a role for microRNAs and developmental timing genes in life-span regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boehm, Michelle -- Slack, Frank -- GM64701/GM/NIGMS NIH HHS/ -- R01 GM064701/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1954-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373574" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/physiology ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Caenorhabditis elegans Proteins/genetics/metabolism/*physiology ; Forkhead Transcription Factors ; Gene Expression Regulation, Developmental ; Genes, Developmental ; Heat-Shock Response ; Insulin/metabolism ; Insulin-Like Growth Factor I/metabolism ; Lipofuscin/metabolism ; Longevity/genetics/*physiology ; MicroRNAs/*physiology ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics/*physiology ; RNA, Helminth/*physiology ; Receptor, Insulin/metabolism ; Repressor Proteins/*physiology ; Signal Transduction ; Transcription Factors/physiology
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    Publication Date: 2005-04-02
    Description: The giant sarcomeric protein titin contains a protein kinase domain (TK) ideally positioned to sense mechanical load. We identified a signaling complex where TK interacts with the zinc-finger protein nbr1 through a mechanically inducible conformation. Nbr1 targets the ubiquitin-associated p62/SQSTM1 to sarcomeres, and p62 in turn interacts with MuRF2, a muscle-specific RING-B-box E3 ligase and ligand of the transactivation domain of the serum response transcription factor (SRF). Nuclear translocation of MuRF2 was induced by mechanical inactivity and caused reduction of nuclear SRF and repression of transcription. A human mutation in the titin protein kinase domain causes hereditary muscle disease by disrupting this pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lange, Stephan -- Xiang, Fengqing -- Yakovenko, Andrey -- Vihola, Anna -- Hackman, Peter -- Rostkova, Elena -- Kristensen, Jakob -- Brandmeier, Birgit -- Franzen, Gereon -- Hedberg, Birgitta -- Gunnarsson, Lars Gunnar -- Hughes, Simon M -- Marchand, Sylvie -- Sejersen, Thomas -- Richard, Isabelle -- Edstrom, Lars -- Ehler, Elisabeth -- Udd, Bjarne -- Gautel, Mathias -- G0200496(63216)/Medical Research Council/United Kingdom -- G0300213/Medical Research Council/United Kingdom -- PG/03/049/15364/British Heart Foundation/United Kingdom -- New York, N.Y. -- Science. 2005 Jun 10;308(5728):1599-603. Epub 2005 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Muscle Signalling and Development, Randall Division, King's College London, London SE1 1UL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15802564" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Catalytic Domain ; Cell Line ; Cell Nucleus/metabolism ; Connectin ; *Gene Expression Regulation ; Heat-Shock Proteins/metabolism ; Humans ; Ligands ; Mice ; Mice, Inbred C3H ; Molecular Sequence Data ; Muscle Proteins/*chemistry/genetics/*metabolism ; Muscle, Skeletal/*metabolism ; Muscular Diseases/genetics ; Mutation ; Myocytes, Cardiac/*metabolism ; Protein Binding ; Protein Conformation ; Protein Kinases/*chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Proteins/metabolism ; Rats ; Respiratory Insufficiency/genetics/metabolism ; Sarcomeres/metabolism ; Serum Response Factor/metabolism ; Signal Transduction ; Two-Hybrid System Techniques ; Ubiquitin-Protein Ligases/metabolism
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    Publication Date: 2005-10-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2005 Sep 30;309(5744):2145.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16195431" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dominance, Ocular/*physiology ; Electrophysiology ; GPI-Linked Proteins ; Mice ; Mutation ; Myelin Proteins/genetics/metabolism/*physiology ; Myelin Sheath/*physiology ; *Neuronal Plasticity ; Neurons/*physiology ; Photic Stimulation ; Receptors, Cell Surface/genetics/*physiology ; Signal Transduction ; Visual Cortex/cytology/growth & development/*physiology
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-04-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abraham, Robert T -- Tibbetts, Randal S -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):510-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Signal Transduction Program, The Burnham Institute, La Jolla, CA 92037, USA. abraham@burnham.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15845843" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Chloroquine/pharmacology ; DNA/*metabolism ; *DNA Damage ; DNA Repair ; DNA Repair Enzymes/*metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; Enzyme Activation ; Histone Deacetylase Inhibitors ; Humans ; Models, Biological ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Recombinant Proteins/metabolism ; Serine/metabolism ; Signal Transduction ; Tumor Suppressor Proteins/chemistry/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-06-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Richard A -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1875-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Geriatrics Center, University of Michigan School of Medicine, and Ann Arbor DVA Medical Center, Ann Arbor, MI 48109-0940, USA. millerr@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976292" target="_blank"〉PubMed〈/a〉
    Keywords: *Aging ; Animals ; Catalase/genetics/*metabolism ; Humans ; Insulin-Like Growth Factor I/genetics/metabolism ; *Longevity ; Mammals/physiology ; Mice ; Mice, Transgenic ; Mitochondria/enzymology ; Mutation ; Oxidation-Reduction ; Oxidative Stress ; Reactive Oxygen Species/*metabolism ; Signal Transduction
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2005-03-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2005 Mar 25;307(5717):1854-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15790818" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Phosphorylation ; *Protein Array Analysis ; *Protein Interaction Mapping ; Protein Kinases/*metabolism ; *Proteomics ; Saccharomyces cerevisiae/*enzymology ; Saccharomyces cerevisiae Proteins/*metabolism ; Signal Transduction ; Transcription Factors/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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