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  • Articles  (44)
  • Phosphorylation
  • 2000-2004  (44)
  • 1970-1974
  • 1955-1959
  • 2002  (44)
  • Natural Sciences in General  (44)
  • Electrical Engineering, Measurement and Control Technology
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  • Articles  (44)
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  • 2000-2004  (44)
  • 1970-1974
  • 1955-1959
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  • 1
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    A distinct signaling pathway used by the IgG-containing B cell antigen receptor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-21
    Description: The immunoglobulin G (IgG)-containing B lymphocyte antigen receptor (IgG-BCR) transmits a signal distinct from that of IgM-BCR or IgD-BCR, although all three use the same signal-transducing component, Igalpha/Igbeta. Here we demonstrate that the inhibitory coreceptor CD22 down-modulates signaling through IgM-BCR and IgD-BCR, but not that through IgG-BCR, because of the IgG cytoplasmic tail, which prevents CD22 phosphorylation. These results suggest that the cytoplasmic tail of IgG specifically enhances IgG-BCR signaling by preventing CD22-mediated signal inhibition. Enhanced signaling through IgG-BCR may be involved in efficient IgG production, which is crucial for immunity to pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wakabayashi, Chisato -- Adachi, Takahiro -- Wienands, Jurgen -- Tsubata, Takeshi -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Medical Research Institute, Tokyo Medical and Dental University, 113-8510 Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493916" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Antigens, Differentiation, B-Lymphocyte/metabolism ; B-Lymphocytes/immunology/metabolism ; Calcium/metabolism ; Calcium Signaling ; *Cell Adhesion Molecules ; Cells, Cultured ; Immunoglobulin D/immunology/metabolism ; Immunoglobulin G/chemistry/immunology/*metabolism ; Intracellular Signaling Peptides and Proteins ; Lectins/metabolism ; Mice ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Receptors, Antigen, B-Cell/chemistry/immunology/*metabolism ; Sialic Acid Binding Ig-like Lectin 2 ; *Signal Transduction ; Transfection ; Tumor Cells, Cultured
    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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    Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: Multicellular organisms have three well-characterized subfamilies of mitogen-activated protein kinases (MAPKs) that control a vast array of physiological processes. These enzymes are regulated by a characteristic phosphorelay system in which a series of three protein kinases phosphorylate and activate one another. The extracellular signal-regulated kinases (ERKs) function in the control of cell division, and inhibitors of these enzymes are being explored as anticancer agents. The c-Jun amino-terminal kinases (JNKs) are critical regulators of transcription, and JNK inhibitors may be effective in control of rheumatoid arthritis. The p38 MAPKs are activated by inflammatory cytokines and environmental stresses and may contribute to diseases like asthma and autoimmunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Gary L -- Lapadat, Razvan -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1911-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado Health Sciences Center, Denver, CO 80262, USA. gary.johnson@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471242" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Cell Division ; Cytokines/metabolism ; Enzyme Activation ; Gene Expression Regulation ; Humans ; MAP Kinase Kinase Kinases/metabolism ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 10 ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinase 9 ; Mitogen-Activated Protein Kinases/*metabolism ; Neoplasms/enzymology/pathology ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Transcription, Genetic ; p38 Mitogen-Activated Protein Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Molecular biology. Untangling checkpoints (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sagata, Noriyuki -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1905-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Kyushu University, Fukuoka 812-8581, Japan. nsagascb@mbox.nc.kyushu-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471241" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastula/metabolism ; CDC2 Protein Kinase/metabolism ; *Cell Cycle ; Cell Line ; Cell Survival ; Checkpoint Kinase 2 ; Cyclin B/metabolism ; DNA Damage ; DNA Replication ; Enzyme Activation ; Humans ; Phosphorylation ; Protein Kinases/*metabolism ; *Protein-Serine-Threonine Kinases ; Radiation, Ionizing ; S Phase ; Xenopus ; cdc25 Phosphatases/*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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  • 4
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    Essay: Amersham Biosciences and Science Prize. PAS domains and metabolic status signaling (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rutter, Jared -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1567-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Texas Southwestern Medical Center, Houston, TX 75390, USA. jrutte@biochem.swmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446897" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Amino Acid Motifs ; Awards and Prizes ; Basic Helix-Loop-Helix Transcription Factors ; Carbohydrate Metabolism ; Carbon Monoxide ; Catalytic Domain ; Circadian Rhythm ; DNA/metabolism ; Gene Expression Regulation ; Glycogen/metabolism ; Glycogen Synthase/metabolism ; Helix-Loop-Helix Motifs ; Insulin/metabolism ; Intracellular Signaling Peptides and Proteins ; NADP/metabolism ; Nerve Tissue Proteins/chemistry/*metabolism ; Oxidation-Reduction ; Phosphorylation ; Protein Biosynthesis ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Saccharomyces cerevisiae/enzymology/genetics/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; *Signal Transduction ; Transcription Factors/chemistry/*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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  • 5
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    Hijacking of host cell IKK signalosomes by the transforming parasite Theileria (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: Parasites have evolved a plethora of mechanisms to ensure their propagation and evade antagonistic host responses. The intracellular protozoan parasite Theileria is the only eukaryote known to induce uncontrolled host cell proliferation. Survival of Theileria-transformed leukocytes depends strictly on constitutive nuclear factor kappa B (NF-kappaB) activity. We found that this was mediated by recruitment of the multisubunit IkappaB kinase (IKK) into large, activated foci on the parasite surface. IKK signalosome assembly was specific for the transforming schizont stage of the parasite and was down-regulated upon differentiation into the nontransforming merozoite stage. Our findings provide insights into IKK activation and how pathogens subvert host-cell signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heussler, Volker T -- Rottenberg, Sven -- Schwab, Rebekka -- Kuenzi, Peter -- Fernandez, Paula C -- McKellar, Susan -- Shiels, Brian -- Chen, Zhijian J -- Orth, Kim -- Wallach, David -- Dobbelaere, Dirk A E -- GM63692/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1033-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Pathology, Institute of Animal Pathology, University of Bern, CH-3012 Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411708" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Antiprotozoal Agents/pharmacology ; Apoptosis ; Cattle ; Cell Cycle ; Cell Division ; Cell Line, Transformed ; Cell Nucleus/metabolism ; Down-Regulation ; I-kappa B Kinase ; I-kappa B Proteins/metabolism ; Leukocytes/enzymology/*parasitology/physiology ; Microscopy, Confocal ; NF-kappa B/metabolism ; Naphthoquinones/pharmacology ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Signal Transduction ; Theileria/growth & development/metabolism/*pathogenicity
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  • 6
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    Self-assembly of highly phosphorylated silaffins and their function in biosilica morphogenesis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: Silaffins are uniquely modified peptides that have been implicated in the biogenesis of diatom biosilica. A method that avoids the harsh anhydrous hydrogen fluoride treatment commonly used to dissolve biosilica allows the extraction of silaffins in their native state. The native silaffins carry further posttranslational modifications in addition to their polyamine moieties. Each serine residue was phosphorylated, and this high level of phosphorylation is essential for biological activity. The zwitterionic structure of native silaffins enables the formation of supramolecular assemblies. Time-resolved analysis of silica morphogenesis in vitro detected a plastic silaffin-silica phase, which may represent a building material for diatom biosilica.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kroger, Nils -- Lorenz, Sonja -- Brunner, Eike -- Sumper, Manfred -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):584-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl Biochemie I, Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, 93053 Regensburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386330" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Wall/chemistry/metabolism ; Chemical Precipitation ; Chromatography, High Pressure Liquid ; Diatoms/*chemistry/metabolism ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Microscopy, Electron, Scanning ; Molecular Weight ; Morphogenesis ; Particle Size ; Peptides ; Phosphates/chemistry ; Phosphorus/analysis ; Phosphorylation ; Phosphoserine/chemistry ; Polyamines/chemistry ; Proteins/*chemistry/*isolation & purification/metabolism ; Silicon Dioxide/*chemistry/metabolism ; Spectrometry, Mass, Electrospray Ionization ; Static Electricity
    Print ISSN: 0036-8075
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  • 7
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    53BP1, a mediator of the DNA damage checkpoint (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-05
    Description: 53BP1 binds to the tumor suppressor protein p53 and has a potential role in DNA damage responses. We used small interfering RNA (siRNA) directed against 53BP1 in mammalian cells to demonstrate that 53BP1 is a key transducer of the DNA damage checkpoint signal. 53BP1 was required for p53 accumulation, G2-M checkpoint arrest, and the intra-S-phase checkpoint in response to ionizing radiation. 53BP1 played a partially redundant role in phosphorylation of the downstream checkpoint effector proteins Brca1 and Chk2 but was required for the formation of Brca1 foci in a hierarchical branched pathway for the recruitment of repair and signaling proteins to sites of DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Bin -- Matsuoka, Shuhei -- Carpenter, Phillip B -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1435-8. Epub 2002 Oct 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Mars McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364621" target="_blank"〉PubMed〈/a〉
    Keywords: BRCA1 Protein/metabolism ; Carrier Proteins/genetics/*metabolism ; Cell Cycle Proteins/metabolism ; Checkpoint Kinase 2 ; DNA/biosynthesis ; *DNA Damage ; *G2 Phase ; Histones/metabolism ; Humans ; *Intracellular Signaling Peptides and Proteins ; *Mitosis ; Nuclear Proteins/metabolism ; *Phosphoproteins ; Phosphorylation ; Protein Kinases/metabolism ; *Protein-Serine-Threonine Kinases ; RNA, Small Interfering ; Radiation, Ionizing ; *S Phase ; Signal Transduction ; Tumor Suppressor Protein p53/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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  • 8
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    Critical role for STAT4 activation by type 1 interferons in the interferon-gamma response to viral infection (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-21
    Description: Interferons (IFNs) are essential for host defense. Although the antiviral effects of the type 1 IFNs IFN-alpha and IFN-beta (IFN-alpha/beta) have been established, their immunoregulatory functions, especially their ability to regulate IFN-gamma production, are poorly understood. Here we show that IFN-alpha/beta activate STAT4 directly (STAT, signal transducers and activators of transcription) and that this is required for IFN-gamma production during viral infections of mice, in concert with T cell receptor-derived signals. In contrast, STAT1 appears to negatively regulate IFN-alpha/beta induction of IFN-gamma. Thus, type 1 IFNs, in addition to interleukin-12, provide pathways for innate regulation of adaptive immunity, and their immunoregulatory functions are controlled by modulating the activity of individual STATs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nguyen, Khuong B -- Watford, Wendy T -- Salomon, Rachelle -- Hofmann, Sigrun R -- Pien, Gary C -- Morinobu, Akio -- Gadina, Massimo -- O'Shea, John J -- Biron, Christine A -- F31-GM20760-02/GM/NIGMS NIH HHS/ -- R01-CA41268/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2063-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Immunology, Division of Biology and Medicine, Brown University, Providence, RI 02912, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242445" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arenaviridae Infections/*immunology ; CD8-Positive T-Lymphocytes/*immunology/metabolism ; Cells, Cultured ; DNA-Binding Proteins/*metabolism ; Female ; Gene Expression Regulation ; Interferon Type I/*immunology/pharmacology ; Interferon-gamma/*biosynthesis/genetics ; Interleukin-12/physiology ; *Lymphocytic choriomeningitis virus ; Male ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Promoter Regions, Genetic ; Receptors, Antigen, T-Cell/immunology/metabolism ; Recombinant Proteins ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Signal Transduction ; Th1 Cells/immunology/metabolism ; Trans-Activators/*metabolism
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  • 9
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    Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: The Golgi-localized, gamma-ear-containing, adenosine diphosphate ribosylation factor-binding proteins (GGAs) are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) in the Golgi and have an essential role in lysosomal enzyme sorting. Here the GGAs and the coat protein adaptor protein-1 (AP-1) were shown to colocalize in clathrin-coated buds of the trans-Golgi networks of mouse L cells and human HeLa cells. Binding studies revealed a direct interaction between the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further, AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3, thereby causing autoinhibition. This could induce the directed transfer of the MPRs from GGAs to AP-1. MPRs that are defective in binding to GGAs are poorly incorporated into AP-1-containing clathrin-coated vesicles. Thus, the GGAs and AP-1 interact to package MPRs into AP-1-containing coated vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doray, Balraj -- Ghosh, Pradipta -- Griffith, Janice -- Geuze, Hans J -- Kornfeld, Stuart -- R01 CA-08759/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1700-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215646" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/*metabolism ; Adaptor Proteins, Vesicular Transport ; Animals ; Biological Transport ; Carrier Proteins/*metabolism ; Cattle ; Cell Line ; Clathrin-Coated Vesicles/metabolism ; HeLa Cells ; Humans ; L Cells (Cell Line) ; Membrane Proteins/*metabolism ; Mice ; Mutation ; Phosphorylation ; Protein Binding ; Receptor, IGF Type 2/genetics/*metabolism ; Recombinant Proteins/metabolism ; trans-Golgi Network/*metabolism
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  • 10
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    MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-10
    Description: Intracellular signaling networks receive and process information to control cellular machines. The mitogen-activated protein kinase (MAPK) 1,2/protein kinase C (PKC) system is one such network that regulates many cellular machines, including the cell cycle machinery and autocrine/paracrine factor synthesizing machinery. We used a combination of computational analysis and experiments in mouse NIH-3T3 fibroblasts to understand the design principles of this controller network. We find that the growth factor-stimulated signaling network containing MAPK 1, 2/PKC can operate with one (monostable) or two (bistable) stable states. At low concentrations of MAPK phosphatase, the system exhibits bistable behavior, such that brief stimulus results in sustained MAPK activation. The MAPK-induced increase in the amounts of MAPK phosphatase eliminates the prolonged response capability and moves the network to a monostable state, in which it behaves as a proportional response system responding acutely to stimulus. Thus, the MAPK 1, 2/PKC controller network is flexibly designed, and MAPK phosphatase may be critical for this flexible response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhalla, Upinder S -- Ram, Prahlad T -- Iyengar, Ravi -- CA-79134/CA/NCI NIH HHS/ -- CA-81050/CA/NCI NIH HHS/ -- GM-54508/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1018-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Biological Sciences, Bangalore 560065 India. bhalla@ncbs.res.in〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169734" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adaptation, Physiological ; Animals ; *Cell Cycle Proteins ; Computer Simulation ; Dose-Response Relationship, Drug ; Dual Specificity Phosphatase 1 ; *Feedback, Physiological ; Immediate-Early Proteins/*metabolism ; *MAP Kinase Signaling System ; Mathematics ; Mice ; Mitogen-Activated Protein Kinase 1/*metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/*metabolism ; Models, Biological ; Phospholipases A/antagonists & inhibitors/metabolism ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Kinase C/metabolism ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/*metabolism
    Print ISSN: 0036-8075
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