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  • Articles  (125)
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  • American Association for the Advancement of Science (AAAS)  (125)
  • Frontiers Media S.A.
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  • 2020-2023
  • 2000-2004  (70)
  • 1995-1999  (55)
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  • Articles  (125)
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  • 2020-2023
  • 2000-2004  (70)
  • 1995-1999  (55)
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  • 1
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    Transcription. Switching partners in a regulatory tango (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishioka, K -- Reinberg, D -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2497-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752565" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; *Gene Expression Regulation ; Histone Acetyltransferases ; Methylation ; Nuclear Proteins/*metabolism ; Phosphorylation ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Trans-Activators/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Development. Staying a boy forever (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wasserman, S A -- DiNardo, S -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Genetics, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093-0634, USA. stevenw@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752564" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Aging ; Cell Division ; Cell Nucleus/metabolism ; Drosophila/cytology/embryology/physiology ; Drosophila Proteins/*metabolism ; Germ Cells/cytology/metabolism/*physiology ; Glycoproteins/*metabolism ; Ligands ; Male ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Signal Transduction ; Spermatids/cytology/physiology ; Spermatogenesis ; Stem Cells/cytology/metabolism/*physiology ; Testis/cytology ; Transcription Factors/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Breakthrough of the year. Scorecard 2000 (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 2001 Dec 21;294(5551):2445.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; Communicable Diseases ; Elementary Particles ; Gene Silencing ; Humans ; Oceanography ; Rna ; *Research ; Research Support as Topic ; *Science ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Calcium signaling by HBx protein in hepatitis B virus DNA replication (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: Hepatitis B virus (HBV) infects more than 300 million people and is a leading cause of liver cancer and disease. The HBV HBx protein is essential for infection; HBx activation of Src is important for HBV DNA replication. In our study, HBx activated cytosolic calcium-dependent proline-rich tyrosine kinase-2 (Pyk2), a Src kinase activator. HBx activation of HBV DNA replication was blocked by inhibiting Pyk2 or calcium signaling mediated by mitochondrial calcium channels, which suggests that HBx targets mitochondrial calcium regulation. Reagents that increased cytosolic calcium substituted for HBx protein in HBV DNA replication. Thus, alteration of cytosolic calcium was a fundamental requirement for HBV replication and was mediated by HBx protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bouchard, M J -- Wang, L H -- Schneider, R J -- F32CA-4476/CA/NCI NIH HHS/ -- R0ICA-565633/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2376-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743208" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/metabolism ; Calcium Channels/metabolism ; *Calcium Signaling ; Cyclosporine/pharmacology ; Cytosol/metabolism ; *DNA Replication ; DNA, Viral/biosynthesis ; Egtazic Acid/*analogs & derivatives/pharmacology ; Enzyme Activation ; Focal Adhesion Kinase 2 ; Genome, Viral ; Hepatitis B virus/genetics/*physiology ; Humans ; Mitochondria/metabolism ; Phosphorylation ; Plasmids ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction ; Trans-Activators/genetics/*metabolism ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Virus Replication ; src-Family Kinases/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Carcinogenic bacteria. Cracking gut bugs' cell-skewing strategy (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferbe, D -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2269.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743174" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Bacterial ; Bacterial Proteins/metabolism ; *Cell Transformation, Neoplastic ; Gastric Mucosa/metabolism/*microbiology/pathology ; Helicobacter Infections/*microbiology/pathology ; Helicobacter pylori/metabolism/*pathogenicity ; Humans ; Intracellular Signaling Peptides and Proteins ; Phosphates/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/*metabolism ; Signal Transduction ; Stomach Neoplasms/*microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Virology. The X files--one step closer to closure (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: There may be drugs and a useful vaccine available to combat the hepatitis B virus, but one aspect of this pathogen remains a puzzle: the function of its HBx protein. As Ganem reveals in his Perspective, new findings (Bouchard et al.) show that this versatile viral protein is an activator of calcium-dependent Ras signaling, an observation that may explain many of its biological effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ganem, D -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2299-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Medicine and Microbiology, University of California, San Francisco, CA 94143, USA. ganem@cgl.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743185" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Signaling ; Cell Line ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; DNA Replication ; DNA, Viral/biosynthesis ; Focal Adhesion Kinase 2 ; Gene Expression Regulation, Viral ; Genes, Viral ; Hepatitis B virus/*genetics/*physiology ; Liver/virology ; Mutation ; Open Reading Frames ; Phosphorylation ; Protein-Tyrosine Kinases/genetics/metabolism ; Signal Transduction ; Trans-Activators/genetics/*metabolism ; Transcription Factor AP-1/metabolism ; Transcription Factors/metabolism ; Virus Replication ; ras Proteins/metabolism ; src-Family Kinases/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-18
    Description: Helicobacter pylori CagA protein is associated with severe gastritis and gastric carcinoma. CagA is injected from the attached Helicobacter pylori into host cells and undergoes tyrosine phosphorylation. Wild-type but not phosphorylation-resistant CagA induced a growth factor-like response in gastric epithelial cells. Furthermore, CagA formed a physical complex with the SRC homology 2 domain (SH2)-containing tyrosine phosphatase SHP-2 in a phosphorylation-dependent manner and stimulated the phosphatase activity. Disruption of the CagA-SHP-2 complex abolished the CagA-dependent cellular response. Conversely, the CagA effect on cells was reproduced by constitutively active SHP-2. Thus, upon translocation, CagA perturbs cellular functions by deregulating SHP-2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Higashi, Hideaki -- Tsutsumi, Ryouhei -- Muto, Syuichi -- Sugiyama, Toshiro -- Azuma, Takeshi -- Asaka, Masahiro -- Hatakeyama, Masanori -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):683-6. Epub 2001 Dec 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Oncology, Institute for Genetic Medicine and Graduate School of Science, Hokkaido University, Sapporo 060-0815, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743164" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; *Antigens, Bacterial ; Bacterial Proteins/genetics/*metabolism ; COS Cells ; Cell Membrane/enzymology/metabolism ; Cell Size ; Dipeptides/pharmacology ; Enzyme Inhibitors/pharmacology ; Gastric Mucosa/cytology/*enzymology ; *Helicobacter pylori/genetics/pathogenicity ; Humans ; Intracellular Signaling Peptides and Proteins ; Mutation ; Phenotype ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; SH2 Domain-Containing Protein Tyrosine Phosphatases ; Transfection ; Virulence ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Signal transduction. RIPping tyrosine kinase receptors apart (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heldin, C H -- Ericsson, J -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2111-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Box 595, Biomedical Center, SE-751 24 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11739942" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amyloid Precursor Protein Secretases ; Animals ; Aspartic Acid Endopeptidases ; Cell Division ; Cell Membrane/*metabolism ; Cell Nucleus/metabolism ; Dimerization ; Endopeptidases/metabolism ; Endoplasmic Reticulum/metabolism ; *Gene Expression Regulation ; Humans ; Ligands ; Mice ; Models, Biological ; Nuclear Localization Signals ; Phosphorylation ; Protein Structure, Tertiary ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Receptor, ErbB-4 ; *Signal Transduction ; Transcription, Genetic ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Taking cell-matrix adhesions to the third dimension (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-27
    Description: Adhesions between fibroblastic cells and extracellular matrix have been studied extensively in vitro, but little is known about their in vivo counterparts. Here, we characterized the composition and function of adhesions in three-dimensional (3D) matrices derived from tissues or cell culture. "3D-matrix adhesions" differ from focal and fibrillar adhesions characterized on 2D substrates in their content of alpha5beta1 and alphavbeta3 integrins, paxillin, other cytoskeletal components, and tyrosine phosphorylation of focal adhesion kinase (FAK). Relative to 2D substrates, 3D-matrix interactions also display enhanced cell biological activities and narrowed integrin usage. These distinctive in vivo 3D-matrix adhesions differ in structure, localization, and function from classically described in vitro adhesions, and as such they may be more biologically relevant to living organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Pankov, R -- Stevens, D R -- Yamada, K M -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1708-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, 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/11721053" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Cell Adhesion/drug effects ; Cell Culture Techniques/methods ; Cell Division ; Cell Movement ; Cell Size ; Cells, Cultured ; Culture Techniques/methods ; Cycloheximide/pharmacology ; Cytoskeletal Proteins/metabolism ; Extracellular Matrix/chemistry/metabolism ; Fibroblasts/chemistry/*cytology/*metabolism ; Fibronectins/metabolism ; Fluorescent Antibody Technique, Indirect ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Focal Adhesions/chemistry/metabolism ; Glutaral/metabolism ; Humans ; Imaging, Three-Dimensional/*methods ; Integrins/metabolism ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Conformation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    ATR and ATRIP: partners in checkpoint signaling (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-27
    Description: The checkpoint kinases ATM (ataxia telangiectasia mutated) and ATR (ATM and Rad3 related) transduce genomic stress signals to halt cell cycle progression and promote DNA repair. We report the identification of an ATR-interacting protein (ATRIP) that is phosphorylated by ATR, regulates ATR expression, and is an essential component of the DNA damage checkpoint pathway. ATR and ATRIP both localize to intranuclear foci after DNA damage or inhibition of replication. Deletion of ATR mediated by the Cre recombinase caused the loss of ATR and ATRIP expression, loss of DNA damage checkpoint responses, and cell death. Therefore, ATR is essential for the viability of human somatic cells. Small interfering RNA directed against ATRIP caused the loss of both ATRIP and ATR expression and the loss of checkpoint responses to DNA damage. Thus, ATRIP and ATR are mutually dependent partners in cell cycle checkpoint signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cortez, D -- Guntuku, S -- Qin, J -- Elledge, S J -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1713-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Mars McLean Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11721054" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Ataxia Telangiectasia Mutated Proteins ; *Cell Cycle ; *Cell Cycle Proteins ; Cell Death ; Cell Line ; Cell Survival ; Conserved Sequence ; DNA Damage ; DNA-Binding Proteins ; *Exodeoxyribonucleases ; Exons/genetics ; Gene Deletion ; Genes, Essential/genetics ; HeLa Cells ; Humans ; Integrases/genetics/metabolism ; Molecular Sequence Data ; Molecular Weight ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Precipitin Tests ; Protein Binding ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Sequence Alignment ; *Signal Transduction ; Viral Proteins/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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