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  • Binding Sites  (63)
  • Rats  (60)
  • 03. Hydrosphere::03.04. Chemical and biological::03.04.06. Hydrothermal systems
  • 04. Solid Earth::04.04. Geology::04.04.08. Sediments: dating, processes, transport
  • 04. Solid Earth::04.04. Geology::04.04.10. Stratigraphy
  • 04. Solid Earth::04.06. Seismology::04.06.08. Volcano seismology
  • Acoustics
  • Applied geophysics
  • Data analysis / ~ processing
  • Schussler
  • American Association for the Advancement of Science (AAAS)  (118)
  • Elsevier  (2)
  • Cambridge U. Press  (1)
  • Cambridge Univ. Press
  • Soc. of Exploration Geophys.
  • Springer
  • W.H. Freeman
  • Wiley
  • 2010-2014
  • 2005-2009
  • 2000-2004  (121)
  • 1980-1984
  • 2002  (121)
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  • 2010-2014
  • 2005-2009
  • 2000-2004  (121)
  • 1980-1984
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  • 1
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    Acoustic and Elastic Wave Fields in Geophysics, II (2002)
    Elsevier
    In:  Amsterdam, 530 pp., Elsevier, vol. 37, no. XVI:, pp. 227-235, (ISBN 0231-12739-1 hb, 0231127383 pb)
    Details
    Publication Date: 2002
    Keywords: Seismics (controlled source seismology) ; Applied geophysics ; Wave propagation ; Waves ; Textbook of geophysics ; Acoustics ; Fluids ; High frequency ... ; Kirchoff ; seismic Migration ; Layers ; Channel waves
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    BIBLIOGRAPHY SEISMOLOGY
  • 2
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    Multi-Component Vertical seismic profiling Analysis for Applied Seismic Anisotropy (2002)
    Elsevier
    In:  Amsterdam, 360 pp., Elsevier, vol. 26, no. 22, pp. 662-664, (ISBN 0-470-87000-1 (HB), ISBN 0-470-87001-X (PB))
    Details
    Publication Date: 2002
    Description: The vertical seismic profile, acquired with an array of 3C receivers and either a single source or several arranged in a multi-component configuration, provides an ideal high fidelity calibration tool for seismic projects involved in the application of seismic anisotropy. This book catalogues the majority of specialized tools necessary to work with P-P, P-S and S-S data from such Vertical seismic profiling surveys at the acquisition design, processing and interpretation stages. In particular, it discusses 3C, 4C, 6C and 9C Vertical seismic profiling, marine and land surveys with near and multiple offsets (walkways), azimuths (walkarounds) or a combination of both. These are considered for TIH or TIV flavours of seismic anisotropy arising from cracks, fractures, sedimentary layering, and shales. The anisotropic adaptation of familiar seismic methods for velocity analysis and inversion, reflected amplitude interpretation, are given together with more multi-component specific algorithms based upon the principles dictated by the vector convolutional model. Thus, multi-component methods are described that provide tests and compensation for source or receiver vector fidelity, tool rotation correction, layer stripping, near-surface correction, wavefield separation, and the Alford rotation with its variants. The work will be of interest to geophysicists involved in research or the application of seismic anisotropy using multi-component seismic. CONTENTS 1. Introduction. 2. Anisotropic replacement media. 3. Fundamentals of seismic anisotropy analysis. 4. Pre-requisites for near-offset Vertical seismic profiling analysis. 5. Anisotropy analysis from near-offset Vertical seismic profiling I - symmetry and uniformity. 6. Anisotropy analysis from far-offset Vertical seismic profiling II - asymmetry and non-uniformity. 7. Multiple-offset Vertical seismic profiling - kinematics. 8. Multiple-offset Vertical seismic profiling - dynamics. 9. The road ahead. Appendix - shear-wave birefringence analysis.
    Keywords: Applied geophysics ; Seismics (controlled source seismology) ; Vertical seismic profiling ; Anisotropy ; Textbook of geophysics
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    BIBLIOGRAPHY SEISMOLOGY
  • 3
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    The Seismic Wavefield. Vol. 2: Interpretation of Seismograms on Regional and Global Scales (2002)
    Cambridge U. Press
    In:  New York (xii + 534 pp.), Cambridge U. Press, vol. 13, no. XVI:, pp. 227-235, (ISBN 0-521-00665-1)
    Details
    Publication Date: 2002
    Keywords: WAVE ; Wave propagation ; Textbook of geophysics ; observations ; (part ; 1), ; theory ; (part ; 2) ; Ray seismics ; Anisotropy ; AnisotropyS ; Earthquake ; Chi-Chi ; Kobe ; Loma ; Prieta ; North ; Ridge ; Tennant ; Creek ; Aftershocks ; Inhomogeneity ; basins ; Data analysis / ~ processing ; Modelling ; wavefiled ; decomposition ; Dispersion ; Three dimensional ; Earth model, also for more shallow analyses ! ; CRUST ; earth mantle ; earth Core ; D-double-prime ; ultra ; Low velocity layer ; NOModelling ; Surface waves ; Tomography ; Receiver functions ; Source ; Moment tensor ; Inversion ; perturbation ; methods ; Handbook of geophysics
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  • 4
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    Enzymology. A moving story (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907122/" 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/PMC3907122/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falke, Joseph J -- R01 GM040731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1480-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biophysics Program and the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. falke@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859184" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Nitrogen/chemistry ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermodynamics
    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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    Cancer. BRCA2 enters the fray (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, John H -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/12228708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BRCA1 Protein/metabolism ; BRCA2 Protein/*chemistry/*metabolism ; Binding Sites ; Breast Neoplasms/genetics ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Damage ; *DNA Repair ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Female ; Genes, BRCA1 ; Genes, BRCA2 ; Genetic Predisposition to Disease ; Humans ; Mice ; Ovarian Neoplasms/genetics ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rad51 Recombinase ; Rats ; Recombination, Genetic ; Replication Protein A
    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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    Control of synaptic strength by glial TNFalpha (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: Activity-dependent modulation of synaptic efficacy in the brain contributes to neural circuit development and experience-dependent plasticity. Although glia are affected by activity and ensheathe synapses, their influence on synaptic strength has largely been ignored. Here, we show that a protein produced by glia, tumor necrosis factor alpha (TNFalpha), enhances synaptic efficacy by increasing surface expression of AMPA receptors. Preventing the actions of endogenous TNFalpha has the opposite effects. Thus, the continual presence of TNFalpha is required for preservation of synaptic strength at excitatory synapses. Through its effects on AMPA receptor trafficking, TNFalpha may play roles in synaptic plasticity and modulating responses to neural injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beattie, Eric C -- Stellwagen, David -- Morishita, Wade -- Bresnahan, Jacqueline C -- Ha, Byeong Keun -- Von Zastrow, Mark -- Beattie, Michael S -- Malenka, Robert C -- DA00439/DA/NIDA NIH HHS/ -- MH063394/MH/NIMH NIH HHS/ -- NS 31193/NS/NINDS NIH HHS/ -- NS38079/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, Palo Alto, CA 94304, USA. beattie.2@osu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/pharmacology ; Astrocytes/*metabolism ; Cells, Cultured ; Culture Media, Conditioned/pharmacology ; Gene Expression Regulation/drug effects ; Hippocampus/cytology/metabolism ; Neuronal Plasticity/drug effects ; Neurons/drug effects/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/metabolism ; Receptors, Tumor Necrosis Factor ; Receptors, Tumor Necrosis Factor, Type I ; Synapses/drug effects/*metabolism ; Synaptic Transmission/drug effects ; Tumor Necrosis Factor-alpha/antagonists & inhibitors/*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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    Visualization and functional analysis of RNA-dependent RNA polymerase lattices (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Positive-strand RNA viruses such as poliovirus replicate their genomes on intracellular membranes of their eukaryotic hosts. Electron microscopy has revealed that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays. The structural integrity of these arrays correlates with cooperative RNA binding and RNA elongation and is sensitive to mutations that disrupt intermolecular contacts predicted by the polymerase structure. Membranous vesicles isolated from poliovirus-infected cells contain structures consistent with the presence of two-dimensional polymerase arrays on their surfaces during infection. Therefore, host cytoplasmic membranes may function as physical foundations for two-dimensional polymerase arrays, conferring the advantages of surface catalysis to viral RNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyle, John M -- Bullitt, Esther -- Bienz, Kurt -- Kirkegaard, Karla -- AI-42119/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2218-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Inclusion Bodies, Viral/metabolism/ultrastructure ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Poliovirus/*enzymology/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; RNA Replicase/*chemistry/isolation & purification/*metabolism/ultrastructure ; RNA, Viral/biosynthesis/*metabolism ; Viral Core Proteins/metabolism ; Virus Replication
    Print ISSN: 0036-8075
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  • 8
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    BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Haijuan -- Jeffrey, Philip D -- Miller, Julie -- Kinnucan, Elspeth -- Sun, Yutong -- Thoma, Nicolas H -- Zheng, Ning -- Chen, Phang-Lang -- Lee, Wen-Hwa -- Pavletich, Nikola P -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1837-48.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Sloan-Kettering Division, Joan and Sanford I. Weill Graduate School of Medical Sciences, Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228710" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; BRCA2 Protein/*chemistry/genetics/*metabolism ; Binding Sites ; Crystallography, X-Ray ; DNA/metabolism ; *DNA Repair ; DNA, Single-Stranded/*metabolism ; DNA-Binding Proteins/metabolism ; Genes, BRCA2 ; Helix-Turn-Helix Motifs ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Mice ; Molecular Sequence Data ; Mutation ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; Rad51 Recombinase ; Rats ; *Recombination, Genetic
    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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    Tackling cancer at the telomeres (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2350.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923505" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Caspases/genetics ; Dendritic Cells/immunology ; Enzyme Inhibitors/*pharmacology/therapeutic use ; Genetic Therapy ; Humans ; Immunotherapy ; Neoplasms/drug therapy/*therapy ; RNA/metabolism ; RNA, Antisense/metabolism/pharmacology/therapeutic use ; Telomerase/antagonists & inhibitors/genetics/immunology/*metabolism ; Telomere/*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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  • 10
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    Protein structure. Harmless proteins twist into troublemakers (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):28-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934996" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid beta-Peptides/chemistry ; Animals ; Humans ; Mice ; Protein Conformation ; *Protein Folding ; *Protein Structure, Quaternary ; Proteins/*chemistry ; Rats
    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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  • 11
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    Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: The second messenger cyclic adenosine monophosphate (cAMP) is the most important modulator of sympathetic control over cardiac contractility. In cardiac myocytes and many other cell types, however, cAMP transduces the signal generated upon stimulation of various receptors and activates different cellular functions, raising the issue of how specificity can be achieved. In the general field of signal transduction, the view is emerging that specificity is guaranteed by tight localization of signaling events. Here, we show that in neonatal rat cardiac myocytes, beta-adrenergic stimulation generates multiple microdomains with increased concentration of cAMP in correspondence with the region of the transverse tubule/junctional sarcoplasmic reticulum membrane. The restricted pools of cAMP show a range of action as small as approximately 1 micrometer, and free diffusion of the second messenger is limited by the activity of phosphodiesterases. Furthermore, we demonstrate that such gradients of cAMP specifically activate a subset of protein kinase A molecules anchored in proximity to the T tubule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaccolo, Manuela -- Pozzan, Tullio -- TCP00089/Telethon/Italy -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1711-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Sciences and Venetian Institute for Molecular Medicine, University of Padua, Via Orus 2, 35129 Padua, Italy. manuela.zaccolo@unipd.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872839" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; A Kinase Anchor Proteins ; Adaptor Proteins, Signal Transducing ; Animals ; Animals, Newborn ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Fluorescence ; Green Fluorescent Proteins ; Intracellular Membranes/metabolism ; Kinetics ; Luminescent Proteins ; Myocardium/*cytology/*metabolism/ultrastructure ; Norepinephrine/pharmacology ; Phosphodiesterase Inhibitors/pharmacology ; Proto-Oncogene Proteins/pharmacology ; Rats ; Receptors, Adrenergic, beta/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sarcoplasmic Reticulum/*metabolism ; Second Messenger Systems ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 12
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    Partitioning of the matrix fraction of the Golgi apparatus during mitosis in animal cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: The Golgi apparatus is partitioned during mitosis in animal cells by a process of fragmentation, dispersal, and reassembly in each daughter cell. We fractionated the Golgi apparatus in vivo using the drug brefeldin A or a dominant-negative mutant of the Sar1p protein. After these treatments, Golgi enzymes moved back to the endoplasmic reticulum, leaving behind a matrix of Golgi structural proteins. Under these conditions, cells still entered and exited mitosis normally, and their Golgi matrix partitioned in a manner very similar to that of the complete organelle. Thus, the matrix may be the partitioning unit of the Golgi apparatus and may carry the Golgi enzyme-containing membranes into the daughter cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemann, Joachim -- Pypaert, Marc -- Taguchi, Tomohiko -- Malsam, Jorg -- Warren, Graham -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823640" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Animals ; Autoantigens ; Brefeldin A/pharmacology ; Cell Line ; Endoplasmic Reticulum/enzymology ; Golgi Apparatus/*metabolism/ultrastructure ; HeLa Cells ; Humans ; Interphase ; Intracellular Membranes/metabolism/ultrastructure ; Mannosidases/metabolism ; Membrane Proteins/metabolism ; Metaphase ; Microscopy, Electron ; Microscopy, Fluorescence ; *Mitosis ; Monomeric GTP-Binding Proteins/pharmacology ; N-Acetylglucosaminyltransferases/metabolism ; Protein Disulfide-Isomerases/metabolism ; Rats ; *Saccharomyces cerevisiae Proteins ; Telophase ; Vesicular Transport Proteins
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  • 13
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    Structural insights into group II intron catalysis and branch-site selection (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: Group II self-splicing introns catalyze autoexcision from precursor RNA transcripts by a mechanism strikingly similar to that of the spliceosome, an RNA-protein assembly responsible for splicing together the protein-coding parts of most eukaryotic pre-mRNAs. Splicing in both cases initiates via nucleophilic attack at the 5' splice site by the 2' OH of a conserved intron adenosine residue, creating a branched (lariat) intermediate. Here, we describe the crystal structure at 3.0 A resolution of a 70-nucleotide RNA containing the catalytically essential domains 5 and 6 of the yeast ai5gamma group II self-splicing intron, revealing an unexpected two-nucleotide bulged structure around the branch-point adenosine in domain 6.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Lan -- Doudna, Jennifer A -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2084-8. Epub 2002 Feb 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry and, Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859154" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/chemistry/metabolism ; Base Pairing ; Binding Sites ; CME-Carbodiimide/*analogs & derivatives ; Catalysis ; Cobalt/metabolism ; Crystallization ; Crystallography, X-Ray ; *Introns ; Magnesium/metabolism ; Manganese/metabolism ; *Nucleic Acid Conformation ; Point Mutation ; RNA Precursors/chemistry/metabolism ; *RNA Splicing ; RNA, Fungal/*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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  • 14
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    Regulation of corepressor function by nuclear NADH (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: The corepressor CtBP (carboxyl-terminal binding protein) is involved in transcriptional pathways important for development, cell cycle regulation, and transformation. We demonstrate that CtBP binding to cellular and viral transcriptional repressors is regulated by the nicotinamide adenine dinucleotides NAD+ and NADH, with NADH being two to three orders of magnitude more effective. Levels of free nuclear nicotinamide adenine dinucleotides, determined using two-photon microscopy, correspond to the levels required for half-maximal CtBP binding and are considerably lower than those previously reported. Agents capable of increasing NADH levels stimulate CtBP binding to its partners in vivo and potentiate CtBP-mediated repression. We propose that this ability to detect changes in nuclear NAD+/NADH ratio allows CtBP to serve as a redox sensor for transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Qinghong -- Piston, David W -- Goodman, Richard H -- K01 CA096561/CA/NCI NIH HHS/ -- R01 CA115468/CA/NCI NIH HHS/ -- R01 CA115468-05/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1895-7. Epub 2002 Feb 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847309" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Alcohol Oxidoreductases ; Amino Acid Sequence ; Animals ; Binding Sites ; Cadherins/genetics ; Cell Nucleus/*metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; *Gene Expression Regulation ; HeLa Cells ; Homeodomain Proteins/metabolism ; Humans ; Microscopy, Fluorescence ; Molecular Sequence Data ; Mutation ; NAD/*metabolism ; Oxidation-Reduction ; Phosphoproteins/chemistry/genetics/*metabolism ; Promoter Regions, Genetic ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Repressor Proteins/*metabolism ; *Transcription Factors ; Transcription, Genetic ; Transfection
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  • 15
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    Structural biology. Not just another ABC transporter (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, Amy L -- New York, N.Y. -- Science. 2002 May 10;296(5570):1038-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, TX 77030, USA. davidson@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004108" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Transport Systems, Basic/chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Carrier Proteins/chemistry/metabolism ; *DNA-Binding Proteins ; Dimerization ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/*chemistry/metabolism ; Fungal Proteins/chemistry/metabolism ; Hydrolysis ; Models, Molecular ; *Periplasmic Binding Proteins ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; *Saccharomyces cerevisiae Proteins ; Vitamin B 12/metabolism
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  • 16
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    Parallel single-cell monitoring of receptor-triggered membrane translocation of a calcium-sensing protein module (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Time courses of translocation of fluorescently conjugated proteins to the plasma membrane were simultaneously measured in thousands of individual rat basophilic leukemia cells. We found that the C2 domain---a calcium-sensing, lipid-binding protein module that is an essential regulator of protein kinase C and numerous other proteins---targeted proteins to the plasma membrane transiently if calcium was released from internal stores, and persistently in response to entry of extracellular calcium across the plasma membrane. The C2 domain translocation time courses of stimulated cells clustered into only two primary modes. Hence, the reversible recruitment of families of signaling proteins from one cellular compartment to another is a rapid bifurcation mechanism for inducing discrete states of cellular signaling networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teruel, Mary N -- Meyer, Tobias -- CA83229/CA/NCI NIH HHS/ -- GM062144/GM/NIGMS NIH HHS/ -- HG00057/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1910-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Stanford University Medical School, 269 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Calcium/*metabolism ; *Calcium Signaling ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Fluorescence ; Fluorescent Dyes ; Isoenzymes/chemistry/*metabolism ; Kinetics ; Luminescent Proteins ; Platelet Activating Factor/pharmacology ; Protein Binding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; Rats ; Receptors, Cell Surface/*metabolism ; Recombinant Fusion Proteins/metabolism ; Software ; Thapsigargin/pharmacology ; Transfection ; Tumor Cells, Cultured
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  • 17
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    Development. Putting the brakes on regeneration (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKerracher, Lisa -- Ellezam, Benjamin -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1819-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Pathologie et Biologie Cellulaire, Universite de Montreal, 2900 Edouard-Montpetit, Montreal, Quebec, H3T 1J4 Canada. mckerral@patho.umontreal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052945" target="_blank"〉PubMed〈/a〉
    Keywords: Amacrine Cells/*physiology ; Animals ; Axonal Transport ; Axons/*physiology ; *Cell Communication ; Cell Differentiation ; Cell Polarity ; Cells, Cultured ; Coculture Techniques ; Dendrites/*physiology ; Embryo, Mammalian ; Nerve Crush ; *Nerve Regeneration ; Optic Nerve/cytology/physiology ; Peripheral Nerves/transplantation ; Rats ; Retinal Ganglion Cells/*physiology ; Signal Transduction ; Spinal Cord/cytology/physiology
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  • 18
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    Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: Electron tomography of vitrified cells is a noninvasive three-dimensional imaging technique that opens up new vistas for exploring the supramolecular organization of the cytoplasm. We applied this technique to Dictyostelium cells, focusing on the actin cytoskeleton. In actin networks reconstructed without prior removal of membranes or extraction of soluble proteins, the cross-linking of individual microfilaments, their branching angles, and membrane attachment sites can be analyzed. At a resolution of 5 to 6 nanometers, single macromolecules with distinct shapes, such as the 26S proteasome, can be identified in an unperturbed cellular environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Medalia, Ohad -- Weber, Igor -- Frangakis, Achilleas S -- Nicastro, Daniela -- Gerisch, Gunther -- Baumeister, Wolfgang -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1209-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424373" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry/metabolism/*ultrastructure ; Actins/ultrastructure ; Animals ; Binding Sites ; Cell Membrane/metabolism/ultrastructure ; Cell Movement ; Dictyostelium/chemistry/physiology/*ultrastructure ; Endoplasmic Reticulum, Rough/ultrastructure ; Freezing ; *Image Processing, Computer-Assisted ; Macromolecular Substances ; Microfilament Proteins/*ultrastructure ; Organelles/*ultrastructure ; Peptide Hydrolases/ultrastructure ; *Proteasome Endopeptidase Complex ; Proteome ; Protozoan Proteins/ultrastructure ; Ribosomes/ultrastructure ; Tomography/*methods
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  • 19
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    Molecular basis of proton motive force generation: structure of formate dehydrogenase-N (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jormakka, Mika -- Tornroth, Susanna -- Byrne, Bernadette -- Iwata, So -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1863-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biomedical Sciences, Imperial College, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884747" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Catalytic Domain ; Cell Membrane/enzymology ; Crystallography, X-Ray ; Electron Transport ; Escherichia coli/*enzymology ; Formate Dehydrogenases/*chemistry/metabolism ; Formates/metabolism ; Guanine Nucleotides/chemistry/metabolism ; Hydrogen Bonding ; Iron-Sulfur Proteins/chemistry/metabolism ; Membrane Potentials ; Models, Molecular ; Nitrate Reductases/chemistry/metabolism ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; *Proton-Motive Force ; Protons ; Pterins/chemistry/metabolism ; Vitamin K 2/chemistry/metabolism
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  • 20
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    Biodegradable, elastic shape-memory polymers for potential biomedical applications (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-27
    Description: The introduction of biodegradable implant materials as well as minimally invasive surgical procedures in medicine has substantially improved health care within the past few decades. This report describes a group of degradable thermoplastic polymers that are able to change their shape after an increase in temperature. Their shape-memory capability enables bulky implants to be placed in the body through small incisions or to perform complex mechanical deformations automatically. A smart degradable suture was created to illustrate the potential of these shape-memory thermoplastics in biomedical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lendlein, Andreas -- Langer, Robert -- New York, N.Y. -- Science. 2002 May 31;296(5573):1673-6. Epub 2002 Apr 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉mnemoScience GmbH, Pauwelsstrabetae 19, D-52074 Aachen, Germany. a.lendlein@mnemoscience.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976407" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biocompatible Materials/chemical synthesis/chemistry ; Chemistry, Physical ; Dioxanes/chemistry ; Elasticity ; Elastomers ; Isocyanates/chemistry ; Mechanics ; Physicochemical Phenomena ; Polyesters/chemistry ; *Polymers/chemical synthesis/chemistry ; *Prostheses and Implants ; Rats ; Stress, Mechanical ; *Sutures ; Temperature ; Thermodynamics
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  • 21
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    Correlated bursts of activity in the neonatal hippocampus in vivo (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-06-18
    Description: The behavior of immature cortical networks in vivo remains largely unknown. Using multisite extracellular and patch-clamp recordings, we observed recurrent bursts of synchronized neuronal activity lasting 0.5 to 3 seconds that occurred spontaneously in the hippocampus of freely moving and anesthetized rat pups. The influence of slow rhythms (0.33 and 0.1 hertz) and the contribution of both gamma-aminobutyric acid A-mediated and glutamate receptor-mediated synaptic signals in the generation of hippocampal bursts was reminiscent of giant depolarizing potentials observed in vitro. This earliest pattern, which diversifies during the second postnatal week, could provide correlated activity for immature neurons and may underlie activity-dependent maturation of the hippocampal network.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leinekugel, Xavier -- Khazipov, Rustem -- Cannon, Robert -- Hirase, Hajime -- Ben-Ari, Yehezkel -- Buzsaki, Gyorgy -- FO6 TW02290/TW/FIC NIH HHS/ -- N0T 43994/PHS HHS/ -- NS 34994/NS/NINDS NIH HHS/ -- NS 43157/NS/NINDS NIH HHS/ -- RR09754/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2049-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INMED, Institut National de la Sante et de la Recherche Medicale (INSERM) U29, Avenue de Luminy, Boite Postale 13, 13273 Marseille Cedex 09, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065842" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Evoked Potentials ; Hippocampus/*physiology ; Neurons/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/physiology ; Rats ; Rats, Wistar ; Receptors, GABA-A/physiology ; Receptors, Glutamate/physiology ; Synapses/physiology ; Synaptic Transmission ; gamma-Aminobutyric Acid/physiology
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  • 22
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    Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-09-28
    Description: Unc104/KIF1A belongs to a class of monomeric kinesin motors that have been thought to possess an unusual motility mechanism. Unlike the unidirectional motion driven by the coordinated actions of the two heads in conventional kinesins, single-headed KIF1A was reported to undergo biased diffusional motion along microtubules. Here, we show that Unc104/KIF1A can dimerize and move unidirectionally and processively with rapid velocities characteristic of transport in living cells. These results suggest that Unc104/KIF1A operates in vivo by a mechanism similar to conventional kinesin and that regulation of motor dimerization may be used to control transport by this class of kinesins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomishige, Michio -- Klopfenstein, Dieter R -- Vale, Ronald D -- AR42895/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2263-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Howard Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351789" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/chemistry/physiology ; Diffusion ; Dimerization ; Humans ; Kinesin/*chemistry/physiology ; Liposomes ; Microtubules/*physiology ; Molecular Motor Proteins/*chemistry/*physiology ; Molecular Sequence Data ; Movement ; Mutation ; Nerve Tissue Proteins/*chemistry/*physiology ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry
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  • 23
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    Mediation of hippocampal mossy fiber long-term potentiation by presynaptic Ih channels (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: Hippocampal mossy fiber long-term potentiation (LTP) is expressed presynaptically, but the exact mechanisms remain unknown. Here, we demonstrate the involvement of the hyperpolarization-activated cation channel (Ih) in the expression of mossy fiber LTP. Established LTP was blocked and reversed by Ih channel antagonists. Whole-cell recording from granule cells revealed that repetitive stimulation causes a calcium- and Ih-dependent long-lasting depolarization mediated by protein kinase A. Depolarization at the terminals would be expected to enhance transmitter release, whereas somatic depolarization would enhance the responsiveness of granule cells to afferent input. Thus, Ih channels play an important role in the long-lasting control of transmitter release and neuronal excitability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mellor, Jack -- Nicoll, Roger A -- Schmitz, Dietmar -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):143-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778053" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Benzazepines/pharmacology ; Calcium/metabolism ; Cesium/pharmacology ; Chlorides/pharmacology ; Colforsin/pharmacology ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cyclic Nucleotide-Gated Cation Channels ; Dentate Gyrus/cytology/drug effects/physiology ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; In Vitro Techniques ; Ion Channels/antagonists & inhibitors/*physiology ; Isoquinolines/pharmacology ; Long-Term Potentiation/drug effects/*physiology ; Membrane Potentials ; *Membrane Proteins ; Models, Neurological ; Mossy Fibers, Hippocampal/drug effects/*physiology ; *Nerve Tissue Proteins ; Patch-Clamp Techniques ; Potassium/pharmacology ; Potassium Channels ; Presynaptic Terminals/*physiology ; Pyramidal Cells/drug effects/physiology ; Pyrimidines/pharmacology ; Rats ; Rats, Sprague-Dawley ; *Sulfonamides ; Synaptic Transmission
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  • 24
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    Signaling pathways for PC12 cell differentiation: making the right connections (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-01
    Description: A key issue in signal transduction is how signaling pathways common to many systems-so-called canonical signaling cassettes-integrate signals from molecules having a wide spectrum of activities, such as hormones and neurotrophins, to deliver distinct biological outcomes. The neuroendocrine cell line PC12, derived from rat pheochromocytoma, provides an example of how one canonical signaling cassette-the Raf --〉 mitogen-activated protein kinase kinase (MEK) --〉 extracellular signal-regulated kinase (ERK) pathway-can promote distinct outcomes, which in this case include neuritogenesis, gene induction, and proliferation. Two growth hormones, epidermal growth factor (EGF) and nerve growth factor (NGF), use the same pathway to cause PC12 proliferation and differentiation, respectively. In addition, pituitary adenylate cyclase-activating polypeptide (PACAP), a neurotransmitter that also causes differentiation, uses the same canonical cassette as NGF but in a different way. The Connections Map for PC12 Cell Differentiation brings into focus the complex array of specific cellular responses that rely on canonical signal transduction systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vaudry, D -- Stork, P J S -- Lazarovici, P -- Eiden, L E -- New York, N.Y. -- Science. 2002 May 31;296(5573):1648-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Molecular Neuroscience, Laboratory of Cellular and Molecular Regulation, National Institute of Mental Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040181" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Differentiation ; Cell Division ; Cyclic AMP/metabolism ; Epidermal Growth Factor/metabolism/pharmacology ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Models, Biological ; Nerve Growth Factor/metabolism/pharmacology ; Neurites/physiology ; Neuropeptides/metabolism/pharmacology ; PC12 Cells/*physiology ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Rats ; Receptor, trkA/metabolism ; Receptors, Cell Surface/metabolism ; Response Elements ; Transcription, Genetic
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  • 25
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    Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of alpha-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)-dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bryk, R -- Lima, C D -- Erdjument-Bromage, H -- Tempst, P -- Nathan, C -- HL61241/HL/NHLBI NIH HHS/ -- P30 CA08748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1073-7. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799204" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/*metabolism ; Amino Acid Sequence ; Antioxidants ; Binding Sites ; Catalysis ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Dihydrolipoamide Dehydrogenase/*metabolism ; Hydrogen Bonding ; Hydrogen Peroxide/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mycobacterium tuberculosis/*enzymology/genetics/metabolism ; NAD/metabolism ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Peroxidases/*chemistry/*metabolism ; Peroxiredoxins ; Peroxynitrous Acid/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Thioctic Acid/*analogs & derivatives/metabolism ; Thioredoxins/chemistry/metabolism
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    Reactivation of ocular dominance plasticity in the adult visual cortex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: In young animals, monocular deprivation leads to an ocular dominance shift, whereas in adults after the critical period there is no such shift. Chondroitin sulphate proteoglycans (CSPGs) are components of the extracellular matrix (ECM) inhibitory for axonal sprouting. We tested whether the developmental maturation of the ECM is inhibitory for experience-dependent plasticity in the visual cortex. The organization of CSPGs into perineuronal nets coincided with the end of the critical period and was delayed by dark rearing. After CSPG degradation with chondroitinase-ABC in adult rats, monocular deprivation caused an ocular dominance shift toward the nondeprived eye. The mature ECM is thus inhibitory for experience-dependent plasticity, and degradation of CSPGs reactivates cortical plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizzorusso, Tommaso -- Medini, Paolo -- Berardi, Nicoletta -- Chierzi, Sabrina -- Fawcett, James W -- Maffei, Lamberto -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scuola Normale Superiore, 56100 Pisa, Italy. tommaso@in.pi.cnr.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Chondroitin ABC Lyase/*metabolism ; Chondroitin Sulfate Proteoglycans/*metabolism ; Darkness ; *Dominance, Ocular ; Extracellular Matrix/*metabolism ; Extracellular Matrix Proteins/metabolism ; Glycosaminoglycans/metabolism ; Lectins, C-Type ; Light ; Nerve Tissue Proteins/metabolism ; *Neuronal Plasticity ; Neurons/physiology ; Rats ; Synapses/physiology ; Time Factors ; Visual Acuity ; Visual Cortex/*physiology
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    Enzyme dynamics during catalysis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenmesser, Elan Zohar -- Bosco, Daryl A -- Akke, Mikael -- Kern, Dorothee -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1520-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859194" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Isomerism ; Kinetics ; Mathematics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation
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    Generation of live young from xenografted mouse ovaries (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snow, Melanie -- Cox, Shae-Lee -- Jenkin, Graham -- Trounson, Alan -- Shaw, Jillian -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2227.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Monash University, Victoria, Australia, 3800.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351780" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Embryo Loss ; Embryo Transfer ; Embryonic and Fetal Development ; Female ; Fertility ; Fertilization in Vitro ; Gonadotropins, Equine/administration & dosage ; Male ; Mice ; Mice, Inbred Strains ; Mice, Nude ; Oocytes/*physiology ; Ovariectomy ; Ovary/*transplantation ; Pregnancy ; Pregnancy Outcome ; Rats ; *Reproductive Techniques, Assisted ; *Transplantation, Heterologous
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 29
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    Synthesis beyond the molecule (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-30
    Description: Weak, noncovalent interactions between molecules control many biological functions. In chemistry, noncovalent interactions are now exploited for the synthesis in solution of large supramolecular aggregates. The aim of these syntheses is not only the creation of a particular structure, but also the introduction of specific chemical functions in these supramolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinhoudt, D N -- Crego-Calama, M -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2403-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Supramolecular Chemistry and Technology, University of Twente, Post Office Box 217, 7500 AE Enschede, Netherlands. d.n.reinhoudt@ct.utwente.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923525" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; *Chemistry/methods ; Chemistry, Physical ; Evolution, Chemical ; Molecular Conformation ; Molecular Structure ; Nanotechnology ; Oligonucleotides/chemistry ; Origin of Life ; Peptides/chemistry ; Physicochemical Phenomena ; Polymers/*chemical synthesis/*chemistry ; Stereoisomerism ; Templates, Genetic
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  • 30
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    Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-21
    Description: Acetyl-coenzyme A (CoA) synthetase (Acs) is an enzyme central to metabolism in prokaryotes and eukaryotes. Acs synthesizes acetyl CoA from acetate, adenosine triphosphate, and CoA through an acetyl-adenosine monophosphate (AMP) intermediate. Immunoblotting and mass spectrometry analysis showed that Salmonella enterica Acs enzyme activity is posttranslationally regulated by acetylation of lysine-609. Acetylation blocks synthesis of the adenylate intermediate but does not affect the thioester-forming activity of the enzyme. Activation of the acetylated enzyme requires the nicotinamide adenine dinucleotide-dependent protein deacetylase activity of the CobB Sir2 protein from S. enterica. We propose that acetylation modulates the activity of all the AMP-forming family of enzymes, including nonribosomal peptide synthetases, luciferase, and aryl- and acyl-CoA synthetases. These findings extend our knowledge of the roles of Sir2 proteins in gene silencing, chromosome stability, and cell aging and imply that lysine acetylation is a common regulatory mechanism in eukaryotes and prokaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Starai, V J -- Celic, I -- Cole, R N -- Boeke, J D -- Escalante-Semerena, J C -- 1S10-RR14702/RR/NCRR NIH HHS/ -- GM62203/GM/NIGMS NIH HHS/ -- GM62385/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2390-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin, Madison, WI 53706-1567, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493915" target="_blank"〉PubMed〈/a〉
    Keywords: Acetate-CoA Ligase/chemistry/genetics/*metabolism ; Acetylation ; Acyl Coenzyme A/metabolism ; Adenosine Monophosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Proteins/*metabolism ; Binding Sites ; Coenzyme A/metabolism ; Conserved Sequence ; Enzyme Activation ; Gene Expression Regulation, Bacterial ; Immunoblotting ; Lysine/*metabolism ; Mass Spectrometry ; NAD/metabolism ; Peptide Mapping ; Salmonella enterica/*enzymology/genetics ; Sirtuins/*metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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    C-O bond formation by polyketide synthases (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-24
    Description: Polyketide synthases (PKSs) assemble the polyketide carbon backbone by sequential decarboxylative condensation of acyl coenzyme A (CoA) precursors, and the C-C bond-forming step in this process is catalyzed by the beta-ketoacyl synthase (KS) domain or subunit. Genetic and biochemical characterization of the nonactin biosynthesis gene cluster from Streptomyces griseus revealed two KSs, NonJ and NonK, that are highly homologous to known KSs but catalyze sequential condensation of the acyl CoA substrates by forming C-O rather than C-C bonds. This chemistry can be used in PKS engineering to increase the scope and diversity of polyketide biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwon, Hyung-Jin -- Smith, Wyatt C -- Scharon, A Janelle -- Hwang, Sung Hee -- Kurth, Mark J -- Shen, Ben -- AI51689/AI/NIAID NIH HHS/ -- T32 GM08505/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1327-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Pharmaceutical Sciences and, Department of Chemistry, University of Wisconsin, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193782" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*chemistry/*metabolism ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalysis ; Chromatography, High Pressure Liquid ; Genes, Bacterial ; Macrolides/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/*metabolism ; Multigene Family ; Mutation ; Protein Engineering ; Protein Subunits ; Sequence Alignment ; Spectrometry, Mass, Electrospray Ionization ; Streptomyces/genetics ; Streptomyces griseus/*enzymology/genetics ; Transformation, Bacterial
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  • 32
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    Phototransduction by retinal ganglion cells that set the circadian clock (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: Light synchronizes mammalian circadian rhythms with environmental time by modulating retinal input to the circadian pacemaker-the suprachiasmatic nucleus (SCN) of the hypothalamus. Such photic entrainment requires neither rods nor cones, the only known retinal photoreceptors. Here, we show that retinal ganglion cells innervating the SCN are intrinsically photosensitive. Unlike other ganglion cells, they depolarized in response to light even when all synaptic input from rods and cones was blocked. The sensitivity, spectral tuning, and slow kinetics of this light response matched those of the photic entrainment mechanism, suggesting that these ganglion cells may be the primary photoreceptors for this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berson, David M -- Dunn, Felice A -- Takao, Motoharu -- EY12793/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1070-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI, 02912 USA. David_Berson@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834835" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/ultrastructure ; *Biological Clocks ; *Circadian Rhythm ; Dendrites/ultrastructure ; Isoquinolines ; Kinetics ; Light ; *Light Signal Transduction ; Patch-Clamp Techniques ; Rats ; Rats, Sprague-Dawley ; Retinal Ganglion Cells/chemistry/cytology/*physiology ; Rod Opsins/analysis/physiology ; Suprachiasmatic Nucleus/cytology/*physiology
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    Immunology. Antibodies kill by producing ozone (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/*physiology ; Arthus Reaction ; Catalysis ; Escherichia coli/*physiology ; Humans ; Hydrogen Peroxide/metabolism ; Neutrophils/metabolism ; Oxidants/metabolism ; Oxidation-Reduction ; Ozone/*metabolism ; Rats ; Singlet Oxygen/metabolism
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    MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-16
    Description: Phosphorylation of mitogen-activated protein kinases (MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism. Here, we report an unexpected activation mechanism for p38alpha MAPK that does not involve the prototypic kinase cascade. Rather it depends on interaction of p38alpha with TAB1 [transforming growth factor-beta-activated protein kinase 1 (TAK1)-binding protein 1] leading to autophosphorylation and activation of p38alpha. We detected formation of a TRAF6-TAB1-p38alpha complex and showed stimulus-specific TAB1-dependent and TAB1-independent p38alpha activation. These findings suggest that alternative activation pathways contribute to the biological responses of p38alpha to various stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Baoxue -- Gram, Hermann -- Di Padova, Franco -- Huang, Betty -- New, Liguo -- Ulevitch, Richard J -- Luo, Ying -- Han, Jiahuai -- AI41637/AI/NIAID NIH HHS/ -- HL07195/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The Scripps Research Institute, 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/11847341" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; *Drosophila Proteins ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Imidazoles/pharmacology ; *Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase 6 ; *MAP Kinase Signaling System ; Membrane Glycoproteins/metabolism ; Mitogen-Activated Protein Kinase 14 ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinases/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Mutation ; Peptide Mapping ; Peroxynitrous Acid/pharmacology ; Phosphorylation ; Proteins/metabolism ; Pyridines/pharmacology ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; TNF Receptor-Associated Factor 6 ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/pharmacology ; Two-Hybrid System Techniques ; p38 Mitogen-Activated Protein Kinases
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    Structure of a cofactor-deficient nitrogenase MoFe protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-16
    Description: One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmid, Benedikt -- Ribbe, Markus W -- Einsle, Oliver -- Yoshida, Mika -- Thomas, Leonard M -- Dean, Dennis R -- Rees, Douglas C -- Burgess, Barbara K -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):352-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, Howard Hughes Medical Institute, 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/11951047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Azotobacter vinelandii/*enzymology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Molybdoferredoxin/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Static Electricity ; Surface Properties
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    Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-21
    Description: To make messenger RNA transcripts, bacteriophage T7 RNA polymerase (T7 RNAP) undergoes a transition from an initiation phase, which only makes short RNA fragments, to a stable elongation phase. We have determined at 2.1 angstrom resolution the crystal structure of a T7 RNAP elongation complex with 30 base pairs of duplex DNA containing a "transcription bubble" interacting with a 17-nucleotide RNA transcript. The transition from an initiation to an elongation complex is accompanied by a major refolding of the amino-terminal 300 residues. This results in loss of the promoter binding site, facilitating promoter clearance, and creates a tunnel that surrounds the RNA transcript after it peels off a seven-base pair heteroduplex. Formation of the exit tunnel explains the enhanced processivity of the elongation complex. Downstream duplex DNA binds to the fingers domain, and its orientation relative to upstream DNA in the initiation complex implies an unwinding that could facilitate formation of the open promoter complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yin, Y Whitney -- Steitz, Thomas A -- GM57510/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1387-95. Epub 2002 Sep 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242451" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T7/enzymology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/genetics/*metabolism ; Models, Molecular ; Mutation ; N-Acetylmuramoyl-L-alanine Amidase/metabolism ; Nucleic Acid Heteroduplexes ; Promoter Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA Polymerase II/chemistry ; RNA, Messenger/*chemistry/metabolism ; Taq Polymerase/chemistry ; Templates, Genetic ; Transcription Initiation Site ; *Transcription, Genetic ; Viral Proteins
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    C-cadherin ectodomain structure and implications for cell adhesion mechanisms (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative "classical" cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boggon, Titus J -- Murray, John -- Chappuis-Flament, Sophie -- Wong, Ellen -- Gumbiner, Barry M -- Shapiro, Lawrence -- NCI-P30-CA-08784/CI/NCPDCID CDC HHS/ -- R01 GM062270/GM/NIGMS NIH HHS/ -- R01 GM52717/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1308-13. Epub 2002 Apr 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Columbia University College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964443" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; CHO Cells ; Cadherins/*chemistry/genetics/metabolism ; *Cell Adhesion ; Cricetinae ; Crystallography, X-Ray ; Dimerization ; Glycosylation ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry ; Tryptophan/chemistry ; Xenopus Proteins
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  • 38
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    Amacrine-signaled loss of intrinsic axon growth ability by retinal ganglion cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: The central nervous system (CNS) loses the ability to regenerate early during development, but it is not known why. The retina has long served as a simple model system for study of CNS regeneration. Here we show that amacrine cells signal neonatal rat retinal ganglion cells (RGCs) to undergo a profound and apparently irreversible loss of intrinsic axon growth ability. Concurrently, retinal maturation triggers RGCs to greatly increase their dendritic growth ability. These results suggest that adult CNS neurons fail to regenerate not only because of CNS glial inhibition but also because of a loss of intrinsic axon growth ability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldberg, Jeffrey L -- Klassen, Matthew P -- Hua, Ying -- Barres, Ben A -- 2T32GM07365/GM/NIGMS NIH HHS/ -- R01 EY11030/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1860-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University School of Medicine, Department of Neurobiology, Sherman Fairchild Science Building D231, 299 Campus Drive, Stanford, CA 94305-5125, USA. jlgoldbe@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052959" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Amacrine Cells/*physiology ; Animals ; Animals, Newborn ; Axons/*physiology/ultrastructure ; Cell Aging ; *Cell Communication ; Cell Separation ; Cells, Cultured ; Culture Media, Conditioned ; Culture Techniques ; Cyclic AMP/metabolism ; Dendrites/physiology/ultrastructure ; Embryo, Mammalian ; Nerve Regeneration ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Rats ; Retina/cytology ; Retinal Ganglion Cells/*physiology/transplantation/ultrastructure ; Signal Transduction ; Superior Colliculi/physiology
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    Neuronal calcium sensor 1 and activity-dependent facilitation of P/Q-type calcium currents at presynaptic nerve terminals (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: P/Q-type presynaptic calcium currents (IpCa) undergo activity-dependent facilitation during repetitive activation at the calyx of the Held synapse. We investigated whether neuronal calcium sensor 1 (NCS-1) may underlie this phenomenon. Direct loading of NCS-1 into the nerve terminal mimicked activity-dependent IpCa facilitation by accelerating the activation time of IpCa in a Ca2+-dependent manner. A presynaptically loaded carboxyl-terminal peptide of NCS-1 abolished IpCa facilitation. These results suggest that residual Ca2+ activates endogenous NCS-1, thereby facilitating IpCa. Because both P/Q-type Ca2+ channels and NCS-1 are widely expressed in mammalian nerve terminals, NCS-1 may contribute to the activity-dependent synaptic facilitation at many synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsujimoto, Tetsuhiro -- Jeromin, Andreas -- Saitoh, Naoto -- Roder, John C -- Takahashi, Tomoyuki -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2276-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, University of Tokyo Faculty of Medicine, Tokyo 113-0033, Japan. tujimoto-tky@umin.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910115" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Amino Acid Sequence ; Animals ; Brain Stem/cytology/drug effects/metabolism ; Calcium/*metabolism/pharmacology ; Calcium Channels/*metabolism ; Calcium-Binding Proteins/administration & ; dosage/chemistry/*metabolism/pharmacology ; Electric Conductivity ; In Vitro Techniques ; Ion Channel Gating/drug effects ; Molecular Sequence Data ; Neuronal Calcium-Sensor Proteins ; Neuropeptides/administration & dosage/chemistry/*metabolism/pharmacology ; Presynaptic Terminals/drug effects/*metabolism ; Rats ; Rats, Wistar
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    Neurobiology. What the synapse tells the neuron (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mel, Bartlett W -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1845-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Engineering and Neuroscience Graduate Program, University of Southern California, Los Angeles, CA 90089, USA. mel@usc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884739" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/metabolism ; Calcium Signaling ; Dendrites/*physiology ; *Excitatory Postsynaptic Potentials ; Hippocampus/cytology/physiology ; Neocortex/cytology/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology ; Rats ; Synapses/*physiology ; Synaptic Transmission
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  • 41
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    Exosome-mediated recognition and degradation of mRNAs lacking a termination codon (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: One role of messenger RNA (mRNA) degradation is to maintain the fidelity of gene expression by degrading aberrant transcripts. Recent results show that mRNAs without translation termination codons are unstable in eukaryotic cells. We used yeast mutants to demonstrate that these "nonstop" mRNAs are degraded by the exosome in a 3'-to-5' direction. The degradation of nonstop transcripts requires the exosome-associated protein Ski7p. Ski7p is closely related to the translation elongation factor EF1A and the translation termination factor eRF3. This suggests that the recognition of nonstop mRNAs involves the binding of Ski7p to an empty aminoacyl-(RNA-binding) site (A site) on the ribosome, thereby bringing the exosome to a mRNA with a ribosome stalled near the 3' end. This system efficiently degrades mRNAs that are prematurely polyadenylated within the coding region and prevents their expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Hoof, Ambro -- Frischmeyer, Pamela A -- Dietz, Harry C -- Parker, Roy -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2262-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, 4000 Jones Bridge Road, Chevy Chase, MD 20815, USA. : ambro@u.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910110" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Alleles ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Codon, Terminator/*genetics ; Fungal Proteins/chemistry/genetics/*metabolism ; *GTP-Binding Proteins ; Gene Expression Regulation, Fungal ; Genes, Fungal/genetics ; Half-Life ; Molecular Sequence Data ; Polyadenylation ; Protein Binding ; Protein Biosynthesis ; RNA 3' End Processing ; *RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/*genetics/*metabolism ; Ribosomes/metabolism ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Sequence Alignment ; Sequence Deletion/*genetics
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    Place cells and place recognition maintained by direct entorhinal-hippocampal circuitry (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Place cells in hippocampal area CA1 may receive positional information from the intrahippocampal associative network in area CA3 or directly from the entorhinal cortex. To determine whether direct entorhinal connections support spatial firing and spatial memory, we removed all input from areas CA3 to CA1, thus isolating the CA1 area. Pyramidal cells in the isolated CA1 area developed sharp and stable place fields. Rats with an isolated CA1 area showed normal acquisition of an associative hippocampal-dependent spatial recognition task. Spatial recall was impaired. These results suggest that the hippocampus contains two functionally separable memory circuits: The direct entorhinal-CA1 system is sufficient for recollection-based recognition memory, but recall depends on intact CA3-CA1 connectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brun, Vegard H -- Otnass, Mona K -- Molden, Sturla -- Steffenach, Hill-Aina -- Witter, Menno P -- Moser, May-Britt -- Moser, Edvard I -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neuroscience Unit, Medical-Technical Research Centre, Norwegian University of Science and Technology, 7489 Trondheim, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077421" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Denervation ; Electrodes, Implanted ; Entorhinal Cortex/*physiology ; Hippocampus/*cytology/*physiology ; Interneurons/physiology ; Maze Learning ; Memory/*physiology ; Mental Recall/physiology ; Nerve Net/physiology ; Neural Pathways ; Pyramidal Cells/*physiology ; Rats ; Space Perception/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Alternative splicing and neuritic mRNA translocation under long-term neuronal hypersensitivity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: To explore neuronal mechanisms underlying long-term consequences of stress, we studied stress-induced changes in the neuritic translocation of acetylcholinesterase (AChE) splice variants. Under normal conditions, we found the synaptic AChE-S mRNA and protein in neurites. Corticosterone, anticholinesterases, and forced swim, each facilitated a rapid (minutes), yet long-lasting (weeks), shift from AChE-S to the normally rare AChE-R mRNA, promoted AChE-R mRNA translocation into neurites, and induced enzyme secretion. Weeks after stress, electrophysiological measurements in hippocampus slices displayed apparently normal evoked synaptic responses but extreme hypersensitivity to both anticholinesterases and atropine. Our findings suggest that neuronal hypersensitivity under stress involves neuritic replacement of AChE-S with AChE-R.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meshorer, Eran -- Erb, Christina -- Gazit, Roi -- Pavlovsky, Lev -- Kaufer, Daniela -- Friedman, Alon -- Glick, David -- Ben-Arie, Nissim -- Soreq, Hermona -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):508-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, The Institute of Life Sciences and The Eric Roland Center for Neurodegenerative Diseases, The Hebrew University of Jerusalem, Israel 91904.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799248" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Acetylcholinesterase/*genetics/*metabolism ; Action Potentials ; *Alternative Splicing ; Animals ; Atropine/pharmacology ; Cells, Cultured ; Cerebellum/cytology ; Cholinesterase Inhibitors/pharmacology ; Corticosterone/pharmacology ; Hippocampus/cytology/metabolism/physiology ; In Situ Hybridization, Fluorescence ; In Vitro Techniques ; Mice ; Mice, Transgenic ; Neurites/*metabolism ; Neurons/*metabolism ; Oligonucleotides, Antisense/pharmacology ; PC12 Cells ; Physostigmine/pharmacology ; RNA, Messenger/genetics/*metabolism ; Rats ; Stress, Physiological/genetics/*physiopathology ; Time Factors
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    Microbiology. A binding contract for anthrax (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bull, James J -- Parrish, Colin R -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):201-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Integrative Biology and Institute for Cellular and Molecular Biology, University of Texas, Austin, TX 78712, USA. bull@bull.biosci.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114612" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/prevention & control/therapy ; Anthrax Vaccines/adverse effects/immunology ; Antibodies, Bacterial/genetics/*immunology/metabolism/therapeutic use ; Antibody Affinity ; Antigen-Antibody Complex/blood ; *Antigens, Bacterial ; Antitoxins/genetics/*immunology/metabolism/therapeutic use ; Bacillus anthracis/*immunology ; Bacterial Toxins/*immunology/metabolism/toxicity ; Bioterrorism ; Drug Industry ; Escherichia coli/genetics ; Genetic Engineering ; Humans ; Immunization, Passive ; Macrophages, Alveolar/metabolism ; Peptide Library ; Rats ; Receptors, Peptide/metabolism ; Recombinant Proteins
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    Retrograde support of neuronal survival without retrograde transport of nerve growth factor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Application of nerve growth factor (NGF) covalently cross-linked to beads increased the phosphorylation of TrkA and Akt, but not of mitogen-activated protein kinase, in cultured rat sympathetic neurons. NGF beads or iodine-125-labeled NGF beads supplied to distal axons resulted in the survival of over 80% of the neurons for 30 hours, with little or no retrograde transport of iodine-125-labeled NGF; whereas application of free iodine-125-labeled NGF (0.5 nanograms per milliliter) produced 20-fold more retrograde transport, but only 29% of the neurons survived. Thus, in contrast to widely accepted theory, a neuronal survival signal can reach the cell bodies unaccompanied by the NGF that initiated it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacInnis, Bronwyn L -- Campenot, Robert B -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1536-9. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, 6-14 Medical Sciences Building, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*metabolism ; Cell Survival/drug effects ; Cells, Cultured ; Chromones/pharmacology ; Cross-Linking Reagents ; Enzyme Inhibitors/pharmacology ; Iodine Radioisotopes ; Microspheres ; Mitogen-Activated Protein Kinases/metabolism ; Morpholines/pharmacology ; Nerve Growth Factor/*metabolism/pharmacology ; Neurons/metabolism/*physiology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors/metabolism ; Phosphorylation ; Protein Transport ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Rats, Sprague-Dawley ; Receptor, trkA/metabolism ; Signal Transduction ; Superior Cervical Ganglion
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    Myeloperoxidase, a leukocyte-derived vascular NO oxidase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-29
    Description: Myeloperoxidase (MPO) is an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense reactions. Although its microbicidal functions are well established in vitro, humans deficient in MPO are not at unusual risk of infection. MPO was observed herein to modulate the vascular signaling and vasodilatory functions of nitric oxide (NO) during acute inflammation. After leukocyte degranulation, MPO localized in and around vascular endothelial cells in a rodent model of acute endotoxemia and impaired endothelium-dependent relaxant responses, to which MPO-deficient mice were resistant. Altered vascular responsiveness was due to catalytic consumption of NO by substrate radicals generated by MPO. Thus MPO can directly modulate vascular inflammatory responses by regulating NO bioavailability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eiserich, Jason P -- Baldus, Stephan -- Brennan, Marie-Luise -- Ma, Wenxin -- Zhang, Chunxiang -- Tousson, Albert -- Castro, Laura -- Lusis, Aldons J -- Nauseef, William M -- White, C Roger -- Freeman, Bruce A -- I01 BX000513/BX/BLRD VA/ -- R01 HL067930/HL/NHLBI NIH HHS/ -- R03 TW005682/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Division of Nephrology, University of California, Davis, CA 95616, USA. jpeiserich@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta ; Catalysis ; Cattle ; Cells, Cultured ; Chromans/metabolism/pharmacology ; Coculture Techniques ; Cyclic GMP/metabolism ; Endothelium, Vascular/enzymology/*physiology ; Endotoxemia/enzymology ; Humans ; Hydrogen Peroxide/metabolism/pharmacology ; Inflammation/*enzymology/physiopathology ; Leukocytes/*enzymology ; Mice ; Mice, Inbred C57BL ; Muscle, Smooth, Vascular/metabolism ; Mutation ; Nitric Oxide/*metabolism ; Oxidation-Reduction ; Peroxidase/genetics/*metabolism ; Rats ; Rats, Sprague-Dawley ; Signal Transduction ; Transfection ; Tumor Cells, Cultured ; *Vasodilation
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    The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: The ABC transporters are ubiquitous membrane proteins that couple adenosine triphosphate (ATP) hydrolysis to the translocation of diverse substrates across cell membranes. Clinically relevant examples are associated with cystic fibrosis and with multidrug resistance of pathogenic bacteria and cancer cells. Here, we report the crystal structure at 3.2 angstrom resolution of the Escherichia coli BtuCD protein, an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and appears to represent a conserved motif among the ABC transporters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Locher, Kaspar P -- Lee, Allen T -- Rees, Douglas C -- New York, N.Y. -- Science. 2002 May 10;296(5570):1091-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA. locher@caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004122" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Biological Transport ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/metabolism ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Vitamin B 12/*metabolism
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    Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The crystal structure of the initiating form of Thermus aquaticus RNA polymerase, containing core RNA polymerase (alpha2betabeta'omega) and the promoter specificity sigma subunit, has been determined at 4 angstrom resolution. Important structural features of the RNA polymerase and their roles in positioning sigma within the initiation complex are delineated, as well as the role played by sigma in modulating the opening of the RNA polymerase active-site channel. The two carboxyl-terminal domains of sigma are separated by 45 angstroms on the surface of the RNA polymerase, but are linked by an extended loop. The loop winds near the RNA polymerase active site, where it may play a role in initiating nucleotide substrate binding, and out through the RNA exit channel. The advancing RNA transcript must displace the loop, leading to abortive initiation and ultimately to sigma release.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, Katsuhiko S -- Masuda, Shoko -- Darst, Seth A -- GM53759/GM/NIGMS NIH HHS/ -- GM61898/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1280-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/*chemistry/*metabolism ; Eukaryotic Cells/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; Sigma Factor/metabolism ; Thermus/*enzymology ; *Transcription, Genetic
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  • 49
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    Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (alpha2betabeta'omegasigmaA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the sigma subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the sigma subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced -10 and -35 elements and provides the basis for models of the closed and open promoter complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, Katsuhiko S -- Masuda, Shoko -- Campbell, Elizabeth A -- Muzzin, Oriana -- Darst, Seth A -- GM20470/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- GM61898/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1285-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016307" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA, Bacterial/*chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Subunits ; Sigma Factor/*chemistry/metabolism ; Templates, Genetic ; Thermus/*enzymology ; *Transcription, Genetic
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    Molecular biology. New proteases in a ubiquitin stew (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-10-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hochstrasser, Mark -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):549-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386321" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Binding Sites ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cysteine Endopeptidases/*metabolism ; DNA-Binding Proteins/metabolism ; Endopeptidases/chemistry/*metabolism ; Fungal Proteins/metabolism ; Metalloendopeptidases/chemistry/*metabolism ; Models, Biological ; Multienzyme Complexes/*metabolism ; Mutation ; Peptide Hydrolases/*metabolism ; Proteasome Endopeptidase Complex ; Proteins/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Transcription Factors/metabolism ; Ubiquitins/*metabolism ; Yeasts/metabolism ; Zinc/metabolism
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    Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: The structural basis for the divalent cation-dependent binding of heterodimeric alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands triggers tertiary and quaternary structural rearrangements in integrins that are needed for cell signaling. Here we report the crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at the major interface between the alphaV and beta3 subunits and makes extensive contacts with both. Both tertiary and quaternary changes are observed in the presence of ligand. The tertiary rearrangements take place in betaA, the ligand-binding domain of beta3; in the complex, betaA acquires two cations, one of which contacts the ligand Asp directly and the other stabilizes the ligand-binding surface. Ligand binding induces small changes in the orientation of alphaV relative to beta3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiong, Jian-Ping -- Stehle, Thilo -- Zhang, Rongguang -- Joachimiak, Andrzej -- Frech, Matthias -- Goodman, Simon L -- Arnaout, M Amin -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):151-5. Epub 2002 Mar 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Renal Unit, Leukocyte Biology and Inflammation Program, Structural Biology Program, Massachusetts General Hospital, 149 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884718" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Ligands ; Manganese/chemistry ; Models, Molecular ; Oligopeptides/chemistry/*metabolism ; Peptides, Cyclic/chemistry/*metabolism ; *Protein Structure, Quaternary ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Receptors, Vitronectin/*chemistry/*metabolism
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    Transcription. Chromatin control--a place for E2F and Myc to meet (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉La Thangue, Nicholas B -- 13058/Cancer Research UK/United Kingdom -- G9400953/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2002 May 10;296(5570):1034-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, Davidson Building, University of Glasgow, Glasgow G12 8QQ, UK. n.lathangue@bio.gla.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004105" target="_blank"〉PubMed〈/a〉
    Keywords: Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; *Cell Cycle Proteins ; Chromatin/*metabolism ; DNA-Binding Proteins/metabolism ; Dimerization ; E2F Transcription Factors ; E2F6 Transcription Factor ; *G0 Phase ; G1 Phase ; *Gene Silencing ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Histone Deacetylases/metabolism ; *Histone-Lysine N-Methyltransferase ; Histones/metabolism ; Humans ; Methyltransferases/metabolism ; *Nuclear Proteins ; Promoter Regions, Genetic ; Protein Methyltransferases ; Proto-Oncogene Proteins c-myc/*metabolism ; Retinoblastoma Protein/metabolism ; Transcription Factors/*metabolism ; Transcription, Genetic
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    Regulation of organogenesis by the Caenorhabditis elegans FoxA protein PHA-4 (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: The pha-4 locus encodes a forkhead box A (FoxA/HNF3) transcription factor homolog that specifies organ identity for Caenorhabditis elegans pharyngeal cells. We used microarrays to identify pharyngeal genes and analyzed those genes to determine which were direct PHA-4 targets. Our data suggest that PHA-4 directly activates most or all pharyngeal genes. Furthermore, the relative affinity of PHA-4 for different TRTTKRY (R = A/G, K = T/G, Y = T/C) elements modulates the onset of gene expression, providing a mechanism to activate pharyngeal genes at different developmental stages. We suggest that direct transcriptional regulation of entire gene networks may be a common feature of organ identity genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaudet, J -- Mango, S E -- CCSG 2P30CA42014/CC/ODCDC CDC HHS/ -- R01 GM056264/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):821-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Huntsman Cancer Institute, University of Utah, 2000 Circle of Hope, Salt Lake City, UT 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823633" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biological Evolution ; Caenorhabditis elegans/*embryology/genetics/metabolism ; Caenorhabditis elegans Proteins/genetics/*metabolism ; Consensus Sequence ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; *Gene Expression Regulation, Developmental ; *Genes, Helminth ; Genes, Reporter ; Introns ; Models, Genetic ; Mutation ; Myosins/genetics ; Oligonucleotide Array Sequence Analysis ; Pharynx/cytology/embryology/metabolism ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/genetics/*metabolism
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    SynCAM, a synaptic adhesion molecule that drives synapse assembly (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: Synapses, the junctions between nerve cells through which they communicate, are formed by the coordinated assembly and tight attachment of pre- and postsynaptic specializations. We now show that SynCAM is a brain-specific, immunoglobulin domain-containing protein that binds to intracellular PDZ-domain proteins and functions as a homophilic cell adhesion molecule at the synapse. Expression of the isolated cytoplasmic tail of SynCAM in neurons inhibited synapse assembly. Conversely, expression of full-length SynCAM in nonneuronal cells induced synapse formation by cocultured hippocampal neurons with normal release properties. Glutamatergic synaptic transmission was reconstituted in these nonneuronal cells by coexpressing glutamate receptors with SynCAM, which suggests that a single type of adhesion molecule and glutamate receptor are sufficient for a functional postsynaptic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biederer, Thomas -- Sara, Yildirim -- Mozhayeva, Marina -- Atasoy, Deniz -- Liu, Xinran -- Kavalali, Ege T -- Sudhof, Thomas C -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1525-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Thomas.Biederer@UTSouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/cytology/*physiology ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/isolation & purification/*physiology ; Cell Adhesion Molecules, Neuronal/chemistry/isolation & purification/*physiology ; Cell Line ; Coculture Techniques ; Exocytosis ; Humans ; Immunoglobulins ; Molecular Sequence Data ; Neurons/physiology ; Prosencephalon/chemistry/physiology ; Protein Structure, Tertiary ; Rats ; Receptors, AMPA/physiology ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; Synapses/chemistry/*physiology ; Synaptic Transmission/physiology ; Transfection ; Tumor Suppressor Proteins
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    Proteomics. Integrating interactomes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerstein, Mark -- Lan, Ning -- Jansen, Ronald -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):284-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA. mark.gerstein@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786630" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; *Computational Biology ; Databases, Genetic ; Databases, Protein ; Gene Expression Profiling ; Genome ; Genome, Fungal ; *Genomics ; Humans ; Peptide Library ; Protein Structure, Tertiary ; Proteins/*chemistry/*metabolism ; *Proteome ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; Two-Hybrid System Techniques
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    S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: Matrix metalloproteinases (MMPs) are implicated in the pathogenesis of neurodegenerative diseases and stroke. However, the mechanism of MMP activation remains unclear. We report that MMP activation involves S-nitrosylation. During cerebral ischemia in vivo, MMP-9 colocalized with neuronal nitric oxide synthase. S-Nitrosylation activated MMP-9 in vitro and induced neuronal apoptosis. Mass spectrometry identified the active derivative of MMP-9, both in vitro and in vivo, as a stable sulfinic or sulfonic acid, whose formation was triggered by S-nitrosylation. These findings suggest a potential extracellular proteolysis pathway to neuronal cell death in which S-nitrosylation activates MMPs, and further oxidation results in a stable posttranslational modification with pathological activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Zezong -- Kaul, Marcus -- Yan, Boxu -- Kridel, Steven J -- Cui, Jiankun -- Strongin, Alex -- Smith, Jeffrey W -- Liddington, Robert C -- Lipton, Stuart A -- AR08505/AR/NIAMS NIH HHS/ -- P01 HD29587/HD/NICHD NIH HHS/ -- R01 AR42750/AR/NIAMS NIH HHS/ -- R01 CA 69306/CA/NCI NIH HHS/ -- R01 EY05477/EY/NEI NIH HHS/ -- R01 EY09024/EY/NEI NIH HHS/ -- R01 NS41207/NS/NINDS NIH HHS/ -- T32 AG00252/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1186-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuroscience and Aging, Program in Cell Adhesion and Extracellular Matrix Biology, The Burnham Institute, 10901 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/12183632" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Brain Ischemia/*enzymology/pathology ; Cell Line ; Cells, Cultured ; Cerebral Cortex/blood supply/*enzymology/pathology ; Cysteine/*analogs & derivatives/metabolism/pharmacology ; Enzyme Activation ; Enzyme Precursors/genetics/metabolism ; Humans ; Matrix Metalloproteinase 9/chemistry/*metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Models, Molecular ; Neurons/*physiology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type I ; Oxidation-Reduction ; Phenylmercuric Acetate/*analogs & derivatives/pharmacology ; Rats ; Recombinant Proteins/metabolism ; Reperfusion ; S-Nitrosothiols/*metabolism/pharmacology ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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    Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: N-methyl-D-aspartate receptors (NMDARs) mediate ischemic brain damage but also mediate essential neuronal excitation. To treat stroke without blocking NMDARs, we transduced neurons with peptides that disrupted the interaction of NMDARs with the postsynaptic density protein PSD-95. This procedure dissociated NMDARs from downstream neurotoxic signaling without blocking synaptic activity or calcium influx. The peptides, when applied either before or 1 hour after an insult, protected cultured neurons from excitotoxicity, reduced focal ischemic brain damage in rats, and improved their neurological function. This approach circumvents the negative consequences associated with blocking NMDARs and may constitute a practical stroke therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aarts, Michelle -- Liu, Yitao -- Liu, Lidong -- Besshoh, Shintaro -- Arundine, Mark -- Gurd, James W -- Wang, Yu-Tian -- Salter, Michael W -- Tymianski, Michael -- NS 39060/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):846-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Toronto Western Hospital Research Institute, 11-416 MC-PAV, 399 Bathurst Street, Toronto, Ontario M5T 2S8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399596" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*drug effects/metabolism ; Brain Ischemia/*drug therapy/metabolism ; Calcium/metabolism ; Cells, Cultured ; Cerebral Infarction/*drug therapy/metabolism ; Cyclic GMP/metabolism ; Guanylate Kinase ; In Vitro Techniques ; Intracellular Signaling Peptides and Proteins ; Male ; Membrane Proteins ; Mice ; Mice, Inbred C57BL ; N-Methylaspartate/pharmacology ; Nerve Tissue Proteins/chemistry/*metabolism ; Neurons/drug effects/physiology ; Patch-Clamp Techniques ; Peptides/administration & dosage/*pharmacology/therapeutic use ; Protein Binding ; Rats ; Rats, Sprague-Dawley ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/*chemistry/*metabolism ; Recombinant Fusion Proteins/administration & dosage/pharmacology/therapeutic use ; Signal Transduction ; Synaptic Transmission/drug effects
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    Enzymology. A trio of transition metals in anaerobic CO2 fixation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, John W -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):552-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA. john.peters@chemistry.montana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12386322" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acetyl Coenzyme A/metabolism ; Aldehyde Oxidoreductases/*chemistry/*metabolism ; Anaerobiosis ; Binding Sites ; Biomass ; Carbon Dioxide/*metabolism ; Carbon Monoxide/metabolism ; Clostridium/enzymology ; Copper/*chemistry ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Iron/*chemistry ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Quaternary
    Print ISSN: 0036-8075
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    Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bracey, Michael H -- Hanson, Michael A -- Masuda, Kim R -- Stevens, Raymond C -- Cravatt, Benjamin F -- R01 DA013173/DA/NIDA NIH HHS/ -- R01 DA013173-02/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1793-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Skaggs Institute for Chemical Biology, Scripps Research Institute, 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/12459591" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/antagonists & inhibitors/*chemistry/metabolism ; Animals ; Arachidonic Acids/metabolism ; *Bacterial Proteins ; Binding Sites ; Cannabinoid Receptor Modulators ; Catalysis ; Catalytic Domain ; Cell Membrane/*enzymology ; Crystallography, X-Ray ; Dimerization ; Endocannabinoids ; Helix-Turn-Helix Motifs ; Lipid Bilayers ; Models, Molecular ; Organophosphonates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Recombinant Proteins/chemistry/metabolism ; Signal Transduction ; Solubility
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    A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-19
    Description: A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doukov, Tzanko I -- Iverson, Tina M -- Seravalli, Javier -- Ragsdale, Stephen W -- Drennan, Catherine L -- R01-GM39451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):567-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, 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/12386327" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acetyl Coenzyme A/metabolism ; Aldehyde Oxidoreductases/*chemistry/*metabolism ; Anaerobiosis ; Binding Sites ; Carbon Dioxide/metabolism ; Carbon Monoxide/metabolism ; Catalysis ; Clostridium/*enzymology ; Copper/*chemistry ; Crystallography, X-Ray ; Dimerization ; Electron Spin Resonance Spectroscopy ; Hydrophobic and Hydrophilic Interactions ; Iron/*chemistry ; Ligands ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Zinc/chemistry
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    DNA repair pathway stimulated by the forkhead transcription factor FOXO3a through the Gadd45 protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: The signaling pathway from phosphoinositide 3-kinase to the protein kinase Akt controls organismal life-span in invertebrates and cell survival and proliferation in mammals by inhibiting the activity of members of the FOXO family of transcription factors. We show that mammalian FOXO3a also functions at the G2 to M checkpoint in the cell cycle and triggers the repair of damaged DNA. By gene array analysis, FOXO3a was found to modulate the expression of several genes that regulate the cellular response to stress at the G2-M checkpoint. The growth arrest and DNA damage response gene Gadd45a appeared to be a direct target of FOXO3a that mediates part of FOXO3a's effects on DNA repair. These findings indicate that in mammals FOXO3a regulates the resistance of cells to stress by inducing DNA repair and thereby may also affect organismal life-span.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tran, Hien -- Brunet, Anne -- Grenier, Jill M -- Datta, Sandeep R -- Fornace, Albert J Jr -- DiStefano, Peter S -- Chiang, Lillian W -- Greenberg, Michael E -- NIHP30-HD18655/HD/NICHD NIH HHS/ -- P01-HD24926/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):530-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital and Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964479" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chromones/pharmacology ; DNA Damage ; *DNA Repair ; DNA-Binding Proteins/genetics/*metabolism ; Forkhead Transcription Factors ; G2 Phase ; Gene Expression Profiling ; Gene Expression Regulation ; Genes, Reporter ; Humans ; Intracellular Signaling Peptides and Proteins ; Mitosis ; Morpholines/pharmacology ; Promoter Regions, Genetic ; Proteins/genetics/*metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; Tamoxifen/*analogs & derivatives/pharmacology ; Transcription Factors/genetics/*metabolism ; Transfection ; Ultraviolet Rays
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    Neuroscience. How neurons know that it's c-c-c-c-cold outside (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seydel, Caroline -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1451-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859171" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cold Temperature ; Face/innervation ; Menthol/*metabolism/pharmacology ; Mice ; Neurons, Afferent/*physiology ; Potassium/metabolism ; Potassium Channels/*physiology ; Rats ; Receptors, Drug/*physiology ; Sensation/*physiology ; Thermoreceptors/*physiology
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    Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Huntington's disease (HD) is an inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein. Transcriptional dysregulation has been implicated in HD pathogenesis. Here, we report that huntingtin interacts with the transcriptional activator Sp1 and coactivator TAFII130. Coexpression of Sp1 and TAFII130 in cultured striatal cells from wild-type and HD transgenic mice reverses the transcriptional inhibition of the dopamine D2 receptor gene caused by mutant huntingtin, as well as protects neurons from huntingtin-induced cellular toxicity. Furthermore, soluble mutant huntingtin inhibits Sp1 binding to DNA in postmortem brain tissues of both presymptomatic and affected HD patients. Understanding these early molecular events in HD may provide an opportunity to interfere with the effects of mutant huntingtin before the development of disease symptoms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunah, Anthone W -- Jeong, Hyunkyung -- Griffin, April -- Kim, Yong-Man -- Standaert, David G -- Hersch, Steven M -- Mouradian, M Maral -- Young, Anne B -- Tanese, Naoko -- Krainc, Dimitri -- 5R37AG13617/AG/NIA NIH HHS/ -- AT00613/AT/NCCIH NIH HHS/ -- NS02174/NS/NINDS NIH HHS/ -- NS34361/NS/NINDS NIH HHS/ -- NS35255/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2238-43. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Center for Aging, Genetics and Neurodegeneration, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Caudate Nucleus/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Corpus Striatum/cytology/embryology/metabolism ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Down-Regulation ; Gene Expression Regulation ; Humans ; Huntington Disease/*genetics/metabolism ; Mice ; Mice, Transgenic ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/physiology ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides ; Promoter Regions, Genetic ; Rats ; Receptors, Dopamine D2/genetics ; Solubility ; Sp1 Transcription Factor/chemistry/*metabolism ; *TATA-Binding Protein Associated Factors ; *Transcription Factor TFIID ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; Transfection ; Trinucleotide Repeat Expansion ; Two-Hybrid System Techniques
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    Structural basis for gluten intolerance in celiac sprue (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: Celiac Sprue, a widely prevalent autoimmune disease of the small intestine, is induced in genetically susceptible individuals by exposure to dietary gluten. A 33-mer peptide was identified that has several characteristics suggesting it is the primary initiator of the inflammatory response to gluten in Celiac Sprue patients. In vitro and in vivo studies in rats and humans demonstrated that it is stable toward breakdown by all gastric, pancreatic, and intestinal brush-border membrane proteases. The peptide reacted with tissue transglutaminase, the major autoantigen in Celiac Sprue, with substantially greater selectivity than known natural substrates of this extracellular enzyme. It was a potent inducer of gut-derived human T cell lines from 14 of 14 Celiac Sprue patients. Homologs of this peptide were found in all food grains that are toxic to Celiac Sprue patients but are absent from all nontoxic food grains. The peptide could be detoxified in in vitro and in vivo assays by exposure to a bacterial prolyl endopeptidase, suggesting a strategy for oral peptidase supplement therapy for Celiac Sprue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shan, Lu -- Molberg, Oyvind -- Parrot, Isabelle -- Hausch, Felix -- Filiz, Ferda -- Gray, Gary M -- Sollid, Ludvig M -- Khosla, Chaitan -- R01 DK100619/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2275-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351792" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Celiac Disease/*immunology/therapy ; Cell Line ; Edible Grain/chemistry ; Endopeptidases/metabolism ; Epitopes, T-Lymphocyte ; GTP-Binding Proteins/metabolism ; Gliadin/*chemistry/*immunology/metabolism ; HLA-DQ Antigens/immunology ; Humans ; Immunodominant Epitopes ; Intestinal Mucosa/enzymology/*immunology ; Intestine, Small/enzymology/*immunology ; Lymphocyte Activation ; Microvilli/enzymology ; Molecular Sequence Data ; Peptide Fragments/chemistry/immunology ; Rats ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; Serine Endopeptidases/administration & dosage/metabolism/therapeutic use ; T-Lymphocytes/*immunology ; Transglutaminases/metabolism
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    Transcription. Of chips and ChIPs (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-04-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shannon, M Frances -- Rao, Sudha -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia. frances.shannon@anu.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Cycle ; Chromatin/genetics/*metabolism ; Computational Biology ; DNA/chemistry/genetics/metabolism ; DNA, Fungal/chemistry/genetics/metabolism ; *Gene Expression Profiling ; *Gene Expression Regulation ; Genome ; Oligonucleotide Array Sequence Analysis ; Precipitin Tests ; Promoter Regions, Genetic ; Regulatory Sequences, Nucleic Acid ; Regulon ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Yeasts/genetics
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    Close before opening (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: As bacteria need iron from the environment to survive, they have evolved active iron transporter proteins in their outer membranes. In her Perspective, Postle discusses new insights into iron transport revealed by the crystal structure of the iron transporter FecA in E. coli (Ferguson et al.).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Postle, K -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1658-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Molecular Biosciences, Washington State University, Pullman, WA 99164, USA. postle@mail.wsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872826" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/chemistry/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Biological Transport, Active ; Carrier Proteins/*chemistry/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli/*metabolism ; Escherichia coli Proteins/chemistry/metabolism ; Ferric Compounds/*metabolism ; Ion Channel Gating ; Ligands ; Membrane Proteins/metabolism ; Models, Biological ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; *Receptors, Cell Surface ; Siderophores/metabolism
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    Melanopsin-containing retinal ganglion cells: architecture, projections, and intrinsic photosensitivity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: The primary circadian pacemaker, in the suprachiasmatic nucleus (SCN) of the mammalian brain, is photoentrained by light signals from the eyes through the retinohypothalamic tract. Retinal rod and cone cells are not required for photoentrainment. Recent evidence suggests that the entraining photoreceptors are retinal ganglion cells (RGCs) that project to the SCN. The visual pigment for this photoreceptor may be melanopsin, an opsin-like protein whose coding messenger RNA is found in a subset of mammalian RGCs. By cloning rat melanopsin and generating specific antibodies, we show that melanopsin is present in cell bodies, dendrites, and proximal axonal segments of a subset of rat RGCs. In mice heterozygous for tau-lacZ targeted to the melanopsin gene locus, beta-galactosidase-positive RGC axons projected to the SCN and other brain nuclei involved in circadian photoentrainment or the pupillary light reflex. Rat RGCs that exhibited intrinsic photosensitivity invariably expressed melanopsin. Hence, melanopsin is most likely the visual pigment of phototransducing RGCs that set the circadian clock and initiate other non-image-forming visual functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885915/" 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/PMC2885915/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattar, S -- Liao, H W -- Takao, M -- Berson, D M -- Yau, K W -- R37 EY006837/EY/NEI NIH HHS/ -- R37 EY006837-13/EY/NEI NIH HHS/ -- R37 EY006837-14/EY/NEI NIH HHS/ -- R37 EY006837-15/EY/NEI NIH HHS/ -- R37 EY006837-15S1/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1065-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834834" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/chemistry ; *Biological Clocks ; Brain/*cytology ; Cell Membrane/chemistry ; *Circadian Rhythm ; Cloning, Molecular ; Dendrites/chemistry ; Fluorescent Antibody Technique ; Lac Operon ; *Light ; Mice ; Microscopy, Confocal ; Molecular Sequence Data ; Optic Nerve/cytology ; Rats ; Retinal Ganglion Cells/*chemistry/physiology ; Rod Opsins/*analysis/chemistry/genetics/*physiology ; Suprachiasmatic Nucleus/cytology ; Visual Pathways/cytology ; beta-Galactosidase/analysis
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    Neurobiology. TRK makes the retrograde (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Freda D -- Kaplan, David R -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1471-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Neuronal Survival and Brain Tumor Research Centre, Montreal Neurological Institute, McGill University, 3801 rue University, Montreal, Quebec H3A 2B4, Canada. freda.miller@mcgill.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859179" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*metabolism ; Cell Survival ; Enzyme Activation ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Models, Neurological ; Nerve Growth Factor/*metabolism ; Neurons/metabolism/*physiology ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Transport ; Rats ; Receptor, trkA/*metabolism ; *Signal Transduction ; Transport Vesicles/metabolism
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    Neuroscience. Researchers thrilled with seminal discovery (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-08-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1460-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202793" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ejaculation/*physiology ; Humans ; Lumbosacral Region ; Male ; Neurons/*physiology ; Rats ; Spinal Cord/cytology/*physiology
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    Plant biology. Prime time for cellulose (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Read, Steve M -- Bacic, Tony -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):59-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Resource Management and Forest Science Centre, University of Melbourne, Creswick, Victoria 3363, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778033" target="_blank"〉PubMed〈/a〉
    Keywords: *Arabidopsis Proteins ; Binding Sites ; Carbohydrate Conformation ; Catalysis ; Cell Membrane/metabolism ; Cellulase ; Cellulose/*analogs & derivatives/*biosynthesis/metabolism ; Dextrins/metabolism ; Glucans/biosynthesis/metabolism ; Glucose/metabolism ; Glucosyltransferases/*metabolism ; Gossypium/enzymology/*metabolism ; Membrane Proteins/*metabolism ; Models, Biological ; Organisms, Genetically Modified ; Plants/enzymology/genetics/*metabolism ; Sitosterols/*metabolism ; Uridine Diphosphate Glucose/metabolism ; Yeasts/genetics/metabolism
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    Vitamin D receptor as an intestinal bile acid sensor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The vitamin D receptor (VDR) mediates the effects of the calcemic hormone 1alpha,25-dihydroxyvitamin D3 [1,25(OH)2D3]. We show that VDR also functions as a receptor for the secondary bile acid lithocholic acid (LCA), which is hepatotoxic and a potential enteric carcinogen. VDR is an order of magnitude more sensitive to LCA and its metabolites than are other nuclear receptors. Activation of VDR by LCA or vitamin D induced expression in vivo of CYP3A, a cytochrome P450 enzyme that detoxifies LCA in the liver and intestine. These studies offer a mechanism that may explain the proposed protective effects of vitamin D and its receptor against colon cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makishima, Makoto -- Lu, Timothy T -- Xie, Wen -- Whitfield, G Kerr -- Domoto, Hideharu -- Evans, Ronald M -- Haussler, Mark R -- Mangelsdorf, David J -- New York, N.Y. -- Science. 2002 May 17;296(5571):1313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016314" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Aryl Hydrocarbon Hydroxylases ; Binding, Competitive ; COS Cells ; Cell Line ; Colonic Neoplasms/prevention & control ; Cytochrome P-450 CYP3A ; Cytochrome P-450 Enzyme System/genetics/metabolism ; DNA-Binding Proteins/metabolism ; Dimerization ; Gene Expression Regulation, Enzymologic ; Histone Acetyltransferases ; Humans ; Intestine, Small/*metabolism ; Ligands ; Lithocholic Acid/analogs & derivatives/*metabolism/pharmacology ; Male ; Mice ; Nuclear Receptor Coactivator 1 ; Oxidoreductases, N-Demethylating/genetics/metabolism ; Promoter Regions, Genetic ; Rats ; Receptors, Calcitriol/agonists/genetics/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Steroid/metabolism ; Transcription Factors/metabolism ; Transfection
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    Germline transmission and tissue-specific expression of transgenes delivered by lentiviral vectors (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-12
    Description: Single-cell mouse embryos were infected in vitro with recombinant lentiviral vectors to generate transgenic mice carrying the green fluorescent protein (GFP) gene driven by a ubiquitously expressing promoter. Eighty percent of founder mice carried at least one copy of the transgene, and 90% of these expressed GFP at high levels. Progeny inherited the transgene(s) and displayed green fluorescence. Mice generated using lentiviral vectors with muscle-specific and T lymphocyte-specific promoters expressed high levels of GFP only in the appropriate cell types. We have also generated transgenic rats that express GFP at high levels, suggesting that this technique can be used to produce other transgenic animal species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lois, Carlos -- Hong, Elizabeth J -- Pease, Shirley -- Brown, Eric J -- Baltimore, David -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):868-72. Epub 2002 Jan 10.〈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/11786607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified ; Blotting, Southern ; Blotting, Western ; Cell Lineage ; Crosses, Genetic ; DNA, Recombinant ; Embryo Transfer ; Embryo, Mammalian/*metabolism/virology ; Female ; Gene Dosage ; *Gene Expression ; Gene Silencing ; Genes, Reporter ; *Genetic Vectors ; Green Fluorescent Proteins ; HIV-1/genetics ; Hepatitis B Virus, Woodchuck/genetics ; Lentivirus/*genetics ; Luminescent Proteins/biosynthesis/genetics ; Male ; Mice ; Mice, Transgenic ; Muscle, Skeletal/embryology/metabolism ; Organ Specificity ; Promoter Regions, Genetic ; Proviruses/genetics ; Rats ; *Transgenes ; Virus Integration
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    Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-19
    Description: Protein-protein interactions and calcium entry through the N-methyl-d-aspartate (NMDA)-type glutamate receptor regulate synaptic development and plasticity in the central nervous system. The EphB receptor tyrosine kinases are localized at excitatory synapses where they cluster and associate with NMDA receptors. We identified a mechanism whereby EphBs modulate NMDA receptor function. EphrinB2 activation of EphB in primary cortical neurons potentiates NMDA receptor-dependent influx of calcium. Treatment of cells with ephrinB2 led to NMDA receptor tyrosine phosphorylation through activation of the Src family of tyrosine kinases. These ephrinB2-dependent events result in enhanced NMDA receptor-dependent gene expression. Our findings indicate that ephrinB2 stimulation of EphB modulates the functional consequences of NMDA receptor activation and suggest a mechanism whereby activity-independent and activity-dependent signals converge to regulate the development and remodeling of synaptic connections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takasu, Mari A -- Dalva, Matthew B -- Zigmond, Richard E -- Greenberg, Michael E -- CA43855/CA/NCI NIH HHS/ -- HD18655/HD/NICHD NIH HHS/ -- NS12651/NS/NINDS NIH HHS/ -- NS17512/NS/NINDS NIH HHS/ -- R01 NS045500/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):491-5. Epub 2001 Dec 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, and the Department of Neurobiology, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/pharmacology ; Calcium/*metabolism ; Cell Line ; Cells, Cultured ; Cerebral Cortex/cytology/embryology ; Cyclic AMP Response Element-Binding Protein/metabolism ; Ephrin-B2 ; *Gene Expression Regulation ; Genes, Reporter ; Glutamic Acid/metabolism ; Humans ; Immunoglobulin Fc Fragments ; Membrane Proteins/*metabolism/pharmacology ; Models, Neurological ; Mutation ; Neurons/*metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; Rats ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptor, EphB4 ; Receptors, Eph Family ; Receptors, N-Methyl-D-Aspartate/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism/pharmacology ; Signal Transduction ; Synapses/metabolism ; Transcription, Genetic ; src-Family Kinases/metabolism
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    Identification of a potential ejaculation generator in the spinal cord (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: We tested the significance of a population of lumbar spinothalamic cells for male sexual behavior in rats. These cells are positioned to relay ejaculation-related signals from reproductive organs to the brain, and they express neurokinin-1 receptors. Ablation of these neurons by the selective toxin SSP-saporin resulted in a complete disruption of ejaculatory behavior. In contrast, other components of sexual behavior remained intact. These results suggest that this population of spinothalamic cells plays a pivotal role in generation of ejaculatory behavior and may be part of a spinal ejaculation generator.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Truitt, William A -- Coolen, Lique M -- MH60781/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Neurobiology, and Anatomy, Neuroscience Graduate Program, University of Cincinnati, College of Medicine, Post Office Box 670521, Cincinnati, OH 45267-0521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202834" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ejaculation/*physiology ; Female ; Immunoenzyme Techniques ; Lumbosacral Region ; Male ; Neural Conduction ; Neurons/drug effects/metabolism/*physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, Neurokinin-1/biosynthesis ; Recombinant Fusion Proteins/pharmacology ; Ribosome Inactivating Proteins, Type 1 ; Sexual Behavior, Animal/physiology ; Spinal Cord/anatomy & histology/cytology/*physiology ; Thalamus/cytology/*physiology
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    Methyltransferase recruitment and DNA hypermethylation of target promoters by an oncogenic transcription factor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: DNA methylation of tumor suppressor genes is a frequent mechanism of transcriptional silencing in cancer. The molecular mechanisms underlying the specificity of methylation are unknown. We report here that the leukemia-promoting PML-RAR fusion protein induces gene hypermethylation and silencing by recruiting DNA methyltransferases to target promoters and that hypermethylation contributes to its leukemogenic potential. Retinoic acid treatment induces promoter demethylation, gene reexpression, and reversion of the transformed phenotype. These results establish a mechanistic link between genetic and epigenetic changes during transformation and suggest that hypermethylation contributes to the early steps of carcinogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Di Croce, Luciano -- Raker, Veronica A -- Corsaro, Massimo -- Fazi, Francesco -- Fanelli, Mirco -- Faretta, Mario -- Fuks, Francois -- Lo Coco, Francesco -- Kouzarides, Tony -- Nervi, Clara -- Minucci, Saverio -- Pelicci, Pier Giuseppe -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1079-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, European Institute of Oncology, Milan, Italy. ldicroce@lar.ieo.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834837" target="_blank"〉PubMed〈/a〉
    Keywords: Azacitidine/*analogs & derivatives/pharmacology ; Binding Sites ; Cell Differentiation/drug effects ; Cell Line ; Cell Nucleus/metabolism ; Cell Transformation, Neoplastic ; Cloning, Molecular ; CpG Islands ; DNA (Cytosine-5-)-Methyltransferase/*metabolism ; *DNA Methylation ; Exons ; Gene Expression ; *Gene Silencing ; Histone Deacetylases/metabolism ; Humans ; Leukemia, Promyelocytic, Acute/genetics ; Mutation ; Neoplasm Proteins/*metabolism ; Oncogene Proteins, Fusion/*metabolism ; *Promoter Regions, Genetic ; Receptors, Retinoic Acid/*genetics ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/metabolism ; Tretinoin/pharmacology ; Tumor Cells, Cultured ; Zinc/pharmacology
    Print ISSN: 0036-8075
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    A natural product that lowers cholesterol as an antagonist ligand for FXR (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Extracts of the resin of the guggul tree (Commiphora mukul) lower LDL (low-density lipoprotein) cholesterol levels in humans. The plant sterol guggulsterone [4,17(20)-pregnadiene-3,16-dione] is the active agent in this extract. We show that guggulsterone is a highly efficacious antagonist of the farnesoid X receptor (FXR), a nuclear hormone receptor that is activated by bile acids. Guggulsterone treatment decreases hepatic cholesterol in wild-type mice fed a high-cholesterol diet but is not effective in FXR-null mice. Thus, we propose that inhibition of FXR activation is the basis for the cholesterol-lowering activity of guggulsterone. Other natural products with specific biologic effects may modulate the activity of FXR or other relatively promiscuous nuclear hormone receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urizar, Nancy L -- Liverman, Amy B -- Dodds, D'Nette T -- Silva, Frank Valentin -- Ordentlich, Peter -- Yan, Yingzhuo -- Gonzalez, Frank J -- Heyman, Richard A -- Mangelsdorf, David J -- Moore, David D -- New York, N.Y. -- Science. 2002 May 31;296(5573):1703-6. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Caco-2 Cells ; Carrier Proteins/genetics/metabolism ; Cells, Cultured ; Chenodeoxycholic Acid/pharmacology ; Cholesterol/*metabolism ; Cholesterol, Dietary/administration & dosage ; DNA/metabolism ; DNA-Binding Proteins/*antagonists & inhibitors/chemistry/genetics/*metabolism ; Hepatocytes/metabolism ; Histone Acetyltransferases ; Humans ; *Hydroxysteroid Dehydrogenases ; Hypolipidemic Agents/metabolism/*pharmacology ; Ligands ; Liver/metabolism ; *Membrane Glycoproteins ; Mice ; Nuclear Receptor Coactivator 1 ; Pregnenediones/metabolism/*pharmacology ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear/antagonists & inhibitors/genetics/metabolism ; Receptors, Steroid/antagonists & inhibitors/metabolism ; Transcription Factors/*antagonists & inhibitors/chemistry/genetics/*metabolism ; Transcriptional Activation/drug effects ; Transfection ; Tumor Cells, Cultured
    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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    Genetics. Do X chromosomes set boundaries? (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Percec, Ivona -- Bartolomei, Marisa S -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):287-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. ipercec@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786631" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antisense Elements (Genetics) ; Binding Sites ; DNA Methylation ; DNA-Binding Proteins/genetics/*metabolism ; *Dosage Compensation, Genetic ; Enhancer Elements, Genetic ; Female ; Gene Expression Regulation ; *Gene Silencing ; Humans ; Mice ; Models, Genetic ; RNA, Long Noncoding ; RNA, Untranslated/genetics/metabolism ; *Repressor Proteins ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic ; X Chromosome/*genetics/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Targeting of cyclic AMP degradation to beta 2-adrenergic receptors by beta-arrestins (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: Catecholamines signal through the beta2-adrenergic receptor by promoting production of the second messenger adenosine 3',5'-monophosphate (cAMP). The magnitude of this signal is restricted by desensitization of the receptors through their binding to beta-arrestins and by cAMP degradation by phosphodiesterase (PDE) enzymes. We show that beta-arrestins coordinate both processes by recruiting PDEs to activated beta2-adrenergic receptors in the plasma membrane of mammalian cells. In doing so, the beta-arrestins limit activation of membrane-associated cAMP-activated protein kinase by simultaneously slowing the rate of cAMP production through receptor desensitization and increasing the rate of its degradation at the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perry, Stephen J -- Baillie, George S -- Kohout, Trudy A -- McPhee, Ian -- Magiera, Maria M -- Ang, Kok Long -- Miller, William E -- McLean, Alison J -- Conti, Marco -- Houslay, Miles D -- Lefkowitz, Robert J -- HD20788/HD/NICHD NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):834-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399592" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/genetics/metabolism ; Adrenergic beta-Agonists/pharmacology ; Animals ; Arrestins/genetics/*metabolism ; COS Cells ; Cell Line ; Cell Membrane/metabolism ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Cytosol/metabolism ; Humans ; Isoenzymes/metabolism ; Isoproterenol/pharmacology ; Mice ; Mutation ; Precipitin Tests ; Rats ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif-EX(n)HXHX(10)D. Mutation of the predicted active-site histidines to alanine (rpn11AXA) was lethal and stabilized ubiquitin pathway substrates in yeast. Rpn11(AXA) mutant proteasomes assembled normally but failed to either deubiquitinate or degrade ubiquitinated Sic1 in vitro. Our findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, Rati -- Aravind, L -- Oania, Robert -- McDonald, W Hayes -- Yates, John R 3rd -- Koonin, Eugene V -- Deshaies, Raymond J -- RR11823-05-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):611-5. Epub 2002 Aug 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Howard Hughes Medical Institute, 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/12183636" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Carbon-Nitrogen Lyases/chemistry/*metabolism ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cysteine Endopeptidases/metabolism ; DNA-Binding Proteins/chemistry ; Endopeptidases/chemistry/*metabolism ; Fungal Proteins/*metabolism ; Metalloendopeptidases/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; Mutation ; Oligopeptides/pharmacology ; Peptide Hydrolases/*metabolism ; Proteasome Endopeptidase Complex ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Transcription Factors/chemistry ; Ubiquitins/*metabolism ; Yeasts/metabolism ; Zinc/metabolism
    Print ISSN: 0036-8075
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    Signaling of rat Frizzled-2 through phosphodiesterase and cyclic GMP (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: The Frizzled-2 receptor (Rfz2) from rat binds Wnt proteins and can signal by activating calcium release from intracellular stores. We show that wild-type Rfz2 and a chimeric receptor consisting of the extracellular and transmembrane portions of the beta2-adrenergic receptor with cytoplasmic domains of Rfz2 also signaled through modulation of cyclic guanosine 3',5'-monophosphate (cGMP). Activation of either receptor led to a decline in the intracellular concentration of cGMP, a process that was inhibited in cells treated with pertussis toxin, reduced by suppression of the expression of the heterotrimeric GTP-binding protein (G protein) transducin, and suppressed through inhibition of cGMP-specific phosphodiesterase (PDE) activity. Moreover, PDE inhibitors blocked Rfz2-induced calcium transients in zebrafish embryos. Thus, Frizzled-2 appears to couple to PDEs and calcium transients through G proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahumada, Adriana -- Slusarski, Diane C -- Liu, Xunxian -- Moon, Randall T -- Malbon, Craig C -- Wang, Hsien-yu -- T32-DK07521/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):2006-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Diabetes and Metabolic Diseases Research Center, University Medical Center, SUNY-Stony Brook, Stony Brook, NY 11794-8651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471263" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Calcium/metabolism ; Cricetinae ; Culture Media, Conditioned ; Cyclic GMP/*metabolism ; Embryo, Nonmammalian/metabolism ; Frizzled Receptors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Molecular Sequence Data ; Pertussis Toxin/pharmacology ; Phosphodiesterase Inhibitors/pharmacology ; Phosphoric Diester Hydrolases/*metabolism ; Rats ; Receptors, Adrenergic, beta-2/chemistry/metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; *Signal Transduction ; Transducin/genetics/metabolism ; Transfection ; Tumor Cells, Cultured ; Zebrafish
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    Myelin-associated glycoprotein as a functional ligand for the Nogo-66 receptor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-29
    Description: Axonal regeneration in the adult central nervous system (CNS) is limited by two proteins in myelin, Nogo and myelin-associated glycoprotein (MAG). The receptor for Nogo (NgR) has been identified as an axonal glycosyl-phosphatidyl-inositol (GPI)-anchored protein, whereas the MAG receptor has remained elusive. Here, we show that MAG binds directly, with high affinity, to NgR. Cleavage of GPI-linked proteins from axons protects growth cones from MAG-induced collapse, and dominant-negative NgR eliminates MAG inhibition of neurite outgrowth. MAG-resistant embryonic neurons are rendered MAG-sensitive by expression of NgR. MAG and Nogo-66 activate NgR independently and serve as redundant NgR ligands that may limit axonal regeneration after CNS injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Betty P -- Fournier, Alyson -- GrandPre, Tadzia -- Strittmatter, Stephen M -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1190-3. Epub 2002 Jun 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Section of Neurobiology, 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/12089450" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Binding Sites ; COS Cells ; Chick Embryo ; Cloning, Molecular ; GPI-Linked Proteins ; Ganglia, Spinal/cytology/embryology/metabolism ; Gene Library ; Ligands ; Mice ; Myelin Proteins/chemistry/metabolism/pharmacology ; Myelin-Associated Glycoprotein/chemistry/genetics/*metabolism ; Nerve Regeneration ; Neurites/*physiology ; Neurons/metabolism ; Peptide Fragments/metabolism/pharmacology ; Phosphatidylinositol Diacylglycerol-Lyase ; Protein Structure, Tertiary ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Sialic Acids/metabolism ; Transfection ; Type C Phospholipases/metabolism
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    Drug delivery. Breaching the membrane (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, Joe -- New York, N.Y. -- Science. 2002 May 3;296(5569):838-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988555" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Membrane/*metabolism ; Cell Membrane Permeability ; Chemistry, Pharmaceutical ; DNA/administration & dosage/pharmacokinetics ; *Drug Carriers ; *Drug Delivery Systems ; Liposomes ; Membrane Fusion ; Membrane Transport Proteins/chemistry/*metabolism ; Nanotechnology ; Prodrugs/administration & dosage/pharmacokinetics ; *Technology, Pharmaceutical
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    Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-06
    Description: The vibrational dynamics of the retinal chromophore all-trans-to-13-cis photoisomerization in bacteriorhodopsin has been studied with mid-infrared absorption spectroscopy at high time resolution (about 200 femtoseconds). After photoexcitation of light-adapted bacteriorhodopsin, the transient infrared absorption was probed in a broad spectral region, including vibrations with dominant C-C, C=C, and C=NH stretching mode amplitude. All photoproduct modes, especially those around 1190 reciprocal-centimeters that are indicative for a 13-cis configuration of the chromophore, rise with a time constant of approximately 0.5 picosecond. The results presented give direct vibrational-spectroscopic evidence for the isomerization taking place within 0.5 picosecond, as has been suggested by previous optical femtosecond time-resolved experiments but questioned recently by picosecond time-resolved vibrational spectroscopy experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herbst, Johannes -- Heyne, Karsten -- Diller, Rolf -- New York, N.Y. -- Science. 2002 Aug 2;297(5582):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Experimentalphysik, Freie Universitat Berlin, Arnimallee 14, 14195 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12161649" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/*chemistry/*metabolism ; Binding Sites ; Isomerism ; Kinetics ; Light ; Photochemistry ; Retinaldehyde/*chemistry/*metabolism ; Spectrophotometry, Infrared/*methods ; Spectroscopy, Fourier Transform Infrared ; Time Factors ; Vibration
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    Oscillatory expression of the bHLH factor Hes1 regulated by a negative feedback loop (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: Transcription of messenger RNAs (mRNAs) for Notch signaling molecules oscillates with 2-hour cycles, and this oscillation is important for coordinated somite segmentation. However, the molecular mechanism of such oscillation remains to be determined. Here, we show that serum treatment of cultured cells induces cyclic expression of both mRNA and protein of the Notch effector Hes1, a basic helix-loop-helix (bHLH) factor, with 2-hour periodicity. Cycling is cell-autonomous and depends on negative autoregulation of hes1 transcription and ubiquitin-proteasome-mediated degradation of Hes1 protein. Because Hes1 oscillation can be seen in many cell types, this clock may regulate timing in many biological systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirata, Hiromi -- Yoshiura, Shigeki -- Ohtsuka, Toshiyuki -- Bessho, Yasumasa -- Harada, Takahiro -- Yoshikawa, Kenichi -- Kageyama, Ryoichiro -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):840-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399594" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/*analogs & derivatives/pharmacology ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks ; Blood ; Cell Line ; Cycloheximide/pharmacology ; Cysteine Endopeptidases/metabolism ; Feedback, Physiological ; Gene Expression Regulation ; Glycosyltransferases/genetics/metabolism ; Half-Life ; Homeodomain Proteins/biosynthesis/*genetics/*metabolism ; Leupeptins/pharmacology ; Mesoderm/metabolism ; Mice ; Multienzyme Complexes/metabolism ; PC12 Cells ; *Periodicity ; Protease Inhibitors/pharmacology ; Proteasome Endopeptidase Complex ; Protein Biosynthesis ; Protein Synthesis Inhibitors/pharmacology ; RNA, Messenger/biosynthesis/genetics/metabolism ; Rats ; Transcription, Genetic ; Transfection ; Ubiquitin/metabolism
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  • 85
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    Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-21
    Description: The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunt, John F -- Weinkauf, Sevil -- Henry, Lisa -- Fak, John J -- McNicholas, Paul -- Oliver, Donald B -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2018-26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, 702A Fairchild Center, MC2434, Columbia University, New York, NY 10027, USA. hunt@sid.bio.columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242434" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/chemistry/*metabolism ; Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/chemistry/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacillus subtilis/*enzymology ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA Helicases/chemistry ; DNA, Bacterial/chemistry/metabolism ; DNA, Single-Stranded/chemistry/metabolism ; Dimerization ; Escherichia coli ; Escherichia coli Proteins/*chemistry/*metabolism ; Eukaryotic Initiation Factor-4A ; Fluorescence Polarization ; Fourier Analysis ; Hydrogen Bonding ; Ligands ; Membrane Transport Proteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptide Initiation Factors/chemistry ; Peptides/chemistry ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Precursors/metabolism ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Temperature
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    Dependence of EPSP efficacy on synapse location in neocortical pyramidal neurons (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Neurons receive thousands of synaptic inputs throughout elaborate dendritic trees. Here we determine the somatic impact of excitatory postsynaptic potentials (EPSPs) generated at known dendritic sites in neocortical pyramidal neurons. As inputs became more distal, somatic EPSP amplitude decreased, whereas use-dependent depression increased. Despite marked attenuation (〉40-fold), when coactivated within a narrow time window (approximately 10 milliseconds), distal EPSPs could directly influence action potential output following dendritic spike generation. These findings reveal that distal EPSPs are ineffective sources of background somatic excitation, but through coincidence detection have a powerful transient signaling role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, Stephen R -- Stuart, Greg J -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1907-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, John Curtin School of Medical Research, Australian National University, Canberra, ACT 0200, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884759" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Axons/physiology ; Dendrites/*physiology ; *Excitatory Postsynaptic Potentials ; Neocortex/cytology/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology ; Rats ; Rats, Wistar ; Synapses/*physiology ; Synaptic Transmission
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    Functional materials based on self-assembly of polymeric supramolecules (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-30
    Description: Self-assembly of polymeric supramolecules is a powerful tool for producing functional materials that combine several properties and may respond to external conditions. We illustrate the concept using a comb-shaped architecture. Examples include the hexagonal self-organization of conjugated conducting polymers and the polarized luminance in solid-state films of rodlike polymers obtained by removing the hydrogen-bonded side chains from the aligned thermotropic smectic phase. Hierarchically structured materials obtained by applying different self-organization and recognition principles and directed assembly form a basis for tunable nanoporous materials, smart membranes, preparation of nano-objects, and anisotropic properties, such as proton conductivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ikkala, Olli -- ten Brinke, Gerrit -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2407-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Engineering Physics and Mathematics and Center for New Materials, Helsinki University of Technology, Post Office Box 2200, FIN-02015 HUT, Espoo, Finland. Olli.Ikkala@hut.fi〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923526" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chemistry, Physical ; DNA/chemistry ; Hydrogen Bonding ; Molecular Conformation ; Molecular Structure ; Nanotechnology ; Physicochemical Phenomena ; Polymers/*chemical synthesis/*chemistry
    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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    Biochemistry. DNA building block reinvented (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murzin, Alexey G -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):61-2. Epub 2002 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, UK. agm@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029066" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/enzymology ; Binding Sites ; Crystallography, X-Ray ; Deoxyuracil Nucleotides/metabolism ; Drug Design ; Enzyme Inhibitors ; Evolution, Molecular ; Flavin-Adenine Dinucleotide/metabolism ; Helicobacter pylori/*enzymology ; Humans ; Methyltransferases/chemistry/metabolism ; Models, Molecular ; Phylogeny ; Protein Conformation ; Protein Structure, Tertiary ; Protozoan Proteins/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Tetrahydrofolates/metabolism ; Thermotoga maritima/*enzymology ; Thymidine Monophosphate/*biosynthesis ; Thymidylate Synthase/antagonists & inhibitors/*chemistry/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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  • 89
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    Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: Cells have evolved multiple mechanisms to inhibit viral replication. To identify previously unknown antiviral activities, we screened mammalian complementary DNA (cDNA) libraries for genes that prevent infection by a genetically marked retrovirus. Virus-resistant cells were selected from pools of transduced clones, and an active antiviral cDNA was recovered. The gene encodes a CCCH-type zinc finger protein designated ZAP. Expression of the gene caused a profound and specific loss of viral messenger RNAs (mRNAs) from the cytoplasm without affecting the levels of nuclear mRNAs. The finding suggests the existence of a previously unknown machinery for the inhibition of virus replication, targeting a step in viral gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Guangxia -- Guo, Xuemin -- Goff, Stephen P -- CA 30488/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1703-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, 701 West 168th Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/chemistry/*genetics/isolation & purification/physiology ; Carrier Proteins/chemistry/*genetics/isolation & purification/physiology ; Cell Line ; Cloning, Molecular ; Gene Library ; Genetic Vectors/genetics ; Open Reading Frames ; Polymerase Chain Reaction ; RNA, Viral/*biosynthesis ; Rats ; Retroviridae/*genetics/immunology ; Tissue Distribution ; Virus Replication ; *Zinc Fingers
    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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  • 90
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    The neurotrophin receptor p75NTR as a positive modulator of myelination (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: Schwann cells in developing and regenerating peripheral nerves express elevated levels of the neurotrophin receptor p75NTR. Neurotrophins are key mediators of peripheral nervous system myelination. Our results show that myelin formation is inhibited in the absence of functional p75NTR and enhanced by blocking TrkC activity. Moreover, the enhancement of myelin formation by endogenous brain-derived neurotrophic factor is mediated by the p75NTR receptor, whereas TrkC receptors are responsible for neurotrophin-3 inhibition. Thus p75NTR and TrkC receptors have opposite effects on myelination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cosgaya, Jose M -- Chan, Jonah R -- Shooter, Eric M -- NS04270/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, 299 Campus Drive, Fairchild Building, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424382" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/immunology ; Axons/physiology ; Brain-Derived Neurotrophic Factor/pharmacology/physiology ; Coculture Techniques ; Ganglia, Spinal/cytology ; Immunohistochemistry ; Mice ; Models, Neurological ; Myelin P0 Protein/metabolism ; Myelin Sheath/*physiology ; Myelin-Associated Glycoprotein/metabolism ; Neurotrophin 3/pharmacology/physiology ; Rats ; Rats, Sprague-Dawley ; Receptor, Nerve Growth Factor ; Receptor, trkB/metabolism ; Receptor, trkC/metabolism ; Receptors, Nerve Growth Factor/immunology/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Schwann Cells/*physiology ; Sciatic Nerve/cytology/metabolism ; Signal Transduction
    Print ISSN: 0036-8075
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  • 91
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    Neuroscience. It takes more than two to Nogo (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woolf, Clifford J -- Bloechlinger, Stefan -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1132-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neural Plasticity Research Group, Department of Anesthesia, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02129, USA. woolf.clifford@mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183616" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/metabolism ; Axons/*physiology ; Binding Sites ; Binding, Competitive ; Central Nervous System/physiology ; GPI-Linked Proteins ; Gangliosides/metabolism ; Growth Cones/physiology ; Models, Neurological ; Myelin Proteins/chemistry/*metabolism/pharmacology ; Myelin-Associated Glycoprotein/chemistry/genetics/*metabolism/pharmacology ; Myelin-Oligodendrocyte Glycoprotein ; Nerve Regeneration ; Neurons/*physiology ; Oligodendroglia/metabolism ; Peptide Fragments/metabolism/pharmacology ; Protein Structure, Tertiary ; Receptor, Nerve Growth Factor ; Receptors, Cell Surface/*metabolism ; Receptors, Nerve Growth Factor/metabolism ; Signal Transduction ; Spinal Cord Injuries/physiopathology ; rho GTP-Binding Proteins/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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  • 92
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    Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: The DJ-1 gene encodes a ubiquitous, highly conserved protein. Here, we show that DJ-1 mutations are associated with PARK7, a monogenic form of human parkinsonism. The function of the DJ-1 protein remains unknown, but evidence suggests its involvement in the oxidative stress response. Our findings indicate that loss of DJ-1 function leads to neurodegeneration. Elucidating the physiological role of DJ-1 protein may promote understanding of the mechanisms of brain neuronal maintenance and pathogenesis of Parkinson's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonifati, Vincenzo -- Rizzu, Patrizia -- van Baren, Marijke J -- Schaap, Onno -- Breedveld, Guido J -- Krieger, Elmar -- Dekker, Marieke C J -- Squitieri, Ferdinando -- Ibanez, Pablo -- Joosse, Marijke -- van Dongen, Jeroen W -- Vanacore, Nicola -- van Swieten, John C -- Brice, Alexis -- Meco, Giuseppe -- van Duijn, Cornelia M -- Oostra, Ben A -- Heutink, Peter -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):256-9. Epub 2002 Nov 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetic-Epidemiologic Unit, Department of Clinical Genetics, Department of Epidemiology and Biostatistics, Erasmus Medical Center Rotterdam, Post Office Box 1738, 3000 DR Rotterdam, Netherlands. bonifati@kgen.fgg.eur.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446870" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Base Sequence ; Brain/metabolism ; COS Cells ; Cell Nucleus/metabolism ; Chromosomes, Human, Pair 1 ; Cloning, Molecular ; Cytoplasm/metabolism ; DNA, Complementary ; Exons ; Genes, Recessive ; Humans ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; *Mutation ; Oncogene Proteins/chemistry/*genetics/metabolism ; Oxidative Stress ; PC12 Cells ; Parkinsonian Disorders/*genetics/metabolism ; Pedigree ; Physical Chromosome Mapping ; Point Mutation ; Protein Structure, Secondary ; Rats ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Deletion ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Identification of signal peptide peptidase, a presenilin-type aspartic protease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. In humans, SPP activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. We have identified human SPP as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. SPP and potential eukaryotic homologs may represent another family of aspartic proteases that promote intramembrane proteolysis to release biologically important peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weihofen, Andreas -- Binns, Kathleen -- Lemberg, Marius K -- Ashman, Keith -- Martoglio, Bruno -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2215-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), ETH-Hoenggerberg, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077416" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Amyloid Precursor Protein Secretases ; Animals ; Aspartic Acid Endopeptidases/*chemistry/genetics/isolation & ; purification/*metabolism ; Azirines/chemical synthesis/pharmacology ; Binding Sites ; Biotin/analogs & derivatives/chemical synthesis/pharmacology ; Cloning, Molecular ; Conserved Sequence ; Endopeptidases/metabolism ; Endoplasmic Reticulum/enzymology ; Glycosylation ; Humans ; Membrane Proteins/*chemistry/genetics/isolation & purification/*metabolism ; Molecular Sequence Data ; Mutation ; Presenilin-1 ; Presenilin-2 ; Protease Inhibitors/chemical synthesis/pharmacology ; Recombinant Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/genetics ; Sequence Alignment ; Sequence Homology, Amino Acid
    Print ISSN: 0036-8075
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    Biomineralization. At the cutting edge (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiner, Steve -- Addadi, Lia -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):375-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. steve.weiner@weizmann.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12376692" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Biomechanical Phenomena ; Chlorides/*analysis/chemistry/metabolism ; Copper/*analysis/chemistry/metabolism ; Hardness ; Humans ; Minerals/*analysis/metabolism ; Polychaeta/anatomy & histology/*chemistry/physiology ; Proteins/chemistry/metabolism ; Tooth/chemistry/physiology ; Vertebrates/anatomy & histology/physiology
    Print ISSN: 0036-8075
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  • 95
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    Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Genetic determinants of longevity include the forkhead-related transcription factor DAF-16 in the worm Caenorhabditis elegans and the p66shc locus in mice. We demonstrate that p66shc regulates intracellular oxidant levels in mammalian cells and that hydrogen peroxide can negatively regulate forkhead activity. In p66shc-/- cells, the activity of the mammalian forkhead homolog FKHRL1 is increased and redox-dependent forkhead inactivation is reduced. In addition, expression of FKHRL1 results in an increase in both hydrogen peroxide scavenging and oxidative stress resistance. These results demonstrate an important functional relation between three distinct elements linked to aging: forkhead proteins, p66shc, and intracellular oxidants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemoto, Shino -- Finkel, Toren -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2450-2. Epub 2002 Mar 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Branch, National Heart, Lung and Blood Institute, National Institutes of Health, Building 10/6N-240, 10 Center Drive, Bethesda, MD 20892-1622, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884717" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/pharmacology ; *Adaptor Proteins, Signal Transducing ; *Adaptor Proteins, Vesicular Transport ; Animals ; Azoles/pharmacology ; Blood ; Cells, Cultured ; Culture Media ; DNA-Binding Proteins/genetics/*metabolism ; Forkhead Transcription Factors ; Free Radical Scavengers/pharmacology ; Humans ; Hydrogen Peroxide/metabolism/pharmacology ; Mice ; Mutation ; Organoselenium Compounds/pharmacology ; Oxidation-Reduction ; Oxidative Stress ; PC12 Cells ; Phosphorylation ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Reactive Oxygen Species/metabolism ; Shc Signaling Adaptor Proteins ; *Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transfection
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    Structural basis of gating by the outer membrane transporter FecA (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Andrew D -- Chakraborty, Ranjan -- Smith, Barbara S -- Esser, Lothar -- van der Helm, Dick -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1715-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872840" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Bacterial Outer Membrane Proteins/chemistry/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Biological Transport, Active ; Carrier Proteins/*chemistry/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli Proteins/chemistry/metabolism ; Ferric Compounds/*metabolism ; Hydrogen Bonding ; *Ion Channel Gating ; Ligands ; Membrane Proteins/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Receptors, Cell Surface ; Siderophores/*metabolism ; Static Electricity
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    Identification of a DNA nonhomologous end-joining complex in bacteria (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: In eukaryotic cells, double-strand breaks (DSBs) in DNA are generally repaired by the pathway of homologous recombination or by DNA nonhomologous end joining (NHEJ). Both pathways have been highly conserved throughout eukaryotic evolution, but no equivalent NHEJ system has been identified in prokaryotes. The NHEJ pathway requires a DNA end-binding component called Ku. We have identified bacterial Ku homologs and show that these proteins retain the biochemical characteristics of the eukaryotic Ku heterodimer. Furthermore, we show that bacterial Ku specifically recruits DNA ligase to DNA ends and stimulates DNA ligation. Loss of these proteins leads to hypersensitivity to ionizing radiation in Bacillus subtilis. These data provide evidence that many bacteria possess a DNA DSB repair apparatus that shares many features with the NHEJ system of eukarya and suggest that this DNA repair pathway arose before the prokaryotic and eukaryotic lineages diverged.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weller, Geoffrey R -- Kysela, Boris -- Roy, Rajat -- Tonkin, Louise M -- Scanlan, Elizabeth -- Della, Marina -- Devine, Susanne Krogh -- Day, Jonathan P -- Wilkinson, Adam -- d'Adda di Fagagna, Fabrizio -- Devine, Kevin M -- Bowater, Richard P -- Jeggo, Penny A -- Jackson, Stephen P -- Doherty, Aidan J -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1686-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Institute for Medical Research & Department of Haematology, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215643" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Nuclear ; Bacillus subtilis/*genetics ; Bacterial Proteins/metabolism ; Binding Sites ; DNA Damage ; *DNA Helicases ; DNA Ligases/*metabolism ; *DNA Repair ; DNA, Bacterial/*biosynthesis/metabolism ; DNA-Binding Proteins/metabolism ; Mutation ; Nuclear Proteins/metabolism ; Protein Binding
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    Stem cells. Plasticity: time for a reappraisal? (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2126-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow Cells/cytology/physiology ; Brain/cytology ; *Cell Differentiation ; *Cell Fusion ; Cell Separation ; Cells, Cultured ; Coculture Techniques ; Embryo, Mammalian/cytology ; Female ; Hematopoietic Stem Cells/physiology ; Humans ; Hybrid Cells/physiology ; Male ; Mesoderm/cytology ; Mice ; Neurons/physiology ; Rats ; Stem Cells/cytology/*physiology
    Print ISSN: 0036-8075
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    Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: Recently, we showed that antibodies catalyze the generation of hydrogen peroxide (H2O2) from singlet molecular oxygen (1O2*) and water. Here, we show that this process can lead to efficient killing of bacteria, regardless of the antigen specificity of the antibody. H2O2 production by antibodies alone was found to be not sufficient for bacterial killing. Our studies suggested that the antibody-catalyzed water-oxidation pathway produced an additional molecular species with a chemical signature similar to that of ozone. This species is also generated during the oxidative burst of activated human neutrophils and during inflammation. These observations suggest that alternative pathways may exist for biological killing of bacteria that are mediated by potent oxidants previously unknown to biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wentworth, Paul Jr -- McDunn, Jonathan E -- Wentworth, Anita D -- Takeuchi, Cindy -- Nieva, Jorge -- Jones, Teresa -- Bautista, Cristina -- Ruedi, Julie M -- Gutierrez, Abel -- Janda, Kim D -- Babior, Bernard M -- Eschenmoser, Albert -- Lerner, Richard A -- 5T32AI07606/AI/NIAID NIH HHS/ -- GM43858/GM/NIGMS NIH HHS/ -- P01CA27489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2195-9. Epub 2002 Nov 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, The Scripps Research Institute, 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/12434011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/immunology/*metabolism ; Arthus Reaction/*immunology/metabolism ; Blood Bactericidal Activity ; Catalase/metabolism ; Catalysis ; Escherichia coli/*immunology ; Hematoporphyrins/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Indigo Carmine/metabolism ; Inflammation/*immunology/metabolism ; Mice ; Neutrophil Activation ; Neutrophils/immunology/*metabolism ; Oxidation-Reduction ; Ozone/*metabolism ; Rabbits ; Rats ; Rats, Sprague-Dawley ; Respiratory Burst ; Singlet Oxygen/metabolism ; Ultraviolet Rays ; Water/metabolism
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    Signal transduction. MAP kinase signaling specificity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weston, Claire R -- Lambright, David G -- Davis, Roger J -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2345-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089430" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; MAP Kinase Kinase 3 ; *MAP Kinase Signaling System ; MEF2 Transcription Factors ; Mitogen-Activated Protein Kinase Kinases/chemistry/*metabolism ; Mitogen-Activated Protein Kinases/*chemistry/*metabolism ; Models, Molecular ; Myogenic Regulatory Factors ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/chemistry/*metabolism ; Transcription Factors/chemistry/*metabolism ; 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
    Published by American Association for the Advancement of Science (AAAS)
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