ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Rats  (65)
  • Models, Molecular  (62)
  • American Association for the Advancement of Science (AAAS)  (126)
  • Springer  (1)
  • American Institute of Physics (AIP)
  • 2015-2019
  • 1995-1999  (127)
  • 1998  (127)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (126)
  • Springer  (1)
  • American Institute of Physics (AIP)
Years
  • 2015-2019
  • 1995-1999  (127)
Year
  • 101
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):389.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381140" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Enzyme Induction ; Enzyme Inhibitors/metabolism ; Heme/chemistry/metabolism ; Humans ; Isoenzymes/antagonists & inhibitors/*chemistry/metabolism ; Models, Molecular ; Nitric Oxide/biosynthesis/physiology ; Nitric Oxide Synthase/antagonists & inhibitors/*chemistry/metabolism ; *Protein Conformation ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 102
    Publication Date: 1998-02-12
    Description: Structural and mechanistic studies show that when the selection criteria of the immune system are changed, catalytic antibodies that have the efficiency of natural enzymes evolve, but the catalytic antibodies are much more accepting of a wide range of substrates. The catalytic antibodies were prepared by reactive immunization, a process whereby the selection criteria of the immune system are changed from simple binding to chemical reactivity. This process yielded aldolase catalytic antibodies that approximated the rate acceleration of the natural enzyme used in glycolysis. Unlike the natural enzyme, however, the antibody aldolases catalyzed a variety of aldol reactions and decarboxylations. The crystal structure of one of these antibodies identified the reactive lysine residue that was selected in the immunization process. This lysine is deeply buried in a hydrophobic pocket at the base of the binding site, thereby accounting for its perturbed pKa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barbas, C F 3rd -- Heine, A -- Zhong, G -- Hoffmann, T -- Gramatikova, S -- Bjornestedt, R -- List, B -- Anderson, J -- Stura, E A -- Wilson, I A -- Lerner, R A -- CA27489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2085-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Skaggs Institute for Chemical Biology and the Department of Molecular Biology, 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/9405338" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/chemistry/immunology/*metabolism ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Decarboxylation ; *Evolution, Molecular ; Fructose-Bisphosphate Aldolase/chemistry/immunology/*metabolism ; Glycolysis ; Hydrogen-Ion Concentration ; Immunization ; Immunoglobulin Fab Fragments/chemistry/immunology/*metabolism ; Kinetics ; Lysine/chemistry/metabolism ; Mice ; Models, Molecular ; Protein Conformation ; Pyridoxal/metabolism ; Selection, Genetic ; Substrate Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 103
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-07
    Description: Molecules with self-complementary surfaces interact through weak intermolecular forces to form assemblies, and the assembled states frequently exhibit distinctive properties. Described here are systems in which symmetrical molecules assemble through hydrogen bonding to produce capsules with dissymmetric cavities. The capsules form and dissipate on a time scale that permits their direct observation by nuclear magnetic resonance measurements, and they act as hosts for smaller molecular guests. Molecular recognition of chiral guests, such as naturally occurring terpenes, determines which dissymmetric cavities are preferentially formed in the assembly process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivera, J M -- Martin, T -- Rebek, J Jr -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1021-3.〈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/9461432" target="_blank"〉PubMed〈/a〉
    Keywords: Bicyclo Compounds, Heterocyclic/*chemistry ; Chemistry, Physical ; Dimerization ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Chemical ; Models, Molecular ; Physicochemical Phenomena ; *Stereoisomerism ; Succinimides/*chemistry ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 104
    Publication Date: 1998-06-06
    Description: RasGRP, a guanyl nucleotide-releasing protein for the small guanosine triphosphatase Ras, was characterized. Besides the catalytic domain, RasGRP has an atypical pair of "EF hands" that bind calcium and a diacylglycerol (DAG)-binding domain. RasGRP activated Ras and caused transformation in fibroblasts. A DAG analog caused sustained activation of Ras-Erk signaling and changes in cell morphology. Signaling was associated with partitioning of RasGRP protein into the membrane fraction. Sustained ligand-induced signaling and membrane partitioning were absent when the DAG-binding domain was deleted. RasGRP is expressed in the nervous system, where it may couple changes in DAG and possibly calcium concentrations to Ras activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebinu, J O -- Bottorff, D A -- Chan, E Y -- Stang, S L -- Dunn, R J -- Stone, J C -- New York, N.Y. -- Science. 1998 May 15;280(5366):1082-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, 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/9582122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*metabolism ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Catalysis ; Cell Cycle Proteins/genetics/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Size ; Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA, Complementary ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Diglycerides/metabolism ; Genes, ras ; *Guanine Nucleotide Exchange Factors ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Molecular Sequence Data ; Neurons/metabolism ; Phosphoprotein Phosphatases/genetics/metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; ras Proteins/*metabolism ; ras-GRF1
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 105
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 1998 Jan 9;279(5348):174.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9446221" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Alzheimer Disease/*genetics/metabolism ; Amyloid beta-Protein Precursor/analysis/biosynthesis/*genetics ; Animals ; Brain/*metabolism ; Brain Chemistry ; Down Syndrome/genetics/metabolism ; Frameshift Mutation ; Humans ; RNA, Messenger/genetics ; Rabbits ; Rats ; Sequence Deletion ; Ubiquitins/analysis/biosynthesis/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 106
    Publication Date: 1998-09-11
    Description: Streptokinase is a plasminogen activator widely used in treating blood-clotting disorders. Complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolves blood clots. A similar binding activation mechanism also occurs in some key steps of blood coagulation. The crystal structure of streptokinase complexed with the catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal domain of streptokinase in the complex is hypothesized to enhance the substrate recognition. The carboxyl-terminal domain of streptokinase, which binds near the activation loop of plasminogen, is likely responsible for the contact activation of plasminogen in the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, X -- Lin, X -- Loy, J A -- Tang, J -- Zhang, X C -- HL 60626/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1662-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crystallography Program, Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, OK 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733510" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; Fibrinolysin/*chemistry/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Streptokinase/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 107
    Publication Date: 1998-02-07
    Description: Dynamin guanosine triphosphatases support the scission of clathrin-coated vesicles from the plasmalemma during endocytosis. By fluorescence microscopy of cultured rat hepatocytes, a green fluorescent protein-dynamin II fusion protein localized with clathrin-coated vesicles at the Golgi complex. A cell-free assay was utilized to demonstrate the role of dynamin in vesicle formation at the trans-Golgi. Addition of peptide-specific anti-dynamin antibodies to the assay mixture inhibited both constitutive exocytic and clathrin-coated vesicle formation. Immunodepletion of dynamin proteins also inhibited vesicle formation, and budding efficiency was restored upon readdition of purified dynamin. These data suggest that dynamin participates in the formation of distinct transport vesicles from the trans-Golgi network.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, S M -- Howell, K E -- Henley, J R -- Cao, H -- McNiven, M A -- P30 CA-46934/CA/NCI NIH HHS/ -- P30 DK-34914/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):573-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Research in Digestive Diseases, Mayo Clinic and Foundation, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438853" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Biological Transport ; Cell Membrane/chemistry ; Cells, Cultured ; Clathrin/analysis ; Coated Vesicles/chemistry/*metabolism/ultrastructure ; Cytosol/metabolism ; Dynamins ; GTP Phosphohydrolases/analysis/immunology/*metabolism ; Golgi Apparatus/chemistry/*metabolism ; Green Fluorescent Proteins ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Liver/ultrastructure ; Luminescent Proteins ; Microscopy, Fluorescence ; Organelles/chemistry/*metabolism/ultrastructure ; Rats ; Recombinant Fusion Proteins/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 108
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-10-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kestenbaum, D -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9786790" target="_blank"〉PubMed〈/a〉
    Keywords: *Algorithms ; *Crystallography, X-Ray ; Models, Molecular ; *Protein Conformation ; Selenomethionine
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 109
    Publication Date: 1998-12-04
    Description: Cortical neurons communicate with various cortical and subcortical targets by way of stereotyped axon projections through the white matter. Slice overlay experiments indicate that the initial growth of cortical axons toward the white matter is regulated by a diffusible chemorepulsive signal localized near the marginal zone. Semaphorin III is a major component of this diffusible signal, and cortical neurons transduce this signal by way of the neuropilin-1 receptor. These observations indicate that semaphorin-neuropilin interactions play a critical role in the initial patterning of projections in the developing cortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Polleux, F -- Giger, R J -- Ginty, D D -- Kolodkin, A L -- Ghosh, A -- NS35165/NS/NINDS NIH HHS/ -- NS36176/NS/NINDS NIH HHS/ -- NS534814/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 4;282(5395):1904-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9836643" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Cell Line ; Cerebral Cortex/*cytology/embryology ; Coculture Techniques ; Gene Targeting ; Glycoproteins/genetics/*physiology ; Humans ; Mice ; Nerve Growth Factors/*metabolism ; Nerve Tissue Proteins/*physiology ; Neurons, Efferent/cytology/*physiology ; Neuropilin-1 ; Rats ; Recombinant Proteins/metabolism ; Semaphorin-3A ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 110
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nash, H A -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1490-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Mental Health, National Institutes of Health, Bethesda, MD 20892, USA. nash@codon.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9508726" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents, Phytogenic/metabolism/pharmacology ; Camptothecin/metabolism/pharmacology ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; DNA Topoisomerases, Type I/*chemistry/metabolism ; DNA, Superhelical/chemistry/metabolism ; Humans ; Integrases/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Protein Conformation ; Protein Structure, Secondary ; Topoisomerase I Inhibitors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 111
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, M -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1623, 1625.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867659" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/*metabolism/pharmacology ; Binding Sites ; Crystallography, X-Ray ; DNA Primers/metabolism ; DNA, Viral/metabolism ; Deoxyribonucleotides/metabolism ; Drug Resistance, Microbial ; HIV Reverse Transcriptase/*chemistry/genetics/metabolism ; HIV-1/*drug effects/*enzymology ; Models, Molecular ; Mutation ; Protein Conformation ; Reverse Transcriptase Inhibitors/*metabolism/pharmacology ; Templates, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 112
    Publication Date: 1998-06-20
    Description: Both the alpha and betagamma subunits of heterotrimeric guanine nucleotide-binding proteins (G proteins) communicate signals from receptors to effectors. Gbetagamma subunits can regulate a diverse array of effectors, including ion channels and enzymes. Galpha subunits bound to guanine diphosphate (Galpha-GDP) inhibit signal transduction through Gbetagamma subunits, suggesting a common interface on Gbetagamma subunits for Galpha binding and effector interaction. The molecular basis for interaction of Gbetagamma with effectors was characterized by mutational analysis of Gbeta residues that make contact with Galpha-GDP. Analysis of the ability of these mutants to regulate the activity of calcium and potassium channels, adenylyl cyclase 2, phospholipase C-beta2, and beta-adrenergic receptor kinase revealed the Gbeta residues required for activation of each effector and provides evidence for partially overlapping domains on Gbeta for regulation of these effectors. This organization of interaction regions on Gbeta for different effectors and Galpha explains why subunit dissociation is crucial for signal transmission through Gbetagamma subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ford, C E -- Skiba, N P -- Bae, H -- Daaka, Y -- Reuveny, E -- Shekter, L R -- Rosal, R -- Weng, G -- Yang, C S -- Iyengar, R -- Miller, R J -- Jan, L Y -- Lefkowitz, R J -- Hamm, H E -- DA02121/DA/NIDA NIH HHS/ -- DA02575/DA/NIDA NIH HHS/ -- MH40165/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 22;280(5367):1271-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Neuroscience and Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, IL 60611, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596582" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate Ribose/metabolism ; Adenylyl Cyclases/metabolism ; Binding Sites ; Calcium Channels/metabolism ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; GTP-Binding Proteins/*chemistry/*metabolism ; Guanosine Diphosphate/metabolism ; *Heterotrimeric GTP-Binding Proteins ; Humans ; Isoenzymes/metabolism ; Models, Molecular ; Mutation ; Phospholipase C beta ; Potassium Channels/metabolism ; *Potassium Channels, Inwardly Rectifying ; Protein Conformation ; Rhodopsin/pharmacology ; *Signal Transduction ; Transducin/metabolism ; Type C Phospholipases/metabolism ; beta-Adrenergic Receptor Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 113
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-07-24
    Description: The ratio of late to early events stimulated by the mast cell receptor for immunoglobulin E (IgE) correlated with the affinity of a ligand for the receptor-bound IgE. Because excess receptors clustered by a weakly binding ligand could hoard a critical initiating kinase, they prevented the outnumbered clusters engendered by the high-affinity ligands from launching the more complete cascade. A similar mechanism could explain the antagonistic action of some peptides on the activation of T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Torigoe, C -- Inman, J K -- Metzger, H -- New York, N.Y. -- Science. 1998 Jul 24;281(5376):568-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arthritis and Rheumatism Branch, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892-1820, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9677201" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dinitrophenol/immunology ; Adaptor Proteins, Signal Transducing ; Animals ; Antibody Affinity ; Antigen-Antibody Reactions ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Dansyl Compounds ; Enzyme Precursors/metabolism ; Focal Adhesion Kinase 2 ; Haptens/*immunology/metabolism ; Immunoglobulin E/immunology/*metabolism ; Intracellular Signaling Peptides and Proteins ; Ligands ; Mast Cells/*immunology ; Mitogen-Activated Protein Kinase 1 ; Oncogene Proteins/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/metabolism ; Rats ; Receptor Aggregation ; Receptors, IgE/immunology/*metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 114
    Publication Date: 1998-06-20
    Description: Activation and covalent attachment of complement component C3 to pathogens is the key step in complement-mediated host defense. Additionally, the antigen-bound C3d fragment interacts with complement receptor 2 (CR2; also known as CD21) on B cells and thereby contributes to the initiation of an acquired humoral response. The x-ray crystal structure of human C3d solved at 2.0 angstroms resolution reveals an alpha-alpha barrel with the residues responsible for thioester formation and covalent attachment at one end and an acidic pocket at the other. The structure supports a model whereby the transition of native C3 to its functionally active state involves the disruption of a complementary domain interface and provides insight into the basis for the interaction between C3d and CR2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nagar, B -- Jones, R G -- Diefenbach, R J -- Isenman, D E -- Rini, J M -- New York, N.Y. -- Science. 1998 May 22;280(5367):1277-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596584" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Complement C3d/*chemistry/metabolism ; Conserved Sequence ; Crystallography, X-Ray ; Humans ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Complement 3d/*metabolism ; Sequence Alignment
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 115
    Publication Date: 1998-01-24
    Description: Developing axons reach their final targets as a result of a series of axonal projections to successive intermediate targets. Long-range chemoattraction by intermediate targets plays a key role in this process. Growing axons, however, do not stall at the intermediate targets, where the chemoattractant concentration is expected to be maximal. Commissural axons in the metencephalon, initially attracted by a chemoattractant released from the floor plate, were shown to lose responsiveness to the chemoattractant when they crossed the floor plate in vitro. Such changes in axon responsiveness to chemoattractants may enable developing axons to continue to navigate toward their final destinations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shirasaki, R -- Katsumata, R -- Murakami, F -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Neuroscience, Division of Biophysical Engineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560, Japan. sirasaki@bpe.es.osaka-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417018" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*physiology ; Carbocyanines ; *Cell Adhesion Molecules, Neuronal ; *Chemotaxis ; Contactin 2 ; Culture Techniques ; Fluorescent Dyes ; Membrane Glycoproteins/analysis ; Nerve Growth Factors/*physiology ; Pons/*embryology/physiology ; Rats ; Rats, Wistar ; Rhombencephalon/*embryology/metabolism ; Tumor Suppressor Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 116
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-09-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1998 Aug 28;281(5381):1264-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9735037" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicyclo Compounds/pharmacology/*therapeutic use ; Dopamine/metabolism ; Excitatory Amino Acid Agonists/pharmacology/*therapeutic use ; Glutamic Acid/*metabolism ; Humans ; Maze Learning/drug effects ; Memory/drug effects ; Phencyclidine/pharmacology ; Prefrontal Cortex/drug effects/*metabolism ; Rats ; Receptors, Metabotropic Glutamate/metabolism ; Schizophrenia/chemically induced/*drug therapy/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 117
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2045-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669958" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Deterrents/therapeutic use ; Alcoholism/drug therapy ; Animals ; Behavior, Addictive/drug therapy/*etiology ; Brain/*metabolism ; Cocaine/administration & dosage ; Cocaine-Related Disorders/drug therapy/*etiology ; Excitatory Amino Acid Antagonists/therapeutic use ; Glutamic Acid/*physiology ; Humans ; Rats ; Receptors, Glutamate/metabolism ; Substance-Related Disorders/drug therapy/*etiology ; Synaptic Transmission ; Taurine/analogs & derivatives/therapeutic use
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 118
    Publication Date: 1998-04-16
    Description: Radiolysis of water with a synchrotron x-ray beam permits the hydroxyl radical-accessible surface of an RNA to be mapped with nucleotide resolution in 10 milliseconds. Application of this method to folding of the Tetrahymena ribozyme revealed that the most stable domain of the tertiary structure, P4-P6, formed cooperatively within 3 seconds. Exterior helices became protected from hydroxyl radicals in 10 seconds, whereas the catalytic center required minutes to be completely folded. The results show that rapid collapse to a partially disordered state is followed by a slow search for the active structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sclavi, B -- Sullivan, M -- Chance, M R -- Brenowitz, M -- Woodson, S A -- GM39929/GM/NIGMS NIH HHS/ -- GM51506/GM/NIGMS NIH HHS/ -- GM52348/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1940-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Center for Synchrotron Biosciences, Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506944" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Hydroxyl Radical ; Kinetics ; Magnesium ; Models, Molecular ; *Nucleic Acid Conformation ; RNA, Catalytic/*chemistry ; Solvents ; Synchrotrons ; Tetrahymena/chemistry ; X-Rays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 119
    Publication Date: 1998-06-26
    Description: Hippocampal pyramidal cells are called place cells because each cell tends to fire only when the animal is in a particular part of the environment-the cell's firing field. Acute pharmacological blockade of N-methyl-D-aspartate (NMDA) glutamate receptors was used to investigate how NMDA-based synaptic plasticity participates in the formation and maintenance of the firing fields. The results suggest that the formation and short-term stability of firing fields in a new environment involve plasticity that is independent of NMDA receptor activation. By contrast, the long-term stabilization of newly established firing fields required normal NMDA receptor function and, therefore, may be related to other NMDA-dependent processes such as long-term potentiation and spatial learning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kentros, C -- Hargreaves, E -- Hawkins, R D -- Kandel, E R -- Shapiro, M -- Muller, R V -- R01 20686/PHS HHS/ -- R01 45923/PHS HHS/ -- T32 AGO 00189/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2121-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, SUNY Health Science Center Brooklyn, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9641919" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Mapping ; Evoked Potentials ; Excitatory Amino Acid Antagonists/pharmacology ; Hippocampus/*physiology ; Long-Term Potentiation/*physiology ; Male ; Memory/*physiology ; Neuronal Plasticity ; Piperazines/pharmacology ; Pyramidal Cells/*physiology ; Rats ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*physiology ; Space Perception/*physiology ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 120
    Publication Date: 1998-02-07
    Description: The three-dimensional structure of the human immunodeficiency virus-type 1 (HIV-1) nucleocapsid protein (NC) bound to the SL3 stem-loop recognition element of the genomic Psi RNA packaging signal has been determined by heteronuclear magnetic resonance spectroscopy. Tight binding (dissociation constant, approximately 100 nM) is mediated by specific interactions between the amino- and carboxyl-terminal CCHC-type zinc knuckles of the NC protein and the G7 and G9 nucleotide bases, respectively, of the G6-G7-A8-G9 RNA tetraloop. A8 packs against the amino-terminal knuckle and forms a hydrogen bond with conserved Arg32, and residues Lys3 to Arg10 of NC form a 310 helix that binds to the major groove of the RNA stem and also packs against the amino-terminal zinc knuckle. The structure provides insights into the mechanism of viral genome recognition, explains extensive amino acid conservation within NC, and serves as a basis for the development of inhibitors designed to interfere with genome encapsidation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Guzman, R N -- Wu, Z R -- Stalling, C C -- Pappalardo, L -- Borer, P N -- Summers, M F -- GM32691/GM/NIGMS NIH HHS/ -- GM42561/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):384-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Maryland-Baltimore County (UMBC), 1000 Hilltop Circle, Baltimore, MD 21250, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430589" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Gene Products, gag/*chemistry/metabolism ; Genome, Viral ; HIV-1/*chemistry/genetics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA, Viral/*chemistry/genetics/metabolism ; Zinc/chemistry/metabolism ; Zinc Fingers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 121
    Publication Date: 1998-10-02
    Description: Polyamide dimers containing three types of aromatic rings-pyrrole, imidazole, and hydroxypyrrole-afford a small-molecule recognition code that discriminates among all four Watson-Crick base pairs in the minor groove. The crystal structure of a specific polyamide dimer-DNA complex establishes the structural basis for distinguishing T.A from A.T base pairs. Specificity for the T.A base pair is achieved by means of distinct hydrogen bonds between pairs of substituted pyrroles on the ligand and the O2 of thymine and N3 of adenine. In addition, shape-selective recognition of an asymmetric cleft between the thymine-O2 and the adenine-C2 was observed. Although hitherto similarities among the base pairs in the minor groove have been emphasized, the structure illustrates differences that allow specific minor groove recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kielkopf, C L -- White, S -- Szewczyk, J W -- Turner, J M -- Baird, E E -- Dervan, P B -- Rees, D C -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):111-5.〈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/9756473" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/*chemistry ; *Base Composition ; DNA/*chemistry ; Dimerization ; Hydrogen Bonding ; Ligands ; Models, Molecular ; *Nucleic Acid Conformation ; Nylons/chemistry ; Oligodeoxyribonucleotides/chemistry ; Thymine/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 122
    Publication Date: 1998-09-25
    Description: If information is stored as activity-driven increases in synaptic weights in the hippocampal formation, saturation of hippocampal long-term potentiation (LTP) should impair learning. Here, rats in which one hippocampus had been lesioned were implanted with a multielectrode stimulating array across and into the angular bundle afferent to the other hippocampus. Repeated cross-bundle tetanization caused cumulative potentiation. Residual synaptic plasticity was assessed by tetanizing a naive test electrode in the center of the bundle. Spatial learning was disrupted in animals with no residual LTP (〈10 percent) but not in animals that were capable of further potentiation. Thus, saturation of hippocampal LTP impairs spatial learning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moser, E I -- Krobert, K A -- Moser, M B -- Morris, R G -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2038-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychology, Norwegian University of Science and Technology, 7034 Trondheim, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748165" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dentate Gyrus/physiology ; Electric Stimulation ; Electrodes, Implanted ; Evoked Potentials ; Excitatory Postsynaptic Potentials ; Hippocampus/*physiology ; Long-Term Potentiation/*physiology ; Male ; Maze Learning/*physiology ; Perforant Pathway ; Rats ; Synapses/physiology ; Tetany
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 123
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-28
    Description: Little is known about the mechanisms that allow the cortex to selectively improve the neural representations of behaviorally important stimuli while ignoring irrelevant stimuli. Diffuse neuromodulatory systems may facilitate cortical plasticity by acting as teachers to mark important stimuli. This study demonstrates that episodic electrical stimulation of the nucleus basalis, paired with an auditory stimulus, results in a massive progressive reorganization of the primary auditory cortex in the adult rat. Receptive field sizes can be narrowed, broadened, or left unaltered depending on specific parameters of the acoustic stimulus paired with nucleus basalis activation. This differential plasticity parallels the receptive field remodeling that results from different types of behavioral training. This result suggests that input characteristics may be able to drive appropriate alterations of receptive fields independently of explicit knowledge of the task. These findings also suggest that the basal forebrain plays an active instructional role in representational plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilgard, M P -- Merzenich, M M -- NS-10414/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 13;279(5357):1714-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Otolaryngology, W. M. Keck Foundation Center for Integrative Neuroscience, University of California, San Francisco, 513 Parnassus Avenue, Box 0732, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9497289" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Acoustic Stimulation ; Animals ; Auditory Cortex/*physiology ; Basal Ganglia/*physiology ; *Brain Mapping ; Conditioning (Psychology) ; Electric Stimulation ; *Neuronal Plasticity ; Neurons/physiology ; Prosencephalon/*physiology ; Rats
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 124
    Publication Date: 1998-04-16
    Description: In the magnesium ion-dependent folding of the Tetrahymena ribozyme, a kinetic intermediate accumulates in which the P4-P6 domain is formed, but the P3-P7 domain is not. The kinetic barriers to P3-P7 formation were investigated with the use of in vitro selection to identify mutant RNA molecules in which the folding rate of the P3-P7 domain was increased. The critical mutations disrupt native tertiary interactions within the P4-P6 domain and increase the rate of P3-P7 formation by destabilizing a kinetically trapped intermediate. Hence, kinetic traps stabilized by native interactions, and not simply by mispaired nonnative structures, can present a substantial barrier to RNA folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Treiber, D K -- Rook, M S -- Zarrinkar, P P -- Williamson, J R -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1943-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, MB33, 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/9506945" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Kinetics ; Magnesium/metabolism ; Models, Molecular ; Mutation ; *Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/genetics/metabolism ; Tetrahymena/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 125
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):479-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454346" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohols/metabolism ; Aldehydes/metabolism ; Binding Sites ; Catalysis ; Copper/chemistry/metabolism ; Electrons ; Galactose Oxidase/*chemistry/*metabolism ; Hydrogen Peroxide/metabolism ; Models, Chemical ; Models, Molecular ; Protons
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 126
    Publication Date: 1998-10-23
    Description: A map of 30,181 human gene-based markers was assembled and integrated with the current genetic map by radiation hybrid mapping. The new gene map contains nearly twice as many genes as the previous release, includes most genes that encode proteins of known function, and is twofold to threefold more accurate than the previous version. A redesigned, more informative and functional World Wide Web site (www.ncbi.nlm.nih.gov/genemap) provides the mapping information and associated data and annotations. This resource constitutes an important infrastructure and tool for the study of complex genetic traits, the positional cloning of disease genes, the cross-referencing of mammalian genomes, and validated human transcribed sequences for large-scale studies of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deloukas, P -- Schuler, G D -- Gyapay, G -- Beasley, E M -- Soderlund, C -- Rodriguez-Tome, P -- Hui, L -- Matise, T C -- McKusick, K B -- Beckmann, J S -- Bentolila, S -- Bihoreau, M -- Birren, B B -- Browne, J -- Butler, A -- Castle, A B -- Chiannilkulchai, N -- Clee, C -- Day, P J -- Dehejia, A -- Dibling, T -- Drouot, N -- Duprat, S -- Fizames, C -- Fox, S -- Gelling, S -- Green, L -- Harrison, P -- Hocking, R -- Holloway, E -- Hunt, S -- Keil, S -- Lijnzaad, P -- Louis-Dit-Sully, C -- Ma, J -- Mendis, A -- Miller, J -- Morissette, J -- Muselet, D -- Nusbaum, H C -- Peck, A -- Rozen, S -- Simon, D -- Slonim, D K -- Staples, R -- Stein, L D -- Stewart, E A -- Suchard, M A -- Thangarajah, T -- Vega-Czarny, N -- Webber, C -- Wu, X -- Hudson, J -- Auffray, C -- Nomura, N -- Sikela, J M -- Polymeropoulos, M H -- James, M R -- Lander, E S -- Hudson, T J -- Myers, R M -- Cox, D R -- Weissenbach, J -- Boguski, M S -- Bentley, D R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Oct 23;282(5389):744-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sanger Centre, Hinxton Hall, Hinxton, Cambridge CB10 1SA UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9784132" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes, Human/*genetics ; Expressed Sequence Tags ; Gene Expression ; Genetic Markers ; *Genome, Human ; Human Genome Project ; Humans ; Internet ; *Physical Chromosome Mapping ; Rats ; Sequence Tagged Sites
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 127
    Publication Date: 1998-05-09
    Description: Pseudoknot formation folds the 3' ends of many plant viral genomic RNAs into structures that resemble transfer RNA in global folding and in their reactivity to transfer RNA-specific proteins. The solution structure of the pseudoknotted T arm and acceptor arm of the transfer RNA-like structure of turnip yellow mosaic virus (TYMV) was determined by nuclear magnetic resonance (NMR) spectroscopy. The molecule is stabilized by the hairpin formed by the 5' end of the RNA, and by the intricate interactions related to the loops of the pseudoknot. Loop 1 spans the major groove of the helix with only two of its four nucleotides. Loop 2, which crosses the minor groove, interacts closely with its opposing helix, in particular through hydrogen bonds with a highly conserved adenine. The structure resulting from this interaction between the minor groove and single-stranded RNA at helical junctions displays internal mobility, which may be a general feature of RNA pseudoknots that regulates their interaction with proteins or other RNA molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolk, M H -- van der Graaf, M -- Wijmenga, S S -- Pleij, C W -- Heus, H A -- Hilbers, C W -- New York, N.Y. -- Science. 1998 Apr 17;280(5362):434-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nijmegen SON Research Center for Molecular Structure, Design and Synthesis, Laboratory of Biophysical Chemistry, University of Nijmegen, Toernooiveld, 6525 ED Nijmegen, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9545221" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acyl-tRNA Synthetases/chemistry/metabolism ; Binding Sites ; Diethyl Pyrocarbonate/chemistry ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Mutation ; *Nucleic Acid Conformation ; RNA, Double-Stranded/*chemistry ; RNA, Transfer/*chemistry ; RNA, Viral/*chemistry ; Tymovirus/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...