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  • Models, Biological
  • American Association for the Advancement of Science (AAAS)  (349)
  • Wiley
  • Wiley-Blackwell
  • 2005-2009  (272)
  • 1995-1999  (77)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spear, P G -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):1999-2000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Northwestern University Medical School, Department of Microbiology-Immunology, Chicago, IL 60611, USA. p-spear@nwu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9874652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Adhesion ; Cytoskeletal Proteins/genetics/*metabolism ; Dystroglycans ; Humans ; Laminin/metabolism ; Lassa Fever/*virology ; Lassa virus/*metabolism ; Leprosy/*microbiology ; Lymphocytic choriomeningitis virus/metabolism ; Membrane Glycoproteins/genetics/*metabolism ; Models, Biological ; Mycobacterium leprae/*metabolism ; Receptors, Virus/metabolism ; Schwann Cells/microbiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-11-20
    Description: Two general models have been proposed for DNA replication. In one model, DNA polymerase moves along the DNA (like a train on a track); in the other model, the polymerase is stationary (like a factory), and DNA is pulled through. To distinguish between these models, we visualized DNA polymerase of the bacterium Bacillus subtilis in living cells by the creation of a fusion protein containing the catalytic subunit (PolC) and green fluorescent protein (GFP). PolC-GFP was localized at discrete intracellular positions, predominantly at or near midcell, rather than being distributed randomly. These results suggest that the polymerase is anchored in place and thus support the model in which the DNA template moves through the polymerase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lemon, K P -- Grossman, A D -- GM41934/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1516-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Building 68-530, 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/9822387" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/enzymology/growth & development/*metabolism ; Chromosomes, Bacterial/*metabolism ; *DNA Replication ; DNA, Bacterial/*biosynthesis ; DNA-Directed DNA Polymerase/*analysis/metabolism ; Green Fluorescent Proteins ; Luminescent Proteins ; Models, Biological ; Recombinant Fusion Proteins/metabolism ; *Replication Origin ; Templates, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1998-03-21
    Description: Host-parasite coevolution has been likened to a molecular arms race, with particular parasite genes evolving to evade specific host defenses. Study of the variants of an antigenic epitope of Plasmodium falciparum that induces a cytotoxic T cell response supports this view. In African children with malaria, the variants present are influenced by the presence of a human leukocyte antigen (HLA) type that restricts the immune response to this epitope. The distribution of parasite variants may be further influenced by the ability of cohabiting parasite strains to facilitate each other's survival by down-regulating cellular immune responses, using altered peptide ligand antagonism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilbert, S C -- Plebanski, M -- Gupta, S -- Morris, J -- Cox, M -- Aidoo, M -- Kwiatkowski, D -- Greenwood, B M -- Whittle, H C -- Hill, A V -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1173-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Windmill Road, Oxford OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469800" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antigens, Protozoan/genetics/*immunology ; Biological Evolution ; Child ; Epitopes ; Evolution, Molecular ; Gambia ; Genes, Protozoan ; Genetic Variation ; HLA-B35 Antigen/*immunology ; Humans ; Ligands ; Malaria, Falciparum/*immunology/parasitology ; Models, Biological ; Plasmodium falciparum/genetics/*immunology ; Protozoan Proteins/genetics/*immunology ; T-Lymphocytes, Cytotoxic/*immunology
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ashcroft, F M -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1059-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University Laboratory of Physiology, Oxford OX1 3PT, UK. frances.ashcroft@physiol.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841452" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/*metabolism/pharmacology ; Animals ; Binding Sites ; Cell Membrane/metabolism ; Islets of Langerhans/metabolism ; Models, Biological ; Myocardium/cytology/metabolism ; Phosphatidylinositol 4,5-Diphosphate/chemistry/*metabolism/pharmacology ; Potassium Channels/chemistry/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Receptors, Drug/chemistry/metabolism ; Sulfonylurea Receptors ; Surface Properties
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cook, P -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1466-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Sir William Dunn School of Pathology, Oxford OX2 3RE, UK. peter.cook@path.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9750117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/*metabolism ; *DNA Replication ; *Genome ; Genome, Human ; Humans ; Models, Biological ; *Transcription, Genetic
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-12-03
    Description: Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over protein structure and function depends on molecular chaperones and proteases, both of which can recognize hydrophobic regions exposed on unfolded polypeptides. Molecular chaperones promote proper protein folding and prevent aggregation, and energy-dependent proteases eliminate irreversibly damaged proteins. The kinetics of partitioning between chaperones and proteases determines whether a protein will be destroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloid diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickner, S -- Maurizi, M R -- Gottesman, S -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1888-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10583944" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Amyloid/metabolism ; Animals ; Endopeptidases/*metabolism ; Eukaryotic Cells/metabolism ; Humans ; Models, Biological ; Molecular Chaperones/*metabolism ; Prions/metabolism ; Prokaryotic Cells/metabolism ; Protein Biosynthesis ; *Protein Folding ; Proteins/*chemistry/*metabolism ; Ubiquitins/metabolism
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-26
    Description: Katanin, a member of the AAA adenosine triphosphatase (ATPase) superfamily, uses nucleotide hydrolysis energy to sever and disassemble microtubules. Many AAA enzymes disassemble stable protein-protein complexes, but their mechanisms are not well understood. A fluorescence resonance energy transfer assay demonstrated that the p60 subunit of katanin oligomerized in an adenosine triphosphate (ATP)- and microtubule-dependent manner. Oligomerization increased the affinity of katanin for microtubules and stimulated its ATPase activity. After hydrolysis of ATP, microtubule-bound katanin oligomers disassembled microtubules and then dissociated into free katanin monomers. Coupling a nucleotide-dependent oligomerization cycle to the disassembly of a target protein complex may be a general feature of ATP-hydrolyzing AAA domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartman, J J -- Vale, R D -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):782-5.〈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/10531065" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/analogs & derivatives/*metabolism ; Amino Acid Sequence ; Centrifugation, Density Gradient ; Fluorescence ; Hydrolysis ; Luminescent Proteins ; Microtubules/*metabolism ; Models, Biological ; Molecular Sequence Data ; Polymers ; Recombinant Fusion Proteins/chemistry/metabolism ; Tubulin/metabolism
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-09-11
    Description: Deleterious mutations with very small phenotypic effects could be important for several evolutionary phenomena, but the extent of their contribution has been unknown. Fitness effects of induced mutations in lines of Caenorhabditis elegans were measured using a system for which the number of deleterious point mutations in the DNA can be estimated. In fitness assays, only about 4 percent of the deleterious mutations fixed in each line were detectable. The remaining 96 percent, though cryptic, are significant for mutation load and, potentially, for the evolution of sex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davies, E K -- Peters, A D -- Keightley, P D -- New York, N.Y. -- Science. 1999 Sep 10;285(5434):1748-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cell, Animal and Population Biology, University of Edinburgh, West Mains Road, Edinburgh EH9 3JT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10481013" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics/*physiology ; Computer Simulation ; Crosses, Genetic ; Disorders of Sex Development ; Ethyl Methanesulfonate/pharmacology ; *Genes, Helminth ; Likelihood Functions ; Models, Biological ; Models, Statistical ; Mutagens/pharmacology ; *Point Mutation ; Reproduction ; Selection, Genetic
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-12-03
    Description: A variety of quality control mechanisms operate in the endoplasmic reticulum and in downstream compartments of the secretory pathway to ensure the fidelity and regulation of protein expression during cell life and differentiation. As a rule, only proteins that pass a stringent selection process are transported to their target organelles and compartments. If proper maturation fails, the aberrant products are degraded. Quality control improves folding efficiency by retaining proteins in the special folding environment of the endoplasmic reticulum, and it prevents harmful effects that could be caused by the deployment of incompletely folded or assembled proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellgaard, L -- Molinari, M -- Helenius, A -- New York, N.Y. -- Science. 1999 Dec 3;286(5446):1882-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), Universitatstrasse 16, CH-8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10583943" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Endoplasmic Reticulum/*metabolism ; Glycoproteins/chemistry/metabolism ; Golgi Apparatus/metabolism ; Membrane Proteins/chemistry/metabolism ; Models, Biological ; Molecular Chaperones/metabolism ; Oligosaccharides/metabolism ; Organelles/metabolism ; Protein Conformation ; *Protein Folding ; Proteins/*chemistry/*metabolism/secretion
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horwitz, A R -- Parsons, J T -- New York, N.Y. -- Science. 1999 Nov 5;286(5442):1102-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Microbiology, Health Sciences Center, University of Virginia, Charlottesville, VA 22908, USA. horwitz@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610524" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; *Cell Adhesion ; Cell Adhesion Molecules/metabolism ; *Cell Movement ; Cytoskeleton/physiology ; Fibroblasts/*cytology/physiology ; Integrins/metabolism ; Microtubules/physiology ; Models, Biological ; Myosin Light Chains/metabolism ; Myosins/metabolism ; cdc42 GTP-Binding Protein/metabolism ; rac GTP-Binding Proteins/metabolism ; rho GTP-Binding Proteins/metabolism
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-02-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zuker, C S -- Ranganathan, R -- New York, N.Y. -- Science. 1999 Jan 29;283(5402):650-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biology, University of California, San Diego, CA 92093-0649, USA. charles@flyeye.ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9988659" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestin/genetics/*metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Membrane/metabolism ; Enzyme Activation ; GTP-Binding Proteins/metabolism ; Humans ; Models, Biological ; Mutation ; Phosphorylation ; Proto-Oncogene Proteins pp60(c-src)/*metabolism ; Receptor Cross-Talk ; Receptors, Adrenergic, beta-2/*metabolism ; *Signal Transduction ; src Homology Domains
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-02
    Description: One of the most striking patterns in biology is the formation of animal aggregations. Classically, aggregation has been viewed as an evolutionarily advantageous state, in which members derive the benefits of protection, mate choice, and centralized information, balanced by the costs of limiting resources. Consisting of individual members, aggregations nevertheless function as an integrated whole, displaying a complex set of behaviors not possible at the level of the individual organism. Complexity theory indicates that large populations of units can self-organize into aggregations that generate pattern, store information, and engage in collective decision-making. This begs the question, are all emergent properties of animal aggregations functional or are some simply pattern? Solutions to this dilemma will necessitate a closer marriage of theoretical and modeling studies linked to empirical work addressing the choices, and trajectories, of individuals constrained by membership in the group.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parrish, J K -- Edelstein-Keshet, L -- New York, N.Y. -- Science. 1999 Apr 2;284(5411):99-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoology Department, University of Washington, Seattle, WA 98195, USA. jparrish@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10102827" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Biological Evolution ; *Cooperative Behavior ; Mathematics ; Models, Biological
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  • 13
    Publication Date: 1999-07-31
    Description: Many psychotropic drugs interfere with the reuptake of dopamine, norepinephrine, and serotonin. Transport capacity is regulated by kinase-linked pathways, particularly those involving protein kinase C (PKC), resulting in transporter phosphorylation and sequestration. Phosphorylation and sequestration of the serotonin transporter (SERT) were substantially impacted by ligand occupancy. Ligands that can permeate the transporter, such as serotonin or the amphetamines, prevented PKC-dependent SERT phosphorylation. Nontransported SERT antagonists such as cocaine and antidepressants were permissive for SERT phosphorylation but blocked serotonin effects. PKC-dependent SERT sequestration was also blocked by serotonin. These findings reveal activity-dependent modulation of neurotransmitter reuptake and identify previously unknown consequences of amphetamine, cocaine, and antidepressant action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramamoorthy, S -- Blakely, R D -- DA07390/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 30;285(5428):763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Center for Molecular Neuroscience, School of Medicine, Vanderbilt University, Nashville, TN 37232-6420, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10427004" target="_blank"〉PubMed〈/a〉
    Keywords: Antidepressive Agents/metabolism/pharmacology ; Biogenic Monoamines/metabolism/pharmacology ; Biotinylation ; Carrier Proteins/antagonists & inhibitors/*metabolism ; Cell Line ; Central Nervous System Agents/metabolism/*pharmacology ; Cocaine/metabolism/pharmacology ; Dextroamphetamine/metabolism/pharmacology ; Enzyme Activation ; Humans ; Ligands ; Membrane Glycoproteins/antagonists & inhibitors/*metabolism ; *Membrane Transport Proteins ; Models, Biological ; *Nerve Tissue Proteins ; Neurotransmitter Agents/metabolism/*pharmacology ; Phosphorylation ; Protein Kinase C/metabolism ; Protein Kinases/metabolism ; Serotonin/*metabolism/pharmacology ; Serotonin Antagonists/pharmacology ; Serotonin Plasma Membrane Transport Proteins ; Serotonin Uptake Inhibitors/metabolism/pharmacology ; Tetradecanoylphorbol Acetate/pharmacology
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-06-26
    Description: Interactions between species are as evolutionarily malleable as the species themselves and have played a central role in the diversification and organization of life. This malleability creates complex geographic mosaics in interspecific interactions that can evolve rapidly over decades, blurring the distinction between evolutionary time and ecological time and making the study of coevolution crucial for human health and welfare.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, J N -- New York, N.Y. -- Science. 1999 Jun 25;284(5423):2116-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Botany and Zoology, Washington State University, Pullman, WA 99164, USA. jnt@wsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10381869" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Drug Resistance, Microbial ; *Ecosystem ; Humans ; Models, Biological ; Parasites/pathogenicity ; *Selection, Genetic ; Virulence/genetics
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oren, D A -- Terman, M -- MH-42931/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):333-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Veterans Affairs, West Haven, CT 06516, USA. dan.oren@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9454328" target="_blank"〉PubMed〈/a〉
    Keywords: Bilirubin/*physiology ; Circadian Rhythm/*physiology ; Hemoglobins/*physiology ; Humans ; Knee ; *Light ; *Light Signal Transduction ; Melatonin/physiology/secretion ; Models, Biological ; Neural Pathways ; Photoreceptor Cells/physiology ; Phototherapy ; Pineal Gland/secretion ; Seasonal Affective Disorder/therapy ; Suprachiasmatic Nucleus/physiology ; Visual Pathways
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagmann, M -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):388-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10577195" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Antigens, Surface/metabolism ; Cell Membrane/metabolism ; Chlorides/metabolism ; Cystic Fibrosis Transmembrane Conductance ; Regulator/chemistry/genetics/*metabolism ; Humans ; *Ion Channel Gating ; Models, Biological ; Mutagenesis ; Nerve Tissue Proteins/metabolism ; Syntaxin 1 ; Xenopus
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-16
    Description: Long-term variability in the abundance of populations depends on the sensitivity of species to environmental fluctuations and the amplification of environmental fluctuations by interactions among species. Although competitive interactions and species number may have diverse effects on variability measured at the individual species level, a combination of theoretical analyses shows that these factors have no effect on variability measured at the community level. Therefore, biodiversity may increase community stability by promoting diversity among species in their responses to environmental fluctuations, but increasing the number and strength of competitive interactions has little effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ives, A R -- Gross, K -- Klug, J L -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):542-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Wisconsin-Madison, Madison, WI 53706, USA. arives@facstaff.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10521351" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biomass ; Competitive Behavior ; *Ecosystem ; Mathematics ; Models, Biological
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-12-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fillingame, R H -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1687-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison, WI 53706, USA. rhfillin@facstaff.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10610565" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Catalysis ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Helix-Loop-Helix Motifs ; Hydrolysis ; Mitochondria/enzymology ; Models, Biological ; *Molecular Motor Proteins/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Proton-Motive Force ; Proton-Translocating ATPases/*chemistry/*metabolism ; Saccharomyces cerevisiae/enzymology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
    Publication Date: 1999-01-29
    Description: The Ras-dependent activation of mitogen-activated protein (MAP) kinase pathways by many receptors coupled to heterotrimeric guanine nucleotide binding proteins (G proteins) requires the activation of Src family tyrosine kinases. Stimulation of beta2 adrenergic receptors resulted in the assembly of a protein complex containing activated c-Src and the receptor. Src recruitment was mediated by beta-arrestin, which functions as an adapter protein, binding both c-Src and the agonist-occupied receptor. beta-Arrestin 1 mutants, impaired either in c-Src binding or in the ability to target receptors to clathrin-coated pits, acted as dominant negative inhibitors of beta2 adrenergic receptor-mediated activation of the MAP kinases Erk1 and Erk2. These data suggest that beta-arrestin binding, which terminates receptor-G protein coupling, also initiates a second wave of signal transduction in which the "desensitized" receptor functions as a critical structural component of a mitogenic signaling complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luttrell, L M -- Ferguson, S S -- Daaka, Y -- Miller, W E -- Maudsley, S -- Della Rocca, G J -- Lin, F -- Kawakatsu, H -- Owada, K -- Luttrell, D K -- Caron, M G -- Lefkowitz, R J -- DK02352/DK/NIDDK NIH HHS/ -- DK55524/DK/NIDDK NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1999 Jan 29;283(5402):655-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and 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/9924018" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/metabolism/pharmacology ; Animals ; Arrestins/genetics/*metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Line ; Cell Membrane/metabolism ; Enzyme Activation ; GTP-Binding Proteins/metabolism ; Humans ; Isoproterenol/metabolism/pharmacology ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinases ; Models, Biological ; Phosphorylation ; Point Mutation ; Precipitin Tests ; Proto-Oncogene Proteins pp60(c-src)/*metabolism ; Receptor Cross-Talk ; Receptors, Adrenergic, beta-2/*metabolism ; Receptors, Cell Surface/metabolism ; *Signal Transduction ; Transfection ; src Homology Domains
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-09-11
    Description: In asexual populations, beneficial mutations that occur in different lineages compete with one another. This phenomenon, known as clonal interference, ensures that those beneficial mutations that do achieve fixation are of large effect. Clonal interference also increases the time between fixations, thereby slowing the adaptation of asexual populations. The effects of clonal interference were measured in the asexual RNA virus vesicular stomatitis virus; rates and average effects of beneficial mutations were quantified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miralles, R -- Gerrish, P J -- Moya, A -- Elena, S F -- New York, N.Y. -- Science. 1999 Sep 10;285(5434):1745-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Cavanilles de Biodiversitat i Biologia Evolutiva and Departament de Genetica, Universitat de Valencia, Apartado 22085, 46071 Valencia, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10481012" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; *Biological Evolution ; Cell Line ; Confidence Intervals ; Cricetinae ; Gene Frequency ; Genes, Viral ; Likelihood Functions ; Models, Biological ; Models, Statistical ; *Mutation ; Vesicular stomatitis Indiana virus/genetics/*physiology ; Virus Replication
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salpeter, M M -- NS09315/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):424-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Behavior, Cornell University, Ithaca, NY 14853, USA. mms13@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10577204" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Animals ; Cell Membrane/metabolism ; Electric Stimulation ; Humans ; Models, Biological ; Muscle Contraction ; Muscle Denervation ; Neuromuscular Junction/*physiology ; Receptors, Cholinergic/chemistry/*metabolism ; Schwann Cells/physiology ; Synaptic Transmission
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-03-05
    Description: The serial endosymbiosis theory is a favored model for explaining the origin of mitochondria, a defining event in the evolution of eukaryotic cells. As usually described, this theory posits that mitochondria are the direct descendants of a bacterial endosymbiont that became established at an early stage in a nucleus-containing (but amitochondriate) host cell. Gene sequence data strongly support a monophyletic origin of the mitochondrion from a eubacterial ancestor shared with a subgroup of the alpha-Proteobacteria. However, recent studies of unicellular eukaryotes (protists), some of them little known, have provided insights that challenge the traditional serial endosymbiosis-based view of how the eukaryotic cell and its mitochondrion came to be. These data indicate that the mitochondrion arose in a common ancestor of all extant eukaryotes and raise the possibility that this organelle originated at essentially the same time as the nuclear component of the eukaryotic cell rather than in a separate, subsequent event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gray, M W -- Burger, G -- Lang, B F -- New York, N.Y. -- Science. 1999 Mar 5;283(5407):1476-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada. M.W.Gray@Dal.Ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10066161" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Archaea/genetics ; Bacteria/genetics ; *Biological Evolution ; DNA, Mitochondrial/chemistry/*genetics ; *Eukaryotic Cells/physiology/ultrastructure ; Evolution, Molecular ; Genes ; Mitochondria/*genetics ; Models, Biological ; Phylogeny ; Symbiosis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, G A -- New York, N.Y. -- Science. 1999 Mar 26;283(5410):2029, 2031-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, Arizona State University, Tempe, AZ 85287-2402, USA. gaclark@asu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10206911" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Archaeology ; *Biological Evolution ; Europe ; History, Ancient ; *Hominidae ; Humans ; Models, Biological ; *Paleontology
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  • 24
    Publication Date: 1998-05-23
    Description: The effects of selection by host immune responses on transmission dynamics was analyzed in a broad class of antigenically diverse pathogens. Strong selection can cause pathogen populations to stably segregate into discrete strains with nonoverlapping antigenic repertoires. However, over a wide range of intermediate levels of selection, strain structure is unstable, varying in a manner that is either cyclical or chaotic. These results have implications for the interpretation of longitudinal epidemiological data on strain or serotype abundance, design of surveillance strategies, and the assessment of multivalent vaccine trials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, S -- Ferguson, N -- Anderson, R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1998 May 8;280(5365):912-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for the Epidemiology of Infectious Disease, Zoology Department, University of Oxford, South Parks Road, Oxford OX1 3PS, UK. sunetra.gupta@zoology.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9572737" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antibody Formation ; *Antigenic Variation ; Antigens, Bacterial/immunology ; Antigens, Protozoan/immunology ; Antigens, Viral/immunology ; Bacteria/classification/genetics/*immunology/pathogenicity ; Cross Reactions ; Eukaryota/classification/genetics/*immunology/pathogenicity ; Humans ; Immunity ; Infection/epidemiology/*immunology/microbiology/parasitology/transmission ; Mathematics ; Models, Biological ; Nonlinear Dynamics ; Serotyping ; Viruses/classification/genetics/*immunology/pathogenicity
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  • 25
    Publication Date: 1999-02-12
    Description: Glucose metabolism in glycolysis and in mitochondria is pivotal to glucose-induced insulin secretion from pancreatic beta cells. One or more factors derived from glycolysis other than pyruvate appear to be required for the generation of mitochondrial signals that lead to insulin secretion. The electrons of the glycolysis-derived reduced form of nicotinamide adenine dinucleotide (NADH) are transferred to mitochondria through the NADH shuttle system. By abolishing the NADH shuttle function, glucose-induced increases in NADH autofluorescence, mitochondrial membrane potential, and adenosine triphosphate content were reduced and glucose-induced insulin secretion was abrogated. The NADH shuttle evidently couples glycolysis with activation of mitochondrial energy metabolism to trigger insulin secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eto, K -- Tsubamoto, Y -- Terauchi, Y -- Sugiyama, T -- Kishimoto, T -- Takahashi, N -- Yamauchi, N -- Kubota, N -- Murayama, S -- Aizawa, T -- Akanuma, Y -- Aizawa, S -- Kasai, H -- Yazaki, Y -- Kadowaki, T -- New York, N.Y. -- Science. 1999 Feb 12;283(5404):981-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan. Tokyo〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9974390" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Aminooxyacetic Acid/pharmacology ; Animals ; Aspartate Aminotransferases/antagonists & inhibitors ; Calcium/metabolism ; Citric Acid Cycle ; Enzyme Inhibitors/pharmacology ; Female ; Gene Targeting ; Glucose/metabolism/*pharmacology ; Glycerolphosphate Dehydrogenase/genetics/metabolism ; Glycolysis ; Insulin/*secretion ; Islets of Langerhans/metabolism/*secretion ; Male ; Membrane Potentials ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mitochondria/*metabolism ; Models, Biological ; Molecular Sequence Data ; NAD/*metabolism ; Pyruvic Acid/metabolism
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birnbaumer, L -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1656.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, CA 90095, USA. lutzb@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10189319" target="_blank"〉PubMed〈/a〉
    Keywords: History, 20th Century ; Models, Biological ; Physiology/history ; *Signal Transduction ; United States
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janknecht, R -- Hunter, T -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):443-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Deparment of Biochemistry, Mayo Clinic, Rochester, MN 55905, USA. janknecht.ralf@mayo.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10232991" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Astrocytes/*cytology/metabolism ; Bone Morphogenetic Protein 2 ; Bone Morphogenetic Protein Receptors ; Bone Morphogenetic Proteins/metabolism/pharmacology ; Cell Differentiation ; Cell Nucleus/metabolism ; Cytokines/metabolism/*pharmacology ; DNA-Binding Proteins/metabolism ; Dimerization ; Glial Fibrillary Acidic Protein/genetics ; Growth Inhibitors/metabolism/pharmacology ; *Interleukin-6 ; Leukemia Inhibitory Factor ; Lymphokines/metabolism/pharmacology ; Models, Biological ; Nuclear Proteins/*metabolism ; Phosphorylation ; Promoter Regions, Genetic ; Receptors, Cell Surface/metabolism ; Receptors, Cytokine/metabolism ; *Receptors, Growth Factor ; Receptors, OSM-LIF ; STAT3 Transcription Factor ; *Signal Transduction ; Smad Proteins ; Trans-Activators/*metabolism ; *Transcriptional Activation ; *Transforming Growth Factor beta
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-01-08
    Description: In several organisms, the success of a male's sperm in multiply inseminated females depends on the male's genotype. In Drosophila, the female also plays a role in determining which sperm are successful. Pairwise tests among six isogenic lines of Drosophila melanogaster were performed to determine whether there is a genotype-specific interaction in the success of sperm. The success of a particular male's sperm was found to depend on the genotype of the female with which he mates, providing evidence for an interaction with profound evolutionary consequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, A G -- Begun, D J -- Prout, T -- New York, N.Y. -- Science. 1999 Jan 8;283(5399):217-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Pennsylvania State University, University Park, PA 16802, USA. c92@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9880253" target="_blank"〉PubMed〈/a〉
    Keywords: Analysis of Variance ; Animals ; *Biological Evolution ; Computer Simulation ; Drosophila melanogaster/genetics/*physiology ; Female ; Genetic Variation ; Genotype ; Male ; Models, Biological ; Sex Characteristics ; *Sexual Behavior, Animal ; Spermatozoa/*physiology
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-08-14
    Description: The life history of medflies is characterized by two physiological modes with different demographic schedules of fertility and survival: a waiting mode in which both mortality and reproduction are low and a reproductive mode in which mortality is very low at the onset of egg laying but accelerates as eggs are laid. Medflies stay in waiting mode when they are fed only sugar. When fed protein, a scarce resource in the wild, medflies switch to reproductive mode. Medflies that switch from waiting to reproductive mode survive longer than medflies kept in either mode exclusively. An understanding of the physiological shift that occurs between the waiting and reproductive modes may yield information about the fundamental processes that determine longevity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carey, J R -- Liedo, P -- Muller, H G -- Wang, J L -- Vaupel, J W -- AG-08761/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 14;281(5379):996-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of California, Davis, CA 95616, USA. jrcarey@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9703516" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*physiology ; Animals ; Dietary Proteins ; Drosophila ; Female ; Longevity ; Male ; Models, Biological ; Reproduction/physiology
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Losick, R -- Shapiro, L -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1430-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. losick@biosun.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867650" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/growth & development/*metabolism ; Cell Nucleus/metabolism ; Chromosomes/metabolism ; Chromosomes, Bacterial/*metabolism ; *DNA Replication ; DNA, Bacterial/*biosynthesis ; DNA-Directed DNA Polymerase/*analysis/metabolism ; Models, Biological ; Recombinant Fusion Proteins/metabolism ; *Replication Origin
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1999 Apr 2;284(5411):80-1, 83.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10215535" target="_blank"〉PubMed〈/a〉
    Keywords: Academies and Institutes ; *Biological Science Disciplines ; Biotechnology ; Chemical Phenomena ; *Chemistry ; Computer Simulation ; *Engineering ; Models, Biological ; Physical Phenomena ; *Physics ; *Research
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  • 32
    Publication Date: 1999-07-31
    Description: A computational method is proposed for inferring protein interactions from genome sequences on the basis of the observation that some pairs of interacting proteins have homologs in another organism fused into a single protein chain. Searching sequences from many genomes revealed 6809 such putative protein-protein interactions in Escherichia coli and 45,502 in yeast. Many members of these pairs were confirmed as functionally related; computational filtering further enriches for interactions. Some proteins have links to several other proteins; these coupled links appear to represent functional interactions such as complexes or pathways. Experimentally confirmed interacting pairs are documented in a Database of Interacting Proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marcotte, E M -- Pellegrini, M -- Ng, H L -- Rice, D W -- Yeates, T O -- Eisenberg, D -- P01 GM 31299/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 30;285(5428):751-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-Department of Energy Laboratory of Structural Biology and Molecular Medicine, University of California at Los Angeles, Los Angeles, CA 90095-1570, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10427000" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/genetics/metabolism/physiology ; Binding Sites ; *Computational Biology ; Databases, Factual ; Escherichia coli/genetics ; Evolution, Molecular ; Fungal Proteins/chemistry/genetics/metabolism ; *Genome ; Genome, Bacterial ; Genome, Fungal ; Humans ; Models, Biological ; Proteins/chemistry/genetics/metabolism/*physiology ; *Sequence Homology, Amino Acid ; *Sequence Homology, Nucleic Acid ; Thermodynamics
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-03
    Description: Cdc13 and Est1 are single-strand telomeric DNA binding proteins that contribute to telomere replication in the yeast Saccharomyces cerevisiae. Here it is shown that fusion of Cdc13 to the telomerase-associated Est1 protein results in greatly elongated telomeres. Fusion proteins consisting of mutant versions of Cdc13 or Est1 confer similar telomere elongation, indicating that close physical proximity can bypass telomerase-defective mutations in either protein. Fusing Cdc13 directly to the catalytic core of telomerase allows stable telomere maintenance in the absence of Est1, consistent with a role for Est1 in mediating telomerase access. Telomere length homeostasis therefore is maintained in part by restricting access of telomerase to chromosome termini, but this limiting situation can be overcome by directly tethering telomerase to the telomere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, S K -- Lundblad, V -- R01GM55867/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Oct 1;286(5437):117-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics, 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/10506558" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cyclin B/genetics/*metabolism ; DNA, Fungal/metabolism ; DNA, Single-Stranded/metabolism ; Fungal Proteins/genetics/*metabolism ; Genetic Complementation Test ; Homeostasis ; Models, Biological ; Mutation ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/*metabolism ; Telomere/*metabolism
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-06-18
    Description: The enhanced aerodynamic performance of insects results from an interaction of three distinct yet interactive mechanisms: delayed stall, rotational circulation, and wake capture. Delayed stall functions during the translational portions of the stroke, when the wings sweep through the air with a large angle of attack. In contrast, rotational circulation and wake capture generate aerodynamic forces during stroke reversals, when the wings rapidly rotate and change direction. In addition to contributing to the lift required to keep an insect aloft, these two rotational mechanisms provide a potent means by which the animal can modulate the direction and magnitude of flight forces during steering maneuvers. A comprehensive theory incorporating both translational and rotational mechanisms may explain the diverse patterns of wing motion displayed by different species of insects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickinson, M H -- Lehmann, F O -- Sane, S P -- New York, N.Y. -- Science. 1999 Jun 18;284(5422):1954-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Biology, University of California, Berkeley, CA 94720, USA. flymannd@socrates.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10373107" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biomechanical Phenomena ; Drosophila melanogaster/*physiology ; Flight, Animal/*physiology ; Kinetics ; Models, Biological ; Movement ; Robotics ; Rotation ; Wings, Animal/*physiology
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-06-12
    Description: Conventional cladistic methods of inferring evolutionary relationships exclude temporal data from the initial search for optimal hypotheses, but stratocladistics includes such data. A comparison of the ability of these methods to recover known, simulated evolutionary histories given the same, evolved character data shows that stratocladistics recovers the true phylogeny in over twice as many cases as cladistics (42 versus 18 percent). The comparison involved 550 unique taxon-by-character matrices, representing 15 evolutionary models and fossil records ranging from 100 to 10 percent complete.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, D L -- Fisher, D C -- Leighton, L R -- New York, N.Y. -- Science. 1999 Jun 11;284(5421):1816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museum of Paleontology, University of Michigan, 1109 Geddes Road, Ann Arbor, MI 48109-1079, USA. dlfox@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10364549" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Computer Simulation ; Fossils ; Models, Biological ; *Phylogeny ; Probability ; Software
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerstein, M -- Chothia, C -- New York, N.Y. -- Science. 1999 Sep 10;285(5434):1682-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biophysics and Biochemistry Department, 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/10523185" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/metabolism ; Bacterial Physiological Phenomena ; Bacteriorhodopsins/chemistry/metabolism ; Binding Sites ; Cell Membrane/chemistry/*metabolism ; Chemotaxis ; Crystallography, X-Ray ; Dimerization ; Electron Spin Resonance Spectroscopy ; Membrane Proteins/chemistry/metabolism ; Models, Biological ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Amino Acid/*chemistry/*metabolism ; Receptors, Nicotinic/chemistry/metabolism ; *Signal Transduction ; Solubility
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tiedemann, R -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1550-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411772" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Elephants/*anatomy & histology/*physiology ; Female ; Incisor/anatomy & histology ; India ; Male ; Models, Biological ; Models, Statistical ; *Sexual Behavior, Animal ; Sri Lanka
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillis, D M -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):218-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin, TX 78712 USA. hillis@bull.zo.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9132943" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Humans ; Likelihood Functions ; Models, Biological ; *Phylogeny ; Software
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riezman, H -- New York, N.Y. -- Science. 1997 Dec 5;278(5344):1728-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum of the University of Basel, Basel, Switzerland. riezman@ubaclu.unibas.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411792" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Carrier Proteins/chemistry/genetics/*metabolism ; Cysteine Endopeptidases/*metabolism ; Cytoplasm/metabolism ; Endoplasmic Reticulum/*metabolism ; Fungal Proteins/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; *Heat-Shock Proteins ; Ligases/metabolism ; Membrane Proteins/chemistry/genetics/*metabolism ; *Membrane Transport Proteins ; Models, Biological ; Multienzyme Complexes/*metabolism ; Proteasome Endopeptidase Complex ; *Protein Folding ; Proteins/chemistry/*metabolism ; Ribosomes/metabolism ; *Saccharomyces cerevisiae Proteins ; *Ubiquitin-Conjugating Enzymes ; Ubiquitins/*metabolism ; Yeasts/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867655" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Biological Evolution ; Computer Simulation ; DNA, Mitochondrial/*genetics ; Dolphins/genetics/physiology ; Female ; *Genetic Variation ; Models, Biological ; Reproduction ; *Vocalization, Animal ; Whales/*genetics/physiology
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  • 41
    Publication Date: 1998-12-16
    Description: The trophoblast cell lineage is essential for the survival of the mammalian embryo in utero. This lineage is specified before implantation into the uterus and is restricted to form the fetal portion of the placenta. A culture of mouse blastocysts or early postimplantation trophoblasts in the presence of fibroblast growth factor 4 (FGF4) permitted the isolation of permanent trophoblast stem cell lines. These cell lines differentiated to other trophoblast subtypes in vitro in the absence of FGF4 and exclusively contributed to the trophoblast lineage in vivo in chimeras.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, S -- Kunath, T -- Hadjantonakis, A K -- Nagy, A -- Rossant, J -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2072-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851926" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/cytology ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Lineage ; Chimera ; Culture Media, Conditioned ; Embryo, Mammalian/cytology ; Female ; Fibroblast Growth Factor 4 ; Fibroblast Growth Factors/*pharmacology/physiology ; Fibroblasts/cytology ; Gene Expression Regulation, Developmental ; Genetic Markers ; Karyotyping ; Male ; Mice ; Models, Biological ; Proto-Oncogene Proteins/*pharmacology/physiology ; Signal Transduction ; Stem Cells/*cytology/metabolism ; Trophoblasts/*cytology/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elledge, S J -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):999-1000.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, Baylor College of Medicine, Housteon, TX 77030, USA. selledge@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9490488" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Calcium-Binding Proteins/*metabolism ; Carrier Proteins/*metabolism ; Cdc20 Proteins ; Cell Cycle Proteins/antagonists & inhibitors/metabolism ; Fungal Proteins/antagonists & inhibitors/*metabolism ; Ligases/*metabolism ; Mad2 Proteins ; *Mitosis ; Models, Biological ; Nuclear Proteins/metabolism ; Saccharomyces cerevisiae/cytology/metabolism ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/metabolism ; *Schizosaccharomyces pombe Proteins ; Securin ; Spindle Apparatus/*metabolism ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-06-11
    Description: The subunit stoichiometry of several ligand-gated ion channel receptors is still unknown. A counting method was developed to determine the number of subunits in one family of brain glutamate receptors. Successful application of this method in an HEK cell line provides evidence that ionotropic glutamate receptors share a tetrameric structure with the voltage-gated potassium channels. The average conductance of these channels depends on how many subunits are occupied by an agonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenmund, C -- Stern-Bach, Y -- Stevens, C F -- NS 12961/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Workgroup Cellular Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616121" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cell Line ; Electric Conductivity ; Excitatory Amino Acid Agonists/metabolism ; Excitatory Amino Acid Antagonists/metabolism ; Humans ; Ligands ; Macromolecular Substances ; Models, Biological ; Patch-Clamp Techniques ; Quinoxalines/metabolism ; Quisqualic Acid/metabolism ; Receptors, AMPA/agonists/antagonists & inhibitors/*chemistry/*metabolism ; Receptors, Glutamate/chemistry/metabolism ; Receptors, Kainic Acid/agonists/antagonists & inhibitors/*chemistry/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, A M -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2201-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina at Chapel Hill 27599-3280, USA. alan_jones@unc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9890827" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/metabolism ; *Arabidopsis Proteins ; Biological Transport ; Carrier Proteins/*genetics/metabolism ; Genes, Plant ; Indoleacetic Acids/*metabolism ; Membrane Proteins/chemistry/*genetics ; *Membrane Transport Proteins ; Models, Biological ; Plant Roots/metabolism ; Plant Shoots/metabolism ; Plants/genetics/*metabolism ; Proton-Motive Force
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-02-07
    Description: In the past few years genetic, biochemical, and cytolocalization data have implicated members of the myosin superfamily of actin-based molecular motors in a variety of cellular functions including membrane trafficking, cell movements, and signal transduction. The importance of myosins is illustrated by the identification of myosin genes as targets for disease-causing mutations. The task at hand is to decipher how the multitude of myosins function at both the molecular and cellular level-a task facilitated by our understanding of myosin structure and function in muscle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mermall, V -- Post, P L -- Mooseker, M S -- DK25387/DK/NIDDK NIH HHS/ -- DK38979/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 23;279(5350):527-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University 342 KBT, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9438839" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*metabolism ; *Cell Movement ; Hearing ; Humans ; Models, Biological ; Mutation ; Myosins/chemistry/genetics/*physiology ; Organelles/*physiology ; *Signal Transduction ; Vision, Ocular
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-12-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werb, Z -- Yan, Y -- CA72006/CA/NCI NIH HHS/ -- HD26732/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1279-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of California, San Francisco, CA 94143-0452, USA. zena@itsa.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9867633" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Animals ; Catalytic Domain ; Cell Adhesion Molecules/metabolism ; Cell Membrane/*metabolism ; Growth Substances/metabolism ; L-Selectin/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/chemistry/*metabolism ; Mice ; Models, Biological ; Receptor, Epidermal Growth Factor/metabolism ; Tumor Necrosis Factor-alpha/*metabolism
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  • 47
    Publication Date: 1998-09-04
    Description: Microscopy shows that individual sites of DNA replication and transcription of mammalian nuclei segregate into sets of roughly 22 and 16 higher order domains, respectively. Each domain set displayed a distinct network-like appearance, including regions of individual domains and interdigitation of domains between the two networks. These data support a dynamic mosaic model for the higher order arrangement of genomic function inside the cell nuclei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wei, X -- Samarabandu, J -- Devdhar, R S -- Siegel, A J -- Acharya, R -- Berezney, R -- GM 23922/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1502-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727975" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Cell Line ; Cell Nucleolus/metabolism/ultrastructure ; Cell Nucleus/*metabolism/ultrastructure ; *DNA Replication ; *Genome ; Genome, Human ; Humans ; Image Processing, Computer-Assisted ; Mice ; Microscopy, Confocal ; Models, Biological ; S Phase ; *Transcription, Genetic
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-01-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Featherstone, C -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2172-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9890821" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Biology/history ; Coated Vesicles/metabolism ; Coatomer Protein ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/*physiology/*ultrastructure ; History, 20th Century ; Membrane Proteins/metabolism ; Microscopy, Electron ; Models, Biological ; Protein Processing, Post-Translational ; Proteins/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-11-30
    Description: Low diversities of mitochondrial DNA (mtDNA) have recently been found in four species of matrilineal whale. No satisfactory explanation for this apparent anomaly has been previously suggested. Culture seems to be an important part of the lives of matrilineal whales. The selection of matrilineally transmitted cultural traits, upon which neutral mtDNA alleles "hitchhike," has the potential to strongly reduce genetic variation. Thus, in contrast to other nonhuman mammals, culture may be an important evolutionary force for the matrilineal whales.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitehead, H -- New York, N.Y. -- Science. 1998 Nov 27;282(5394):1708-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4J1. hwhitehe@is.dal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9831562" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Biological Evolution ; Computer Simulation ; DNA, Mitochondrial/*genetics ; Dolphins/genetics/physiology ; Female ; *Genetic Variation ; Models, Biological ; Selection, Genetic ; *Vocalization, Animal ; Whales/*genetics/physiology
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  • 50
    Publication Date: 1998-10-02
    Description: To better understand the dynamics of hepatitis C virus and the antiviral effect of interferon-alpha-2b (IFN), viral decline in 23 patients during therapy was analyzed with a mathematical model. The analysis indicates that the major initial effect of IFN is to block virion production or release, with blocking efficacies of 81, 95, and 96% for daily doses of 5, 10, and 15 million international units, respectively. The estimated virion half-life (t1/2) was, on average, 2.7 hours, with pretreatment production and clearance of 10(12) virions per day. The estimated infected cell death rate exhibited large interpatient variation (corresponding t1/2 = 1.7 to 70 days), was inversely correlated with baseline viral load, and was positively correlated with alanine aminotransferase levels. Fast death rates were predictive of virus being undetectable by polymerase chain reaction at 3 months. These findings show that infection with hepatitis C virus is highly dynamic and that early monitoring of viral load can help guide therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, A U -- Lam, N P -- Dahari, H -- Gretch, D R -- Wiley, T E -- Layden, T J -- Perelson, A S -- A1/DK41320-2/DK/NIDDK NIH HHS/ -- A139049-2/PHS HHS/ -- RR06555/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):103-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9756471" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine Transaminase/blood ; Antiviral Agents/administration & dosage/*therapeutic use ; Cell Death ; Dose-Response Relationship, Drug ; Half-Life ; Hepacivirus/*physiology ; Hepatitis C/immunology/*therapy/*virology ; Humans ; Interferon-alpha/administration & dosage/*therapeutic use ; Kinetics ; Models, Biological ; RNA, Viral/blood ; Recombinant Proteins ; Regression Analysis ; Viral Load ; Viremia/virology ; Virion/physiology ; Virus Replication
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  • 51
    Publication Date: 1998-03-21
    Description: Studies of lymphocyte turnover in animal models have implications for understanding the mechanism of cell killing and the extent of lymphocyte regeneration in human immunodeficiency virus infection. Quantitative analyses of the sequential changes in bromodeoxyuridine labeling of CD4 and CD8 T lymphocytes not only revealed the normal proliferation and death rates of these cell populations in uninfected macaques, but also showed a substantial increase in these rates associated with simian immunodeficiency virus (SIV) infection. Faster labeling and delabeling in memory and naive T lymphocyte subpopulations as well as in NK (natural killer) and B cells were also observed in infected macaques, suggesting a state of generalized activation induced by SIV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mohri, H -- Bonhoeffer, S -- Monard, S -- Perelson, A S -- Ho, D D -- AI40387/AI/NIAID NIH HHS/ -- AI41534/AI/NIAID NIH HHS/ -- AI45128/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1223-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, The Rockefeller University, 455 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469816" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bromodeoxyuridine/metabolism ; CD4 Lymphocyte Count ; CD4-Positive T-Lymphocytes/*immunology/pathology ; CD8-Positive T-Lymphocytes/*immunology/pathology ; Cell Death ; Cell Division ; Humans ; Kinetics ; Lymphocyte Activation ; Lymphocyte Count ; Macaca mulatta ; Mathematics ; Models, Biological ; Regression Analysis ; Simian Acquired Immunodeficiency Syndrome/*immunology/virology ; Simian Immunodeficiency Virus/physiology ; T-Lymphocyte Subsets/*immunology/pathology ; Viral Load
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):476-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biology ; Computer Simulation ; Game Theory ; Humans ; Models, Biological
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-09-05
    Description: Arrest of the cell cycle at the G2 checkpoint, induced by DNA damage, requires inhibitory phosphorylation of the kinase Cdc2 in both fission yeast and human cells. The kinase Wee1 and the phosphatase Cdc25, which regulate Cdc2 phosphorylation, were evaluated as targets of Chk1, a kinase essential for the checkpoint. Fission yeast cdc2-3w Deltacdc25 cells, which express activated Cdc2 and lack Cdc25, were responsive to Wee1 but insensitive to Chk1 and irradiation. Expression of large amounts of Chk1 produced the same phenotype as did loss of the cdc25 gene in cdc2-3w cells. Cdc25 associated with Chk1 in vivo and was phosphorylated when copurified in Chk1 complexes. These findings identify Cdc25, but not Wee1, as a target of the DNA damage checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furnari, B -- Rhind, N -- Russell, P -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278510" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/*metabolism ; Cell Division ; *DNA Damage ; DNA Helicases/metabolism ; Fungal Proteins/*metabolism ; G2 Phase ; Gamma Rays ; Genes, Fungal ; *Mitosis ; Models, Biological ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/genetics/*metabolism/radiation effects ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Temperature ; *ras-GRF1
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunlap, J -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1548-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA. jay.c.dunlap@dartmouth.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9644021" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks ; CLOCK Proteins ; Circadian Rhythm/genetics/*physiology ; Dimerization ; *Drosophila Proteins ; Feedback ; Insect Proteins/genetics/*metabolism ; Models, Biological ; Nuclear Proteins/genetics/*metabolism ; Period Circadian Proteins ; Promoter Regions, Genetic ; RNA, Messenger/genetics/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/*metabolism ; Transcriptional Activation
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  • 55
    Publication Date: 1998-09-04
    Description: Cyanobacteria are the simplest organisms known to have a circadian clock. A circadian clock gene cluster kaiABC was cloned from the cyanobacterium Synechococcus. Nineteen clock mutations were mapped to the three kai genes. Promoter activities upstream of the kaiA and kaiB genes showed circadian rhythms of expression, and both kaiA and kaiBC messenger RNAs displayed circadian cycling. Inactivation of any single kai gene abolished these rhythms and reduced kaiBC-promoter activity. Continuous kaiC overexpression repressed the kaiBC promoter, whereas kaiA overexpression enhanced it. Temporal kaiC overexpression reset the phase of the rhythms. Thus, a negative feedback control of kaiC expression by KaiC generates a circadian oscillation in cyanobacteria, and KaiA sustains the oscillation by enhancing kaiC expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ishiura, M -- Kutsuna, S -- Aoki, S -- Iwasaki, H -- Andersson, C R -- Tanabe, A -- Golden, S S -- Johnson, C H -- Kondo, T -- MH01179/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 4;281(5382):1519-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. ishiura@bio.nagoya-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9727980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Biological Clocks/*genetics ; Circadian Rhythm/*genetics ; Circadian Rhythm Signaling Peptides and Proteins ; Cloning, Molecular ; Cyanobacteria/*genetics/physiology ; Feedback ; *Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genes, Reporter ; Luminescence ; Models, Biological ; Molecular Sequence Data ; Multigene Family ; Mutation ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Transcription, Genetic
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steneck, Robert S -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):480-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Marine Sciences, University of Maine, Darling Marine Center, Walpole, ME 04573, USA. steneck@maine.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; Caribbean Region ; Computer Simulation ; Conservation of Natural Resources ; *Ecosystem ; Fishes/growth & development/*physiology ; Larva/physiology ; Models, Biological ; Population Dynamics ; *Seawater ; *Swimming ; Water Movements
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-13
    Description: The replication of many viruses is associated with specific intracellular compartments called virus factories or virioplasm. These are thought to provide a physical scaffold to concentrate viral components and thereby increase the efficiency of replication. The formation of virus replication sites often results in rearrangement of cellular membranes and reorganization of the cytoskeleton. Similar rearrangements are seen in cells in response to protein aggregation, where aggresomes and autophagosomes are produced to facilitate protein degradation. Here I review the evidence that some viruses induce aggresomes and autophagosomes to generate sites of replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wileman, Thomas -- New York, N.Y. -- Science. 2006 May 12;312(5775):875-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Medicine, Health Policy and Practice, University of East Anglia, Norwich NR4 7TJ, UK. t.wileman@uea.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690857" target="_blank"〉PubMed〈/a〉
    Keywords: *Autophagy ; Cell Membrane Structures/ultrastructure/virology ; Cell Nucleus/ultrastructure/virology ; Cell Nucleus Structures/ultrastructure/virology ; Cytoplasmic Vesicles/physiology/ultrastructure/*virology ; DNA Viruses/*physiology ; Models, Biological ; Phagosomes/physiology/*virology ; Proteins/metabolism ; RNA Viruses/*physiology ; *Virus Replication
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  • 58
    Publication Date: 2006-10-21
    Description: Dey and Joshi (Reports, 21 April 2006, p. 434) studied replicate laboratory populations of Drosophila and reported that low migration led to asynchrony among subpopulations. We argue that this unexpected outcome may be due to variation in the initial size of the subpopulations and uncontrolled stochasticity in the experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranta, Esa -- Kaitala, Veijo -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):420; author reply 420.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrative Ecology Unit, Department of Biological and Environmental Sciences, P.O. Box 65 (Viikinkaari 1), FIN-00014 University of Helsinki, Finland. esa.ranta@helsinki.fi〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053132" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Computer Simulation ; Drosophila melanogaster/*physiology ; Models, Biological ; Population Dynamics ; Population Growth ; Stochastic Processes
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  • 59
    Publication Date: 2006-04-22
    Description: Given the considerable challenges to the rapid development of an effective vaccine against influenza, antiviral agents will play an important role as a first-line defense if a new pandemic occurs. The large-scale use of drugs for chemoprophylaxis and treatment will impose strong selection for the evolution of drug-resistant strains. The ensuing transmission of those strains could substantially limit the effectiveness of the drugs as a first-line defense. Summarizing recent data on the rate at which the treatment of influenza infection generates resistance de novo and on the transmission fitness of resistant virus, we discuss possible implications for the epidemiological spread of drug resistance in the context of an established population dynamic model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regoes, Roland R -- Bonhoeffer, Sebastian -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):389-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Integrative Biology, ETH Zurich, ETH Zentrum CHN K12.1, Universitatsstrasse 16, CH 8092 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627735" target="_blank"〉PubMed〈/a〉
    Keywords: Acetamides/pharmacology/therapeutic use ; Amantadine/pharmacology/therapeutic use ; Antiviral Agents/*pharmacology/*therapeutic use ; Computer Simulation ; Disease Outbreaks ; *Drug Resistance, Viral/genetics ; Humans ; Influenza A virus/*drug effects/genetics/pathogenicity ; Influenza, Human/*drug therapy/epidemiology/*prevention & control/virology ; Mathematics ; Models, Biological ; Mutation ; Neuraminidase/antagonists & inhibitors ; Orthomyxoviridae/*drug effects/genetics/pathogenicity ; Oseltamivir ; Population Dynamics
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brasaemle, Dawn L -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1581-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Nutritional Sciences, Rutgers, State University of New Jersey, New Brunswick, NJ 08901, USA. brasaemle@aesop.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973864" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Caveolae/metabolism ; Caveolin 1/genetics/*physiology ; Cell Cycle ; Cell Membrane/metabolism ; Cell Proliferation ; Fatty Acids/metabolism ; Glucose/administration & dosage ; Hepatocytes/cytology/*metabolism ; Hydrolysis ; *Lipid Metabolism ; *Liver Regeneration ; Mice ; Models, Biological ; Phospholipids/biosynthesis ; Triglycerides/metabolism
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: Long-distance dispersal (LDD) of plants poses challenges to research because it involves rare events driven by complex and highly stochastic processes. The current surge of renewed interest in LDD, motivated by growing recognition of its critical importance for natural populations and communities and for humanity, promises an improved, quantitatively derived understanding of LDD. To gain deep insights into the patterns, mechanisms, causes, and consequences of LDD, we must look beyond the standard dispersal vectors and the mean trend of the distribution of dispersal distances. "Nonstandard" mechanisms such as extreme climatic events and generalized LDD vectors seem to hold the greatest explanatory power for the drastic deviations from the mean trend, deviations that make the nearly impossible LDD a reality.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathan, Ran -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):786-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Movement Ecology Laboratory, Department of Evolution, Systematics and Ecology, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Givat Ram, 91904 Jerusalem, Israel. rnathan@cc.huji.ac.il〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902126" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; *Ecosystem ; *Environment ; Humans ; Models, Biological ; *Plants ; Pollen ; Population Dynamics ; Probability ; *Seeds ; Selection, Genetic ; Stochastic Processes ; Water Movements ; *Weather ; Wind
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  • 62
    Publication Date: 2006-03-18
    Description: During development, cells monitor and adjust their rates of accumulation to produce organs of predetermined size. We show here that central nervous system-specific deletion of the essential adherens junction gene, alphaE-catenin, causes abnormal activation of the hedgehog pathway, resulting in shortening of the cell cycle, decreased apoptosis, and cortical hyperplasia. We propose that alphaE-catenin connects cell-density-dependent adherens junctions with the developmental hedgehog pathway and that this connection may provide a negative feedback loop controlling the size of developing cerebral cortex.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2556178/" 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/PMC2556178/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lien, Wen-Hui -- Klezovitch, Olga -- Fernandez, Tania E -- Delrow, Jeff -- Vasioukhin, Valeri -- P41 RR011823/RR/NCRR NIH HHS/ -- P41 RR011823-128171/RR/NCRR NIH HHS/ -- R01 CA098161/CA/NCI NIH HHS/ -- R01 CA098161-01A1/CA/NCI NIH HHS/ -- R01 CA098161-02/CA/NCI NIH HHS/ -- R01 CA098161-03/CA/NCI NIH HHS/ -- R01 CA098161-04/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 17;311(5767):1609-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16543460" target="_blank"〉PubMed〈/a〉
    Keywords: Adherens Junctions/*physiology/ultrastructure ; Animals ; Apoptosis ; Cell Adhesion ; Cell Count ; Cell Cycle ; Cell Differentiation ; Cell Polarity ; Central Nervous System/embryology ; Cerebral Cortex/cytology/*embryology/pathology/physiology ; Hedgehog Proteins ; Hyperplasia ; Mice ; Mitosis ; Models, Biological ; Mutation ; Neurons/cytology/*physiology/ultrastructure ; Oligonucleotide Array Sequence Analysis ; *Signal Transduction ; Stem Cells/cytology/ultrastructure ; Trans-Activators/*metabolism ; Up-Regulation ; alpha Catenin/genetics/*physiology
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neels, Jaap G -- Olefsky, Jerrold M -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1756-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0673, USA. jolefsky@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794069" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl-CoA Carboxylase/antagonists & inhibitors/*metabolism ; Adipocytes/metabolism ; Adipose Tissue/*metabolism ; Animals ; Cell Cycle Proteins/*metabolism ; Energy Intake ; Energy Metabolism ; Enzyme Activation ; Fasting ; Fatty Acids/metabolism ; Hepatocytes/metabolism ; Insulin/physiology ; Insulin Resistance ; *Lipid Metabolism ; Lipogenesis ; Liver/metabolism ; Malonyl Coenzyme A/metabolism ; Mice ; Models, Biological ; Nuclear Proteins/*metabolism ; Obesity/therapy ; Oxidation-Reduction ; Phosphorylation ; Proto-Oncogene Proteins c-akt/antagonists & inhibitors/metabolism ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/*metabolism
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  • 64
    Publication Date: 2006-08-19
    Description: Eukaryotic flagella and cilia are built on a 9 + 2 array of microtubules plus 〉250 accessory proteins, forming a biological machine called the axoneme. Here we describe the three-dimensional structure of rapidly frozen axonemes from Chlamydomonas and sea urchin sperm, using cryoelectron tomography and image processing to focus on the motor enzyme dynein. Our images suggest a model for the way dynein generates force to slide microtubules. They also reveal two dynein linkers that may provide "hard-wiring" to coordinate motor enzyme action, both circumferentially and along the axoneme. Periodic densities were also observed inside doublet microtubules; these may contribute to doublet stability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nicastro, Daniela -- Schwartz, Cindi -- Pierson, Jason -- Gaudette, Richard -- Porter, Mary E -- McIntosh, J Richard -- 2R37-GM55667/GM/NIGMS NIH HHS/ -- RR 000592/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):944-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for 3D Electron Microscopy of Cells, Department of Molecular, Cellular, and Developmental Biology, CB 347, University of Colorado, Boulder, CO 80309-0347, USA. nicastro@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917055" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/chemistry/ultrastructure ; Chlamydomonas reinhardtii/ultrastructure ; Cryoelectron Microscopy ; Dyneins/*chemistry/physiology/*ultrastructure ; Flagella/chemistry/physiology/*ultrastructure ; Freezing ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Male ; Microtubule-Associated Proteins ; Microtubules/chemistry/physiology/*ultrastructure ; Models, Biological ; Molecular Motor Proteins/chemistry/ultrastructure ; Protein Structure, Tertiary ; Sea Urchins ; Sperm Tail/chemistry/physiology/*ultrastructure ; Tomography
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  • 65
    Publication Date: 2006-04-22
    Description: Very few experimental studies have examined how migration rate affects metapopulation dynamics and stability. We studied the dynamics of replicate laboratory metapopulations of Drosophila under different migration rates. Low migration stabilized metapopulation dynamics, while promoting unstable subpopulation dynamics, by inducing asynchrony among neighboring subpopulations. High migration synchronized subpopulation dynamics, thereby destabilizing the metapopulations. Contrary to some theoretical predictions, increased migration did not affect average population size. Simulations based on a simple non-species-specific population growth model captured most features of the data, which suggests that our results are generalizable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dey, Sutirth -- Joshi, Amitabh -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):434-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Evolutionary Biology Laboratory, Evolutionary & Organismal Biology Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur P.O., Bangalore 560 064, India.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627743" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Computer Simulation ; Drosophila melanogaster/*physiology ; Models, Biological ; Population Density ; Population Dynamics ; Population Growth
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  • 66
    Publication Date: 2006-02-25
    Description: Sibly et al. (Reports, 22 July 2005, p. 607) recently estimated the relationship between population size and growth rate for 1780 time series of various species. I explain why some aspects of their analysis are questionable and, therefore, why their results and estimation procedure should be used with care.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, Joshua V -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1100; author reply 1100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Mathematics, University of Queensland, St. Lucia, QLD 4072, Australia. jvr@maths.uq.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497916" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Birds ; Conservation of Natural Resources ; Ecosystem ; *Fishes ; *Insects ; Logistic Models ; *Mammals ; Mathematics ; Models, Biological ; Population Density ; Population Dynamics ; Population Growth ; Regression Analysis
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Linden, Joel -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1689-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Virginia, Charlottesville, VA 22908, USA. jlinden@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170280" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/metabolism ; Adenosine Monophosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Animals ; Apyrase/pharmacology ; *Autocrine Communication ; Blood Platelets/metabolism ; Cell Membrane/metabolism ; *Chemotaxis, Leukocyte/drug effects ; Endothelial Cells/metabolism ; Mice ; Models, Biological ; N-Formylmethionine Leucyl-Phenylalanine ; Neutrophils/drug effects/*metabolism/physiology ; Receptor, Adenosine A3/metabolism ; Receptors, Purinergic/*metabolism ; Receptors, Purinergic P2/metabolism ; Receptors, Purinergic P2Y2 ; Respiratory Burst/drug effects ; Signal Transduction
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  • 68
    Publication Date: 2006-12-13
    Description: Mounting evidence has revealed pathological interactions between HIV and malaria in dually infected patients, but the public health implications of the interplay have remained unclear. A transient almost one-log elevation in HIV viral load occurs during febrile malaria episodes; in addition, susceptibility to malaria is enhanced in HIV-infected patients. A mathematical model applied to a setting in Kenya with an adult population of roughly 200,000 estimated that, since 1980, the disease interaction may have been responsible for 8,500 excess HIV infections and 980,000 excess malaria episodes. Co-infection might also have facilitated the geographic expansion of malaria in areas where HIV prevalence is high. Hence, transient and repeated increases in HIV viral load resulting from recurrent co-infection with malaria may be an important factor in promoting the spread of HIV in sub-Saharan Africa.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abu-Raddad, Laith J -- Patnaik, Padmaja -- Kublin, James G -- P30 AI 27757/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1603-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Statistical Center for HIV/AIDS Research and Prevention, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA. laith@scharp.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158329" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Africa South of the Sahara/epidemiology ; Antimalarials/therapeutic use ; Disease Susceptibility ; Endemic Diseases ; Female ; HIV Infections/*complications/*epidemiology/transmission/virology ; HIV-1/physiology ; Humans ; Kenya/epidemiology ; Malaria, Falciparum/*complications/drug therapy/*epidemiology/transmission ; Male ; Mathematics ; Models, Biological ; Prevalence ; Recurrence ; Sexual Behavior ; Viral Load ; Viremia ; Virus Replication
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  • 69
    Publication Date: 2006-03-11
    Description: A biosynthetic approach was developed to control and probe cooperativity in multiunit biomotor assemblies by linking molecular motors to artificial protein scaffolds. This approach provides precise control over spatial and elastic coupling between motors. Cooperative interactions between monomeric kinesin-1 motors attached to protein scaffolds enhance hydrolysis activity and microtubule gliding velocity. However, these interactions are not influenced by changes in the elastic properties of the scaffold, distinguishing multimotor transport from that powered by unorganized monomeric motors. These results highlight the role of supramolecular architecture in determining mechanisms of collective transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diehl, Michael R -- Zhang, Kechun -- Lee, Heun Jin -- Tirrell, David A -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1468-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. diehl@rice.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527982" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry ; Amino Acid Sequence ; Elasticity ; Elastin/chemistry ; Hydrolysis ; Kinesin/chemistry ; Microtubules/physiology ; Models, Biological ; Molecular Motor Proteins/*physiology ; Molecular Sequence Data ; Protein Engineering ; Protein Structure, Tertiary ; Proteins/chemistry/*physiology ; Recombinant Proteins/chemistry ; Structure-Activity Relationship
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-25
    Description: Bacteria use diverse small molecules for extra- and intracellular signaling. They scan small-molecule mixtures to access information about both their extracellular environment and their intracellular physiological status, and based on this information, they continuously interpret their circumstances and react rapidly to changes. Bacteria must integrate extra- and intracellular signaling information to mount appropriate responses to changes in their environment. We review recent research into two fundamental bacterial small-molecule signaling pathways: extracellular quorum-sensing signaling and intracellular cyclic dinucleotide signaling. We suggest how these two pathways may converge to control complex processes including multicellularity, biofilm formation, and virulence. We also outline new questions that have arisen from recent studies in these fields.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2776824/" 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/PMC2776824/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camilli, Andrew -- Bassler, Bonnie L -- R01 AI045746/AI/NIAID NIH HHS/ -- R01 AI045746-04/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, 136 Harrison Avenue, Boston, MA 02111-1817, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497924" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Butyrolactone/*analogs & derivatives/metabolism ; *Bacterial Physiological Phenomena ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Cyclic GMP/*analogs & derivatives/metabolism ; Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Homoserine/*analogs & derivatives/metabolism ; Lactones/*metabolism ; Models, Biological ; Oligopeptides/metabolism ; Phosphoric Diester Hydrolases/metabolism ; Phosphorus-Oxygen Lyases/metabolism ; Purine Nucleotides/metabolism ; Quinolones/metabolism ; Second Messenger Systems ; *Signal Transduction ; Virulence/genetics
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  • 71
    Publication Date: 2006-09-23
    Description: Vandermeer and Perfecto (Reports, 17 February 2006, p. 1000) reported a general power law pattern in the distribution of a common agricultural pest. However, there is an exact analytical solution for the expected cluster distribution under the proposed null model of density-independent growth in a patchy landscape. Reanalysis of the data shows that the system is not in a critical state but confirms the importance of a mutualism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alonso, David -- Pascual, Mercedes -- New York, N.Y. -- Science. 2006 Sep 22;313(5794):1739; author reply 1739.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecology and Evolutionary Biology, University of Michigan, 830 North University Avenue, Ann Arbor, MI 48109-1048, USA. dalonso@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16990534" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ants/*physiology ; *Coffea ; *Ecosystem ; Hemiptera/*physiology ; Mathematics ; Models, Biological ; Population Density ; Population Growth ; Probability ; *Symbiosis
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-07-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szathmary, Eors -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):306-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biology, Eotvos University Budapest, and Collegium Budapest (Institute for Advanced Study), 2 Szentharomsag utca, H-1014 Budapest, Hungary. szathmary@colbud.hu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857926" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Chemical Phenomena ; Chemistry ; Computational Biology ; Cooperative Behavior ; Cultural Evolution ; Exobiology ; Humans ; Language ; Models, Biological ; Models, Theoretical ; Molecular Biology ; Origin of Life ; *Research ; Selection, Genetic
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Irene A -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1558-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Health Sciences and Technology at Harvard Medical School and Massachusetts Institute of Technology, Boston, MA 02115, USA. ichen@post.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158315" target="_blank"〉PubMed〈/a〉
    Keywords: Awards and Prizes ; *Biological Evolution ; *Cells ; Hydrogen-Ion Concentration ; Lipid Bilayers ; *Liposomes/chemistry ; Models, Biological ; *Origin of Life ; Osmotic Pressure ; *Rna ; RNA, Catalytic
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  • 74
    Publication Date: 2006-04-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, Anthony W -- Gunderson, Carla A -- Post, Wilfred M -- Weston, David J -- Wullschleger, Stan D -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):536-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Environmental Sciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA. kingaw@ornl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645083" target="_blank"〉PubMed〈/a〉
    Keywords: *Acclimatization ; Atmosphere ; Carbon/*metabolism ; Carbon Dioxide/metabolism ; *Climate ; Computer Simulation ; Ecosystem ; Mathematics ; Models, Biological ; *Oxygen Consumption ; Plant Leaves/*metabolism ; Soil/analysis ; *Temperature
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  • 75
    Publication Date: 2006-02-04
    Description: Latimer et al. (Reports, 9 September 2005, p. 1722) used an approximate likelihood function to estimate parameters of Hubbell's neutral model of biodiversity. Reanalysis with the exact likelihood not only yields different estimates but also shows that two similar likelihood maxima for very different parameter combinations can occur. This reveals a limitation of using species abundance data to gain insight into speciation and dispersal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Etienne, Rampal S -- Latimer, Andrew M -- Silander, John A Jr -- Cowling, Richard M -- New York, N.Y. -- Science. 2006 Feb 3;311(5761):610.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Community and Conservation Ecology Group, University of Groningen, Box 14, 9750 AA Haren, The Netherlands. r.s.etienne@rug.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16456064" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bayes Theorem ; *Biodiversity ; *Ecology ; Ecosystem ; *Genetic Speciation ; Likelihood Functions ; Models, Biological ; *Plants/classification/genetics ; South Africa
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-08-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):779-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902122" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Migration ; Animals ; Behavior, Animal ; Computer Simulation ; *Ecology ; Flight, Animal ; Humans ; Models, Biological ; *Movement ; Plant Physiological Phenomena ; Population Dynamics ; Wind
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartek, Jiri -- Lukas, Jiri -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):261-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Biology and Centre for Genotoxic Stress Research, Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen, Denmark. jb@cancer.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038611" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; BRCA2 Protein/metabolism ; Cell Cycle ; Cell Nucleus/metabolism ; Cell Survival ; Cyclin-Dependent Kinase 2/antagonists & inhibitors/*metabolism ; *DNA Damage ; DNA Repair ; DNA Replication ; Forkhead Transcription Factors/*metabolism ; Gene Expression Regulation ; Humans ; Mice ; Models, Biological ; Phosphorylation ; RNA, Small Interfering ; Transcription, Genetic ; cdc25 Phosphatases/metabolism
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  • 78
    Publication Date: 2007-04-07
    Description: Pleckstrin homology (PH) domain-mediated protein recruitment to cellular membranes is of paramount importance for signal transduction. The recruitment of many PH domains is controlled through production and turnover of their membrane ligand, phosphatidylinositol 3,4,5-trisphosphate (PIP3). We show that phosphorylation of the second messenger inositol 1,4,5-trisphosphate (IP3) into inositol 1,3,4,5-tetrakisphosphate (IP4) establishes another mode of PH domain regulation through a soluble ligand. At physiological concentrations, IP4 promoted PH domain binding to PIP3. In primary mouse CD4+CD8+ thymocytes, this was required for full activation of the protein tyrosine kinase Itk after T cell receptor engagement. Our data suggest that IP4 establishes a feedback loop of phospholipase C-gamma1 activation through Itk that is essential for T cell development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Yina H -- Grasis, Juris A -- Miller, Andrew T -- Xu, Ruo -- Soonthornvacharin, Stephen -- Andreotti, Amy H -- Tsoukas, Constantine D -- Cooke, Michael P -- Sauer, Karsten -- AR048848/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 11;316(5826):886-9. Epub 2007 Apr 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412921" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; *Amino Acid Motifs ; Animals ; Diglycerides/metabolism ; Feedback, Physiological ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol Phosphates/*metabolism/pharmacology ; Lymphopoiesis ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Models, Biological ; Organ Culture Techniques ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C gamma/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Protein-Tyrosine Kinases/chemistry/*metabolism ; Receptors, Antigen, T-Cell/immunology ; Second Messenger Systems ; Signal Transduction ; Solubility ; T-Lymphocytes/cytology/immunology/*metabolism
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-08-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, Sheila -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):606-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Gene Expression Center, USDA Agricultural Research Service-UC Berkeley, 800 Buchanan Street, Albany, CA 94710, USA. sheilamc@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673644" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/enzymology/genetics/*physiology ; Arabidopsis Proteins/genetics/*metabolism ; Cell Membrane/enzymology ; Crosses, Genetic ; Evolution, Molecular ; Flowers/cytology/enzymology/*physiology ; Genes, Plant ; Ligands ; Models, Biological ; Mutation ; Phosphotransferases/*genetics/*metabolism ; Pollen Tube/growth & development/*physiology ; Reproduction ; Signal Transduction ; Species Specificity
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  • 80
    Publication Date: 2006-06-24
    Description: Organisms ranging from bacteria to humans synchronize their internal clocks to daily cycles of light and dark. Photic entrainment of the Drosophila clock is mediated by proteasomal degradation of the clock protein TIMELESS (TIM). We have identified mutations in jetlag-a gene coding for an F-box protein with leucine-rich repeats-that result in reduced light sensitivity of the circadian clock. Mutant flies show rhythmic behavior in constant light, reduced phase shifts in response to light pulses, and reduced light-dependent degradation of TIM. Expression of JET along with the circadian photoreceptor cryptochrome (CRY) in cultured S2R cells confers light-dependent degradation onto TIM, thereby reconstituting the acute response + of the circadian clock to light in a cell culture system. Our results suggest that JET is essential for resetting the clock by transmitting light signals from CRY to TIM.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2767177/" 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/PMC2767177/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koh, Kyunghee -- Zheng, Xiangzhong -- Sehgal, Amita -- NS048471/NS/NINDS NIH HHS/ -- R01 NS048471/NS/NINDS NIH HHS/ -- R01 NS048471-02/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1809-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Neuroscience, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794082" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cells, Cultured ; *Circadian Rhythm ; Cryptochromes ; Drosophila/chemistry/genetics/physiology ; Drosophila Proteins/chemistry/*genetics/*metabolism/*physiology ; Drosophila melanogaster/chemistry/*genetics/*physiology ; Eye Proteins/metabolism ; F-Box Proteins/chemistry/*genetics/*physiology ; Female ; *Light ; Male ; Models, Biological ; Molecular Sequence Data ; Mutation ; Protein Structure, Tertiary ; Receptors, G-Protein-Coupled/metabolism ; Transgenes ; Ubiquitin/metabolism
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-07-07
    Description: Understanding the relationship between diversity and stability requires a knowledge of how species interact with each other and how each is affected by the environment. The relationship is also complex, because the concept of stability is multifaceted; different types of stability describing different properties of ecosystems lead to multiple diversity-stability relationships. A growing number of empirical studies demonstrate positive diversity-stability relationships. These studies, however, have emphasized only a few types of stability, and they rarely uncover the mechanisms responsible for stability. Because anthropogenic changes often affect stability and diversity simultaneously, diversity-stability relationships cannot be understood outside the context of the environmental drivers affecting both. This shifts attention away from diversity-stability relationships toward the multiple factors, including diversity, that dictate the stability of ecosystems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ives, Anthony R -- Carpenter, Stephen R -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):58-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Wisconsin, Madison, WI 53706, USA. arives@wisc.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615333" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Ecosystem ; Environment ; Extinction, Biological ; Models, Biological ; Population Dynamics
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Mar 9;315(5817):1352-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17347420" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Biomechanical Phenomena ; Extremities/innervation/physiology ; Mesencephalon/physiology ; Models, Biological ; Models, Neurological ; Muscle Contraction ; Nerve Net/*physiology ; *Robotics ; Salamandra/anatomy & histology/*physiology ; Spinal Cord/*physiology ; Swimming ; *Walking
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  • 83
    Publication Date: 2007-08-25
    Description: Most plasmalemmal proteins organize in submicrometer-sized clusters whose architecture and dynamics are still enigmatic. With syntaxin 1 as an example, we applied a combination of far-field optical nanoscopy, biochemistry, fluorescence recovery after photobleaching (FRAP) analysis, and simulations to show that clustering can be explained by self-organization based on simple physical principles. On average, the syntaxin clusters exhibit a diameter of 50 to 60 nanometers and contain 75 densely crowded syntaxins that dynamically exchange with freely diffusing molecules. Self-association depends on weak homophilic protein-protein interactions. Simulations suggest that clustering immobilizes and conformationally constrains the molecules. Moreover, a balance between self-association and crowding-induced steric repulsions is sufficient to explain both the size and dynamics of syntaxin clusters and likely of many oligomerizing membrane proteins that form supramolecular structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sieber, Jochen J -- Willig, Katrin I -- Kutzner, Carsten -- Gerding-Reimers, Claas -- Harke, Benjamin -- Donnert, Gerald -- Rammner, Burkhard -- Eggeling, Christian -- Hell, Stefan W -- Grubmuller, Helmut -- Lang, Thorsten -- New York, N.Y. -- Science. 2007 Aug 24;317(5841):1072-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717182" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Cell Membrane/chemistry/*metabolism ; Chemistry, Physical ; Computer Simulation ; Diffusion ; Fluorescence Recovery After Photobleaching ; Green Fluorescent Proteins ; Immunoblotting ; Microscopy, Confocal ; Microscopy, Fluorescence ; Models, Biological ; Nanotechnology ; PC12 Cells ; Physicochemical Phenomena ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Syntaxin 1/*chemistry/*metabolism
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  • 84
    Publication Date: 2007-03-31
    Description: Plastid-to-nucleus retrograde signaling coordinates nuclear gene expression with chloroplast function and is essential for the photoautotrophic life-style of plants. Three retrograde signals have been described, but little is known of their signaling pathways. We show here that GUN1, a chloroplast-localized pentatricopeptide-repeat protein, and ABI4, an Apetala 2 (AP2)-type transcription factor, are common to all three pathways. ABI4 binds the promoter of a retrograde-regulated gene through a conserved motif found in close proximity to a light-regulatory element. We propose a model in which multiple indicators of aberrant plastid function in Arabidopsis are integrated upstream of GUN1 within plastids, which leads to ABI4-mediated repression of nuclear-encoded genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koussevitzky, Shai -- Nott, Ajit -- Mockler, Todd C -- Hong, Fangxin -- Sachetto-Martins, Gilberto -- Surpin, Marci -- Lim, Jason -- Mittler, Ron -- Chory, Joanne -- DRG-1865-05/PHS HHS/ -- F32 GM 18172/GM/NIGMS NIH HHS/ -- F32 GM 69090/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 4;316(5825):715-9. Epub 2007 Mar 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Salk Institute for Biological Studies, 10010 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/17395793" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid ; Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Cell Nucleus/*metabolism/*microbiology ; Chloroplasts/*metabolism ; DNA, Plant/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Electron Transport ; *Gene Expression Regulation, Plant ; Light-Harvesting Protein Complexes/genetics ; Lincomycin/pharmacology ; Models, Biological ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Protoporphyrins/metabolism ; Pyridazines/pharmacology ; Signal Transduction ; Transcription Factors/*metabolism
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  • 85
    Publication Date: 2007-08-19
    Description: In Gram-negative bacteria and eukaryotic organelles, beta-barrel proteins of the outer membrane protein 85-two-partner secretion B (Omp85-TpsB) superfamily are essential components of protein transport machineries. The TpsB transporter FhaC mediates the secretion of Bordetella pertussis filamentous hemagglutinin (FHA). We report the 3.15 A crystal structure of FhaC. The transporter comprises a 16-stranded beta barrel that is occluded by an N-terminal alpha helix and an extracellular loop and a periplasmic module composed of two aligned polypeptide-transport-associated (POTRA) domains. Functional data reveal that FHA binds to the POTRA 1 domain via its N-terminal domain and likely translocates the adhesin-repeated motifs in an extended hairpin conformation, with folding occurring at the cell surface. General features of the mechanism obtained here are likely to apply throughout the superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clantin, Bernard -- Delattre, Anne-Sophie -- Rucktooa, Prakash -- Saint, Nathalie -- Meli, Albano C -- Locht, Camille -- Jacob-Dubuisson, Francoise -- Villeret, Vincent -- New York, N.Y. -- Science. 2007 Aug 17;317(5840):957-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UMR8161 CNRS, Institut de Biologie de Lille, Universite de Lille 1, Universite de Lille 2, 1 rue du Prof. Calmette, F-59021 Lille cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17702945" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/*metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/genetics/*metabolism ; Bordetella pertussis/*chemistry/metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers/chemistry/metabolism ; Membrane Transport Proteins/chemistry/metabolism ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Transport ; Virulence Factors, Bordetella/chemistry/*metabolism
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  • 86
    Publication Date: 2007-03-31
    Description: A marine ecosystem model seeded with many phytoplankton types, whose physiological traits were randomly assigned from ranges defined by field and laboratory data, generated an emergent community structure and biogeography consistent with observed global phytoplankton distributions. The modeled organisms included types analogous to the marine cyanobacterium Prochlorococcus. Their emergent global distributions and physiological properties simultaneously correspond to observations. This flexible representation of community structure can be used to explore relations between ecosystems, biogeochemical cycles, and climate change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Follows, Michael J -- Dutkiewicz, Stephanie -- Grant, Scott -- Chisholm, Sallie W -- New York, N.Y. -- Science. 2007 Mar 30;315(5820):1843-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology, 54-1514 MIT, Cambridge, MA 02139, USA. mick@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17395828" target="_blank"〉PubMed〈/a〉
    Keywords: Biomass ; Computer Simulation ; *Ecosystem ; Geography ; Light ; Mathematics ; Models, Biological ; Oceans and Seas ; Phytoplankton/growth & development/*physiology ; Prochlorococcus/growth & development/*physiology ; Seawater/*microbiology ; Temperature
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  • 87
    Publication Date: 2007-05-26
    Description: Telford et al. (Brevia, 19 May 2006, p. 1015) reported that freshwater diatoms exhibit regional-scale richness-pH relationships that depend substantially on regional habitat availability. On this basis, the authors argued that, despite their microscopic size, diatoms are not ubiquitously dispersed. Here, I describe my demonstration that their primary evidence against the ubiquitous dispersal hypothesis is spurious.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pither, Jason -- New York, N.Y. -- Science. 2007 May 25;316(5828):1124; author reply 1124.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of Arizona, BSW 310, 1041 East Lowell Street, Tucson, AZ 85721, USA. pitherj@email.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525319" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; Diatoms/*physiology ; *Ecosystem ; *Environmental Microbiology ; Europe ; Fresh Water ; Hydrogen-Ion Concentration ; Models, Biological ; North America ; Water Microbiology
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  • 88
    Publication Date: 2007-02-10
    Description: A central issue in the regulation of apoptosis by the Bcl-2 family is whether its BH3-only members initiate apoptosis by directly binding to the essential cell-death mediators Bax and Bak, or whether they can act indirectly, by engaging their pro-survival Bcl-2-like relatives. Contrary to the direct-activation model, we show that Bax and Bak can mediate apoptosis without discernable association with the putative BH3-only activators (Bim, Bid, and Puma), even in cells with no Bim or Bid and reduced Puma. Our results indicate that BH3-only proteins induce apoptosis at least primarily by engaging the multiple pro-survival relatives guarding Bax and Bak.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willis, Simon N -- Fletcher, Jamie I -- Kaufmann, Thomas -- van Delft, Mark F -- Chen, Lin -- Czabotar, Peter E -- Ierino, Helen -- Lee, Erinna F -- Fairlie, W Douglas -- Bouillet, Philippe -- Strasser, Andreas -- Kluck, Ruth M -- Adams, Jerry M -- Huang, David C S -- CA43540/CA/NCI NIH HHS/ -- CA80188/CA/NCI NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):856-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289999" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptosis Regulatory Proteins/chemistry/genetics/*metabolism ; BH3 Interacting Domain Death Agonist Protein/chemistry/genetics/*metabolism ; Cell Line ; Cells, Cultured ; Humans ; Ligands ; Membrane Proteins/chemistry/genetics/*metabolism ; Mice ; Mice, Knockout ; Models, Biological ; Mutation ; Myeloid Cell Leukemia Sequence 1 Protein ; Neoplasm Proteins/metabolism ; Protein Structure, Tertiary ; Proteins/metabolism ; Proto-Oncogene Proteins/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-bcl-2/*metabolism ; Tumor Suppressor Proteins/genetics/metabolism ; bcl-2 Homologous Antagonist-Killer Protein/metabolism ; bcl-2-Associated X Protein/chemistry/*metabolism ; bcl-Associated Death Protein/metabolism ; bcl-X Protein/metabolism
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-05-26
    Description: Single-molecule force experiments in vitro enable the characterization of the mechanical response of biological matter at the nanometer scale. However, they do not reveal the molecular mechanisms underlying mechanical function. These can only be readily studied through molecular dynamics simulations of atomic structural models: "in silico" (by computer analysis) single-molecule experiments. Steered molecular dynamics simulations, in which external forces are used to explore the response and function of macromolecules, have become a powerful tool complementing and guiding in vitro single-molecule experiments. The insights provided by in silico experiments are illustrated here through a review of recent research in three areas of protein mechanics: elasticity of the muscle protein titin and the extracellular matrix protein fibronectin; linker-mediated elasticity of the cytoskeleton protein spectrin; and elasticity of ankyrin repeats, a protein module found ubiquitously in cells but with an as-yet unclear function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sotomayor, Marcos -- Schulten, Klaus -- 1 R01 GM073655/GM/NIGMS NIH HHS/ -- P41 RR05969/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2007 May 25;316(5828):1144-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of Illinois at Urbana-Champaign, and Beckman Institute for Advanced Science and Technology, 405 North Mathews Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17525328" target="_blank"〉PubMed〈/a〉
    Keywords: Ankyrin Repeat/*physiology ; Computer Simulation ; Connectin ; Elasticity ; Fibronectins/*physiology ; Humans ; Models, Biological ; Muscle Proteins/*physiology ; Protein Kinases/*physiology ; Spectrin/*physiology ; Spectrum Analysis/*methods
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kahl, Barbara C -- Peters, Georg -- New York, N.Y. -- Science. 2007 Feb 23;315(5815):1082-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Medical Microbiology, University of Munster, Domagkstrasse 10, D-49149 Munster, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17322047" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/genetics/metabolism ; Animals ; Bacterial Toxins/analysis ; Exotoxins/analysis/*physiology ; Gene Expression Regulation, Bacterial ; Hemorrhage ; Leukocidins/analysis/*physiology ; Lung/chemistry/microbiology/*pathology ; Methicillin Resistance ; Mice ; Models, Biological ; Necrosis ; Phagocytosis ; Pneumonia, Staphylococcal/*microbiology/*pathology ; Respiratory Mucosa/microbiology ; Staphylococcal Protein A/genetics/*metabolism ; Staphylococcus aureus/genetics/growth & development/metabolism/*pathogenicity ; Virulence Factors/analysis/*physiology
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Proud, Christopher G -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):926-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia V6T 1Z3, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Cells, Cultured ; Guanosine Triphosphate/metabolism ; Humans ; Insulin/metabolism ; Models, Biological ; Monomeric GTP-Binding Proteins/*metabolism ; Multiprotein Complexes ; Neuropeptides/*metabolism ; Protein Binding ; Protein Kinases/*metabolism ; Proteins ; *Signal Transduction ; Sirolimus/metabolism/pharmacology ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Protein 1A/metabolism ; Tacrolimus Binding Proteins/antagonists & inhibitors/*metabolism ; Transcription Factors/*metabolism
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  • 92
    Publication Date: 2007-02-10
    Description: The bacterium Myxococcus xanthus has two motility systems: S motility, which is powered by type IV pilus retraction, and A motility, which is powered by unknown mechanism(s). We found that A motility involved transient adhesion complexes that remained at fixed positions relative to the substratum as cells moved forward. Complexes assembled at leading cell poles and dispersed at the rear of the cells. When cells reversed direction, the A-motility clusters relocalized to the new leading poles together with S-motility proteins. The Frz chemosensory system coordinated the two motility systems. The dynamics of protein cluster localization suggest that intracellular motors and force transmission by dynamic focal adhesions can power bacterial motility.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4095873/" 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/PMC4095873/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mignot, Tam -- Shaevitz, Joshua W -- Hartzell, Patricia L -- Zusman, David R -- GM20509/GM/NIGMS NIH HHS/ -- R01 GM020509/GM/NIGMS NIH HHS/ -- R01 GM075242-03/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. tmignot@berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289998" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/pharmacology ; *Bacterial Adhesion ; Bacterial Proteins/analysis/genetics/metabolism/*physiology ; Cephalexin/pharmacology ; Fimbriae, Bacterial/physiology ; Focal Adhesions/*physiology ; Luminescent Proteins ; Models, Biological ; Molecular Motor Proteins/analysis/genetics/*physiology ; Movement ; Myxococcus xanthus/cytology/genetics/*physiology ; Recombinant Fusion Proteins/analysis
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-11-10
    Description: Prions are lethal mammalian pathogens composed of aggregated conformational isomers of a host-encoded glycoprotein and which appear to lack nucleic acids. Their unique biology, allied with the public-health risks posed by prion zoonoses such as bovine spongiform encephalopathy, has focused much attention on the molecular basis of prion propagation and the "species barrier" that controls cross-species transmission. Both are intimately linked to understanding how multiple prion "strains" are encoded by a protein-only agent. The underlying mechanisms are clearly of much wider importance, and analogous protein-based inheritance mechanisms are recognized in yeast and fungi. Recent advances suggest that prions themselves are not directly neurotoxic, but rather their propagation involves production of toxic species, which may be uncoupled from infectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collinge, John -- Clarke, Anthony R -- MC_U123160656/Medical Research Council/United Kingdom -- MC_U123192748/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):930-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Prion Unit, Department of Neurodegenerative Disease, UCL Institute of Neurology, London WC1N 3BG, UK. j.collinge@prion.ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17991853" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Chemistry ; Humans ; Models, Biological ; PrPC Proteins/chemistry/isolation & purification/metabolism ; PrPSc Proteins/*chemistry/isolation & purification/metabolism/*pathogenicity ; Prion Diseases/*metabolism/*transmission ; Prions/*chemistry/isolation & purification/*pathogenicity ; Protein Conformation ; Protein Folding ; Recombinant Proteins/chemistry ; Species Specificity
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  • 94
    Publication Date: 2007-01-06
    Description: Endoplasmic reticulum-localized protein-tyrosine phosphatase PTP1B terminates growth factor signal transduction by dephosphorylation of receptor tyrosine kinases (RTKs). But how PTP1B allows for RTK signaling in the cytoplasm is unclear. In order to test whether PTP1B activity is spatially regulated, we developed a method based on Forster resonant energy transfer for imaging enzyme-substrate (ES) intermediates in live cells. We observed the establishment of a steady-state ES gradient across the cell. This gradient exhibited robustness to cell-to-cell variability, growth factor activation, and RTK localization, which demonstrated spatial regulation of PTP1B activity. Such regulation may be important for generating distinct cellular environments that permit RTK signal transduction and that mediate its eventual termination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yudushkin, Ivan A -- Schleifenbaum, Andreas -- Kinkhabwala, Ali -- Neel, Benjamin G -- Schultz, Carsten -- Bastiaens, Philippe I H -- R01 DK60838/DK/NIDDK NIH HHS/ -- R37 49152/PHS HHS/ -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):115-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204654" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Catalysis ; Cell Line, Tumor ; Cercopithecus aethiops ; Epidermal Growth Factor/metabolism/pharmacology ; Fluorescence Resonance Energy Transfer ; Humans ; Kinetics ; Mathematics ; Microscopy, Fluorescence ; Models, Biological ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 ; Protein Tyrosine Phosphatases/*metabolism ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kearns, Daniel B -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):773-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington, IN 47405, USA. dbkearns@indiana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289965" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Adhesion ; Bacterial Proteins/genetics/*physiology ; Fimbriae, Bacterial/physiology ; Focal Adhesions/*physiology ; Models, Biological ; Molecular Motor Proteins/genetics/*physiology ; Movement ; Myxococcus xanthus/*physiology
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  • 96
    Publication Date: 2007-10-06
    Description: The simple circadian oscillator found in cyanobacteria can be reconstituted in vitro using three proteins-KaiA, KaiB, and KaiC. The total phosphorylation level of KaiC oscillates with a circadian period, but the mechanism underlying its sustained oscillation remains unclear. We have shown that four forms of KaiC differing in their phosphorylation state appear in an ordered pattern arising from the intrinsic autokinase and autophosphatase rates of KaiC and their modulation by KaiA. Kinetic and biochemical data indicate that one of these phosphoforms inhibits the activity of KaiA through interaction with KaiB, providing the crucial feedback that sustains oscillation. A mathematical model constrained by experimental data quantitatively reproduces the circadian period and the distinctive dynamics of the four phosphoforms.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2427396/" 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/PMC2427396/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rust, Michael J -- Markson, Joseph S -- Lane, William S -- Fisher, Daniel S -- O'Shea, Erin K -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):809-12. Epub 2007 Oct 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Faculty of Arts and Sciences Center for Systems Biology, Departments of Molecular and Cellular Biology and of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916691" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*physiology ; Biological Clocks/*physiology ; Circadian Rhythm/*physiology ; Circadian Rhythm Signaling Peptides and Proteins ; Models, Biological ; Phosphorylation ; Synechococcus/*physiology
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  • 97
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-02-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hajnoczky, Gyorgy -- Hoek, Jan B -- New York, N.Y. -- Science. 2007 Feb 2;315(5812):607-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA. gyorgy.hajnoczky@jefferson.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17272709" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*metabolism ; Animals ; *Apoptosis ; Autophagy ; Calcium Signaling ; *Cell Aging ; Cytoplasm/metabolism ; Hydrogen Peroxide/metabolism/pharmacology ; Intracellular Membranes/metabolism ; Mice ; Mitochondria/*metabolism ; Models, Biological ; Peptidylprolyl Isomerase/metabolism ; Permeability ; Phosphorylation ; Protein Kinase C/metabolism ; Protein Kinase C beta ; Protein Transport ; Reactive Oxygen Species/metabolism ; Shc Signaling Adaptor Proteins ; *Signal Transduction
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  • 98
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dolan, Liam -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):377-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK. liam.dolan@bbsrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446377" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/cytology/genetics/growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Biological Evolution ; Cell Nucleus/metabolism ; Feedback, Physiological ; Genetic Engineering ; Models, Biological ; Plant Cells ; Plant Development ; Plant Roots/cytology/growth & development/*metabolism ; Plants/genetics/metabolism ; Protein Transport ; Transcription Factors/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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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2007-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oldroyd, Giles E D -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):52-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Disease and Stress Biology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK. giles.oldroyd@bbsrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204633" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/metabolism ; Cytokinins/*metabolism ; Lipopolysaccharides/metabolism ; Lotus/cytology/metabolism/*microbiology/*physiology ; Models, Biological ; Mutation ; Nitrogen Fixation ; Plant Epidermis/cytology/metabolism ; Plant Roots/cytology/microbiology ; Protein Kinases/genetics/*metabolism ; Receptors, Cell Surface/genetics/metabolism ; Rhizobiaceae/physiology ; Root Nodules, Plant/cytology/*growth & development/microbiology ; *Signal Transduction ; Symbiosis ; Transcription Factors/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 2007-04-07
    Description: Kinesin-1 is a two-headed molecular motor that walks along microtubules, with each step gated by adenosine triphosphate (ATP) binding. Existing models for the gating mechanism propose a role for the microtubule lattice. We show that unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate (ADP). With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-1 dimer binds two tubulin heterodimers. The data reveal an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of a steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2504013/" 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/PMC2504013/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alonso, Maria C -- Drummond, Douglas R -- Kain, Susan -- Hoeng, Julia -- Amos, Linda -- Cross, Robert A -- G0200542/Medical Research Council/United Kingdom -- G0200542(63814)/Medical Research Council/United Kingdom -- MC_U105184313/Medical Research Council/United Kingdom -- U.1051.04.002(78842)/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):120-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Motors Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412962" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Adenylyl Imidodiphosphate/metabolism ; Animals ; Binding Sites ; Dimerization ; Kinesin/chemistry/*metabolism ; Microtubules/*metabolism ; Models, Biological ; Molecular Motor Proteins/*metabolism ; Neurospora ; Protein Conformation ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Schizosaccharomyces ; Tubulin/chemistry/*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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