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  • Molecular Sequence Data  (98)
  • Models, Biological  (68)
  • Fisheries
  • Industrial Chemistry
  • Inorganic Chemistry
  • Seismology
  • American Association for the Advancement of Science (AAAS)  (167)
  • Victoria: Seychelles Fishing Authority  (2)
  • Am. Meteor. Soc.
  • WWF Programa Marino para Latinoamérica y el Caribe
  • 2005-2009  (169)
  • 1950-1954
  • 2006  (169)
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  • 2005-2009  (169)
  • 1950-1954
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  • 1
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    Victoria: Seychelles Fishing Authority
    Publication Date: 2021-05-19
    Description: Seychelles is composed of over 100 islands with a land area of approximately 455 km², centred close to 4°30'S and 55°30'E. The combined coastline is approximately 600 km long, the oceanic shelf totals about 50 000 km² and the Exclusive Economic Zone (EEZ) is over 1 370 000 km². The total population (1994 census) stands at just under 74 000. in 1994, the population registered a growth rate of 2.2%. The GDP (1994) was SR 2373.8 million, fisheries representing 4.8% of this sum. Licensing agreements for foreign fishing activities provided a yearly revenue of SR8 million. Port Victoria is seen as a prime centre for tuna fishing operations in the Indian Ocean. In the artisanal fishery just under 900 persons are working. The largest contributor to catch by vessel type are the traditional whaler vessels representing 47.8% of the total catch. Over 66.3% of the catch is by the handline method. Carangidae representing 24% and Lutjanidae 19% of total landings. There are six specific objectives to the fisheries sector policy, which aims as resource development and maximisation of potential benefits. Nearshore fishery resources are considered to be heavily exploited, however opportunities exist around the distant islands and in deeper waters off the Mahe plateau shelf. Aquaculture of molluscs and prawns is being developed and carried out. The main constraints to development are seen as the lack of skilled manpower and foreign exchange.
    Description: Published
    Keywords: Country profile ; Fisheries ; Seychelles ; Statistics ; Fisheries ; Fishery statistics
    Repository Name: AquaDocs
    Type: Report , Non-Refereed
    Format: 186058 bytes
    Format: 520444 bytes
    Format: application/pdf
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  • 2
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    Victoria: Seychelles Fishing Authority | Victoria
    Publication Date: 2021-08-09
    Description: Published
    Description: Industrial tuna fishing
    Keywords: Tuna ; Fisheries ; Fishery economics ; Fishery industry ; Fishery statistics ; Tuna fisheries
    Repository Name: AquaDocs
    Type: Report , Non-Refereed
    Format: 1589602 bytes
    Format: application/pdf
    Format: 28
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  • 3
    Publication Date: 2006-09-09
    Description: CD8-positive T lymphocytes recognize peptides that are usually derived from the degradation of cellular proteins and are presented by class I molecules of the major histocompatibility complex. Here we describe a human minor histocompatibility antigen created by a polymorphism in the SP110 nuclear phosphoprotein gene. The antigenic peptide comprises two noncontiguous SP110 peptide segments spliced together in reverse order to that in which they occur in the predicted SP110 protein. The antigenic peptide could be produced in vitro by incubation of precursor peptides with highly purified 20S proteasomes. Cutting and splicing probably occur within the proteasome by transpeptidation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warren, Edus H -- Vigneron, Nathalie J -- Gavin, Marc A -- Coulie, Pierre G -- Stroobant, Vincent -- Dalet, Alexandre -- Tykodi, Scott S -- Xuereb, Suzanne M -- Mito, Jeffrey K -- Riddell, Stanley R -- Van den Eynde, Benoit J -- CA106512/CA/NCI NIH HHS/ -- CA18029/CA/NCI NIH HHS/ -- P01 CA018029/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 8;313(5792):1444-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Immunology, Clinical Research Division, 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/16960008" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; *Antigen Presentation ; B-Lymphocytes/immunology ; Cell Line, Transformed ; Cytotoxicity, Immunologic ; Electroporation ; HLA-A Antigens/immunology ; Humans ; Interferon-gamma/metabolism ; Male ; Middle Aged ; Minor Histocompatibility Antigens/genetics/*immunology/*metabolism ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*immunology/*metabolism ; Peptide Fragments/metabolism ; Polymorphism, Single Nucleotide ; Proteasome Endopeptidase Complex/metabolism ; *Protein Splicing ; T-Lymphocytes, Cytotoxic/*immunology
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    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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  • 5
    Publication Date: 2006-08-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crowder, L B -- Osherenko, G -- Young, O R -- Airame, S -- Norse, E A -- Baron, N -- Day, J C -- Douvere, F -- Ehler, C N -- Halpern, B S -- Langdon, S J -- McLeod, K L -- Ogden, J C -- Peach, R E -- Rosenberg, A A -- Wilson, J A -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):617-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Marine Conservation, Nicholas School of the Environment and Earth Sciences, Duke University Marine Laboratory, Beaufort, NC 28516, USA. lcrowder@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16888124" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Conservation of Natural Resources ; *Ecosystem ; Environment ; Fisheries ; Fishes ; *Government Regulation ; *Marine Biology ; Oceans and Seas ; Population Dynamics ; Seawater ; United States
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  • 6
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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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  • 7
    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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  • 8
    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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  • 9
    Publication Date: 2006-11-18
    Description: Using single-molecule DNA nanomanipulation, we show that abortive initiation involves DNA "scrunching"--in which RNA polymerase (RNAP) remains stationary and unwinds and pulls downstream DNA into itself--and that scrunching requires RNA synthesis and depends on RNA length. We show further that promoter escape involves scrunching, and that scrunching occurs in most or all instances of promoter escape. Our results support the existence of an obligatory stressed intermediate, with approximately one turn of additional DNA unwinding, in escape and are consistent with the proposal that stress in this intermediate provides the driving force to break RNAP-promoter and RNAP-initiation-factor interactions in escape.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2754787/" 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/PMC2754787/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Revyakin, Andrey -- Liu, Chenyu -- Ebright, Richard H -- Strick, Terence R -- GM41376/GM/NIGMS NIH HHS/ -- R01 GM041376/GM/NIGMS NIH HHS/ -- R01 GM041376-15/GM/NIGMS NIH HHS/ -- R01 GM041376-16/GM/NIGMS NIH HHS/ -- R01 GM041376-17/GM/NIGMS NIH HHS/ -- R01 GM041376-18/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1139-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110577" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biomechanical Phenomena ; DNA/chemistry/*metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; RNA/biosynthesis ; Transcription Initiation Site/physiology ; Transcription, Genetic/*physiology
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  • 10
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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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  • 11
    Publication Date: 2006-11-25
    Description: The Dobzhansky-Muller model proposes that hybrid incompatibilities are caused by the interaction between genes that have functionally diverged in the respective hybridizing species. Here, we show that Lethal hybrid rescue (Lhr) has functionally diverged in Drosophila simulans and interacts with Hybrid male rescue (Hmr), which has functionally diverged in D. melanogaster, to cause lethality in F1 hybrid males. LHR localizes to heterochromatic regions of the genome and has diverged extensively in sequence between these species in a manner consistent with positive selection. Rapidly evolving heterochromatic DNA sequences may be driving the evolution of this incompatibility gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brideau, Nicholas J -- Flores, Heather A -- Wang, Jun -- Maheshwari, Shamoni -- Wang, Xu -- Barbash, Daniel A -- R01 GM074737-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1292-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124320" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Mapping ; Crosses, Genetic ; Drosophila/*genetics/physiology ; Drosophila Proteins/chemistry/*genetics/metabolism ; Drosophila melanogaster/*genetics/physiology ; *Evolution, Molecular ; Female ; *Genes, Insect ; Genetic Speciation ; *Hybridization, Genetic ; Male ; Molecular Sequence Data ; Selection, Genetic ; Transformation, Genetic ; Transgenes
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  • 12
    Publication Date: 2006-03-11
    Description: Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Bo -- Yu, John Paul J -- Brunzelle, Joseph S -- Moll, Gert N -- van der Donk, Wilfred A -- Nair, Satish K -- GM58822/GM/NIGMS NIH HHS/ -- R01 GM079038/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527981" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/*biosynthesis/chemistry ; Carbon-Sulfur Lyases/chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Farnesyltranstransferase/chemistry ; Humans ; Lactococcus lactis/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Nisin/*biosynthesis/chemistry ; Protein Conformation ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-03-11
    Description: Crop domestication frequently began with the selection of plants that did not naturally shed ripe fruits or seeds. The reduction in grain shattering that led to cereal domestication involved genetic loci of large effect. The molecular basis of this key domestication transition, however, remains unknown. Here we show that human selection of an amino acid substitution in the predicted DNA binding domain encoded by a gene of previously unknown function was primarily responsible for the reduction of grain shattering in rice domestication. The substitution undermined the gene function necessary for the normal development of an abscission layer that controls the separation of a grain from the pedicel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Changbao -- Zhou, Ailing -- Sang, Tao -- New York, N.Y. -- Science. 2006 Mar 31;311(5769):1936-9. Epub 2006 Mar 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527928" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Biological Evolution ; Chromosome Mapping ; Computational Biology ; Crops, Agricultural/*genetics/growth & development ; Flowers/growth & development ; Gene Expression ; Genes, Plant ; Genotype ; Molecular Sequence Data ; Mutation ; Oryza/cytology/*genetics/growth & development ; Phenotype ; Plant Proteins/chemistry/*genetics ; Plants, Genetically Modified ; Quantitative Trait Loci ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, DNA ; Transcription Factors/chemistry/*genetics ; Transformation, Genetic
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  • 14
    Publication Date: 2006-06-17
    Description: Vesicular stomatitis virus is a negative-stranded RNA virus. Its nucleoprotein (N) binds the viral genomic RNA and is involved in multiple functions including transcription, replication, and assembly. We have determined a 2.9 angstrom structure of a complex containing 10 molecules of the N protein and 90 bases of RNA. The RNA is tightly sequestered in a cavity at the interface between two lobes of the N protein. This serves to protect the RNA in the absence of polynucleotide synthesis. For the RNA to be accessed, some conformational change in the N protein should be necessary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, Todd J -- Zhang, Xin -- Wertz, Gail W -- Luo, Ming -- AI050066/AI/NIAID NIH HHS/ -- R37 AI012464/AI/NIAID NIH HHS/ -- R37 AI012464-28/AI/NIAID NIH HHS/ -- R37 AI012464-29/AI/NIAID NIH HHS/ -- R37 AI012464-30/AI/NIAID NIH HHS/ -- R37 AI012464-31/AI/NIAID NIH HHS/ -- R37AI012464/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):357-60. Epub 2006 Jun 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, School of Medicine, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35294, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778022" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Viral/*chemistry/metabolism ; Ribonucleoproteins/*chemistry ; Sequence Alignment ; Vesicular stomatitis Indiana virus/*chemistry
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  • 15
    Publication Date: 2006-07-01
    Description: The formation of glutaminyl transfer RNA (Gln-tRNA(Gln)) differs among the three domains of life. Most bacteria employ an indirect pathway to produce Gln-tRNA(Gln) by a heterotrimeric glutamine amidotransferase CAB (GatCAB) that acts on the misacylated Glu-tRNA(Gln). Here, we describe a series of crystal structures of intact GatCAB from Staphylococcus aureus in the apo form and in the complexes with glutamine, asparagine, Mn2+, and adenosine triphosphate analog. Two identified catalytic centers for the glutaminase and transamidase reactions are markedly distant but connected by a hydrophilic ammonia channel 30 A in length. Further, we show that the first U-A base pair in the acceptor stem and the D loop of tRNA(Gln) serve as identity elements essential for discrimination by GatCAB and propose a complete model for the overall concerted reactions to synthesize Gln-tRNA(Gln).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, Akiyoshi -- Yao, Min -- Chimnaronk, Sarin -- Sakai, Naoki -- Tanaka, Isao -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809541" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Aminoacyltransferases/metabolism ; Ammonia/*metabolism ; Apoenzymes/chemistry/metabolism ; Asparagine/metabolism ; Base Pairing ; Catalytic Domain ; Crystallography, X-Ray ; Glutaminase/metabolism ; Glutamine/*chemistry/metabolism ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Magnesium/metabolism ; Manganese/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; RNA, Bacterial/chemistry/metabolism ; RNA, Transfer, Amino Acyl/chemistry/*metabolism ; RNA, Transfer, Gln/*chemistry/metabolism ; Staphylococcus aureus/*enzymology/genetics/metabolism
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  • 16
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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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  • 17
    Publication Date: 2006-11-11
    Description: The molecular mechanisms controlling human hair growth and scalp hair loss are poorly understood. By screening about 350,000 individuals in two populations from the Volga-Ural region of Russia, we identified a gene mutation in families who show an inherited form of hair loss and a hair growth defect. Affected individuals were homozygous for a deletion in the LIPH gene on chromosome 3q27, caused by short interspersed nuclear element-retrotransposon-mediated recombination. The LIPH gene is expressed in hair follicles and encodes a phospholipase called lipase H (alternatively known as membrane-associated phosphatidic acid-selective phospholipase A1alpha), an enzyme that regulates the production of bioactive lipids. These results suggest that lipase H participates in hair growth and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kazantseva, Anastasiya -- Goltsov, Andrey -- Zinchenko, Rena -- Grigorenko, Anastasia P -- Abrukova, Anna V -- Moliaka, Yuri K -- Kirillov, Alexander G -- Guo, Zhiru -- Lyle, Stephen -- Ginter, Evgeny K -- Rogaev, Evgeny I -- K08-AR02179/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):982-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brudnick Neuropsychiatric Research Institute, Department of Psychiatry, University of Massachusetts Medical School, 303 Belmont Street, Worcester, MA 01604, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095700" target="_blank"〉PubMed〈/a〉
    Keywords: Alu Elements ; Amino Acid Sequence ; Base Sequence ; Chromosomes, Human, Pair 3/genetics ; Exons ; Female ; Gene Deletion ; Gene Expression ; Genetic Markers ; Hair/*growth & development ; Hair Follicle/enzymology ; Heterozygote ; Homozygote ; Humans ; Hypotrichosis/*genetics ; Lipase/chemistry/*genetics/metabolism ; Lipid Metabolism ; Lod Score ; Male ; Molecular Sequence Data ; Pedigree ; Protein Structure, Tertiary ; Recombination, Genetic ; Retroelements ; Russia ; Tandem Repeat Sequences
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  • 18
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
    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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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-29
    Description: Microbial pathogens that normally inhabit our environment can adapt to thrive inside mammalian hosts. There are six dimorphic fungi that cause disease worldwide, which switch from nonpathogenic molds in soil to pathogenic yeast after spores are inhaled and exposed to elevated temperature. Mechanisms that regulate this switch remain obscure. We show that a hybrid histidine kinase senses host signals and triggers the transition from mold to yeast. The kinase also regulates cell-wall integrity, sporulation, and expression of virulence genes in vivo. This global regulator shapes how dimorphic fungal pathogens adapt to the mammalian host, which has broad implications for treating and preventing systemic fungal disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemecek, Julie C -- Wuthrich, Marcel -- Klein, Bruce S -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):583-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology and Immunology, University of Wisconsin Medical School, University of Wisconsin Hospital and Clinics, Madison, WI 53792, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645097" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastomyces/cytology/enzymology/*genetics/*pathogenicity ; Blastomycosis/microbiology ; Coccidioides/enzymology/genetics/pathogenicity ; Fungal Proteins/genetics/physiology ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Genetic Complementation Test ; Histoplasma/enzymology/genetics/pathogenicity ; Histoplasmosis/microbiology ; Lung Diseases, Fungal/microbiology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutagenesis, Insertional ; Open Reading Frames ; Protein Kinases/chemistry/*genetics/*physiology ; RNA Interference ; Saccharomyces cerevisiae/genetics ; Soil Microbiology ; Spores, Fungal/physiology ; Temperature ; Virulence/genetics
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  • 22
    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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  • 23
    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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  • 24
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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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  • 25
    Publication Date: 2006-11-25
    Description: For microbial pathogens, phylogeographic differentiation seems to be relatively common. However, the neutral population structure of Salmonella enterica serovar Typhi reflects the continued existence of ubiquitous haplotypes over millennia. In contrast, clinical use of fluoroquinolones has yielded at least 15 independent gyrA mutations within a decade and stimulated clonal expansion of haplotype H58 in Asia and Africa. Yet, antibiotic-sensitive strains and haplotypes other than H58 still persist despite selection for antibiotic resistance. Neutral evolution in Typhi appears to reflect the asymptomatic carrier state, and adaptive evolution depends on the rapid transmission of phenotypic changes through acute infections.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652035/" 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/PMC2652035/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roumagnac, Philippe -- Weill, Francois-Xavier -- Dolecek, Christiane -- Baker, Stephen -- Brisse, Sylvain -- Chinh, Nguyen Tran -- Le, Thi Anh Hong -- Acosta, Camilo J -- Farrar, Jeremy -- Dougan, Gordon -- Achtman, Mark -- 076962/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1301-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Infektionsbiologie, Department of Molecular Biology, Chariteplatz 1, 10117 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124322" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Africa ; Alleles ; Anti-Bacterial Agents/pharmacology/therapeutic use ; Asia ; *Biological Evolution ; Carrier State/*microbiology ; DNA Gyrase/genetics ; Drug Resistance, Bacterial ; Drug Resistance, Multiple, Bacterial ; Fluoroquinolones/pharmacology/therapeutic use ; *Genes, Bacterial ; Genetic Variation ; Haplotypes ; Humans ; Molecular Sequence Data ; Mutation ; Polymorphism, Genetic ; Polymorphism, Single Nucleotide ; Salmonella typhi/drug effects/*genetics ; Selection, Genetic ; Typhoid Fever/drug therapy/*microbiology
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  • 26
    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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  • 27
    Publication Date: 2006-08-12
    Description: Mutations in the human neurotrypsin gene are associated with autosomal recessive mental retardation. To further understand the pathophysiological consequences of the lack of this serine protease, we studied Tequila (Teq), the Drosophila neurotrypsin ortholog, using associative memory as a behavioral readout. We found that teq inactivation resulted in a long-term memory (LTM)-specific defect. After LTM conditioning of wild-type flies, teq expression transiently increased in the mushroom bodies. Moreover, specific inhibition of teq expression in adult mushroom bodies resulted in a reversible LTM defect. Hence, the Teq pathway is essential for information processing in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Didelot, Gerard -- Molinari, Florence -- Tchenio, Paul -- Comas, Daniel -- Milhiet, Elodie -- Munnich, Arnold -- Colleaux, Laurence -- Preat, Thomas -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):851-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genes et Dynamique des Systemes de Memoire, UMR CNRS 7637, Ecole Superieure de Physique et de Chimie Industrielles, 10 Rue Vauquelin 75005 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Conditioning, Classical ; Drosophila Proteins/chemistry/genetics/*physiology ; Drosophila melanogaster/genetics/*physiology ; Gene Expression ; Gene Expression Regulation ; Humans ; Learning ; *Memory ; Mifepristone/pharmacology ; Models, Animal ; Molecular Sequence Data ; Mushroom Bodies/anatomy & histology/physiology ; Mutation ; Odors ; RNA Interference ; RNA, Messenger/genetics/metabolism ; Serine Endopeptidases/chemistry/genetics/*physiology
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  • 28
    Publication Date: 2006-11-18
    Description: Our knowledge of Neanderthals is based on a limited number of remains and artifacts from which we must make inferences about their biology, behavior, and relationship to ourselves. Here, we describe the characterization of these extinct hominids from a new perspective, based on the development of a Neanderthal metagenomic library and its high-throughput sequencing and analysis. Several lines of evidence indicate that the 65,250 base pairs of hominid sequence so far identified in the library are of Neanderthal origin, the strongest being the ascertainment of sequence identities between Neanderthal and chimpanzee at sites where the human genomic sequence is different. These results enabled us to calculate the human-Neanderthal divergence time based on multiple randomly distributed autosomal loci. Our analyses suggest that on average the Neanderthal genomic sequence we obtained and the reference human genome sequence share a most recent common ancestor approximately 706,000 years ago, and that the human and Neanderthal ancestral populations split approximately 370,000 years ago, before the emergence of anatomically modern humans. Our finding that the Neanderthal and human genomes are at least 99.5% identical led us to develop and successfully implement a targeted method for recovering specific ancient DNA sequences from metagenomic libraries. This initial analysis of the Neanderthal genome advances our understanding of the evolutionary relationship of Homo sapiens and Homo neanderthalensis and signifies the dawn of Neanderthal genomics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2583069/" 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/PMC2583069/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noonan, James P -- Coop, Graham -- Kudaravalli, Sridhar -- Smith, Doug -- Krause, Johannes -- Alessi, Joe -- Chen, Feng -- Platt, Darren -- Paabo, Svante -- Pritchard, Jonathan K -- Rubin, Edward M -- 1-F32-GM074367/GM/NIGMS NIH HHS/ -- HL066681/HL/NHLBI NIH HHS/ -- R01 HG002772/HG/NHGRI NIH HHS/ -- R01 HG002772-01/HG/NHGRI NIH HHS/ -- R01 HG002772-1/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1113-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110569" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones ; Cell Nucleus ; DNA/*genetics/isolation & purification ; DNA, Mitochondrial ; *Fossils ; Gene Pool ; Genome ; Genome, Human ; Genomic Library ; History, Ancient ; Hominidae/*genetics ; Humans ; Male ; Molecular Sequence Data ; Pan troglodytes/genetics ; Polymerase Chain Reaction ; Sequence Alignment ; *Sequence Analysis, DNA/methods ; Time
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  • 29
    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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  • 30
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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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  • 31
    Publication Date: 2006-11-25
    Description: Clostridium novyi-NT is an anaerobic bacterium that can infect hypoxic regions within experimental tumors. Because C. novyi-NT lyses red blood cells, we hypothesized that its membrane-disrupting properties could be exploited to enhance the release of liposome-encapsulated drugs within tumors. Here, we show that treatment of mice bearing large, established tumors with C. novyi-NT plus a single dose of liposomal doxorubicin often led to eradication of the tumors. The bacterial factor responsible for the enhanced drug release was identified as a previously unrecognized protein termed liposomase. This protein could potentially be incorporated into diverse experimental approaches for the specific delivery of chemotherapeutic agents to tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheong, Ian -- Huang, Xin -- Bettegowda, Chetan -- Diaz, Luis A Jr -- Kinzler, Kenneth W -- Zhou, Shibin -- Vogelstein, Bert -- CA062924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1308-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and the Ludwig Center for Cancer Genetics and Therapeutics, Johns Hopkins Kimmel Comprehensive Cancer Center, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124324" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antineoplastic Agents/*administration & dosage/pharmacokinetics/therapeutic use ; Bacterial Proteins/chemistry/genetics/*metabolism ; Base Sequence ; Camptothecin/administration & dosage/analogs & ; derivatives/pharmacokinetics/therapeutic use ; Cell Line, Tumor ; Cloning, Molecular ; Clostridium/*chemistry/genetics ; Colorectal Neoplasms/*drug therapy ; Doxorubicin/*administration & dosage/pharmacokinetics/therapeutic use ; Drug Carriers ; Humans ; Lipase/chemistry/genetics/*metabolism ; Lipid Bilayers/chemistry ; Liposomes/chemistry/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasm Transplantation ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
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  • 32
    Publication Date: 2006-01-28
    Description: The spread of H5N1 avian influenza viruses (AIVs) from China to Europe has raised global concern about their potential to infect humans and cause a pandemic. In spite of their substantial threat to human health, remarkably little AIV whole-genome information is available. We report here a preliminary analysis of the first large-scale sequencing of AIVs, including 2196 AIV genes and 169 complete genomes. We combine this new information with public AIV data to identify new gene alleles, persistent genotypes, compensatory mutations, and a potential virulence determinant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Obenauer, John C -- Denson, Jackie -- Mehta, Perdeep K -- Su, Xiaoping -- Mukatira, Suraj -- Finkelstein, David B -- Xu, Xiequn -- Wang, Jinhua -- Ma, Jing -- Fan, Yiping -- Rakestraw, Karen M -- Webster, Robert G -- Hoffmann, Erich -- Krauss, Scott -- Zheng, Jie -- Zhang, Ziwei -- Naeve, Clayton W -- AI95357/AI/NIAID NIH HHS/ -- CA 21765/CA/NCI NIH HHS/ -- R01 GM061739/GM/NIGMS NIH HHS/ -- R01 GM069916/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 17;311(5767):1576-80. Epub 2006 Jan 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hartwell Center for Bioinformatics and Biotechnology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439620" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds/virology ; Computational Biology ; *Genes, Viral ; Genome, Viral ; Humans ; Influenza A Virus, H1N1 Subtype/genetics ; Influenza A Virus, H2N2 Subtype/genetics ; Influenza A Virus, H3N2 Subtype/genetics ; Influenza A Virus, H3N8 Subtype/genetics ; Influenza A Virus, H5N1 Subtype/chemistry/*genetics/pathogenicity ; Influenza A Virus, H5N2 Subtype/genetics ; Influenza A Virus, H7N7 Subtype/genetics ; Influenza A Virus, H9N2 Subtype/genetics ; Influenza A virus/chemistry/*genetics/isolation & purification/pathogenicity ; Influenza in Birds/virology ; Influenza, Human/virology ; Molecular Sequence Data ; Mutation ; Phylogeny ; RNA, Viral/genetics ; Reassortant Viruses/genetics ; Sequence Analysis, DNA ; Viral Nonstructural Proteins/*chemistry/genetics ; Viral Proteins/chemistry/genetics ; Virulence Factors/*chemistry/genetics
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  • 33
    Publication Date: 2006-10-28
    Description: The social amoebas (Dictyostelia) display conditional multicellularity in a wide variety of forms. Despite widespread interest in Dictyostelium discoideum as a model system, almost no molecular data exist from the rest of the group. We constructed the first molecular phylogeny of the Dictyostelia with parallel small subunit ribosomal RNA and a-tubulin data sets, and we found that dictyostelid taxonomy requires complete revision. A mapping of characters onto the phylogeny shows that the dominant trend in dictyostelid evolution is increased size and cell type specialization of fruiting structures, with some complex morphologies evolving several times independently. Thus, the latter may be controlled by only a few genes, making their underlying mechanisms relatively easy to unravel.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173941/" 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/PMC2173941/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaap, Pauline -- Winckler, Thomas -- Nelson, Michaela -- Alvarez-Curto, Elisa -- Elgie, Barrie -- Hagiwara, Hiromitsu -- Cavender, James -- Milano-Curto, Alicia -- Rozen, Daniel E -- Dingermann, Theodor -- Mutzel, Rupert -- Baldauf, Sandra L -- 057137/Wellcome Trust/United Kingdom -- 076618/Wellcome Trust/United Kingdom -- BB/D013453/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- COD16760/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):661-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Life Sciences, University of Dundee, DD15EH Dundee, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068267" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; DNA, Protozoan/genetics ; DNA, Ribosomal/genetics ; Dictyosteliida/*classification/*cytology/genetics/growth & development ; Dictyostelium/classification/cytology/genetics/growth & development ; Genes, Protozoan ; Molecular Sequence Data ; *Phylogeny ; RNA, Ribosomal/genetics ; Spores, Protozoan/cytology ; Tubulin/genetics
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  • 34
    Publication Date: 2006-09-02
    Description: Glycosyltransferases (GTs), an essential class of ubiquitous enzymes, are generally perceived as unidirectional catalysts. In contrast, we report that four glycosyltransferases from two distinct natural product biosynthetic pathways-calicheamicin and vancomycin-readily catalyze reversible reactions, allowing sugars and aglycons to be exchanged with ease. As proof of the broader applicability of these new reactions, more than 70 differentially glycosylated calicheamicin and vancomycin variants are reported. This study suggests the reversibility of GT-catalyzed reactions may be general and useful for generating exotic nucleotide sugars, establishing in vitro GT activity in complex systems, and enhancing natural product diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Changsheng -- Griffith, Byron R -- Fu, Qiang -- Albermann, Christoph -- Fu, Xun -- Lee, In-Kyoung -- Li, Lingjun -- Thorson, Jon S -- AI52218/AI/NIAID NIH HHS/ -- CA84374/CA/NCI NIH HHS/ -- GM70637/GM/NIGMS NIH HHS/ -- U19 CA113297/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, National Cooperative Drug Discovery Group Program, University of Wisconsin (UW)-Madison, 777 Highland Avenue, Madison, WI 53705-2222, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946071" target="_blank"〉PubMed〈/a〉
    Keywords: Aminoglycosides/biosynthesis/chemistry/*metabolism ; Carbohydrate Sequence ; Catalysis ; Enediynes ; Glucosyltransferases/*metabolism ; Glycosylation ; Glycosyltransferases/genetics/*metabolism ; Micromonospora/enzymology/genetics ; Molecular Sequence Data ; Molecular Structure ; Nucleoside Diphosphate Sugars/metabolism ; Pentoses/metabolism ; Thymine Nucleotides/metabolism ; Vancomycin/*analogs & derivatives/biosynthesis/chemistry/metabolism
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  • 35
    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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  • 36
    Publication Date: 2006-01-18
    Description: The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macrae, Ian J -- Zhou, Kaihong -- Li, Fei -- Repic, Adrian -- Brooks, Angela N -- Cande, W Zacheus -- Adams, Paul D -- Doudna, Jennifer A -- New York, N.Y. -- Science. 2006 Jan 13;311(5758):195-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16410517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Conserved Sequence ; Crystallography, X-Ray ; Giardia lamblia/enzymology ; Humans ; Lanthanoid Series Elements/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; RNA Interference ; RNA, Double-Stranded/*metabolism ; RNA, Protozoan/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribonuclease III/*chemistry/metabolism ; Schizosaccharomyces/genetics ; Structure-Activity Relationship
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  • 37
    Publication Date: 2006-03-25
    Description: Tracheal cytotoxin (TCT), a naturally occurring fragment of Gram-negative peptidoglycan, is a potent elicitor of innate immune responses in Drosophila. It induces the heterodimerization of its recognition receptors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficiency pathway. The crystal structure at 2.1 angstrom resolution of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the LCx ectodomain for recognition by the LCa ectodomain; the latter lacks a canonical peptidoglycan-docking groove conserved in other PGRPs. The interface, revealed in atomic detail, between TCT and the receptor complex highlights the importance of the anhydro-containing disaccharide in bridging the two ectodomains together and the critical role of diaminopimelic acid as the specificity determinant for PGRP interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Chung-I -- Chelliah, Yogarany -- Borek, Dominika -- Mengin-Lecreulx, Dominique -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1761-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park Road, Dallas, TX 75390-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556841" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Cytotoxins/*chemistry/metabolism ; Drosophila melanogaster ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Peptidoglycan/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 38
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    Unknown
    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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  • 39
    Publication Date: 2006-04-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, Demian D F -- Pikitch, Ellen K -- Babcock, Elizabeth A -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):526-8; author reply 526-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; Biomass ; Caribbean Region ; *Conservation of Natural Resources ; *Ecosystem ; Fisheries ; *Fishes ; Predatory Behavior ; *Sharks
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  • 40
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    Unknown
    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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  • 41
    Publication Date: 2006-06-17
    Description: The Xist noncoding RNA is the key initiator of the process of X chromosome inactivation in eutherian mammals, but its precise function and origin remain unknown. Although Xist is well conserved among eutherians, until now, no homolog has been identified in other mammals. We show here that Xist evolved, at least partly, from a protein-coding gene and that the loss of protein-coding function of the proto-Xist coincides with the four flanking protein genes becoming pseudogenes. This event occurred after the divergence between eutherians and marsupials, which suggests that mechanisms of dosage compensation have evolved independently in both lineages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duret, Laurent -- Chureau, Corinne -- Samain, Sylvie -- Weissenbach, Jean -- Avner, Philip -- New York, N.Y. -- Science. 2006 Jun 16;312(5780):1653-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biometrie et Biologie Evolutive (UMR 5558), CNRS and Universite Lyon 1, 16 rue Raphael Dubois, 69622 Villeurbanne Cedex, France. duret@biomserv.univ-lyon1.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778056" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle/genetics ; Chickens/genetics ; Dogs/genetics ; *Evolution, Molecular ; Exons ; Female ; Humans ; Male ; Mammals/*genetics ; Mice/genetics ; Molecular Sequence Data ; Opossums/genetics ; Phylogeny ; *Pseudogenes ; RNA, Long Noncoding ; RNA, Untranslated/*genetics ; Sequence Alignment ; Sequence Homology, Nucleic Acid ; Vertebrates/*genetics ; X Chromosome Inactivation ; Xenopus/genetics
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  • 42
    Publication Date: 2006-08-12
    Description: Transient infection of eukaryotic cells with commensal and extraintestinal pathogenic Escherichia coli of phylogenetic group B2 blocks mitosis and induces megalocytosis. This trait is linked to a widely spread genomic island that encodes giant modular nonribosomal peptide and polyketide synthases. Contact with E. coli expressing this gene cluster causes DNA double-strand breaks and activation of the DNA damage checkpoint pathway, leading to cell cycle arrest and eventually to cell death. Discovery of hybrid peptide-polyketide genotoxins in E. coli will change our view on pathogenesis and commensalism and open new biotechnological applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nougayrede, Jean-Philippe -- Homburg, Stefan -- Taieb, Frederic -- Boury, Michele -- Brzuszkiewicz, Elzbieta -- Gottschalk, Gerhard -- Buchrieser, Carmen -- Hacker, Jorg -- Dobrindt, Ulrich -- Oswald, Eric -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INRA, UMR1225, Ecole Nationale Veterinaire de Toulouse, Toulouse F-31076, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902142" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/chemistry ; Cytotoxins/*metabolism ; DNA/analysis ; *DNA Damage ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics/*pathogenicity/*physiology ; G2 Phase ; *Genomic Islands ; HeLa Cells ; Histones/metabolism ; Humans ; Intestinal Mucosa/cytology/microbiology ; Molecular Sequence Data ; Mutagenesis ; Mutagens/*metabolism ; Peptides/*metabolism ; Phosphorylation ; Polyketide Synthases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Rats ; Signal Transduction ; Tumor Suppressor Proteins/metabolism
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  • 43
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 44
    Publication Date: 2006-07-22
    Description: Rice fields are a global source of the greenhouse gas methane, which is produced by methanogenic archaea, and by methanogens of Rice Cluster I (RC-I) in particular. RC-I methanogens are not yet available in pure culture, and the mechanistic reasons for their prevalence in rice fields are unknown. We reconstructed a complete RC-I genome (3.18 megabases) using a metagenomic approach. Sequence analysis demonstrated an aerotolerant, H2/CO2-dependent lifestyle and enzymatic capacities for carbohydrate metabolism and assimilatory sulfate reduction, hitherto unknown among methanogens. These capacities and a unique set of antioxidant enzymes and DNA repair mechanisms as well as oxygen-insensitive enzymes provide RC-I with a selective advantage over other methanogens in its habitats, thereby explaining the prevalence of RC-I methanogens in the rice rhizosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erkel, Christoph -- Kube, Michael -- Reinhardt, Richard -- Liesack, Werner -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):370-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Terrestrial Microbiology, Karl-von-Frisch-Strasse, 35043 Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/biosynthesis/metabolism ; Carbohydrate Metabolism ; DNA Repair ; Euryarchaeota/classification/*genetics/metabolism/physiology ; *Genome, Archaeal ; Genomics ; Glycolysis ; Methane/*biosynthesis ; Methanomicrobiales/classification/genetics/metabolism/physiology ; Methanosarcinales/classification/genetics/metabolism/physiology ; Molecular Sequence Data ; Oryza/*microbiology ; Oxidative Stress ; Pyruvic Acid/metabolism ; Sequence Alignment ; Sequence Analysis, DNA ; *Soil Microbiology ; Sulfates/metabolism ; Sulfur/metabolism
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  • 45
    Publication Date: 2006-07-22
    Description: CorA family members are ubiquitously distributed transporters of divalent metal cations and are considered to be the primary Mg2+ transporter of Bacteria and Archaea. We have determined a 2.9 angstrom resolution structure of CorA from Thermotoga maritima that reveals a pentameric cone-shaped protein. Two potential regulatory metal binding sites are found in the N-terminal domain that bind both Mg2+ and Co2+. The structure of CorA supports an efflux system involving dehydration and rehydration of divalent metal ions potentially mediated by a ring of conserved aspartate residues at the cytoplasmic entrance and a carbonyl funnel at the periplasmic side of the pore.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eshaghi, Said -- Niegowski, Damian -- Kohl, Andreas -- Martinez Molina, Daniel -- Lesley, Scott A -- Nordlund, Par -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-171 77 Stockholm, Sweden. Said.Eshaghi@ki.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857941" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cation Transport Proteins/*chemistry/metabolism ; Chlorides/analysis/metabolism ; Cobalt/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrophobic and Hydrophilic Interactions ; Magnesium/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Thermotoga maritima/*chemistry ; Water/chemistry
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  • 46
    Publication Date: 2006-07-29
    Description: Comparative genomics of 45 epidemiologically varied variola virus isolates from the past 30 years of the smallpox era indicate low sequence diversity, suggesting that there is probably little difference in the isolates' functional gene content. Phylogenetic clustering inferred three clades coincident with their geographical origin and case-fatality rate; the latter implicated putative proteins that mediate viral virulence differences. Analysis of the viral linear DNA genome suggests that its evolution involved direct descent and DNA end-region recombination events. Knowing the sequences will help understand the viral proteome and improve diagnostic test precision, therapeutics, and systems for their assessment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Esposito, Joseph J -- Sammons, Scott A -- Frace, A Michael -- Osborne, John D -- Olsen-Rasmussen, Melissa -- Zhang, Ming -- Govil, Dhwani -- Damon, Inger K -- Kline, Richard -- Laker, Miriam -- Li, Yu -- Smith, Geoffrey L -- Meyer, Hermann -- Leduc, James W -- Wohlhueter, Robert M -- G0501257/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):807-12. Epub 2006 Jul 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Core Facility Branch, Division of Scientific Resources, National Center for Preparedness, Detection, and Control of Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, GA 30329, USA. jesposito@cdc.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16873609" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Viral/*genetics ; Disease Outbreaks ; *Evolution, Molecular ; Gene Deletion ; *Genetic Variation ; *Genome, Viral ; Genomics ; Humans ; Molecular Sequence Data ; Open Reading Frames ; Phylogeny ; Proteome/analysis/genetics ; Recombination, Genetic ; Sequence Analysis, DNA ; Smallpox/epidemiology/mortality/*virology ; Variola virus/classification/*genetics/isolation & purification/pathogenicity ; Viral Proteins/chemistry/genetics ; Virulence/genetics
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  • 47
    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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  • 48
    Publication Date: 2006-07-22
    Description: Resistance to the limited number of available antifungal drugs is a serious problem in the treatment of Candida albicans. We found that aneuploidy in general and a specific segmental aneuploidy, consisting of an isochromosome composed of the two left arms of chromosome 5, were associated with azole resistance. The isochromosome forms around a single centromere flanked by an inverted repeat and was found as an independent chromosome or fused at the telomere to a full-length homolog of chromosome 5. Increases and decreases in drug resistance were strongly associated with gain and loss of this isochromosome, which bears genes expressing the enzyme in the ergosterol pathway targeted by azole drugs, efflux pumps, and a transcription factor that positively regulates a subset of efflux pump genes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1717021/" 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/PMC1717021/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selmecki, Anna -- Forche, Anja -- Berman, Judith -- DE10641-S/DE/NIDCR NIH HHS/ -- R01 AI062427/AI/NIAID NIH HHS/ -- R01 AIO62427/PHS HHS/ -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Cell Biology, and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church Street SE, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16857942" target="_blank"〉PubMed〈/a〉
    Keywords: *Aneuploidy ; Antifungal Agents/*pharmacology ; Azoles/pharmacology ; Candida albicans/*drug effects/*genetics/growth & development ; Centromere/ultrastructure ; Chromosomes, Fungal ; Cytochrome P-450 Enzyme System/genetics/metabolism ; Drug Resistance, Fungal/*genetics ; Ergosterol/biosynthesis ; Fluconazole/*pharmacology ; Fungal Proteins/genetics/metabolism ; Gene Dosage ; Gene Expression Profiling ; Genes, Fungal ; *Isochromosomes ; Karyotyping ; Molecular Sequence Data ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA ; Transcription Factors/genetics/metabolism ; Trisomy
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  • 49
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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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  • 50
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    Unknown
    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):777.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902121" target="_blank"〉PubMed〈/a〉
    Keywords: *Acoustics ; *Animal Identification Systems ; Animals ; *Ecosystem ; Environment ; Fisheries ; *Fishes ; International Cooperation ; Movement ; Oceans and Seas ; Seawater ; Telemetry
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  • 51
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    Unknown
    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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  • 52
    Publication Date: 2006-07-11
    Description: The spindle checkpoint delays cell cycle progression until microtubules attach each pair of sister chromosomes to opposite poles of the mitotic spindle. Following sister chromatid separation, however, the checkpoint ignores chromosomes whose kinetochores are attached to only one spindle pole, a state that activates the checkpoint prior to metaphase. We demonstrate that, in budding yeast, mutual inhibition between the anaphase-promoting complex (APC) and Mps1, an essential component of the checkpoint, leads to sustained inactivation of the spindle checkpoint. Mps1 protein abundance decreases in anaphase, and Mps1 is a target of the APC. Furthermore, expression of Mps1 in anaphase, or repression of the APC in anaphase, reactivates the spindle checkpoint. This APC-Mps1 feedback circuit allows cells to irreversibly inactivate the checkpoint during anaphase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palframan, William J -- Meehl, Janet B -- Jaspersen, Sue L -- Winey, Mark -- Murray, Andrew W -- GM43987/GM/NIGMS NIH HHS/ -- GM51312/GM/NIGMS NIH HHS/ -- R37 GM043987/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):680-4. Epub 2006 Jul 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase/*physiology ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/metabolism ; Chromosomes, Fungal/physiology ; Feedback, Physiological ; GTP-Binding Proteins/metabolism ; Kinetochores/physiology ; Mad2 Proteins ; Mitosis ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*cytology/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Securin ; Spindle Apparatus/*physiology ; Ubiquitin-Protein Ligase Complexes/*metabolism
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  • 53
    Publication Date: 2006-12-16
    Description: A methanogenic archaeon isolated from deep-sea hydrothermal vent fluid was found to reduce N(2) to NH(3) at up to 92 degrees C, which is 28 degrees C higher than the current upper temperature limit of biological nitrogen fixation. The 16S ribosomal RNA gene of the hyperthermophilic nitrogen fixer, designated FS406-22, was 99% similar to that of non-nitrogen fixing Methanocaldococcus jannaschii DSM 2661. At its optimal growth temperature of 90 degrees C, FS406-22 incorporated (15)N(2) and expressed nifH messenger RNA. This increase in the temperature limit of nitrogen fixation could reveal a broader range of conditions for life in the subseafloor biosphere and other nitrogen-limited ecosystems than previously estimated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mehta, Mausmi P -- Baross, John A -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1783-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Oceanography, University of Washington, Seattle, WA 98195, USA. mausmi@alum.mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170307" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaea/classification/genetics/*isolation & purification/*metabolism ; Archaeal Proteins/chemistry/genetics/metabolism ; Base Sequence ; *Ecosystem ; Genes, Archaeal ; Genes, rRNA ; Geologic Sediments/microbiology ; *Hot Temperature ; Molecular Sequence Data ; Nitrogen/metabolism ; *Nitrogen Fixation/genetics ; Nitrogenase/chemistry/*genetics/metabolism ; Operon ; Oxidation-Reduction ; Oxidoreductases/chemistry/genetics/metabolism ; Pacific Ocean ; Phylogeny ; RNA, Ribosomal, 16S/genetics ; Seawater/*microbiology ; Volcanic Eruptions
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  • 54
    Publication Date: 2006-04-08
    Description: Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by "effector" proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain-containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure, and the unusual fold is required for its ability to bind methylated histone tails. The cocrystal structure of the JMJD2A double tudor domain with a trimethylated H3-K4 peptide reveals that the trimethyl-K4 is bound in a cage of three aromatic residues, two of which are from the tudor-2 motif, whereas the binding specificity is determined by side-chain interactions involving amino acids from the tudor-1 motif. Our study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Ying -- Fang, Jia -- Bedford, Mark T -- Zhang, Yi -- Xu, Rui-Ming -- DK62248/DK/NIDDK NIH HHS/ -- GM 63718/GM/NIGMS NIH HHS/ -- GM68804/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 May 5;312(5774):748-51. Epub 2006 Apr 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Histones/*chemistry/*metabolism ; Humans ; Hydrogen Bonding ; Jumonji Domain-Containing Histone Demethylases ; Lysine/metabolism ; Methylation ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oxidoreductases, N-Demethylating ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Static Electricity ; Transcription Factors/*chemistry/genetics/*metabolism
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  • 55
    Publication Date: 2006-10-28
    Description: Large-conductance calcium- and voltage-activated potassium channels (BKCa) are dually activated by membrane depolarization and elevation of cytosolic calcium ions (Ca2+). Under normal cellular conditions, BKCa channel activation requires Ca2+ concentrations that typically occur in close proximity to Ca2+ sources. We show that BKCa channels affinity-purified from rat brain are assembled into macromolecular complexes with the voltage-gated calcium channels Cav1.2 (L-type), Cav2.1 (P/Q-type), and Cav2.2 (N-type). Heterologously expressed BKCa-Cav complexes reconstitute a functional "Ca2+ nanodomain" where Ca2+ influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics. Complex formation with distinct Cav channels enables BKCa-mediated membrane hyperpolarization that controls neuronal firing pattern and release of hormones and transmitters in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berkefeld, Henrike -- Sailer, Claudia A -- Bildl, Wolfgang -- Rohde, Volker -- Thumfart, Jorg-Oliver -- Eble, Silke -- Klugbauer, Norbert -- Reisinger, Ellen -- Bischofberger, Josef -- Oliver, Dominik -- Knaus, Hans-Gunther -- Schulte, Uwe -- Fakler, Bernd -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):615-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068255" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain Chemistry ; CHO Cells ; Calcium/*metabolism ; Calcium Channels, L-Type/drug effects/isolation & purification/*metabolism ; Calcium Channels, N-Type/drug effects/isolation & purification/*metabolism ; Calcium Signaling ; Chromaffin Cells/drug effects/metabolism ; Cricetinae ; Cricetulus ; Egtazic Acid/analogs & derivatives/pharmacology ; Large-Conductance Calcium-Activated Potassium Channels/drug effects/isolation & ; purification/*metabolism ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Patch-Clamp Techniques ; Potassium/*metabolism ; Rats ; *Signal Transduction ; Transfection ; Xenopus
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  • 56
    Publication Date: 2006-11-04
    Description: Guanosine triphosphatases of the Rab family are key regulators of membrane trafficking, with Rab11 playing a specific role in membrane recycling. We identified a mammalian protein, protrudin, that promoted neurite formation through interaction with the guanosine diphosphate (GDP)-bound form of Rab11. Phosphorylation of protrudin by extracellular signal-regulated kinase (ERK) in response to nerve growth factor promoted protrudin association with Rab11-GDP. Down-regulation of protrudin by RNA interference induced membrane extension in all directions and inhibited neurite formation. Thus, protrudin regulates Rab11-dependent membrane recycling to promote the directional membrane trafficking required for neurite formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shirane, Michiko -- Nakayama, Keiichi I -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):818-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082457" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Adhesion Molecules/metabolism ; Cell Line ; Cell Membrane/*metabolism ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Guanosine Diphosphate/metabolism ; HeLa Cells ; Humans ; MAP Kinase Kinase 1/metabolism ; Membrane Proteins ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Nerve Growth Factor/pharmacology/physiology ; Neurites/*physiology ; PC12 Cells ; Phosphorylation ; RNA Interference ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Vesicular Transport Proteins ; rab GTP-Binding Proteins/metabolism
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  • 57
    Publication Date: 2006-10-28
    Description: Neuropeptides, critical brain peptides that modulate animal behavior by affecting the activity of almost every neuronal circuit, are inherently difficult to predict directly from a nascent genome sequence because of extensive posttranslational processing. The combination of bioinformatics and proteomics allows unprecedented neuropeptide discovery from an unannotated genome. Within the Apis mellifera genome, we have inferred more than 200 neuropeptides and have confirmed the sequences of 100 peptides. This study lays the groundwork for future molecular studies of Apis neuropeptides with the identification of 36 genes, 33 of which were previously unreported.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hummon, Amanda B -- Richmond, Timothy A -- Verleyen, Peter -- Baggerman, Geert -- Huybrechts, Jurgen -- Ewing, Michael A -- Vierstraete, Evy -- Rodriguez-Zas, Sandra L -- Schoofs, Liliane -- Robinson, Gene E -- Sweedler, Jonathan V -- DC006395/DC/NIDCD NIH HHS/ -- GM068946/GM/NIGMS NIH HHS/ -- NS31609/NS/NINDS NIH HHS/ -- P30 DA01830/DA/NIDA NIH HHS/ -- P30 DA018310/DA/NIDA NIH HHS/ -- R01 GM068946/GM/NIGMS NIH HHS/ -- R01 NS031609/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):647-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Illinois, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068263" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Bees/*chemistry/*genetics ; Brain Chemistry ; Codon ; Computational Biology ; *Genes, Insect ; Genome, Insect ; Insect Proteins/*chemistry/*genetics ; Mass Spectrometry ; Molecular Sequence Data ; Neuropeptides/*chemistry/*genetics ; Protein Precursors/chemistry/genetics ; Proteome
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  • 58
    Publication Date: 2006-04-29
    Description: Rice blast is caused by the fungus Magnaporthe grisea, which elaborates specialized infection cells called appressoria to penetrate the tough outer cuticle of the rice plant Oryza sativa. We found that the formation of an appressorium required, sequentially, the completion of mitosis, nuclear migration, and death of the conidium (fungal spore) from which the infection originated. Genetic intervention during mitosis prevented both appressorium development and conidium death. Impairment of autophagy, by the targeted mutation of the MgATG8 gene, arrested conidial cell death but rendered the fungus nonpathogenic. Thus, the initiation of rice blast requires autophagic cell death of the conidium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veneault-Fourrey, Claire -- Barooah, Madhumita -- Egan, Martin -- Wakley, Gavin -- Talbot, Nicholas J -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Biosciences, University of Exeter, Washington Singer Laboratories, Perry Road, Exeter EX4 4QG, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Autophagy ; Benomyl/pharmacology ; Cell Nucleus/physiology ; Cell Nucleus Division ; Genes, Fungal ; Hydroxyurea/pharmacology ; Magnaporthe/*cytology/genetics/pathogenicity/*physiology ; Microtubule-Associated Proteins/genetics/physiology ; Mitosis/drug effects ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Oryza/*microbiology ; Plant Diseases/*microbiology ; Spores, Fungal/cytology/*physiology
    Print ISSN: 0036-8075
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  • 59
    Publication Date: 2006-12-23
    Description: Cartilaginous fishes represent the living group of jawed vertebrates that diverged from the common ancestor of human and teleost fish lineages about 530 million years ago. We generated approximately 1.4x genome sequence coverage for a cartilaginous fish, the elephant shark (Callorhinchus milii), and compared this genome with the human genome to identify conserved noncoding elements (CNEs). The elephant shark sequence revealed twice as many CNEs as were identified by whole-genome comparisons between teleost fishes and human. The ancient vertebrate-specific CNEs in the elephant shark and human genomes are likely to play key regulatory roles in vertebrate gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venkatesh, Byrappa -- Kirkness, Ewen F -- Loh, Yong-Hwee -- Halpern, Aaron L -- Lee, Alison P -- Johnson, Justin -- Dandona, Nidhi -- Viswanathan, Lakshmi D -- Tay, Alice -- Venter, J Craig -- Strausberg, Robert L -- Brenner, Sydney -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1892.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673. mcbbv@imcb.a-star.edu.sg〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185593" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Conserved Sequence ; DNA, Intergenic ; Enhancer Elements, Genetic ; Evolution, Molecular ; Genome ; *Genome, Human ; Humans ; Molecular Sequence Data ; *Regulatory Sequences, Nucleic Acid ; Sharks/*genetics ; Takifugu/genetics ; Zebrafish/genetics
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  • 60
    Publication Date: 2006-12-02
    Description: We describe a transgenesis platform for Drosophila melanogaster that integrates three recently developed technologies: a conditionally amplifiable bacterial artificial chromosome (BAC), recombineering, and bacteriophage PhiC31-mediated transgenesis. The BAC is maintained at low copy number, facilitating plasmid maintenance and recombineering, but is induced to high copy number for plasmid isolation. Recombineering allows gap repair and mutagenesis in bacteria. Gap repair efficiently retrieves DNA fragments up to 133 kilobases long from P1 or BAC clones. PhiC31-mediated transgenesis integrates these large DNA fragments at specific sites in the genome, allowing the rescue of lethal mutations in the corresponding genes. This transgenesis platform should greatly facilitate structure/function analyses of most Drosophila genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Venken, Koen J T -- He, Yuchun -- Hoskins, Roger A -- Bellen, Hugo J -- GM067858-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1747-51. Epub 2006 Nov 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Developmental Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138868" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; *Chromosomes, Artificial, Bacterial ; Cloning, Molecular/*methods ; DNA Repair ; *DNA Transposable Elements ; Drosophila melanogaster/*genetics ; *Gene Transfer Techniques ; Genes, Insect ; Genetic Vectors ; Molecular Sequence Data ; Mutagenesis ; Plasmids ; Recombination, Genetic ; Siphoviridae/*genetics ; Transgenes ; Transposases/metabolism
    Print ISSN: 0036-8075
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  • 61
    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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  • 62
    Publication Date: 2006-12-16
    Description: Antibody class switching in activated B cells uses class switch recombination (CSR), which joins activation-induced cytidine deaminase (AID)-dependent double-strand breaks (DSBs) within two large immunoglobulin heavy chain (IgH) locus switch (S) regions that lie up to 200 kilobases apart. To test postulated roles of S regions and AID in CSR, we generated mutant B cells in which donor Smu and accepter Sgamma1 regions were replaced with yeast I-SceI endonuclease sites. We found that site-specific I-SceI DSBs mediate recombinational IgH locus class switching from IgM to IgG1 without S regions or AID. We propose that CSR evolved to exploit a general DNA repair process that promotes joining of widely separated DSBs within a chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zarrin, Ali A -- Del Vecchio, Catherine -- Tseng, Eva -- Gleason, Megan -- Zarin, Payam -- Tian, Ming -- Alt, Frederick W -- 2P01AI031541-15/AI/NIAID NIH HHS/ -- P01CA092625-05/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 19;315(5810):377-81. Epub 2006 Dec 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Children's Hospital, CBR Institute for Biomedical Research, and Department of Genetics, Harvard University Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170253" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Base Sequence ; Cell Line ; Cytidine Deaminase/*metabolism ; *DNA Breaks, Double-Stranded ; DNA Repair ; Deoxyribonucleases, Type II Site-Specific/genetics/*metabolism ; Embryonic Stem Cells ; Gene Targeting ; Genes, Immunoglobulin Heavy Chain ; Hybridomas ; *Immunoglobulin Class Switching ; Immunoglobulin G/biosynthesis/genetics ; Immunoglobulin M/biosynthesis/genetics ; *Immunoglobulin Switch Region ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Recombination, Genetic ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins
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  • 63
    Publication Date: 2006-12-23
    Description: Double-stranded RNA, processed to small interfering RNAs (siRNAs) by Dicer and incorporated into the RNA-induced silencing complex (RISC), triggers gene silencing by a variety of pathways in eukaryotes. RNA interference involving the degradation of homologous transcripts is the best-characterized mechanism. However, the fate of the RNA fragments resulting from siRNA-directed cleavage is poorly understood. We have identified a gene (MUT68) in the unicellular green alga Chlamydomonas reinhardtii that is required for the efficient decay of siRNA-targeted transcripts. MUT68 encodes a noncanonical polyadenylate polymerase that adds untemplated adenines to the 5' RNA fragments after siRNA-mediated cleavage and appears to stimulate their exosome-dependent degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibrahim, Fadia -- Rohr, Jennifer -- Jeong, Won-Joong -- Hesson, Jennifer -- Cerutti, Heriberto -- GM62915/GM/NIGMS NIH HHS/ -- R01 GM062915-06/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 22;314(5807):1893.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Sciences and Plant Science Initiative, University of Nebraska, Lincoln, NE 68588, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185594" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/*metabolism ; Animals ; Chlamydomonas reinhardtii/enzymology/*genetics/*metabolism ; Exoribonucleases/metabolism ; Molecular Sequence Data ; Oligoribonucleotides/*metabolism ; Polynucleotide Adenylyltransferase/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; RNA, Small Interfering/metabolism ; RNA-Induced Silencing Complex/*metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Templates, Genetic ; Transgenes ; Tryptophan Synthase/genetics ; Uracil Nucleotides/metabolism
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  • 64
    Publication Date: 2006-08-12
    Description: The Arabidopsis CLAVATA3 (CLV3) gene encodes a stem cell-specific protein presumed to be a precursor of a secreted peptide hormone. Matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS) applied to in situ Arabidopsis tissues determined the structure of a modified 12-amino acid peptide (MCLV3), which was derived from a conserved motif in the CLV3 sequence. Synthetic MCLV3 induced shoot and root meristem consumption as cells differentiated into other organs, displaying the typical phenotype of transgenic plants overexpressing CLV3. These results suggest that the functional peptide of CLV3 is MCLV3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kondo, Tatsuhiko -- Sawa, Shinichiro -- Kinoshita, Atsuko -- Mizuno, Satoko -- Kakimoto, Tatsuo -- Fukuda, Hiroo -- Sakagami, Youji -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):845-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Bio-Agricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/*cytology/genetics/metabolism ; Arabidopsis Proteins/*chemistry/genetics/*metabolism/pharmacology ; Cell Differentiation ; Cells, Cultured ; Hydroxyproline/chemistry ; Meristem/*cytology/drug effects/metabolism ; Molecular Sequence Data ; Oligopeptides/chemistry/*metabolism/pharmacology ; Plant Roots/growth & development ; Plants, Genetically Modified ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Stem Cells/cytology
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  • 65
    Publication Date: 2006-04-15
    Description: Loss of seed shattering was a key event in the domestication of major cereals. We revealed that the qSH1 gene, a major quantitative trait locus of seed shattering in rice, encodes a BEL1-type homeobox gene and demonstrated that a single-nucleotide polymorphism (SNP) in the 5' regulatory region of the qSH1 gene caused loss of seed shattering owing to the absence of abscission layer formation. Haplotype analysis and association analysis in various rice collections revealed that the SNP was highly associated with shattering among japonica subspecies of rice, implying that it was a target of artificial selection during rice domestication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Konishi, Saeko -- Izawa, Takeshi -- Lin, Shao Yang -- Ebana, Kaworu -- Fukuta, Yoshimichi -- Sasaki, Takuji -- Yano, Masahiro -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1392-6. Epub 2006 Apr 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of the Society for Techno-Innovation of Agriculture, Forestry, and Fisheries, 446-1 Ippaizuka, Kamiyokoba Tsukuba, Ibaraki 305-0854, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614172" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/*history ; Alleles ; Chromosome Mapping ; Chromosomes, Plant ; Crops, Agricultural/*genetics/history ; Genes, Plant ; History, Ancient ; Humans ; Molecular Sequence Data ; Oryza/*genetics/history ; Plant Proteins/genetics ; *Polymorphism, Single Nucleotide ; Quantitative Trait Loci ; *Seeds ; Transcription Factors/genetics
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sieberer, Tobias -- Leyser, Ottoline -- BBS/B/09392/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 May 12;312(5775):858-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of York, York YO10 4YW, UK. ts20@york.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690849" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/metabolism ; Arabidopsis/cytology/growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Biological Transport ; Cell Membrane/metabolism ; Indoleacetic Acids/*metabolism ; Membrane Proteins/genetics/metabolism ; Models, Biological ; Phthalimides/metabolism ; Plant Proteins/genetics/*metabolism ; Plant Roots/metabolism ; Tobacco/cytology/growth & development/*metabolism
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  • 67
    Publication Date: 2006-02-25
    Description: Sibly et al. (Reports, 22 July 2005, p. 607) concluded that density dependence acts far below the carrying capacity in most animal populations. We argue that the authors confused discrete and continuous models, that their best-fit models cannot explain observed oscillations, and that their estimation procedures appear biased. They also neglected trophic and migratory processes, which we demonstrate could underlie their empirical findings.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Getz, Wayne M -- Lloyd-Smith, James O -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1100; author reply 1100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Sciences, Policy, and Management, University of California at Berkeley, CA 94720-3114, USA. getz@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497915" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Birds ; Conservation of Natural Resources ; Databases, Factual ; Ecosystem ; *Fishes ; *Insects ; Logistic Models ; *Mammals ; Mathematics ; Models, Biological ; Population Density ; Population Dynamics ; Population Growth ; Regression Analysis
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  • 68
    Publication Date: 2006-08-05
    Description: Almost every vertebrate cell has a specialized cell surface projection called a primary cilium. Although these structures were first described more than a century ago, the full scope of their functions remains poorly understood. Here, we review emerging evidence that in addition to their well-established roles in sight, smell, and mechanosensation, primary cilia are key participants in intercellular signaling. This new appreciation of primary cilia as cellular antennae that sense a wide variety of signals could help explain why ciliary defects underlie such a wide range of human disorders, including retinal degeneration, polycystic kidney disease, Bardet-Biedl syndrome, and neural tube defects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Singla, Veena -- Reiter, Jeremy F -- R21 DK069423/DK/NIDDK NIH HHS/ -- R21DK69423/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):629-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Developmental and Stem Cell Biology, and Diabetes Center, University of California, San Francisco, CA 94143-0525, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16888132" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bardet-Biedl Syndrome/pathology/physiopathology ; Biological Evolution ; Cell Polarity ; Cilia/*physiology ; Hedgehog Proteins ; Humans ; Mechanoreceptors/physiology ; Models, Biological ; Neural Tube Defects/pathology/physiopathology ; Polycystic Kidney Diseases/pathology/physiopathology ; Retinal Degeneration/pathology/physiopathology ; *Signal Transduction ; Smell/physiology ; Trans-Activators/metabolism ; Vision, Ocular/physiology ; Wnt Proteins/metabolism
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  • 69
    Publication Date: 2006-06-24
    Description: The orb web is a spectacular evolutionary innovation that enables spiders to catch flying prey. This elegant, geometric structure is woven with silk fibers that are renowned for their superior mechanical properties. We used silk gland expression libraries to address a long-standing controversy concerning the evolution of the orb-web architecture. Contrary to the view that the orb-web design evolved multiple times, we found that the distribution and phylogeny of silk proteins support a single, ancient origin of the orb web at least 136 million years ago. Furthermore, we substantially expanded the repository of silk sequences that can be used for the synthesis of high-performance biomaterials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garb, Jessica E -- Dimauro, Teresa -- Vo, Victoria -- Hayashi, Cheryl Y -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1762.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, Riverside, CA 92521, USA. jessica.garb@ucr.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794073" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Complementary ; Fibroins/*genetics ; *Genes ; Molecular Sequence Data ; Phylogeny ; Silk/*genetics ; Spiders/classification/*genetics/physiology
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  • 70
    Publication Date: 2006-01-28
    Description: Directly transmitted parasites often provide substantial information about the temporal and spatial characteristics of host-to-host contact. Here, we demonstrate that a fast-evolving virus (feline immunodeficiency virus, FIV) can reveal details of the contemporary population structure and recent demographic history of its natural wildlife host (Puma concolor) that were not apparent from host genetic data and would be impossible to obtain by other means. We suggest that rapidly evolving pathogens may provide a complementary tool for studying population dynamics of their hosts in "shallow" time.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biek, Roman -- Drummond, Alexei J -- Poss, Mary -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):538-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wildlife Biology Program, University of Montana, Missoula, MT 59812, USA. rbiek@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439664" target="_blank"〉PubMed〈/a〉
    Keywords: Alberta/epidemiology ; Animals ; Bayes Theorem ; British Columbia/epidemiology ; Ecosystem ; *Evolution, Molecular ; Genes, env ; Genes, pol ; Geography ; Immunodeficiency Virus, Feline/*classification/*genetics ; Lentivirus Infections/epidemiology/*veterinary/virology ; Microsatellite Repeats ; Molecular Sequence Data ; Montana/epidemiology ; Phylogeny ; Population Dynamics ; *Puma/genetics/virology ; Time Factors ; Wyoming/epidemiology
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  • 71
    Publication Date: 2006-07-01
    Description: The clock gene period-4 (prd-4) in Neurospora was identified by a single allele displaying shortened circadian period and altered temperature compensation. Positional cloning followed by functional tests show that PRD-4 is an ortholog of mammalian checkpoint kinase 2 (Chk2). Expression of prd-4 is regulated by the circadian clock and, reciprocally, PRD-4 physically interacts with the clock component FRQ, promoting its phosphorylation. DNA-damaging agents can reset the clock in a manner that depends on time of day, and this resetting is dependent on PRD-4. Thus, prd-4, the Neurospora Chk2, identifies a molecular link that feeds back conditionally from circadian output to input and the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pregueiro, Antonio M -- Liu, Qiuyun -- Baker, Christopher L -- Dunlap, Jay C -- Loros, Jennifer J -- MH44651/MH/NIMH NIH HHS/ -- P01 GM068087/GM/NIGMS NIH HHS/ -- R01 GM034985/GM/NIGMS NIH HHS/ -- R37GM34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):644-9. Epub 2006 Jun 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Dartmouth Medical School, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809488" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle ; Checkpoint Kinase 2 ; *Circadian Rhythm ; Cloning, Molecular ; DNA Damage ; Feedback, Physiological ; Fungal Proteins/chemistry/genetics/metabolism ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutation ; Neurospora/*enzymology/genetics ; Neurospora crassa/cytology/*enzymology/*physiology ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*genetics/*metabolism
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  • 72
    Publication Date: 2006-10-14
    Description: Intracellular bacteria are characterized by genome reduction. The 422,434-base pair genome of Buchnera aphidicola BCc, primary endosymbiont of the aphid Cinara cedri, is approximately 200 kilobases smaller than the previously sequenced B. aphidicola genomes. B. aphidicola BCc has lost most metabolic functions, including the ability to synthesize the essential amino acid tryptophan and riboflavin. In addition, most retained genes are evolving rapidly. Possibly, B. aphidicola BCc is losing its symbiotic capacity and is being complemented (and might be replaced) by the highly abundant coexisting secondary symbiont.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perez-Brocal, Vicente -- Gil, Rosario -- Ramos, Silvia -- Lamelas, Araceli -- Postigo, Marina -- Michelena, Jose Manuel -- Silva, Francisco J -- Moya, Andres -- Latorre, Amparo -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):312-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Cavanilles de Biodiversitat i Biologia Evolutiva, Universitat de Valencia, Apartado Postal 22085, 46071 Valencia, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038625" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/biosynthesis ; Animals ; Aphids/*microbiology/physiology ; Base Pairing ; Buchnera/*genetics/metabolism/physiology ; Chromosomes, Bacterial/genetics ; Evolution, Molecular ; Genes, Bacterial ; *Genome, Bacterial ; Molecular Sequence Data ; Sequence Analysis, DNA ; Serratia/genetics/metabolism/physiology ; *Symbiosis ; Tryptophan/biosynthesis
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  • 73
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1230-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946049" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*growth & development/metabolism ; Arabidopsis Proteins/chemistry/*metabolism ; Bacteria/metabolism ; Bacterial Physiological Phenomena ; Computer Simulation ; F-Box Proteins/chemistry/*metabolism ; Gene Expression Regulation, Plant ; Indoleacetic Acids/*metabolism ; MicroRNAs/metabolism ; Models, Biological ; *Plant Development ; Plant Growth Regulators/*metabolism ; Plant Proteins/*metabolism ; Plants/genetics/metabolism/microbiology ; RNA Interference ; RNA, Plant/metabolism ; Receptors, Cell Surface/chemistry/*metabolism ; Signal Transduction
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  • 74
    Publication Date: 2006-11-04
    Description: Nuclear pore complexes permit rapid passage of cargoes bound to nuclear transport receptors, but otherwise suppress nucleocytoplasmic fluxes of inert macromolecules 〉/=30 kilodaltons. To explain this selectivity, a sieve structure of the permeability barrier has been proposed that is created through reversible cross-linking between Phe and Gly (FG)-rich nucleoporin repeats. According to this model, nuclear transport receptors overcome the size limit of the sieve and catalyze their own nuclear pore-passage by a competitive disruption of adjacent inter-repeat contacts, which transiently opens adjoining meshes. Here, we found that phenylalanine-mediated inter-repeat interactions indeed cross-link FG-repeat domains into elastic and reversible hydrogels. Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frey, Steffen -- Richter, Ralf P -- Gorlich, Dirk -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):815-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie der Universitat Heidelberg (ZMBH), INF 282, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082456" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Motifs ; Amino Acid Sequence ; Biopolymers ; Calcium-Binding Proteins/*chemistry/genetics/*metabolism ; Fluorescence Recovery After Photobleaching ; HeLa Cells ; Humans ; Hydrogels ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Models, Biological ; Molecular Sequence Data ; Mutation ; Nuclear Pore/chemistry/*metabolism ; Nuclear Pore Complex Proteins/*chemistry/*metabolism ; Nuclear Proteins/*chemistry/genetics/*metabolism ; Nucleocytoplasmic Transport Proteins/*metabolism ; Permeability ; Phenylalanine/chemistry ; Protein Structure, Tertiary ; Repetitive Sequences, Amino Acid ; Saccharomyces cerevisiae/chemistry/physiology ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
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  • 75
    Publication Date: 2006-08-19
    Description: To understand evolutionary paths connecting diverse biological forms, we defined a three-dimensional genotypic space separating two flower color morphs of Antirrhinum. A hybrid zone between morphs showed a steep cline specifically at genes controlling flower color differences, indicating that these loci are under selection. Antirrhinum species with diverse floral phenotypes formed a U-shaped cloud within the genotypic space. We propose that this cloud defines an evolutionary path that allows flower color to evolve while circumventing less-adaptive regions. Hybridization between morphs located in different arms of the U-shaped path yields low-fitness genotypes, accounting for the observed steep clines at hybrid zones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whibley, Annabel C -- Langlade, Nicolas B -- Andalo, Christophe -- Hanna, Andrew I -- Bangham, Andrew -- Thebaud, Christophe -- Coen, Enrico -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):963-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917061" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Alleles ; Antirrhinum/classification/*genetics ; Base Sequence ; *Biological Evolution ; Crosses, Genetic ; Flowers/*genetics ; Gene Flow ; Gene Frequency ; Genes, Plant ; *Genetic Speciation ; Genotype ; Haplotypes ; Hybridization, Genetic ; Models, Genetic ; Molecular Sequence Data ; Phenotype ; Phylogeny ; Pigmentation/*genetics ; Pigments, Biological/genetics ; Principal Component Analysis ; Selection, Genetic
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  • 76
    Publication Date: 2006-06-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bosch, Xavier -- Vogel, Gretchen -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1295.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741086" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes ; Models, Biological ; Spain ; *Systems Biology
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  • 77
    Publication Date: 2006-10-07
    Description: The evolutionary dynamics underlying the latitudinal gradient in biodiversity have been controversial for over a century. Using a spatially explicit approach that incorporates not only origination and extinction but immigration, a global analysis of genera and subgenera of marine bivalves over the past 11 million years supports an "out of the tropics" model, in which taxa preferentially originate in the tropics and expand toward the poles without losing their tropical presence. The tropics are thus both a cradle and a museum of biodiversity, contrary to the conceptual dichotomy dominant since 1974; a tropical diversity crisis would thus have profound evolutionary effects at all latitudes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jablonski, David -- Roy, Kaustuv -- Valentine, James W -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):102-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geophysical Sciences, University of Chicago, 5734 South Ellis Avenue, Chicago, IL 60637, USA. djablons@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Bivalvia/classification ; *Fossils ; Geography ; Models, Biological ; Phylogeny ; Population Dynamics ; *Tropical Climate
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  • 78
    Publication Date: 2006-08-05
    Description: Assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) syntaxin 1, SNAP-25, and synaptobrevin 2 is thought to be the driving force for the exocytosis of synaptic vesicles. However, whereas exocytosis is triggered at a millisecond time scale, the SNARE-mediated fusion of liposomes requires hours for completion, which challenges the idea of a key role for SNAREs in the final steps of exocytosis. We found that liposome fusion was dramatically accelerated when a stabilized syntaxin/SNAP-25 acceptor complex was used. Thus, SNAREs do have the capacity to execute fusion at a speed required for neuronal secretion, demonstrating that the maintenance of acceptor complexes is a critical step in biological fusion reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pobbati, Ajaybabu V -- Stein, Alexander -- Fasshauer, Dirk -- P01 GM072694/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):673-6.〈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/16888141" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Circular Dichroism ; Dimerization ; Exocytosis ; Liposomes/*chemistry ; *Membrane Fusion ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Secondary ; Qa-SNARE Proteins/chemistry/*metabolism ; R-SNARE Proteins/chemistry/metabolism ; Rats ; Synaptosomal-Associated Protein 25/chemistry/*metabolism
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  • 79
    Publication Date: 2006-07-01
    Description: We found an extraordinary level of bacterial biodiversity in the tree leaf canopy of a tropical Atlantic forest by using culture-independent molecular methods. Our survey suggests that each tree species selects for a distinct microbial community. Analysis of the bacterial 16S ribosomal RNA gene sequences revealed that about 97% of the bacteria were unknown species and that the phyllosphere of any one tree species carries at least 95 to 671 bacterial species. The tree canopies of tropical forests likely represent a large reservoir of unexplored microbial diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lambais, M R -- Crowley, D E -- Cury, J C -- Bull, R C -- Rodrigues, R R -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1917.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Soils and Soil Science, University of Sao Paulo, Piracicaba, Sao Paulo, Brazil. mlambais@esalq.usp.br〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809531" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*classification/genetics/*isolation & purification ; *Biodiversity ; Brazil ; DNA Fingerprinting ; *Ecosystem ; Genes, rRNA ; Molecular Sequence Data ; Plant Leaves/*microbiology ; RNA, Ribosomal, 16S/genetics ; Trees/*microbiology ; Tropical Climate
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  • 80
    Publication Date: 2006-11-18
    Description: N-linked protein glycosylation is found in all domains of life. In eukaryotes, it is the most abundant protein modification of secretory and membrane proteins, and the process is coupled to protein translocation and folding. We found that in bacteria, N-glycosylation can occur independently of the protein translocation machinery. In an in vitro assay, bacterial oligosaccharyltransferase glycosylated a folded endogenous substrate protein with high efficiency and folded bovine ribonuclease A with low efficiency. Unfolding the eukaryotic substrate greatly increased glycosylation. We propose that in the bacterial system, glycosylation sites are located in flexible parts of folded proteins, whereas the eukaryotic cotranslational glycosylation evolved to a mechanism presenting the substrate in a flexible form before folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kowarik, Michael -- Numao, Shin -- Feldman, Mario F -- Schulz, Benjamin L -- Callewaert, Nico -- Kiermaier, Eva -- Catrein, Ina -- Aebi, Markus -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1148-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Microbiology, Department of Biology, Eidgenossische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/*metabolism ; Campylobacter jejuni ; Cattle ; Escherichia coli ; Glycoproteins/*metabolism ; Glycosylation ; Hexosyltransferases/metabolism ; Membrane Proteins/metabolism ; Molecular Sequence Data ; *Protein Folding ; Protein Transport ; Recombinant Proteins/metabolism
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  • 81
    Publication Date: 2006-03-25
    Description: Prochlorococcus ecotypes are a useful system for exploring the origin and function of diversity among closely related microbes. The genetic variability between phenotypically distinct strains that differ by less that 1% in 16S ribosomal RNA sequences occurs mostly in genomic islands. Island genes appear to have been acquired in part by phage-mediated lateral gene transfer, and some are differentially expressed under light and nutrient stress. Furthermore, genome fragments directly recovered from ocean ecosystems indicate that these islands are variable among cooccurring Prochlorococcus cells. Genomic islands in this free-living photoautotroph share features with pathogenicity islands of parasitic bacteria, suggesting a general mechanism for niche differentiation in microbial species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coleman, Maureen L -- Sullivan, Matthew B -- Martiny, Adam C -- Steglich, Claudia -- Barry, Kerrie -- Delong, Edward F -- Chisholm, Sallie W -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1768-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts Institute of Technology, Department of Civil and Environmental Engineering, 15 Vassar Street, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Atlantic Ocean ; Bacteriophages/*genetics/physiology ; *Biological Evolution ; *Ecosystem ; Gene Expression Regulation, Bacterial ; Gene Transfer, Horizontal ; Genes, Bacterial ; Genome, Bacterial ; *Genomic Islands ; Light ; Molecular Sequence Data ; Pacific Ocean ; Phylogeny ; Prochlorococcus/classification/*genetics/isolation & purification/*physiology ; Seawater/*microbiology
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  • 82
    Publication Date: 2006-06-03
    Description: The human intestinal microbiota is composed of 10(13) to 10(14) microorganisms whose collective genome ("microbiome") contains at least 100 times as many genes as our own genome. We analyzed approximately 78 million base pairs of unique DNA sequence and 2062 polymerase chain reaction-amplified 16S ribosomal DNA sequences obtained from the fecal DNAs of two healthy adults. Using metabolic function analyses of identified genes, we compared our human genome with the average content of previously sequenced microbial genomes. Our microbiome has significantly enriched metabolism of glycans, amino acids, and xenobiotics; methanogenesis; and 2-methyl-d-erythritol 4-phosphate pathway-mediated biosynthesis of vitamins and isoprenoids. Thus, humans are superorganisms whose metabolism represents an amalgamation of microbial and human attributes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3027896/" 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/PMC3027896/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gill, Steven R -- Pop, Mihai -- Deboy, Robert T -- Eckburg, Paul B -- Turnbaugh, Peter J -- Samuel, Buck S -- Gordon, Jeffrey I -- Relman, David A -- Fraser-Liggett, Claire M -- Nelson, Karen E -- AI51259/AI/NIAID NIH HHS/ -- DK70977/DK/NIDDK NIH HHS/ -- R01 AI051259/AI/NIAID NIH HHS/ -- R01 AI051259-04/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 2;312(5778):1355-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA. srgill@buffalo.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16741115" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Bacteria/classification/*genetics/isolation & purification ; Bifidobacterium/genetics ; *DNA, Ribosomal ; Dietary Carbohydrates/metabolism ; Dietary Fiber/metabolism ; Feces/microbiology ; Female ; Fermentation ; *Genetic Variation ; Genome, Bacterial ; Genomics ; Humans ; Intestinal Mucosa/metabolism/microbiology ; Intestines/metabolism/*microbiology ; Male ; Molecular Sequence Data ; Open Reading Frames ; Phylogeny ; RNA, Ribosomal, 16S/genetics ; Xenobiotics/metabolism
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  • 83
    Publication Date: 2006-08-12
    Description: In plants and animals, small peptide ligands that signal in cell-cell communication have been suggested to be a crucial component of development. A bioassay of single-cell transdifferentation demonstrates that a dodecapeptide with two hydroxyproline residues is the functional product of genes from the CLE family, which includes CLAVATA3 in Arabidopsis. The dodecapeptide suppresses xylem cell development at a concentration of 10(-11) M and promotes cell division. An application, corresponding to all 26 Arabidopsis CLE protein family members, of synthetic dodecapeptides reveals two counteracting signaling pathways involved in stem cell fate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ito, Yasuko -- Nakanomyo, Ikuko -- Motose, Hiroyasu -- Iwamoto, Kuninori -- Sawa, Shinichiro -- Dohmae, Naoshi -- Fukuda, Hiroo -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):842-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902140" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/cytology ; Arabidopsis Proteins/chemistry/metabolism ; Asteraceae/*cytology ; Base Sequence ; Biological Assay ; Cell Communication ; *Cell Differentiation ; Cells, Cultured ; Ligands ; Meristem/cytology ; Molecular Sequence Data ; Oligopeptides/chemistry/isolation & purification/*metabolism/pharmacology ; Plant Proteins/chemistry/*metabolism ; Plant Roots/cytology/growth & development ; Plant Structures/*cytology ; *Signal Transduction ; Stem Cells/*cytology
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  • 84
    Publication Date: 2006-05-13
    Description: The interface between an infectious agent and its host represents the ultimate battleground for survival: The microbe must secure a niche for replication, whereas the host must limit the pathogen's advance. Among the host's arsenal of antimicrobial factors, the type 1 interferons (IFNs) induce potent defense mechanisms against viruses and are key in the host-virus standoff. Viruses have evolved multiple tricks to avoid the immediate antiviral effects of IFNs and, in turn, hosts have adapted use of this innate cytokine system to galvanize multiple additional layers of immune defense. The plasticity that exists in these interactions provides us with a lesson in detente.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia-Sastre, Adolfo -- Biron, Christine A -- P01AI52106/AI/NIAID NIH HHS/ -- P01AI58113/AI/NIAID NIH HHS/ -- R01AI46954/AI/NIAID NIH HHS/ -- R01AI55677/AI/NIAID NIH HHS/ -- R01CA41268/CA/NCI NIH HHS/ -- U19AI62623/AI/NIAID NIH HHS/ -- U54AI57158/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 May 12;312(5775):879-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690858" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytokines/physiology ; *Immunity, Innate ; Interferon Regulatory Factors/physiology ; Interferon Type I/biosynthesis/genetics/*physiology ; Models, Biological ; RNA Helicases/metabolism ; Signal Transduction ; Toll-Like Receptors/physiology ; Viral Proteins/metabolism ; *Virus Physiological Phenomena ; Viruses/*immunology
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  • 85
    Publication Date: 2006-09-02
    Description: Extreme gene duplication is a major source of evolutionary novelty. A genome-wide survey of gene copy number variation among human and great ape lineages revealed that the most striking human lineage-specific amplification was due to an unknown gene, MGC8902, which is predicted to encode multiple copies of a protein domain of unknown function (DUF1220). Sequences encoding these domains are virtually all primate-specific, show signs of positive selection, and are increasingly amplified generally as a function of a species' evolutionary proximity to humans, where the greatest number of copies (212) is found. DUF1220 domains are highly expressed in brain regions associated with higher cognitive function, and in brain show neuron-specific expression preferentially in cell bodies and dendrites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popesco, Magdalena C -- Maclaren, Erik J -- Hopkins, Janet -- Dumas, Laura -- Cox, Michael -- Meltesen, Lynne -- McGavran, Loris -- Wyckoff, Gerald J -- Sikela, James M -- AA11853/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1304-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Medical Genetics, University of Colorado at Denver and Health Sciences Center, Aurora, CO 80045, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946073" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Brain/*metabolism ; Cognition ; Exons ; *Gene Amplification ; Gene Dosage ; Gene Duplication ; Gene Expression ; Genome, Human ; Humans ; Macaca mulatta/genetics ; Mice ; Molecular Sequence Data ; Neocortex/metabolism ; Neurons/*metabolism ; Pan troglodytes/genetics ; Phylogeny ; Polymerase Chain Reaction ; *Protein Structure, Tertiary ; Proteins/*chemistry/genetics ; Rats ; *Selection, Genetic
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  • 86
    Publication Date: 2006-07-22
    Description: Brassinosteroids, the steroid hormones of plants, are perceived at the plasma membrane by a leucine-rich repeat receptor serine/threonine kinase called BRI1. We report a BRI1-interacting protein, BKI1, which is a negative regulator of brassinosteroid signaling. Brassinosteroids cause the rapid dissociation of BKI1-yellow fluorescent protein from the plasma membrane in a process that is dependent on BRI1-kinase. BKI1 is a substrate of BRI1 kinase and limits the interaction of BRI1 with its proposed coreceptor, BAK1, suggesting that BKI1 prevents the activation of BRI1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xuelu -- Chory, Joanne -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1118-22. Epub 2006 Jul 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Plant Biology Laboratory, 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/16857903" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Brassinosteroids ; Cell Membrane/*metabolism ; Cholestanols/*metabolism/pharmacology ; Gene Expression Regulation, Plant ; Meristem/metabolism ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; Plants, Genetically Modified ; Protein Binding ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Steroids, Heterocyclic/*metabolism/pharmacology ; Two-Hybrid System Techniques
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  • 87
    Publication Date: 2006-01-21
    Description: Magnetotactic bacteria contain membrane-bound intracellular iron crystals (magnetosomes) and respond to magnetic fields. Polar magnetotactic bacteria in vertical chemical gradients are thought to respond to high oxygen levels by swimming downward into areas with low or no oxygen (toward geomagnetic north in the Northern Hemisphere and geomagnetic south in the Southern Hemisphere). We identified populations of polar magnetotactic bacteria in the Northern Hemisphere that respond to high oxygen levels by swimming toward geomagnetic south, the opposite of all previously reported magnetotactic behavior. The percentage of magnetotactic bacteria with south polarity in the environment is positively correlated with higher redox potential. The coexistence of magnetotactic bacteria with opposing polarities in the same redox environment conflicts with current models of the adaptive value of magnetotaxis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, Sheri L -- Bazylinski, Dennis A -- Edwards, Katrina J -- New York, N.Y. -- Science. 2006 Jan 20;311(5759):371-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Massachusetts Institute of Technology-Woods Hole Oceanographic Institution (MIT-WHOI) Joint Program in Oceanography, Department of Marine Chemistry and Geochemistry, MS 52, WHOI, Woods Hole, MA 02543, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424338" target="_blank"〉PubMed〈/a〉
    Keywords: Colony Count, Microbial ; DNA, Bacterial/chemistry/genetics ; DNA, Ribosomal/chemistry/genetics ; Deltaproteobacteria/classification/cytology/isolation & purification/*physiology ; Geography ; In Situ Hybridization ; *Magnetics ; Molecular Sequence Data ; Movement ; Oxidation-Reduction ; Oxygen ; Water/chemistry ; *Water Microbiology
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  • 88
    Publication Date: 2006-07-01
    Description: Mathematical models predict that the future of the multidrug-resistant tuberculosis epidemic will depend on the fitness cost of drug resistance. We show that in laboratory-derived mutants of Mycobacterium tuberculosis, rifampin resistance is universally associated with a competitive fitness cost and that this cost is determined by the specific resistance mutation and strain genetic background. In contrast, we demonstrate that prolonged patient treatment can result in multidrug-resistant strains with no fitness defect and that strains with low- or no-cost resistance mutations are also the most frequent among clinical isolates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gagneux, Sebastien -- Long, Clara Davis -- Small, Peter M -- Van, Tran -- Schoolnik, Gary K -- Bohannan, Brendan J M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1944-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases and Geographic Medicine, Stanford University, Stanford, CA 94305, USA. sgagneux@systemsbiology.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antibiotics, Antitubercular/*pharmacology/therapeutic use ; Bacterial Proteins/genetics ; DNA-Directed RNA Polymerases/genetics ; *Drug Resistance, Multiple, Bacterial ; Humans ; Models, Biological ; Mutation ; Mutation, Missense ; Mycobacterium tuberculosis/*drug effects/genetics/*growth & development ; Rifampin/*pharmacology/therapeutic use ; Tuberculosis, Multidrug-Resistant/drug therapy/*microbiology
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  • 89
    Publication Date: 2006-01-18
    Description: In contrast to current models, fluorescence resonance energy transfer measurements using a single-cell imaging assay with fluorescent forms of PER and TIM showed that these proteins bind rapidly and persist in the cytoplasm while gradually accumulating in discrete foci. After approximately 6 hours, complexes abruptly dissociated, as PER and TIM independently moved to the nucleus in a narrow time frame. The per(L) mutation delayed nuclear accumulation in vivo and in our cultured cell system, but without affecting rates of PER/TIM assembly or dissociation. This finding points to a previously unrecognized form of temporal regulation that underlies the periodicity of the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, Pablo -- Saez, Lino -- Young, Michael W -- GM54339/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 13;311(5758):226-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16410523" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Cell Line ; Cell Nucleus/metabolism ; Circadian Rhythm/*physiology ; Cytoplasm/metabolism ; Drosophila Proteins/*metabolism ; Drosophila melanogaster ; Fluorescence Resonance Energy Transfer ; Models, Biological ; Nuclear Proteins/*metabolism ; Period Circadian Proteins ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Time Factors
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  • 90
    Publication Date: 2006-05-20
    Description: The endemic species richness on Madagascar, relative to landmass area, is unparalleled in the world. Many organisms on the island have restricted geographical ranges. A comprehensive hypothesis explaining the evolution of this microendemism has yet to be developed. Using an analysis of watersheds in the context of Quaternary climatic shifts, we provide a new mechanistic model to explain the process of explosive speciation on the island. River catchments with sources at relatively low elevations were zones of isolation and hence led to the speciation of locally endemic taxa, whereas those at higher elevations were zones of retreat and dispersion and hence contain proportionately lower levels of microendemism. These results provide a framework for biogeographic and phylogeographic studies, as well as a basis for prioritizing conservation actions of the remaining natural forest habitats on the island.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilme, Lucienne -- Goodman, Steven M -- Ganzhorn, Jorg U -- New York, N.Y. -- Science. 2006 May 19;312(5776):1063-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Missouri Botanical Garden, Boite Postale 3391, Antananarivo (101), Madagascar.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16709785" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; Climate ; Genetic Speciation ; Geography ; Madagascar ; Models, Biological ; Rivers ; Trees ; Vertebrates
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  • 91
    Publication Date: 2006-01-21
    Description: Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharyya, Roby P -- Remenyi, Attila -- Good, Matthew C -- Bashor, Caleb J -- Falick, Arnold M -- Lim, Wendell A -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):822-6. Epub 2006 Jan 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424299" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*chemistry/genetics/*metabolism ; Allosteric Regulation ; Amino Acid Motifs ; Binding Sites ; Crystallography, X-Ray ; Down-Regulation ; Enzyme Activation ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*chemistry/*metabolism ; Models, Biological ; Models, Molecular ; Mutation ; Pheromones/*physiology ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism ; Transcription, Genetic
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  • 92
    Publication Date: 2006-12-02
    Description: Signaling by cell surface receptors and heterotrimeric guanine nucleotide-binding proteins (G proteins) is one of the most exhaustively studied processes in the cell but remains a major focus of molecular pharmacology research. The pheromone-response system in yeast (see the Connections Map at Science's Signal Transduction Knowledge Environment) has provided numerous major advances in our understanding of G protein signaling and regulation. However, the basic features of this prototypical pathway have remained largely unchanged since the mid-1990s. New tools available in yeast are beginning to uncover new pathway components and interactions and have revealed signaling in unexpected locations within the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slessareva, Janna E -- Dohlman, Henrik G -- P01-GM065533/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1412-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138892" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/*metabolism ; Endosomal Sorting Complexes Required for Transport ; Endosomes/*metabolism ; GTP-Binding Protein alpha Subunits/metabolism ; GTP-Binding Protein alpha Subunits, Gq-G11 ; GTP-Binding Protein beta Subunits/metabolism ; GTP-Binding Protein gamma Subunits/metabolism ; GTPase-Activating Proteins ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Intracellular Membranes/metabolism ; Models, Biological ; Phosphatidylinositol 3-Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; RGS Proteins/metabolism ; Receptors, Mating Factor/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; *Signal Transduction ; Vacuolar Sorting Protein VPS15
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-04-22
    Description: The threat of pandemic human influenza looms as we survey the ongoing avian influenza pandemic and wonder if and when it will jump species. What are the risks and how can we plan? The nub of the problem lies in the inherent variability of the virus, which makes prediction difficult. However, it is not impossible; mathematical models can help determine and quantify critical parameters and thresholds in the relationships of those parameters, even if the relationships are nonlinear and obscure to simple reasoning. Mathematical models can derive estimates for the levels of drug stockpiles needed to buy time, how and when to modify vaccines, whom to target with vaccines and drugs, and when to enforce quarantine measures. Regardless, the models used for pandemic planning must be tested, and for this we must continue to gather data, not just for exceptional scenarios but also for seasonal influenza.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Derek J -- DP1-OD000490-01/OD/NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):392-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Cambridge, Downing Street, Cambridge, CB2 3EJ, UK. dsmith@zoo.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627736" target="_blank"〉PubMed〈/a〉
    Keywords: Antigenic Variation ; Antiviral Agents/administration & dosage/*therapeutic use ; Disease Outbreaks/*prevention & control ; Evolution, Molecular ; Forecasting ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Humans ; Immunization Programs ; Influenza A Virus, H3N2 Subtype/genetics/immunology ; Influenza A Virus, H5N1 Subtype/genetics/immunology/pathogenicity ; Influenza A virus/immunology ; *Influenza Vaccines ; Influenza, Human/epidemiology/*prevention & control/transmission/virology ; Mathematics ; Models, Biological ; Mutation ; Quarantine
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-05-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garber, Ken -- New York, N.Y. -- Science. 2006 May 26;312(5777):1158-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728625" target="_blank"〉PubMed〈/a〉
    Keywords: ATP Citrate (pro-S)-Lyase/antagonists & inhibitors/metabolism ; Adenosine Triphosphate/metabolism ; Antineoplastic Agents/pharmacology/therapeutic use ; Cell Respiration ; Cell Transformation, Neoplastic ; *Energy Metabolism ; Enzyme Inhibitors/pharmacology/therapeutic use ; Glucose/metabolism ; *Glycolysis ; Hexokinase/antagonists & inhibitors/metabolism ; Humans ; Hypoxia-Inducible Factor 1/metabolism ; Models, Biological ; Neoplasms/drug therapy/genetics/*metabolism/pathology ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins c-akt/metabolism
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  • 95
    Publication Date: 2006-10-28
    Description: DNA methylation systems are well characterized in vertebrates, but methylation in Drosophila melanogaster and other invertebrates remains controversial. Using the recently sequenced honey bee genome, we present a bioinformatic, molecular, and biochemical characterization of a functional DNA methylation system in an insect. We report on catalytically active orthologs of the vertebrate DNA methyltransferases Dnmt1 and Dnmt3a and b, two isoforms that contain a methyl-DNA binding domain, genomic 5-methyl-deoxycytosine, and CpG-methylated genes. The honey bee provides an opportunity to study the roles of methylation in social contexts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Ying -- Jorda, Mireia -- Jones, Peter L -- Maleszka, Ryszard -- Ling, Xu -- Robertson, Hugh M -- Mizzen, Craig A -- Peinado, Miguel A -- Robinson, Gene E -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):645-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068262" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Composition ; Bees/enzymology/*genetics/*metabolism ; Computational Biology ; DNA/chemistry/metabolism ; DNA (Cytosine-5-)-Methyltransferase/chemistry/*genetics/*metabolism ; *DNA Methylation ; DNA-Binding Proteins/genetics/metabolism ; Dinucleoside Phosphates/*metabolism ; Genes, Insect ; Genome, Insect ; Insect Proteins/genetics/metabolism ; Molecular Sequence Data
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  • 96
    Publication Date: 2006-09-23
    Description: Vandermeer and Perfecto (Reports, 17 February 2006, p. 1000) maintain that a mutualist ant disrupts the power law distribution of scale insect abundances. However, reanalysis of the data reveals that ants cause an increase in the range of the power law and modify its exponent. We present a tentative, but more realistic, model that is suitable for quantitative predictions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pueyo, Salvador -- Jovani, Roger -- New York, N.Y. -- Science. 2006 Sep 22;313(5794):1739; author reply 1739.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departament d'Ecologia, Universitat de Barcelona, Avinguda Diagonal 645, 08028 Barcelona, Catalonia, Spain. spueyo@ub.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16990535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ants/*physiology ; *Coffea ; *Ecosystem ; Hemiptera/parasitology/*physiology ; Mathematics ; Models, Biological ; Population Density ; *Symbiosis
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  • 97
    Publication Date: 2006-12-13
    Description: Noncoding small RNAs regulate gene expression in all organisms, in some cases through direct association with RNA polymerase (RNAP). Here we report that the mechanism of 6S RNA inhibition of transcription is through specific, stable interactions with the active site of Escherichia coli RNAP that exclude promoter DNA binding. In fact, the DNA-dependent RNAP uses bound 6S RNA as a template for RNA synthesis, producing 14-to 20-nucleotide RNA products (pRNA). These results demonstrate that 6S RNA is functionally engaged in the active site of RNAP. Synthesis of pRNA destabilizes 6S RNA-RNAP complexes leading to release of the pRNA-6S RNA hybrid. In vivo, 6S RNA-directed RNA synthesis occurs during outgrowth from the stationary phase and likely is responsible for liberating RNAP from 6S RNA in response to nutrient availability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wassarman, Karen M -- Saecker, Ruth M -- GM23467/GM/NIGMS NIH HHS/ -- GM67955/GM/NIGMS NIH HHS/ -- R01 GM067955/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1601-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA. wassarman@bact.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158328" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA, Bacterial/chemistry/metabolism ; DNA-Directed RNA Polymerases/antagonists & inhibitors/chemistry/*metabolism ; Escherichia coli/genetics/growth & development/*metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; RNA Stability ; RNA, Bacterial/biosynthesis/chemistry/genetics/*metabolism ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Untranslated/chemistry/genetics/*metabolism ; Sigma Factor/*metabolism ; Templates, Genetic ; Transcription, Genetic
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  • 98
    Publication Date: 2006-03-18
    Description: The hemagglutinin (HA) structure at 2.9 angstrom resolution, from a highly pathogenic Vietnamese H5N1 influenza virus, is more related to the 1918 and other human H1 HAs than to a 1997 duck H5 HA. Glycan microarray analysis of this Viet04 HA reveals an avian alpha2-3 sialic acid receptor binding preference. Introduction of mutations that can convert H1 serotype HAs to human alpha2-6 receptor specificity only enhanced or reduced affinity for avian-type receptors. However, mutations that can convert avian H2 and H3 HAs to human receptor specificity, when inserted onto the Viet04 H5 HA framework, permitted binding to a natural human alpha2-6 glycan, which suggests a path for this H5N1 virus to gain a foothold in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, James -- Blixt, Ola -- Tumpey, Terrence M -- Taubenberger, Jeffery K -- Paulson, James C -- Wilson, Ian A -- AI058113/AI/NIAID NIH HHS/ -- AI42266/AI/NIAID NIH HHS/ -- CA55896/CA/NCI NIH HHS/ -- GM060938/GM/NIGMS NIH HHS/ -- GM062116/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):404-10. Epub 2006 Mar 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. jstevens@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16543414" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Antigenic Variation ; Binding Sites ; Birds ; Carbohydrate Conformation ; Cloning, Molecular ; Crystallography, X-Ray ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza ; Virus/*chemistry/genetics/immunology/*metabolism ; Humans ; Influenza A Virus, H5N1 Subtype/*chemistry/genetics/metabolism/*pathogenicity ; Lung/virology ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Polysaccharides/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Receptors, Virus/chemistry/*metabolism ; Respiratory Mucosa/virology ; Sialic Acids/chemistry/metabolism ; Species Specificity ; Virulence
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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-06-24
    Description: RNA viruses infect marine organisms from bacteria to whales, but RNA virus communities in the sea remain essentially unknown. Reverse-transcribed whole-genome shotgun sequencing was used to characterize the diversity of uncultivated marine RNA virus assemblages. A diverse assemblage of RNA viruses, including a broad group of marine picorna-like viruses, and distant relatives of viruses infecting arthropods and higher plants were found. Communities were dominated by distinct genotypes with small genome sizes, and we completely assembled the genomes of several hitherto undiscovered viruses. Our results show that the oceans are a reservoir of previously unknown RNA viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culley, Alexander I -- Lang, Andrew S -- Suttle, Curtis A -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1795-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of British Columbia, 3529-6270 University Boulevard, Vancouver, BC V6T 1Z4, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794078" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropods/virology ; Contig Mapping ; DNA, Complementary ; *Ecosystem ; *Genetic Variation ; *Genome, Viral ; Genomic Library ; *Genomics ; Genotype ; Molecular Sequence Data ; Pacific Ocean ; Phylogeny ; Picornaviridae/classification/genetics ; Plants/virology ; RNA Viruses/*genetics ; RNA, Viral/classification/*genetics/isolation & purification ; Reverse Transcriptase Polymerase Chain Reaction ; Seawater/*virology ; Sequence Analysis, DNA ; Synteny ; Tombusviridae/classification/genetics
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  • 100
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2006-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breitkreutz, Ashton -- Tyers, Mike -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):789-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Campbell Family Institute for Breast Cancer Research, Toronto Medical Discovery Tower, Toronto, Canada M5G 1L7. abreitkr@uhnres.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469909" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/chemistry/genetics/*metabolism ; Binding Sites ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase Kinases ; Mitogen-Activated Protein Kinases/chemistry/*metabolism ; Models, Biological ; Mutation ; Pheromones/physiology ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Kinases/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Tyrosine/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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