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  • Molecular Sequence Data  (76)
  • American Association for the Advancement of Science (AAAS)  (76)
  • Springer Nature
  • 2010-2014  (76)
  • 1980-1984
  • 1925-1929
  • 2011  (76)
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  • 2010-2014  (76)
  • 1980-1984
  • 1925-1929
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  • 1
    Publication Date: 2011-02-26
    Description: Metarhizium anisopliae infects mosquitoes through the cuticle and proliferates in the hemolymph. To allow M. anisopliae to combat malaria in mosquitoes with advanced malaria infections, we produced recombinant strains expressing molecules that target sporozoites as they travel through the hemolymph to the salivary glands. Eleven days after a Plasmodium-infected blood meal, mosquitoes were treated with M. anisopliae expressing salivary gland and midgut peptide 1 (SM1), which blocks attachment of sporozoites to salivary glands; a single-chain antibody that agglutinates sporozoites; or scorpine, which is an antimicrobial toxin. These reduced sporozoite counts by 71%, 85%, and 90%, respectively. M. anisopliae expressing scorpine and an [SM1](8):scorpine fusion protein reduced sporozoite counts by 98%, suggesting that Metarhizium-mediated inhibition of Plasmodium development could be a powerful weapon for combating malaria.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153607/" 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/PMC4153607/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fang, Weiguo -- Vega-Rodriguez, Joel -- Ghosh, Anil K -- Jacobs-Lorena, Marcelo -- Kang, Angray -- St Leger, Raymond J -- 5R21A1079429-02/PHS HHS/ -- R01 AI031478/AI/NIAID NIH HHS/ -- R21 AI079429/AI/NIAID NIH HHS/ -- R21 AI088033/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2011 Feb 25;331(6020):1074-7. doi: 10.1126/science.1199115.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of Maryland, 4112 Plant Sciences Building, College Park, MD 20742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles gambiae/*microbiology/*parasitology/physiology ; Antibodies, Protozoan/immunology ; Base Sequence ; Cloning, Molecular ; Defensins/genetics/metabolism ; Feeding Behavior ; Female ; Hemolymph/metabolism/microbiology/parasitology ; Humans ; Insect Vectors/*microbiology/*parasitology/physiology ; Malaria, Falciparum/transmission ; Metarhizium/*genetics/physiology ; Molecular Sequence Data ; Oligopeptides/genetics/metabolism ; Organisms, Genetically Modified ; Pest Control, Biological ; Plasmodium falciparum/*physiology ; Protozoan Proteins/immunology ; Salivary Glands/metabolism/parasitology ; Spores, Fungal/physiology ; Sporozoites/physiology ; Transformation, Genetic ; Transgenes
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  • 2
    Publication Date: 2011-09-10
    Description: Engineered fluorescent protein (FP) chimeras that modulate their fluorescence in response to changes in calcium ion (Ca(2+)) concentration are powerful tools for visualizing intracellular signaling activity. However, despite a decade of availability, the palette of single FP-based Ca(2+) indicators has remained limited to a single green hue. We have expanded this palette by developing blue, improved green, and red intensiometric indicators, as well as an emission ratiometric indicator with an 11,000% ratio change. This series enables improved single-color Ca(2+) imaging in neurons and transgenic Caenorhabditis elegans. In HeLa cells, Ca(2+) was imaged in three subcellular compartments, and, in conjunction with a cyan FP-yellow FP-based indicator, Ca(2+) and adenosine 5'-triphosphate were simultaneously imaged. This palette of indicators paints the way to a colorful new era of Ca(2+) imaging.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3560286/" 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/PMC3560286/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhao, Yongxin -- Araki, Satoko -- Wu, Jiahui -- Teramoto, Takayuki -- Chang, Yu-Fen -- Nakano, Masahiro -- Abdelfattah, Ahmed S -- Fujiwara, Manabi -- Ishihara, Takeshi -- Nagai, Takeharu -- Campbell, Robert E -- 94487/Canadian Institutes of Health Research/Canada -- 99085/Canadian Institutes of Health Research/Canada -- Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2011 Sep 30;333(6051):1888-91. doi: 10.1126/science.1208592. Epub 2011 Sep 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21903779" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans ; Calcium/*analysis ; *Calcium Signaling ; *Directed Molecular Evolution ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Green Fluorescent Proteins/*chemistry/genetics ; HeLa Cells ; Humans ; Luminescent Proteins/*chemistry/genetics ; Molecular Sequence Data ; Neurons/metabolism ; *Protein Engineering ; Rats ; Recombinant Fusion Proteins/*chemistry ; Spectrometry, Fluorescence ; Transfection
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  • 3
    Publication Date: 2011-03-12
    Description: Disruption of the circadian clock exacerbates metabolic diseases, including obesity and diabetes. We show that histone deacetylase 3 (HDAC3) recruitment to the genome displays a circadian rhythm in mouse liver. Histone acetylation is inversely related to HDAC3 binding, and this rhythm is lost when HDAC3 is absent. Although amounts of HDAC3 are constant, its genomic recruitment in liver corresponds to the expression pattern of the circadian nuclear receptor Rev-erbalpha. Rev-erbalpha colocalizes with HDAC3 near genes regulating lipid metabolism, and deletion of HDAC3 or Rev-erbalpha in mouse liver causes hepatic steatosis. Thus, genomic recruitment of HDAC3 by Rev-erbalpha directs a circadian rhythm of histone acetylation and gene expression required for normal hepatic lipid homeostasis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3389392/" 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/PMC3389392/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Dan -- Liu, Tao -- Sun, Zheng -- Bugge, Anne -- Mullican, Shannon E -- Alenghat, Theresa -- Liu, X Shirley -- Lazar, Mitchell A -- DK19525/DK/NIDDK NIH HHS/ -- DK43806/DK/NIDDK NIH HHS/ -- DK45586/DK/NIDDK NIH HHS/ -- DK49210/DK/NIDDK NIH HHS/ -- HG4069/HG/NHGRI NIH HHS/ -- P30 DK019525/DK/NIDDK NIH HHS/ -- R01 DK045586/DK/NIDDK NIH HHS/ -- R37 DK043806/DK/NIDDK NIH HHS/ -- R37 DK043806-20/DK/NIDDK NIH HHS/ -- RC1 DK086239/DK/NIDDK NIH HHS/ -- RC1DK08623/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2011 Mar 11;331(6022):1315-9. doi: 10.1126/science.1198125.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Endocrinology, Diabetes, and Metabolism, Department of Medicine, 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/21393543" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Chromatin Immunoprecipitation ; Chronobiology Disorders/genetics/metabolism ; *Circadian Clocks ; *Circadian Rhythm ; DNA/metabolism ; Epigenesis, Genetic ; Fatty Liver/*metabolism ; Gene Expression Regulation ; *Genome ; Histone Deacetylases/*metabolism ; Histones/metabolism ; Homeostasis ; *Lipid Metabolism ; Lipogenesis/genetics ; Liver/*metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Molecular Sequence Data ; Nuclear Receptor Co-Repressor 1/metabolism ; Nuclear Receptor Subfamily 1, Group D, Member 1/genetics/metabolism ; RNA Polymerase II/metabolism ; Up-Regulation
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  • 4
    Publication Date: 2011-08-13
    Description: Estimates suggest that only one-tenth of the true fungal diversity has been described. Among numerous fungal lineages known only from environmental DNA sequences, Soil Clone Group 1 is the most ubiquitous. These globally distributed fungi may dominate below-ground fungal communities, but their placement in the fungal tree of life has been uncertain. Here, we report cultures of this group and describe the class, Archaeorhizomycetes, phylogenetically placed within subphylum Taphrinomycotina in the Ascomycota. Archaeorhizomycetes comprises hundreds of cryptically reproducing filamentous species that do not form recognizable mycorrhizal structures and have saprotrophic potential, yet are omnipresent in roots and rhizosphere soil and show ecosystem and host root habitat specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosling, Anna -- Cox, Filipa -- Cruz-Martinez, Karelyn -- Ihrmark, Katarina -- Grelet, Gwen-Aelle -- Lindahl, Bjorn D -- Menkis, Audrius -- James, Timothy Y -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):876-9. doi: 10.1126/science.1206958.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Forest Mycology and Pathology, Uppsala BioCentre, SLU, Box 7026, 750 07 Uppsala, Sweden. anna.rosling@slu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21836015" target="_blank"〉PubMed〈/a〉
    Keywords: *Ascomycota/classification/genetics/growth & development/isolation & purification ; Coniferophyta/microbiology ; *Ecosystem ; Genes, Fungal ; Genes, rRNA ; Meristem/*microbiology ; Molecular Sequence Data ; *Mycorrhizae/classification/genetics ; Phylogeny ; Rhizosphere ; *Soil Microbiology
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-03-10
    Description: DNA transposons are mobile genetic elements that have shaped the genomes of eukaryotes for millions of years, yet their origins remain obscure. We discovered a virophage that, on the basis of genetic homology, likely represents an evolutionary link between double-stranded DNA viruses and Maverick/Polinton eukaryotic DNA transposons. The Mavirus virophage parasitizes the giant Cafeteria roenbergensis virus and encodes 20 predicted proteins, including a retroviral integrase and a protein-primed DNA polymerase B. On the basis of our data, we conclude that Maverick/Polinton transposons may have originated from ancient relatives of Mavirus, and thereby influenced the evolution of eukaryotic genomes, although we cannot rule out alternative evolutionary scenarios.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischer, Matthias G -- Suttle, Curtis A -- New York, N.Y. -- Science. 2011 Apr 8;332(6026):231-4. doi: 10.1126/science.1199412. Epub 2011 Mar 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, 1365-2350 Health Sciences Mall, University of British Columbia, Vancouver V6T 1Z3, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21385722" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *DNA Transposable Elements ; DNA Viruses/*genetics/*physiology ; DNA, Viral/genetics ; DNA-Directed DNA Polymerase/genetics ; *Evolution, Molecular ; Genome, Viral ; Integrases/chemistry/genetics ; Molecular Sequence Data ; Phylogeny ; Satellite Viruses/*genetics/*physiology ; Stramenopiles/virology ; Viral Proteins/chemistry/genetics ; Virus Replication
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  • 6
    Publication Date: 2011-05-14
    Description: We describe a general computational method for designing proteins that bind a surface patch of interest on a target macromolecule. Favorable interactions between disembodied amino acid residues and the target surface are identified and used to anchor de novo designed interfaces. The method was used to design proteins that bind a conserved surface patch on the stem of the influenza hemagglutinin (HA) from the 1918 H1N1 pandemic virus. After affinity maturation, two of the designed proteins, HB36 and HB80, bind H1 and H5 HAs with low nanomolar affinity. Further, HB80 inhibits the HA fusogenic conformational changes induced at low pH. The crystal structure of HB36 in complex with 1918/H1 HA revealed that the actual binding interface is nearly identical to that in the computational design model. Such designed binding proteins may be useful for both diagnostics and therapeutics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164876/" 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/PMC3164876/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fleishman, Sarel J -- Whitehead, Timothy A -- Ekiert, Damian C -- Dreyfus, Cyrille -- Corn, Jacob E -- Strauch, Eva-Maria -- Wilson, Ian A -- Baker, David -- AI057141/AI/NIAID NIH HHS/ -- AI058113/AI/NIAID NIH HHS/ -- GM080209/GM/NIGMS NIH HHS/ -- P01 AI058113/AI/NIAID NIH HHS/ -- P01 AI058113-07/AI/NIAID NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 May 13;332(6031):816-21. doi: 10.1126/science.1202617.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21566186" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Sequence ; Binding Sites ; Computational Biology ; *Computer Simulation ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/*metabolism ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; *Models, Molecular ; Molecular Sequence Data ; Mutation ; Peptide Library ; Protein Binding ; Protein Conformation ; *Protein Engineering ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary ; Proteins/*chemistry/genetics/*metabolism ; Software
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-02-19
    Description: Dyneins are microtubule-based motor proteins that power ciliary beating, transport intracellular cargos, and help to construct the mitotic spindle. Evolved from ring-shaped hexameric AAA-family adenosine triphosphatases (ATPases), dynein's large size and complexity have posed challenges for understanding its structure and mechanism. Here, we present a 6 angstrom crystal structure of a functional dimer of two ~300-kilodalton motor domains of yeast cytoplasmic dynein. The structure reveals an unusual asymmetric arrangement of ATPase domains in the ring-shaped motor domain, the manner in which the mechanical element interacts with the ATPase ring, and an unexpected interaction between two coiled coils that create a base for the microtubule binding domain. The arrangement of these elements provides clues as to how adenosine triphosphate-driven conformational changes might be transmitted across the motor domain.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3169322/" 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/PMC3169322/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, Andrew P -- Cho, Carol -- Jin, Lan -- Vale, Ronald D -- MC_UP_A025_1011/Medical Research Council/United Kingdom -- R01 GM097312/GM/NIGMS NIH HHS/ -- R01 GM097312-01/GM/NIGMS NIH HHS/ -- R01 GM097312-02/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Mar 4;331(6021):1159-65. doi: 10.1126/science.1202393. Epub 2011 Feb 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California-San Francisco, 600 16th Street, San Francisco, CA 94158, USA. cartera@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21330489" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Allosteric Regulation ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Cytoplasmic Dyneins/*chemistry/*metabolism ; Methionine/chemistry ; Microtubules/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry ; Saccharomyces cerevisiae Proteins/*chemistry/*metabolism
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  • 8
    Publication Date: 2011-05-21
    Description: The transmission of information from DNA to RNA is a critical process. We compared RNA sequences from human B cells of 27 individuals to the corresponding DNA sequences from the same individuals and uncovered more than 10,000 exonic sites where the RNA sequences do not match that of the DNA. All 12 possible categories of discordances were observed. These differences were nonrandom as many sites were found in multiple individuals and in different cell types, including primary skin cells and brain tissues. Using mass spectrometry, we detected peptides that are translated from the discordant RNA sequences and thus do not correspond exactly to the DNA sequences. These widespread RNA-DNA differences in the human transcriptome provide a yet unexplored aspect of genome variation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3204392/" 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/PMC3204392/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Mingyao -- Wang, Isabel X -- Li, Yun -- Bruzel, Alan -- Richards, Allison L -- Toung, Jonathan M -- Cheung, Vivian G -- R01 HG005854/HG/NHGRI NIH HHS/ -- R01 HG005854-01/HG/NHGRI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Jul 1;333(6038):53-8. doi: 10.1126/science.1207018. Epub 2011 May 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biostatistics, 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/21596952" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Amino Acid Sequence ; B-Lymphocytes ; Base Sequence ; Cell Line ; Cerebral Cortex/cytology ; DNA/chemistry/*genetics ; Exons ; Expressed Sequence Tags ; Fibroblasts ; Gene Expression Profiling ; *Genetic Variation ; *Genome, Human ; Genotype ; Humans ; Mass Spectrometry ; Middle Aged ; Molecular Sequence Data ; Polymorphism, Single Nucleotide ; Protein Biosynthesis ; Proteins/chemistry ; Proteome/chemistry ; RNA, Messenger/chemistry/*genetics ; Sequence Analysis, DNA ; Sequence Analysis, RNA ; Skin/cytology ; Untranslated Regions
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  • 9
    Publication Date: 2011-04-23
    Description: The fission yeast clade--comprising Schizosaccharomyces pombe, S. octosporus, S. cryophilus, and S. japonicus--occupies the basal branch of Ascomycete fungi and is an important model of eukaryote biology. A comparative annotation of these genomes identified a near extinction of transposons and the associated innovation of transposon-free centromeres. Expression analysis established that meiotic genes are subject to antisense transcription during vegetative growth, which suggests a mechanism for their tight regulation. In addition, trans-acting regulators control new genes within the context of expanded functional modules for meiosis and stress response. Differences in gene content and regulation also explain why, unlike the budding yeast of Saccharomycotina, fission yeasts cannot use ethanol as a primary carbon source. These analyses elucidate the genome structure and gene regulation of fission yeast and provide tools for investigation across the Schizosaccharomyces clade.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3131103/" 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/PMC3131103/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhind, Nicholas -- Chen, Zehua -- Yassour, Moran -- Thompson, Dawn A -- Haas, Brian J -- Habib, Naomi -- Wapinski, Ilan -- Roy, Sushmita -- Lin, Michael F -- Heiman, David I -- Young, Sarah K -- Furuya, Kanji -- Guo, Yabin -- Pidoux, Alison -- Chen, Huei Mei -- Robbertse, Barbara -- Goldberg, Jonathan M -- Aoki, Keita -- Bayne, Elizabeth H -- Berlin, Aaron M -- Desjardins, Christopher A -- Dobbs, Edward -- Dukaj, Livio -- Fan, Lin -- FitzGerald, Michael G -- French, Courtney -- Gujja, Sharvari -- Hansen, Klavs -- Keifenheim, Dan -- Levin, Joshua Z -- Mosher, Rebecca A -- Muller, Carolin A -- Pfiffner, Jenna -- Priest, Margaret -- Russ, Carsten -- Smialowska, Agata -- Swoboda, Peter -- Sykes, Sean M -- Vaughn, Matthew -- Vengrova, Sonya -- Yoder, Ryan -- Zeng, Qiandong -- Allshire, Robin -- Baulcombe, David -- Birren, Bruce W -- Brown, William -- Ekwall, Karl -- Kellis, Manolis -- Leatherwood, Janet -- Levin, Henry -- Margalit, Hanah -- Martienssen, Rob -- Nieduszynski, Conrad A -- Spatafora, Joseph W -- Friedman, Nir -- Dalgaard, Jacob Z -- Baumann, Peter -- Niki, Hironori -- Regev, Aviv -- Nusbaum, Chad -- BB/E023754/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- DP1 OD003958/OD/NIH HHS/ -- R01 GM069957/GM/NIGMS NIH HHS/ -- R01 GM076396/GM/NIGMS NIH HHS/ -- R01 HG004037/HG/NHGRI NIH HHS/ -- U54 HG003067/HG/NHGRI NIH HHS/ -- U54 HG003067-06/HG/NHGRI NIH HHS/ -- Biotechnology and Biological Sciences Research Council/United Kingdom -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 May 20;332(6032):930-6. doi: 10.1126/science.1203357. Epub 2011 Apr 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA. nick.rhind@umassmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21511999" target="_blank"〉PubMed〈/a〉
    Keywords: Centromere/genetics/physiology/ultrastructure ; DNA Transposable Elements ; Evolution, Molecular ; Gene Expression Profiling ; Gene Expression Regulation, Fungal ; Genes, Mating Type, Fungal ; *Genome, Fungal ; Genomics ; Glucose/metabolism ; Meiosis ; Molecular Sequence Annotation ; Molecular Sequence Data ; Phylogeny ; RNA, Antisense/genetics ; RNA, Fungal/genetics ; RNA, Small Interfering/genetics ; RNA, Untranslated/genetics ; Regulatory Elements, Transcriptional ; Schizosaccharomyces/*genetics/growth & development/metabolism ; Schizosaccharomyces pombe Proteins/genetics/metabolism ; Sequence Analysis, DNA ; Species Specificity ; Transcription Factors/genetics/metabolism ; Transcription, Genetic
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  • 10
    Publication Date: 2011-07-23
    Description: Apicomplexan parasites such as Toxoplasma gondii and Plasmodium species actively invade host cells through a moving junction (MJ) complex assembled at the parasite-host cell interface. MJ assembly is initiated by injection of parasite rhoptry neck proteins (RONs) into the host cell, where RON2 spans the membrane and functions as a receptor for apical membrane antigen 1 (AMA1) on the parasite. We have determined the structure of TgAMA1 complexed with a RON2 peptide at 1.95 angstrom resolution. A stepwise assembly mechanism results in an extensive buried surface area, enabling the MJ complex to resist the mechanical forces encountered during host cell invasion. Besides providing insights into host cell invasion by apicomplexan parasites, the structure offers a basis for designing therapeutics targeting these global pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tonkin, Michelle L -- Roques, Magali -- Lamarque, Mauld H -- Pugniere, Martine -- Douguet, Dominique -- Crawford, Joanna -- Lebrun, Maryse -- Boulanger, Martin J -- MOP82915/Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2011 Jul 22;333(6041):463-7. doi: 10.1126/science.1204988.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21778402" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Antibodies, Monoclonal/immunology ; Antibodies, Protozoan/immunology ; Antigens, Protozoan/*chemistry/genetics/immunology/*metabolism ; *Host-Parasite Interactions ; Hydrophobic and Hydrophilic Interactions ; Membrane Proteins/chemistry/immunology/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Peptide Fragments/chemistry/metabolism ; Plasmodium falciparum/chemistry/metabolism/pathogenicity ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary ; Protozoan Proteins/*chemistry/immunology/*metabolism ; Toxoplasma/chemistry/*metabolism/*pathogenicity/ultrastructure
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  • 11
    Publication Date: 2011-04-02
    Description: Heparan and chondroitin sulfate proteoglycans (HSPGs and CSPGs, respectively) regulate numerous cell surface signaling events, with typically opposite effects on cell function. CSPGs inhibit nerve regeneration through receptor protein tyrosine phosphatase sigma (RPTPsigma). Here we report that RPTPsigma acts bimodally in sensory neuron extension, mediating CSPG inhibition and HSPG growth promotion. Crystallographic analyses of a shared HSPG-CSPG binding site reveal a conformational plasticity that can accommodate diverse glycosaminoglycans with comparable affinities. Heparan sulfate and analogs induced RPTPsigma ectodomain oligomerization in solution, which was inhibited by chondroitin sulfate. RPTPsigma and HSPGs colocalize in puncta on sensory neurons in culture, whereas CSPGs occupy the extracellular matrix. These results lead to a model where proteoglycans can exert opposing effects on neuronal extension by competing to control the oligomerization of a common receptor.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3154093/" 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/PMC3154093/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coles, Charlotte H -- Shen, Yingjie -- Tenney, Alan P -- Siebold, Christian -- Sutton, Geoffrey C -- Lu, Weixian -- Gallagher, John T -- Jones, E Yvonne -- Flanagan, John G -- Aricescu, A Radu -- 090532/Wellcome Trust/United Kingdom -- 10976/Cancer Research UK/United Kingdom -- EY11559/EY/NEI NIH HHS/ -- G0700232/Medical Research Council/United Kingdom -- G0900084/Medical Research Council/United Kingdom -- HD29417/HD/NICHD NIH HHS/ -- R01 EY011559/EY/NEI NIH HHS/ -- R01 EY011559-19/EY/NEI NIH HHS/ -- R37 HD029417/HD/NICHD NIH HHS/ -- R37 HD029417-20/HD/NICHD NIH HHS/ -- Cancer Research UK/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2011 Apr 22;332(6028):484-8. doi: 10.1126/science.1200840. Epub 2011 Mar 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21454754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/*physiology ; Binding Sites ; Cell Membrane/metabolism ; Cells, Cultured ; Chondroitin Sulfate Proteoglycans/chemistry/*metabolism ; Chondroitin Sulfates/chemistry/metabolism ; Crystallography, X-Ray ; Extracellular Matrix ; Ganglia, Spinal ; Glypicans/metabolism ; Growth Cones/metabolism ; Heparan Sulfate Proteoglycans/chemistry/*metabolism ; Heparitin Sulfate/analogs & derivatives/chemistry/metabolism ; Humans ; Mice ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Neurites/physiology ; Neurocan/metabolism ; Protein Conformation ; Protein Multimerization ; Protein Structure, Tertiary ; Receptor-Like Protein Tyrosine Phosphatases, Class 2/*chemistry/*metabolism ; Sensory Receptor Cells/*physiology
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  • 12
    Publication Date: 2011-08-13
    Description: When not transporting cargo, kinesin-1 is autoinhibited by binding of a tail region to the motor domains, but the mechanism of inhibition is unclear. We report the crystal structure of a motor domain dimer in complex with its tail domain at 2.2 angstroms and compare it with a structure of the motor domain alone at 2.7 angstroms. These structures indicate that neither an induced conformational change nor steric blocking is the cause of inhibition. Instead, the tail cross-links the motor domains at a second position, in addition to the coiled coil. This "double lockdown," by cross-linking at two positions, prevents the movement of the motor domains that is needed to undock the neck linker and release adenosine diphosphate. This autoinhibition mechanism could extend to some other kinesins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339660/" 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/PMC3339660/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaan, Hung Yi Kristal -- Hackney, David D -- Kozielski, Frank -- NS058848/NS/NINDS NIH HHS/ -- R01 NS058848/NS/NINDS NIH HHS/ -- R01 NS058848-01A2/NS/NINDS NIH HHS/ -- Cancer Research UK/United Kingdom -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):883-5. doi: 10.1126/science.1204824.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Beatson Institute for Cancer Research, Switchback Road, Bearsden, Glasgow G61 1BD, Scotland, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21836017" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Drosophila Proteins/*antagonists & inhibitors/*chemistry/metabolism ; Hydrogen Bonding ; Kinesin/*antagonists & inhibitors/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Multimerization ; Protein Structure, Tertiary
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  • 13
    Publication Date: 2011-11-19
    Description: Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4098850/" 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/PMC4098850/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armache, Karim-Jean -- Garlick, Joseph D -- Canzio, Daniele -- Narlikar, Geeta J -- Kingston, Robert E -- GM043901/GM/NIGMS NIH HHS/ -- P41 RR012408/RR/NCRR NIH HHS/ -- R01 GM043901/GM/NIGMS NIH HHS/ -- R37 GM048405/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Nov 18;334(6058):977-82. doi: 10.1126/science.1210915.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22096199" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; *Gene Silencing ; Histones/*chemistry/metabolism ; Hydrogen Bonding ; Methylation ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Mutant Proteins/chemistry/metabolism ; Nucleosomes/*chemistry/metabolism/ultrastructure ; Physicochemical Processes ; Protein Folding ; *Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/chemistry/*genetics/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; Silent Information Regulator Proteins, Saccharomyces ; cerevisiae/*chemistry/genetics/metabolism ; Static Electricity
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  • 14
    Publication Date: 2011-06-18
    Description: Innate immune responses are triggered by the activation of pattern-recognition receptors (PRRs). The Arabidopsis PRR FLAGELLIN-SENSING 2 (FLS2) senses bacterial flagellin and initiates immune signaling through association with BAK1. The molecular mechanisms underlying the attenuation of FLS2 activation are largely unknown. We report that flagellin induces recruitment of two closely related U-box E3 ubiquitin ligases, PUB12 and PUB13, to FLS2 receptor complex in Arabidopsis. BAK1 phosphorylates PUB12 and PUB13 and is required for FLS2-PUB12/13 association. PUB12 and PUB13 polyubiquitinate FLS2 and promote flagellin-induced FLS2 degradation, and the pub12 and pub13 mutants displayed elevated immune responses to flagellin treatment. Our study has revealed a unique regulatory circuit of direct ubiquitination and turnover of FLS2 by BAK1-mediated phosphorylation and recruitment of specific E3 ligases for attenuation of immune signaling.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3243913/" 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/PMC3243913/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Dongping -- Lin, Wenwei -- Gao, Xiquan -- Wu, Shujing -- Cheng, Cheng -- Avila, Julian -- Heese, Antje -- Devarenne, Timothy P -- He, Ping -- Shan, Libo -- R01 GM092893/GM/NIGMS NIH HHS/ -- R01 GM092893-02/GM/NIGMS NIH HHS/ -- R01 GM097247/GM/NIGMS NIH HHS/ -- R01GM092893/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Jun 17;332(6036):1439-42. doi: 10.1126/science.1204903.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21680842" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/genetics/*immunology/metabolism/microbiology ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Flagellin/*immunology ; *Immunity, Innate ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Peptide Fragments/immunology ; Phosphorylation ; Plant Diseases/*immunology/microbiology ; Protein Interaction Domains and Motifs ; Protein Kinases/chemistry/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Pseudomonas syringae/growth & development/immunology ; Receptors, Pattern Recognition/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Ubiquitin-Protein Ligases/chemistry/genetics/*metabolism ; Ubiquitinated Proteins/metabolism ; Ubiquitination
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  • 15
    Publication Date: 2011-07-19
    Description: Passive transfer of broadly neutralizing HIV antibodies can prevent infection, which suggests that vaccines that elicit such antibodies would be protective. Thus far, however, few broadly neutralizing HIV antibodies that occur naturally have been characterized. To determine whether these antibodies are part of a larger group of related molecules, we cloned 576 new HIV antibodies from four unrelated individuals. All four individuals produced expanded clones of potent broadly neutralizing CD4-binding-site antibodies that mimic binding to CD4. Despite extensive hypermutation, the new antibodies shared a consensus sequence of 68 immunoglobulin H (IgH) chain amino acids and arise independently from two related IgH genes. Comparison of the crystal structure of one of the antibodies to the broadly neutralizing antibody VRC01 revealed conservation of the contacts to the HIV spike.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3351836/" 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/PMC3351836/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheid, Johannes F -- Mouquet, Hugo -- Ueberheide, Beatrix -- Diskin, Ron -- Klein, Florian -- Oliveira, Thiago Y K -- Pietzsch, John -- Fenyo, David -- Abadir, Alexander -- Velinzon, Klara -- Hurley, Arlene -- Myung, Sunnie -- Boulad, Farid -- Poignard, Pascal -- Burton, Dennis R -- Pereyra, Florencia -- Ho, David D -- Walker, Bruce D -- Seaman, Michael S -- Bjorkman, Pamela J -- Chait, Brian T -- Nussenzweig, Michel C -- P01 AI081677/AI/NIAID NIH HHS/ -- P30 AI060354/AI/NIAID NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- RR00862/RR/NCRR NIH HHS/ -- RR022220/RR/NCRR NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1633-7. doi: 10.1126/science.1207227. Epub 2011 Jul 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, The Rockefeller University, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21764753" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/*immunology/metabolism ; Antibody Affinity ; Antibody Specificity ; Antigens, CD4/immunology/*metabolism ; Binding Sites ; Binding Sites, Antibody ; Cloning, Molecular ; Consensus Sequence ; Crystallography, X-Ray ; Genes, Immunoglobulin Heavy Chain ; HIV Antibodies/*chemistry/*immunology/metabolism ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV Infections/immunology ; Humans ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Heavy Chains/chemistry ; Immunoglobulin Light Chains/chemistry ; Molecular Mimicry ; Molecular Sequence Data ; Mutation ; Protein Conformation
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  • 16
    Publication Date: 2011-02-26
    Description: The fire ant Solenopsis invicta is a significant pest that was inadvertently introduced into the southern United States almost a century ago and more recently into California and other regions of the world. An assessment of genetic variation at a diverse set of molecular markers in 2144 fire ant colonies from 75 geographic sites worldwide revealed that at least nine separate introductions of S. invicta have occurred into newly invaded areas and that the main southern U.S. population is probably the source of all but one of these introductions. The sole exception involves a putative serial invasion from the southern United States to California to Taiwan. These results illustrate in stark fashion a severe negative consequence of an increasingly massive and interconnected global trade and travel system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ascunce, Marina S -- Yang, Chin-Cheng -- Oakey, Jane -- Calcaterra, Luis -- Wu, Wen-Jer -- Shih, Cheng-Jen -- Goudet, Jerome -- Ross, Kenneth G -- Shoemaker, DeWayne -- New York, N.Y. -- Science. 2011 Feb 25;331(6020):1066-8. doi: 10.1126/science.1198734.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉USDA-ARS Center for Medical, Agricultural, and Veterinary Entomology, 1600/1700 Southwest 23rd Drive, Gainesville, FL, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350177" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ants/genetics ; Asia ; Australia ; Bayes Theorem ; Commerce ; Computer Simulation ; DNA, Mitochondrial/genetics ; Female ; Genes, Insect ; Genetic Variation ; Genotype ; Haplotypes ; *Introduced Species ; Male ; Microsatellite Repeats ; Molecular Sequence Data ; Population Dynamics ; Sequence Analysis, DNA ; South America ; Travel ; United States
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  • 17
    Publication Date: 2011-03-26
    Description: Caenorhabditis elegans proteins AFF-1 and EFF-1 [C. elegans fusion family (CeFF) proteins] are essential for developmental cell-to-cell fusion and can merge insect cells. To study the structure and function of AFF-1, we constructed vesicular stomatitis virus (VSV) displaying AFF-1 on the viral envelope, substituting the native fusogen VSV glycoprotein. Electron microscopy and tomography revealed that AFF-1 formed distinct supercomplexes resembling pentameric and hexameric "flowers" on pseudoviruses. Viruses carrying AFF-1 infected mammalian cells only when CeFFs were on the target cell surface. Furthermore, we identified fusion family (FF) proteins within and beyond nematodes, and divergent members from the human parasitic nematode Trichinella spiralis and the chordate Branchiostoma floridae could also fuse mammalian cells. Thus, FF proteins are part of an ancient family of cellular fusogens that can promote fusion when expressed on a viral particle.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084904/" 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/PMC3084904/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Avinoam, Ori -- Fridman, Karen -- Valansi, Clari -- Abutbul, Inbal -- Zeev-Ben-Mordehai, Tzviya -- Maurer, Ulrike E -- Sapir, Amir -- Danino, Dganit -- Grunewald, Kay -- White, Judith M -- Podbilewicz, Benjamin -- 090532/Wellcome Trust/United Kingdom -- 090895/Wellcome Trust/United Kingdom -- AI22470/AI/NIAID NIH HHS/ -- R01 AI022470/AI/NIAID NIH HHS/ -- R01 AI022470-24/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2011 Apr 29;332(6029):589-92. doi: 10.1126/science.1202333. Epub 2011 Mar 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21436398" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arthropods/chemistry ; Biological Evolution ; Caenorhabditis elegans/chemistry ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism/ultrastructure ; *Cell Fusion ; Cell Line ; Cell Membrane/*metabolism ; Chordata, Nonvertebrate/chemistry ; Ctenophora/chemistry ; *Membrane Fusion ; Membrane Glycoproteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Naegleria fowleri/chemistry ; Nematoda/chemistry ; Recombinant Proteins/metabolism ; Recombination, Genetic ; Vesicular stomatitis Indiana virus/genetics/*physiology/ultrastructure ; Viral Envelope Proteins/metabolism
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  • 18
    Publication Date: 2011-01-08
    Description: NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an alpha(2)beta(2) tetramer that is homologous to the catalytic molybdenum-iron (MoFe) protein (NifDK) component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK. Here, we present the structure of the precursor-bound NifEN of Azotobacter vinelandii at 2.6 angstrom resolution. From a structural comparison of NifEN with des-M-cluster NifDK and holo NifDK, we propose similar pathways of cluster insertion for the homologous NifEN and NifDK proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3138709/" 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/PMC3138709/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jens T -- Hu, Yilin -- Wiig, Jared A -- Rees, Douglas C -- Ribbe, Markus W -- GM-45162/GM/NIGMS NIH HHS/ -- GM-67626/GM/NIGMS NIH HHS/ -- R01 GM067626/GM/NIGMS NIH HHS/ -- R01 GM067626-09/GM/NIGMS NIH HHS/ -- R37 GM045162/GM/NIGMS NIH HHS/ -- R37 GM045162-22/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Jan 7;331(6013):91-4. doi: 10.1126/science.1196954.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Mail Code 114-96, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21212358" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Azotobacter vinelandii/*chemistry/enzymology ; Bacterial Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Molybdoferredoxin/*chemistry/metabolism ; Nitrogenase/*chemistry/metabolism ; Protein Multimerization ; Protein Precursors/chemistry/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary
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  • 19
    Publication Date: 2011-10-25
    Description: The manipulation of protein backbone structure to control interaction and function is a challenge for protein engineering. We integrated computational design with experimental selection for grafting the backbone and side chains of a two-segment HIV gp120 epitope, targeted by the cross-neutralizing antibody b12, onto an unrelated scaffold protein. The final scaffolds bound b12 with high specificity and with affinity similar to that of gp120, and crystallographic analysis of a scaffold bound to b12 revealed high structural mimicry of the gp120-b12 complex structure. The method can be generalized to design other functional proteins through backbone grafting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azoitei, Mihai L -- Correia, Bruno E -- Ban, Yih-En Andrew -- Carrico, Chris -- Kalyuzhniy, Oleksandr -- Chen, Lei -- Schroeter, Alexandria -- Huang, Po-Ssu -- McLellan, Jason S -- Kwong, Peter D -- Baker, David -- Strong, Roland K -- Schief, William R -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Oct 21;334(6054):373-6. doi: 10.1126/science.1209368.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22021856" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Motifs ; Amino Acid Sequence ; Antibodies, Monoclonal/chemistry/immunology/metabolism ; Antibodies, Neutralizing/*chemistry/*immunology/metabolism ; Antibody Affinity ; Antibody Specificity ; Antigens, CD4/metabolism ; Computational Biology ; Computer Simulation ; Crystallography, X-Ray ; Epitopes/immunology ; HIV Antibodies/chemistry/*immunology/metabolism ; HIV Envelope Protein gp120/*chemistry/*immunology/metabolism ; Models, Molecular ; Molecular Mimicry ; Molecular Sequence Data ; Mutagenesis ; Protein Conformation ; *Protein Engineering ; Protein Interaction Domains and Motifs ; Surface Plasmon Resonance
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  • 20
    Publication Date: 2011-05-14
    Description: Pluripotent cells in the embryo can generate all cell types, but lineage-restricted cells are generally thought to replenish adult tissues. Planarians are flatworms and regenerate from tiny body fragments, a process requiring a population of proliferating cells (neoblasts). Whether regeneration is accomplished by pluripotent cells or by the collective activity of multiple lineage-restricted cell types is unknown. We used ionizing radiation and single-cell transplantation to identify neoblasts that can form large descendant-cell colonies in vivo. These clonogenic neoblasts (cNeoblasts) produce cells that differentiate into neuronal, intestinal, and other known postmitotic cell types and are distributed throughout the body. Single transplanted cNeoblasts restored regeneration in lethally irradiated hosts. We conclude that broadly distributed, adult pluripotent stem cells underlie the remarkable regenerative abilities of planarians.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3338249/" 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/PMC3338249/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagner, Daniel E -- Wang, Irving E -- Reddien, Peter W -- R01 GM080639/GM/NIGMS NIH HHS/ -- R01 GM080639-05/GM/NIGMS NIH HHS/ -- R01GM080639/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 May 13;332(6031):811-6. doi: 10.1126/science.1203983.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biology, Massachusetts Institute of Technology (MIT), Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21566185" target="_blank"〉PubMed〈/a〉
    Keywords: Adult Stem Cells/cytology/*physiology/transplantation ; Animals ; Base Sequence ; Cell Differentiation ; Cell Lineage ; Cell Proliferation ; Cell Separation ; Clone Cells/cytology/physiology ; Genes, Helminth ; Genotype ; Intestines/cytology ; Molecular Sequence Data ; Neurons/cytology ; Planarians/*cytology/genetics/*physiology/radiation effects ; Pluripotent Stem Cells/cytology/*physiology/transplantation ; *Regeneration
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  • 21
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-07-23
    Description: A 7000-year record of Coccolithovirus and its host, the calcifying haptophyte Emiliania huxleyi, was reconstructed on the basis of genetic signatures preserved in sediments underlying the Black Sea. The data show that the same virus and host populations can persist for centuries. Major changes in virus and host populations occurred during early sapropel deposition, ~5600 years ago, and throughout the formation of the coccolith-bearing sediments of Unit I during the past 2500 years, when the Black Sea experienced dramatic changes in hydrologic and nutrient regimes. Unit I saw a reoccurrence of the same host genotype thousands of years later in the presence of a different subset of viruses. Historical plankton virus populations can thus be included in paleoecological and paleoenvironmental studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coolen, Marco J L -- New York, N.Y. -- Science. 2011 Jul 22;333(6041):451-2. doi: 10.1126/science.1200072.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Marine Chemistry and Geochemistry Department, Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA. mcoolen@whoi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21778399" target="_blank"〉PubMed〈/a〉
    Keywords: Black Sea ; Capsid Proteins/genetics ; DNA, Viral/classification/genetics ; Denaturing Gradient Gel Electrophoresis ; *Ecosystem ; Electron Transport Complex IV/genetics ; *Genes, Viral ; Genotype ; *Geologic Sediments ; *Haptophyta/classification/genetics/virology ; Molecular Sequence Data ; Phosphoglycerate Mutase/genetics ; *Phycodnaviridae/classification/genetics/isolation & purification ; Phylogeny ; Polymerase Chain Reaction ; Population Dynamics ; Seawater ; Sequence Analysis, DNA ; Time
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  • 22
    Publication Date: 2011-01-06
    Description: Rhizobium-root nodule symbiosis is generally considered to be unique for legumes. However, there is one exception, and that is Parasponia. In this nonlegume, the rhizobial nodule symbiosis evolved independently and is, as in legumes, induced by rhizobium Nod factors. We used Parasponia andersonii to identify genetic constraints underlying evolution of Nod factor signaling. Part of the signaling cascade, downstream of Nod factor perception, has been recruited from the more-ancient arbuscular endomycorrhizal symbiosis. However, legume Nod factor receptors that activate this common signaling pathway are not essential for arbuscular endomycorrhizae. Here, we show that in Parasponia a single Nod factor-like receptor is indispensable for both symbiotic interactions. Therefore, we conclude that the Nod factor perception mechanism also is recruited from the widespread endomycorrhizal symbiosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Op den Camp, Rik -- Streng, Arend -- De Mita, Stephane -- Cao, Qingqin -- Polone, Elisa -- Liu, Wei -- Ammiraju, Jetty S S -- Kudrna, Dave -- Wing, Rod -- Untergasser, Andreas -- Bisseling, Ton -- Geurts, Rene -- New York, N.Y. -- Science. 2011 Feb 18;331(6019):909-12. doi: 10.1126/science.1198181. Epub 2010 Dec 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Sciences, Wageningen University, Wageningen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21205637" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cloning, Molecular ; Evolution, Molecular ; Gene Duplication ; Genes, Plant ; Glomeromycota/physiology ; Lipopolysaccharides/*metabolism ; Molecular Sequence Data ; Mycorrhizae/*physiology ; Nitrogen Fixation ; Phylogeny ; Plant Proteins/genetics/*metabolism ; Plant Root Nodulation ; Protein Kinases/genetics/*metabolism ; RNA Interference ; Root Nodules, Plant/microbiology/physiology ; Signal Transduction ; Sinorhizobium/*physiology ; *Symbiosis ; Ulmaceae/genetics/*microbiology/*physiology
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  • 23
    Publication Date: 2011-02-19
    Description: Meiosis requires that each chromosome find its homologous partner and undergo at least one crossover. X-Y chromosome segregation hinges on efficient crossing-over in a very small region of homology, the pseudoautosomal region (PAR). We find that mouse PAR DNA occupies unusually long chromosome axes, potentially as shorter chromatin loops, predicted to promote double-strand break (DSB) formation. Most PARs show delayed appearance of RAD51/DMC1 foci, which mark DSB ends, and all PARs undergo delayed DSB-mediated homologous pairing. Analysis of Spo11beta isoform-specific transgenic mice revealed that late RAD51/DMC1 foci in the PAR are genetically distinct from both early PAR foci and global foci and that late PAR foci promote efficient X-Y pairing, recombination, and male fertility. Our findings uncover specific mechanisms that surmount the unique challenges of X-Y recombination.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3151169/" 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/PMC3151169/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kauppi, Liisa -- Barchi, Marco -- Baudat, Frederic -- Romanienko, Peter J -- Keeney, Scott -- Jasin, Maria -- R01 HD040916/HD/NICHD NIH HHS/ -- R01 HD040916-01/HD/NICHD NIH HHS/ -- R01 HD040916-10/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2011 Feb 18;331(6019):916-20. doi: 10.1126/science.1195774.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21330546" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Cycle Proteins/metabolism ; Chromatin/chemistry/metabolism ; *Chromosome Pairing ; Chromosome Segregation ; *Crossing Over, Genetic ; DNA Breaks, Double-Stranded ; Endodeoxyribonucleases/genetics/*metabolism ; Female ; In Situ Hybridization, Fluorescence ; Male ; *Meiosis ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Protein Isoforms ; Rad51 Recombinase/metabolism ; X Chromosome/*physiology ; Y Chromosome/*physiology
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  • 24
    Publication Date: 2011-01-15
    Description: The synthesis of both proinflammatory leukotrienes and anti-inflammatory lipoxins requires the enzyme 5-lipoxygenase (5-LOX). 5-LOX activity is short-lived, apparently in part because of an intrinsic instability of the enzyme. We identified a 5-LOX-specific destabilizing sequence that is involved in orienting the carboxyl terminus, which binds the catalytic iron. Here, we report the crystal structure at 2.4 angstrom resolution of human 5-LOX stabilized by replacement of this sequence.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245680/" 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/PMC3245680/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilbert, Nathaniel C -- Bartlett, Sue G -- Waight, Maria T -- Neau, David B -- Boeglin, William E -- Brash, Alan R -- Newcomer, Marcia E -- GM-15431/GM/NIGMS NIH HHS/ -- P01 GM015431/GM/NIGMS NIH HHS/ -- P01 GM015431-44/GM/NIGMS NIH HHS/ -- R01 HL107887/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2011 Jan 14;331(6014):217-9. doi: 10.1126/science.1197203.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21233389" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arachidonate 5-Lipoxygenase/*chemistry/genetics/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Stability ; Humans ; Iron/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutant Proteins/chemistry ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 25
    Publication Date: 2011-09-24
    Description: Although many eukaryotic proteins are amino (N)-terminally acetylated, structural mechanisms by which N-terminal acetylation mediates protein interactions are largely unknown. Here, we found that N-terminal acetylation of the E2 enzyme, Ubc12, dictates distinctive E3-dependent ligation of the ubiquitin-like protein Nedd8 to Cul1. Structural, biochemical, biophysical, and genetic analyses revealed how complete burial of Ubc12's N-acetyl-methionine in a hydrophobic pocket in the E3, Dcn1, promotes cullin neddylation. The results suggest that the N-terminal acetyl both directs Ubc12's interactions with Dcn1 and prevents repulsion of a charged N terminus. Our data provide a link between acetylation and ubiquitin-like protein conjugation and define a mechanism for N-terminal acetylation-dependent recognition.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3214010/" 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/PMC3214010/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, Daniel C -- Monda, Julie K -- Bennett, Eric J -- Harper, J Wade -- Schulman, Brenda A -- P30 CA021765/CA/NCI NIH HHS/ -- P30 CA021765-33/CA/NCI NIH HHS/ -- R01 GM054137/GM/NIGMS NIH HHS/ -- R01 GM054137-13/GM/NIGMS NIH HHS/ -- R01 GM069530/GM/NIGMS NIH HHS/ -- R01 GM069530-10/GM/NIGMS NIH HHS/ -- R01 GM070565/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Nov 4;334(6056):674-8. doi: 10.1126/science.1209307. Epub 2011 Sep 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Department, 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/21940857" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Cullin Proteins/metabolism ; Humans ; Molecular Sequence Data ; Multiprotein Complexes/*metabolism ; Protein Binding ; Saccharomyces cerevisiae Proteins/*metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitins/metabolism
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  • 26
    Publication Date: 2011-05-10
    Description: Vascular plants appeared ~410 million years ago, then diverged into several lineages of which only two survive: the euphyllophytes (ferns and seed plants) and the lycophytes. We report here the genome sequence of the lycophyte Selaginella moellendorffii (Selaginella), the first nonseed vascular plant genome reported. By comparing gene content in evolutionarily diverse taxa, we found that the transition from a gametophyte- to a sporophyte-dominated life cycle required far fewer new genes than the transition from a nonseed vascular to a flowering plant, whereas secondary metabolic genes expanded extensively and in parallel in the lycophyte and angiosperm lineages. Selaginella differs in posttranscriptional gene regulation, including small RNA regulation of repetitive elements, an absence of the trans-acting small interfering RNA pathway, and extensive RNA editing of organellar genes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166216/" 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/PMC3166216/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banks, Jo Ann -- Nishiyama, Tomoaki -- Hasebe, Mitsuyasu -- Bowman, John L -- Gribskov, Michael -- dePamphilis, Claude -- Albert, Victor A -- Aono, Naoki -- Aoyama, Tsuyoshi -- Ambrose, Barbara A -- Ashton, Neil W -- Axtell, Michael J -- Barker, Elizabeth -- Barker, Michael S -- Bennetzen, Jeffrey L -- Bonawitz, Nicholas D -- Chapple, Clint -- Cheng, Chaoyang -- Correa, Luiz Gustavo Guedes -- Dacre, Michael -- DeBarry, Jeremy -- Dreyer, Ingo -- Elias, Marek -- Engstrom, Eric M -- Estelle, Mark -- Feng, Liang -- Finet, Cedric -- Floyd, Sandra K -- Frommer, Wolf B -- Fujita, Tomomichi -- Gramzow, Lydia -- Gutensohn, Michael -- Harholt, Jesper -- Hattori, Mitsuru -- Heyl, Alexander -- Hirai, Tadayoshi -- Hiwatashi, Yuji -- Ishikawa, Masaki -- Iwata, Mineko -- Karol, Kenneth G -- Koehler, Barbara -- Kolukisaoglu, Uener -- Kubo, Minoru -- Kurata, Tetsuya -- Lalonde, Sylvie -- Li, Kejie -- Li, Ying -- Litt, Amy -- Lyons, Eric -- Manning, Gerard -- Maruyama, Takeshi -- Michael, Todd P -- Mikami, Koji -- Miyazaki, Saori -- Morinaga, Shin-ichi -- Murata, Takashi -- Mueller-Roeber, Bernd -- Nelson, David R -- Obara, Mari -- Oguri, Yasuko -- Olmstead, Richard G -- Onodera, Naoko -- Petersen, Bent Larsen -- Pils, Birgit -- Prigge, Michael -- Rensing, Stefan A -- Riano-Pachon, Diego Mauricio -- Roberts, Alison W -- Sato, Yoshikatsu -- Scheller, Henrik Vibe -- Schulz, Burkhard -- Schulz, Christian -- Shakirov, Eugene V -- Shibagaki, Nakako -- Shinohara, Naoki -- Shippen, Dorothy E -- Sorensen, Iben -- Sotooka, Ryo -- Sugimoto, Nagisa -- Sugita, Mamoru -- Sumikawa, Naomi -- Tanurdzic, Milos -- Theissen, Gunter -- Ulvskov, Peter -- Wakazuki, Sachiko -- Weng, Jing-Ke -- Willats, William W G T -- Wipf, Daniel -- Wolf, Paul G -- Yang, Lixing -- Zimmer, Andreas D -- Zhu, Qihui -- Mitros, Therese -- Hellsten, Uffe -- Loque, Dominique -- Otillar, Robert -- Salamov, Asaf -- Schmutz, Jeremy -- Shapiro, Harris -- Lindquist, Erika -- Lucas, Susan -- Rokhsar, Daniel -- Grigoriev, Igor V -- GM065383/GM/NIGMS NIH HHS/ -- GM84051/GM/NIGMS NIH HHS/ -- HG004164/HG/NHGRI NIH HHS/ -- R01 GM043644/GM/NIGMS NIH HHS/ -- R01 GM084051/GM/NIGMS NIH HHS/ -- R01 GM084051-01A1/GM/NIGMS NIH HHS/ -- R01 HG004164/HG/NHGRI NIH HHS/ -- R01 HG004164-02/HG/NHGRI NIH HHS/ -- R01 HG004164-03/HG/NHGRI NIH HHS/ -- R01 HG004164-04/HG/NHGRI NIH HHS/ -- T32 GM007757/GM/NIGMS NIH HHS/ -- T32-HG00035/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2011 May 20;332(6032):960-3. doi: 10.1126/science.1203810. Epub 2011 May 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Purdue University, West Lafayette, IN 47907, USA. banksj@purdue.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21551031" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/chemistry/genetics ; *Biological Evolution ; Bryopsida/genetics ; Chlamydomonas/chemistry/genetics ; DNA Transposable Elements ; Evolution, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; *Genome, Plant ; MicroRNAs/genetics ; Molecular Sequence Data ; Phylogeny ; Plant Proteins/genetics/metabolism ; Proteome/analysis ; RNA Editing ; RNA, Plant/genetics ; Repetitive Sequences, Nucleic Acid ; Selaginellaceae/*genetics/growth & development/metabolism ; Sequence Analysis, DNA
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  • 27
    Publication Date: 2011-01-22
    Description: The NLR (nucleotide binding and oligomerization, leucine-rich repeat) family of proteins senses microbial infections and activates the inflammasome, a multiprotein complex that promotes microbial clearance. Kaposi's sarcoma-associated herpesvirus (KSHV) is linked to several human malignancies. We found that KSHV Orf63 is a viral homolog of human NLRP1. Orf63 blocked NLRP1-dependent innate immune responses, including caspase-1 activation and processing of interleukins IL-1beta and IL-18. KSHV Orf63 interacted with NLRP1, NLRP3, and NOD2. Inhibition of Orf63 expression resulted in increased expression of IL-1beta during the KSHV life cycle. Furthermore, inhibition of NLRP1 was necessary for efficient reactivation and generation of progeny virus. The viral homolog subverts the function of cellular NLRs, which suggests that modulation of NLR-mediated innate immunity is important for the lifelong persistence of herpesviruses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3072027/" 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/PMC3072027/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gregory, Sean M -- Davis, Beckley K -- West, John A -- Taxman, Debra J -- Matsuzawa, Shu-ichi -- Reed, John C -- Ting, Jenny P Y -- Damania, Blossom -- 5R21CA131645/CA/NCI NIH HHS/ -- AI057157/AI/NIAID NIH HHS/ -- AI077437/AI/NIAID NIH HHS/ -- AI56324/AI/NIAID NIH HHS/ -- AI91967/AI/NIAID NIH HHS/ -- CA096500/CA/NCI NIH HHS/ -- CA156330/CA/NCI NIH HHS/ -- DE018281/DE/NIDCR NIH HHS/ -- F32-AI78735/AI/NIAID NIH HHS/ -- R01 AI091967/AI/NIAID NIH HHS/ -- R01 CA096500/CA/NCI NIH HHS/ -- R01 CA096500-10/CA/NCI NIH HHS/ -- R01 DE018281/DE/NIDCR NIH HHS/ -- R01 DE018281-05/DE/NIDCR NIH HHS/ -- T32-AI007001/AI/NIAID NIH HHS/ -- T32-AI007419/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2011 Jan 21;331(6015):330-4. doi: 10.1126/science.1199478.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21252346" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Amino Acid Sequence ; Apoptosis ; Apoptosis Regulatory Proteins/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Carrier Proteins/metabolism ; Caspase 1/metabolism ; Caspase Inhibitors ; Cell Line ; Cell Line, Tumor ; Herpesvirus 8, Human/genetics/immunology/*physiology ; Humans ; *Immune Evasion ; *Immunity, Innate ; Inflammasomes/*antagonists & inhibitors/metabolism ; Interleukin-1beta/metabolism ; Molecular Sequence Data ; Monocytes/virology ; Nod2 Signaling Adaptor Protein/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Transfection ; Viral Proteins/chemistry/genetics/*metabolism ; Virus Activation ; Virus Latency ; Virus Replication
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  • 28
    Publication Date: 2011-04-09
    Description: Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3151171/" 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/PMC3151171/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhabha, Gira -- Lee, Jeeyeon -- Ekiert, Damian C -- Gam, Jongsik -- Wilson, Ian A -- Dyson, H Jane -- Benkovic, Stephen J -- Wright, Peter E -- GM080209/GM/NIGMS NIH HHS/ -- GM75995/GM/NIGMS NIH HHS/ -- R01 GM075995/GM/NIGMS NIH HHS/ -- U54 GM094586/GM/NIGMS NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Apr 8;332(6026):234-8. doi: 10.1126/science.1198542.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21474759" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biocatalysis ; Catalytic Domain ; Crystallography, X-Ray ; Escherichia coli/*enzymology ; Folic Acid/chemistry ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; NADP/chemistry ; Protein Conformation ; Tetrahydrofolate Dehydrogenase/*chemistry/genetics/*metabolism
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  • 29
    Publication Date: 2011-08-13
    Description: Pyrazinamide (PZA) is a first-line tuberculosis drug that plays a unique role in shortening the duration of tuberculosis chemotherapy. PZA is hydrolyzed intracellularly to pyrazinoic acid (POA) by pyrazinamidase (PZase, encoded by pncA), an enzyme frequently lost in PZA-resistant strains, but the target of POA in Mycobacterium tuberculosis has remained elusive. Here, we identify a previously unknown target of POA as the ribosomal protein S1 (RpsA), a vital protein involved in protein translation and the ribosome-sparing process of trans-translation. Three PZA-resistant clinical isolates without pncA mutation harbored RpsA mutations. RpsA overexpression conferred increased PZA resistance, and we confirmed that POA bound to RpsA (but not a clinically identified DeltaAla mutant) and subsequently inhibited trans-translation rather than canonical translation. Trans-translation is essential for freeing scarce ribosomes in nonreplicating organisms, and its inhibition may explain the ability of PZA to eradicate persisting organisms.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3502614/" 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/PMC3502614/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, Wanliang -- Zhang, Xuelian -- Jiang, Xin -- Yuan, Haiming -- Lee, Jong Seok -- Barry, Clifton E 3rd -- Wang, Honghai -- Zhang, Wenhong -- Zhang, Ying -- AI44063/AI/NIAID NIH HHS/ -- ZIA AI000783-16/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1630-2. doi: 10.1126/science.1208813. Epub 2011 Aug 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W. Harry Feinstone Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21835980" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/genetics/metabolism ; Amino Acid Sequence ; Antitubercular Agents/metabolism/*pharmacology ; Bacterial Proteins/chemistry/genetics/*metabolism ; Drug Resistance, Bacterial ; Molecular Sequence Data ; Mutant Proteins/metabolism ; Mutation ; Mycobacterium tuberculosis/*drug effects/genetics/metabolism ; Prodrugs/metabolism/pharmacology ; Protein Binding ; Protein Biosynthesis/drug effects ; Protein Structure, Tertiary ; Pyrazinamide/*analogs & derivatives/metabolism/*pharmacology ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; RNA, Transfer/metabolism ; Ribosomal Proteins/chemistry/genetics/*metabolism ; Ribosomes/metabolism
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  • 30
    Publication Date: 2011-08-13
    Description: Plants and their arbuscular mycorrhizal fungal symbionts interact in complex underground networks involving multiple partners. This increases the potential for exploitation and defection by individuals, raising the question of how partners maintain a fair, two-way transfer of resources. We manipulated cooperation in plants and fungal partners to show that plants can detect, discriminate, and reward the best fungal partners with more carbohydrates. In turn, their fungal partners enforce cooperation by increasing nutrient transfer only to those roots providing more carbohydrates. On the basis of these observations we conclude that, unlike many other mutualisms, the symbiont cannot be "enslaved." Rather, the mutualism is evolutionarily stable because control is bidirectional, and partners offering the best rate of exchange are rewarded.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kiers, E Toby -- Duhamel, Marie -- Beesetty, Yugandhar -- Mensah, Jerry A -- Franken, Oscar -- Verbruggen, Erik -- Fellbaum, Carl R -- Kowalchuk, George A -- Hart, Miranda M -- Bago, Alberto -- Palmer, Todd M -- West, Stuart A -- Vandenkoornhuyse, Philippe -- Jansa, Jan -- Bucking, Heike -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):880-2. doi: 10.1126/science.1208473.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Ecological Science, Vrije Universiteit, 1081 HV Amsterdam, Netherlands. toby.kiers@vu.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21836016" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Carbohydrate Metabolism ; Carbon/metabolism ; Glomeromycota/genetics/growth & development/*physiology ; Medicago truncatula/*microbiology/*physiology ; Molecular Sequence Data ; Mycorrhizae/genetics/growth & development/*physiology ; Phosphorus/metabolism ; Plant Roots/*microbiology/physiology ; RNA, Fungal/metabolism ; Species Specificity ; *Symbiosis
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  • 31
    Publication Date: 2011-06-28
    Description: The ribonuclease (RNase) H class of enzymes degrades the RNA component of RNA:DNA hybrids and is important in nucleic acid metabolism. RNase H2 is specialized to remove single ribonucleotides [ribonucleoside monophosphates (rNMPs)] from duplex DNA, and its absence in budding yeast has been associated with the accumulation of deletions within short tandem repeats. Here, we demonstrate that rNMP-associated deletion formation requires the activity of Top1, a topoisomerase that relaxes supercoils by reversibly nicking duplex DNA. The reported studies extend the role of Top1 to include the processing of rNMPs in genomic DNA into irreversible single-strand breaks, an activity that can have distinct mutagenic consequences and may be relevant to human disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3380281/" 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/PMC3380281/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Nayun -- Huang, Shar-yin N -- Williams, Jessica S -- Li, Yue C -- Clark, Alan B -- Cho, Jang-Eun -- Kunkel, Thomas A -- Pommier, Yves -- Jinks-Robertson, Sue -- R01 GM038464/GM/NIGMS NIH HHS/ -- R01 GM093197/GM/NIGMS NIH HHS/ -- R01 GM38464/GM/NIGMS NIH HHS/ -- R01 GM93197/GM/NIGMS NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Jun 24;332(6037):1561-4. doi: 10.1126/science.1205016.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21700875" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Transport Systems, Basic/genetics ; Base Sequence ; Camptothecin/pharmacology ; Canavanine/pharmacology ; DNA Breaks ; DNA Topoisomerases, Type I/*metabolism ; DNA, Fungal/chemistry/*metabolism ; DNA, Single-Stranded/metabolism ; Microsatellite Repeats ; Molecular Sequence Data ; *Mutagenesis ; Nucleic Acid Conformation ; Ribonuclease H/genetics/metabolism ; Ribonucleotides/*metabolism ; Saccharomyces cerevisiae/enzymology/*genetics/*metabolism ; Saccharomyces cerevisiae Proteins/genetics ; *Sequence Deletion ; Transcription, Genetic
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  • 32
    Publication Date: 2011-06-11
    Description: Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-alpha. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meinema, Anne C -- Laba, Justyna K -- Hapsari, Rizqiya A -- Otten, Renee -- Mulder, Frans A A -- Kralt, Annemarie -- van den Bogaart, Geert -- Lusk, C Patrick -- Poolman, Bert -- Veenhoff, Liesbeth M -- New York, N.Y. -- Science. 2011 Jul 1;333(6038):90-3. doi: 10.1126/science.1205741. Epub 2011 Jun 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Netherlands Proteomics Centre, Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21659568" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Endoplasmic Reticulum/metabolism ; Karyopherins/chemistry/metabolism ; Membrane Proteins/*chemistry/genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Nuclear Envelope/*metabolism ; Nuclear Localization Signals ; Nuclear Pore/*metabolism ; Nuclear Pore Complex Proteins/chemistry/genetics/*metabolism ; Nuclear Proteins/chemistry/genetics/metabolism ; Protein Folding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism
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  • 33
    Publication Date: 2011-02-26
    Description: Chronic mucocutaneous candidiasis disease (CMCD) is characterized by recurrent or persistent infections of the skin, nails, and oral and genital mucosae caused by Candida albicans and, to a lesser extent, Staphylococcus aureus, in patients with no other infectious or autoimmune manifestations. We report two genetic etiologies of CMCD: autosomal recessive deficiency in the cytokine receptor, interleukin-17 receptor A (IL-17RA), and autosomal dominant deficiency of the cytokine interleukin-17F (IL-17F). IL-17RA deficiency is complete, abolishing cellular responses to IL-17A and IL-17F homo- and heterodimers. By contrast, IL-17F deficiency is partial, with mutant IL-17F-containing homo- and heterodimers displaying impaired, but not abolished, activity. These experiments of nature indicate that human IL-17A and IL-17F are essential for mucocutaneous immunity against C. albicans, but otherwise largely redundant.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3070042/" 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/PMC3070042/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puel, Anne -- Cypowyj, Sophie -- Bustamante, Jacinta -- Wright, Jill F -- Liu, Luyan -- Lim, Hye Kyung -- Migaud, Melanie -- Israel, Laura -- Chrabieh, Maya -- Audry, Magali -- Gumbleton, Matthew -- Toulon, Antoine -- Bodemer, Christine -- El-Baghdadi, Jamila -- Whitters, Matthew -- Paradis, Theresa -- Brooks, Jonathan -- Collins, Mary -- Wolfman, Neil M -- Al-Muhsen, Saleh -- Galicchio, Miguel -- Abel, Laurent -- Picard, Capucine -- Casanova, Jean-Laurent -- 5UL1RR024143-04/RR/NCRR NIH HHS/ -- UL1 RR024143/RR/NCRR NIH HHS/ -- UL1 RR024143-04/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2011 Apr 1;332(6025):65-8. doi: 10.1126/science.1200439. Epub 2011 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Human Genetics of Infectious Diseases, Necker Branch, Institut National de la Sante et de la Recherche Medicale, U980, and University Paris Descartes, Necker Medical School, 75015 Paris, France. anne.puel@inserm.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350122" target="_blank"〉PubMed〈/a〉
    Keywords: Candida albicans ; Candidiasis, Chronic Mucocutaneous/*genetics/*immunology ; Child ; Child, Preschool ; Female ; Genes, Dominant ; Genes, Recessive ; Humans ; Interleukin-17/*immunology ; Male ; Molecular Sequence Data ; Mutation ; Pedigree ; Receptors, Interleukin-17/genetics ; Signal Transduction/genetics ; Th17 Cells/immunology
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  • 34
    Publication Date: 2011-10-29
    Description: Antibodies against the CD4 binding site (CD4bs) on the HIV-1 spike protein gp120 can show exceptional potency and breadth. We determined structures of NIH45-46, a more potent clonal variant of VRC01, alone and bound to gp120. Comparisons with VRC01-gp120 revealed that a four-residue insertion in heavy chain complementarity-determining region 3 (CDRH3) contributed to increased interaction between NIH45-46 and the gp120 inner domain, which correlated with enhanced neutralization. We used structure-based design to create NIH45-46(G54W), a single substitution in CDRH2 that increases contact with the gp120 bridging sheet and improves breadth and potency, critical properties for potential clinical use, by an order of magnitude. Together with the NIH45-46-gp120 structure, these results indicate that gp120 inner domain and bridging sheet residues should be included in immunogens to elicit CD4bs antibodies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3232316/" 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/PMC3232316/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diskin, Ron -- Scheid, Johannes F -- Marcovecchio, Paola M -- West, Anthony P Jr -- Klein, Florian -- Gao, Han -- Gnanapragasam, Priyanthi N P -- Abadir, Alexander -- Seaman, Michael S -- Nussenzweig, Michel C -- Bjorkman, Pamela J -- P01 AI081677-01/AI/NIAID NIH HHS/ -- RR00862/RR/NCRR NIH HHS/ -- RR022220/RR/NCRR NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Dec 2;334(6060):1289-93. doi: 10.1126/science.1213782. Epub 2011 Oct 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22033520" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Amino Acid Sequence ; Antibodies, Neutralizing/chemistry/*immunology/metabolism ; Antibody Affinity ; Antigens, CD4/chemistry/metabolism ; Binding Sites ; Complementarity Determining Regions ; Crystallography, X-Ray ; HIV Antibodies/chemistry/*immunology/metabolism ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV-1/*immunology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Immunoglobulin Heavy Chains/chemistry/immunology/metabolism ; Molecular Mimicry ; Molecular Sequence Data ; Mutant Proteins/chemistry/immunology/metabolism ; Protein Conformation ; *Protein Engineering ; Protein Structure, Tertiary
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  • 35
    Publication Date: 2011-05-14
    Description: Regeneration requires initiation of programs tailored to the identity of missing parts. Head-versus-tail regeneration in planarians presents a paradigm for study of this phenomenon. After injury, Wnt signaling promotes tail regeneration. We report that wounding elicits expression of the Wnt inhibitor notum preferentially at anterior-facing wounds. This expression asymmetry occurs at essentially any wound, even if the anterior pole is intact. Inhibition of notum with RNA interference (RNAi) causes regeneration of an anterior-facing tail instead of a head, and double-RNAi experiments indicate that notum inhibits Wnt signaling to promote head regeneration. notum expression is itself controlled by Wnt signaling, suggesting that regulation of feedback inhibition controls the binary head-tail regeneration outcome. We conclude that local detection of wound orientation with respect to tissue axes results in distinct signaling environments that initiate appropriate regeneration responses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3320723/" 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/PMC3320723/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petersen, Christian P -- Reddien, Peter W -- R01 GM080639/GM/NIGMS NIH HHS/ -- R01 GM080639-04/GM/NIGMS NIH HHS/ -- R01GM080639/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 May 13;332(6031):852-5. doi: 10.1126/science.1202143.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21566195" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Feedback, Physiological ; Gene Expression Regulation ; Genes, Helminth ; Head ; Helminth Proteins/genetics/*metabolism ; Hydrolases/genetics/*metabolism ; Molecular Sequence Data ; Planarians/cytology/genetics/*physiology ; RNA Interference ; *Regeneration ; *Signal Transduction ; Tail ; Wnt Proteins/genetics/*metabolism ; Wnt1 Protein/genetics/metabolism ; beta Catenin/genetics/metabolism
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  • 36
    Publication Date: 2011-05-10
    Description: Disease-suppressive soils are exceptional ecosystems in which crop plants suffer less from specific soil-borne pathogens than expected owing to the activities of other soil microorganisms. For most disease-suppressive soils, the microbes and mechanisms involved in pathogen control are unknown. By coupling PhyloChip-based metagenomics of the rhizosphere microbiome with culture-dependent functional analyses, we identified key bacterial taxa and genes involved in suppression of a fungal root pathogen. More than 33,000 bacterial and archaeal species were detected, with Proteobacteria, Firmicutes, and Actinobacteria consistently associated with disease suppression. Members of the gamma-Proteobacteria were shown to have disease-suppressive activity governed by nonribosomal peptide synthetases. Our data indicate that upon attack by a fungal root pathogen, plants can exploit microbial consortia from soil for protection against infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendes, Rodrigo -- Kruijt, Marco -- de Bruijn, Irene -- Dekkers, Ester -- van der Voort, Menno -- Schneider, Johannes H M -- Piceno, Yvette M -- DeSantis, Todd Z -- Andersen, Gary L -- Bakker, Peter A H M -- Raaijmakers, Jos M -- New York, N.Y. -- Science. 2011 May 27;332(6033):1097-100. doi: 10.1126/science.1203980. Epub 2011 May 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, Wageningen 6700 EE, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21551032" target="_blank"〉PubMed〈/a〉
    Keywords: Actinobacteria/genetics/isolation & purification/physiology ; *Antibiosis ; Archaea/classification/genetics/isolation & purification/physiology ; Bacteria/classification/genetics/isolation & purification ; Beta vulgaris/microbiology ; *Metagenome ; *Microbial Consortia ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Peptide Synthases/genetics/metabolism ; Plant Diseases/microbiology/*prevention & control ; Plant Roots/microbiology ; Proteobacteria/genetics/isolation & purification/physiology ; Pseudomonadaceae/genetics/isolation & purification/physiology ; Rhizoctonia/*physiology ; *Rhizosphere ; *Soil Microbiology
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  • 37
    Publication Date: 2011-01-06
    Description: Eukaryotic ribosomes are substantially larger and more complex than their bacterial counterparts. Although their core function is conserved, bacterial and eukaryotic protein synthesis differ considerably at the level of initiation. The eukaryotic small ribosomal subunit (40S) plays a central role in this process; it binds initiation factors that facilitate scanning of messenger RNAs and initiation of protein synthesis. We have determined the crystal structure of the Tetrahymena thermophila 40S ribosomal subunit in complex with eukaryotic initiation factor 1 (eIF1) at a resolution of 3.9 angstroms. The structure reveals the fold of the entire 18S ribosomal RNA and of all ribosomal proteins of the 40S subunit, and defines the interactions with eIF1. It provides insights into the eukaryotic-specific aspects of protein synthesis, including the function of eIF1 as well as signaling and regulation mediated by the ribosomal proteins RACK1 and rpS6e.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabl, Julius -- Leibundgut, Marc -- Ataide, Sandro F -- Haag, Andrea -- Ban, Nenad -- New York, N.Y. -- Science. 2011 Feb 11;331(6018):730-6. doi: 10.1126/science.1198308. Epub 2010 Dec 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, Schafmattstrasse 20, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21205638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallization ; Crystallography, X-Ray ; Eukaryotic Initiation Factor-1/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Biosynthesis ; Protein Conformation ; Protein Folding ; Protozoan Proteins/chemistry/metabolism ; RNA, Messenger/chemistry ; RNA, Protozoan/chemistry ; RNA, Ribosomal, 18S/*chemistry ; Ribosomal Proteins/*chemistry/metabolism ; Ribosome Subunits, Small, Eukaryotic/*chemistry/metabolism/*ultrastructure ; Signal Transduction ; Tetrahymena thermophila/*chemistry/*ultrastructure
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  • 38
    Publication Date: 2011-07-02
    Description: Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor and are posttranslationally delivered to the endoplasmic reticulum (ER) membrane by the Get3 adenosine triphosphatase interacting with the hetero-oligomeric Get1/2 receptor. We have determined crystal structures of Get3 in complex with the cytosolic domains of Get1 and Get2 in different functional states at 3.0, 3.2, and 4.6 angstrom resolution. The structural data, together with biochemical experiments, show that Get1 and Get2 use adjacent, partially overlapping binding sites and that both can bind simultaneously to Get3. Docking to the Get1/2 complex allows for conformational changes in Get3 that are required for TA protein insertion. These data suggest a molecular mechanism for nucleotide-regulated delivery of TA proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3601824/" 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/PMC3601824/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stefer, Susanne -- Reitz, Simon -- Wang, Fei -- Wild, Klemens -- Pang, Yin-Yuin -- Schwarz, Daniel -- Bomke, Jorg -- Hein, Christopher -- Lohr, Frank -- Bernhard, Frank -- Denic, Vladimir -- Dotsch, Volker -- Sinning, Irmgard -- R01 GM099943/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Aug 5;333(6043):758-62. doi: 10.1126/science.1207125. Epub 2011 Jun 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, Goethe University, D-60325 Frankfurt am Main, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21719644" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport/*chemistry/*metabolism ; Adenosine Triphosphatases/*chemistry/*metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; Cytosol/chemistry ; Endoplasmic Reticulum/metabolism ; Guanine Nucleotide Exchange Factors/*chemistry/*metabolism ; Membrane Proteins/*chemistry/*metabolism ; Microsomes/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Saccharomyces cerevisiae/*chemistry/metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/*metabolism
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  • 39
    Publication Date: 2011-06-02
    Description: Members of the gammaretroviruses--such as murine leukemia viruses (MLVs), most notably XMRV [xenotropic murine leukemia virus (X-MLV)-related virus--have been reported to be present in the blood of patients with chronic fatigue syndrome (CFS). We evaluated blood samples from 61 patients with CFS from a single clinical practice, 43 of whom had previously been identified as XMRV-positive. Our analysis included polymerase chain reaction and reverse transcription polymerase chain reaction procedures for detection of viral nucleic acids and assays for detection of infectious virus and virus-specific antibodies. We found no evidence of XMRV or other MLVs in these blood samples. In addition, we found that these gammaretroviruses were strongly (X-MLV) or partially (XMRV) susceptible to inactivation by sera from CFS patients and healthy controls, which suggested that establishment of a successful MLV infection in humans would be unlikely. Consistent with previous reports, we detected MLV sequences in commercial laboratory reagents. Our results indicate that previous evidence linking XMRV and MLVs to CFS is likely attributable to laboratory contamination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knox, Konstance -- Carrigan, Donald -- Simmons, Graham -- Teque, Fernando -- Zhou, Yanchen -- Hackett, John Jr -- Qiu, Xiaoxing -- Luk, Ka-Cheung -- Schochetman, Gerald -- Knox, Allyn -- Kogelnik, Andreas M -- Levy, Jay A -- New York, N.Y. -- Science. 2011 Jul 1;333(6038):94-7. doi: 10.1126/science.1204963. Epub 2011 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wisconsin Viral Research Group, Milwaukee, WI 53226, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21628393" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Antibodies, Viral/blood ; Base Sequence ; Blood/*virology ; Child ; Child, Preschool ; Complement System Proteins/immunology ; DNA Contamination ; DNA, Viral/blood ; Drug Contamination ; Fatigue Syndrome, Chronic/blood/immunology/*virology ; Female ; Humans ; Indicators and Reagents ; Leukemia Virus, Murine/genetics/isolation & purification ; Leukocytes, Mononuclear/*virology ; Male ; Middle Aged ; Molecular Sequence Data ; Polymerase Chain Reaction ; Retroviridae Infections/diagnosis/*virology ; Xenotropic murine leukemia virus-related virus/genetics/immunology/*isolation & ; purification ; Young Adult
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-02-05
    Description: Confinement of enzymes in protein nanocompartments represents a potentially powerful strategy for controlling catalytic activity in cells. By using a simple electrostatically based tagging system for protein encapsulation, we successfully sequestered HIV protease, a toxic enzyme when produced cytoplasmically, within an engineered lumazine synthase capsid. The growth advantage resulting from protecting the Escherichia coli host from the protease enabled directed evolution of improved capsids. After four rounds of mutagenesis and selection, we obtained a variant with a 5- to 10-fold higher loading capacity than the starting capsid, which permitted efficient growth even at high intracellular concentrations of HIV protease. The superior properties of the evolved capsid can be ascribed to multiple mutations that increase the net negative charge on its luminal surface and thereby enhance engineered Coulombic interactions between host and guest. Such structures could be used for diverse biotechnological applications in living cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worsdorfer, Bigna -- Woycechowsky, Kenneth J -- Hilvert, Donald -- New York, N.Y. -- Science. 2011 Feb 4;331(6017):589-92. doi: 10.1126/science.1199081.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Organic Chemistry, 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/21292977" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA Shuffling ; *Directed Molecular Evolution ; *Escherichia coli/genetics/growth & development ; HIV Protease/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/genetics ; Point Mutation ; *Protein Engineering ; Selection, Genetic ; Static Electricity ; Transformation, Bacterial
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  • 41
    Publication Date: 2011-07-02
    Description: The Tammar wallaby (Macropus eugenii) harbors unique gut bacteria and produces only one-fifth the amount of methane produced by ruminants per unit of digestible energy intake. We have isolated a dominant bacterial species (WG-1) from the wallaby microbiota affiliated with the family Succinivibrionaceae and implicated in lower methane emissions from starch-containing diets. This was achieved by using a partial reconstruction of the bacterium's metabolism from binned metagenomic data (nitrogen and carbohydrate utilization pathways and antibiotic resistance) to devise cultivation-based strategies that produced axenic WG-1 cultures. Pure-culture studies confirm that the bacterium is capnophilic and produces succinate, further explaining a microbiological basis for lower methane emissions from macropodids. This knowledge also provides new strategic targets for redirecting fermentation and reducing methane production in livestock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pope, P B -- Smith, W -- Denman, S E -- Tringe, S G -- Barry, K -- Hugenholtz, P -- McSweeney, C S -- McHardy, A C -- Morrison, M -- New York, N.Y. -- Science. 2011 Jul 29;333(6042):646-8. doi: 10.1126/science.1205760. Epub 2011 Jun 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSIRO Livestock Industries, Queensland Bioscience Precinct, St Lucia 4067, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21719642" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbohydrate Metabolism ; Digestive System/*microbiology ; Female ; Fermentation ; Genome, Bacterial ; Macropodidae/*microbiology ; Metagenome ; Methane/*metabolism ; Molecular Sequence Data ; Starch/metabolism ; Succinic Acid/*metabolism ; Succinivibrionaceae/genetics/growth & development/*isolation & ; purification/*metabolism
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  • 42
    Publication Date: 2011-02-12
    Description: Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popow, Johannes -- Englert, Markus -- Weitzer, Stefan -- Schleiffer, Alexander -- Mierzwa, Beata -- Mechtler, Karl -- Trowitzsch, Simon -- Will, Cindy L -- Luhrmann, Reinhard -- Soll, Dieter -- Martinez, Javier -- New York, N.Y. -- Science. 2011 Feb 11;331(6018):760-4. doi: 10.1126/science.1197847.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), A-1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21311021" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Exons ; HeLa Cells ; Humans ; Introns ; Molecular Sequence Data ; Proteins/*chemistry/isolation & purification/*metabolism ; RNA Interference ; RNA Ligase (ATP)/*chemistry/isolation & purification/*metabolism ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Transfer/*metabolism ; Spliceosomes/metabolism
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  • 43
    Publication Date: 2011-09-17
    Description: Eukaryotic and archaeal multisubunit RNA polymerases (Pols) are structurally related and require several similar components for transcription initiation. However, none of the Pol I factors were known to share homology with transcription factor IIB (TFIIB) or TFIIB-related proteins, key factors in the initiation mechanisms of the other Pols. Here we show that Rrn7, a subunit of the yeast Pol I core factor, and its human ortholog TAF1B are TFIIB-like factors. Although distantly related, Rrn7 shares many activities associated with TFIIB-like factors. Domain swaps between TFIIB-related factors show that Rrn7 is most closely related to the Pol III general factor Brf1. Our results point to the conservation of initiation mechanisms among multisubunit Pols and reveal a key function of yeast core factor/human SL1 in Pol I transcription.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3319074/" 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/PMC3319074/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knutson, Bruce A -- Hahn, Steven -- GM053451/GM/NIGMS NIH HHS/ -- R01 GM053451/GM/NIGMS NIH HHS/ -- R01 GM053451-17/GM/NIGMS NIH HHS/ -- T32 CA009657/CA/NCI NIH HHS/ -- T32 CA009657-22/CA/NCI NIH HHS/ -- T32 CA09657/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1637-40. doi: 10.1126/science.1207699.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Division of Basic Sciences, 1100 Fairview Avenue N, Post Office Box 19024, Mailstop A1-162, Seattle, WA 98109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21921198" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Humans ; Molecular Sequence Data ; Pol1 Transcription Initiation Complex Proteins/*chemistry/genetics/*metabolism ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Polymerase I/*metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism ; Sequence Alignment ; TATA-Box Binding Protein/metabolism ; Transcription Factor TFIIB/chemistry/metabolism ; Transcription Factor TFIIIB/chemistry/genetics/metabolism ; Transcription, Genetic
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  • 44
    Publication Date: 2011-06-11
    Description: The evolutionarily conserved serine-threonine kinase mammalian target of rapamycin (mTOR) plays a critical role in regulating many pathophysiological processes. Functional characterization of the mTOR signaling pathways, however, has been hampered by the paucity of known substrates. We used large-scale quantitative phosphoproteomics experiments to define the signaling networks downstream of mTORC1 and mTORC2. Characterization of one mTORC1 substrate, the growth factor receptor-bound protein 10 (Grb10), showed that mTORC1-mediated phosphorylation stabilized Grb10, leading to feedback inhibition of the phosphatidylinositol 3-kinase (PI3K) and extracellular signal-regulated, mitogen-activated protein kinase (ERK-MAPK) pathways. Grb10 expression is frequently down-regulated in various cancers, and loss of Grb10 and loss of the well-established tumor suppressor phosphatase PTEN appear to be mutually exclusive events, suggesting that Grb10 might be a tumor suppressor regulated by mTORC1.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195509/" 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/PMC3195509/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Yonghao -- Yoon, Sang-Oh -- Poulogiannis, George -- Yang, Qian -- Ma, Xiaoju Max -- Villen, Judit -- Kubica, Neil -- Hoffman, Gregory R -- Cantley, Lewis C -- Gygi, Steven P -- Blenis, John -- CA46595/CA/NCI NIH HHS/ -- GM051405/GM/NIGMS NIH HHS/ -- HG3456/HG/NHGRI NIH HHS/ -- R00 CA140789/CA/NCI NIH HHS/ -- R00 CA140789-04/CA/NCI NIH HHS/ -- R00CA140789/CA/NCI NIH HHS/ -- R01 GM041890/GM/NIGMS NIH HHS/ -- R01 GM051405/GM/NIGMS NIH HHS/ -- R01 GM051405-14/GM/NIGMS NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- R01 HG003456/HG/NHGRI NIH HHS/ -- R01 HG003456-07/HG/NHGRI NIH HHS/ -- R37 CA046595/CA/NCI NIH HHS/ -- R37 CA046595-22/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2011 Jun 10;332(6035):1322-6. doi: 10.1126/science.1199484.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21659605" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibiotics, Antineoplastic/pharmacology ; Cell Line ; GRB10 Adaptor Protein/*metabolism ; Humans ; Insulin/*metabolism ; Mice ; Molecular Sequence Data ; Multiprotein Complexes ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphoproteins/metabolism ; Phosphorylation/drug effects ; Proteins/*metabolism ; Proteome/metabolism ; *Signal Transduction/drug effects ; Sirolimus/pharmacology ; TOR Serine-Threonine Kinases
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  • 45
    Publication Date: 2011-02-12
    Description: The unconventional myosin VIIa (MYO7A) is one of the five proteins that form a network of complexes involved in formation of stereocilia. Defects in these proteins cause syndromic deaf-blindness in humans [Usher syndrome I (USH1)]. Many disease-causing mutations occur in myosin tail homology 4-protein 4.1, ezrin, radixin, moesin (MyTH4-FERM) domains in the myosin tail that binds to another USH1 protein, Sans. We report the crystal structure of MYO7A MyTH4-FERM domains in complex with the central domain (CEN) of Sans at 2.8 angstrom resolution. The MyTH4 and FERM domains form an integral structural and functional supramodule binding to two highly conserved segments (CEN1 and 2) of Sans. The MyTH4-FERM/CEN complex structure provides mechanistic explanations for known deafness-causing mutations in MYO7A MyTH4-FERM. The structure will also facilitate mechanistic and functional studies of MyTH4-FERM domains in other myosins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Lin -- Pan, Lifeng -- Wei, Zhiyi -- Zhang, Mingjie -- New York, N.Y. -- Science. 2011 Feb 11;331(6018):757-60. doi: 10.1126/science.1198848.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Life Science, Molecular Neuroscience Center, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21311020" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Humans ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation, Missense ; Myosins/*chemistry/metabolism ; Nerve Tissue Proteins/*chemistry/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism
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  • 46
    Publication Date: 2011-08-13
    Description: Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1 isolates. To understand how such broadly neutralizing antibodies develop, we used x-ray crystallography and 454 pyrosequencing to characterize additional VRC01-like antibodies from HIV-1-infected individuals. Crystal structures revealed a convergent mode of binding for diverse antibodies to the same CD4-binding-site epitope. A functional genomics analysis of expressed heavy and light chains revealed common pathways of antibody-heavy chain maturation, confined to the IGHV1-2*02 lineage, involving dozens of somatic changes, and capable of pairing with different light chains. Broadly neutralizing HIV-1 immunity associated with VRC01-like antibodies thus involves the evolution of antibodies to a highly affinity-matured state required to recognize an invariant viral structure, with lineages defined from thousands of sequences providing a genetic roadmap of their development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3516815/" 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/PMC3516815/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Xueling -- Zhou, Tongqing -- Zhu, Jiang -- Zhang, Baoshan -- Georgiev, Ivelin -- Wang, Charlene -- Chen, Xuejun -- Longo, Nancy S -- Louder, Mark -- McKee, Krisha -- O'Dell, Sijy -- Perfetto, Stephen -- Schmidt, Stephen D -- Shi, Wei -- Wu, Lan -- Yang, Yongping -- Yang, Zhi-Yong -- Yang, Zhongjia -- Zhang, Zhenhai -- Bonsignori, Mattia -- Crump, John A -- Kapiga, Saidi H -- Sam, Noel E -- Haynes, Barton F -- Simek, Melissa -- Burton, Dennis R -- Koff, Wayne C -- Doria-Rose, Nicole A -- Connors, Mark -- NISC Comparative Sequencing Program -- Mullikin, James C -- Nabel, Gary J -- Roederer, Mario -- Shapiro, Lawrence -- Kwong, Peter D -- Mascola, John R -- 5U19 AI 067854-06/AI/NIAID NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- U19 AI067854/AI/NIAID NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1593-602. doi: 10.1126/science.1207532. Epub 2011 Aug 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21835983" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/genetics/*immunology/isolation & purification ; Antibody Affinity ; Antibody Specificity ; Antigens, CD4/metabolism ; Base Sequence ; Binding Sites ; Binding Sites, Antibody ; Complementarity Determining Regions/genetics ; Crystallography, X-Ray ; Epitopes ; *Evolution, Molecular ; Genes, Immunoglobulin Heavy Chain ; HIV Antibodies/*chemistry/genetics/*immunology/isolation & purification ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV Infections/immunology ; HIV-1/chemistry/*immunology ; High-Throughput Nucleotide Sequencing ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology ; Immunoglobulin Heavy Chains/chemistry/immunology ; Immunoglobulin J-Chains/genetics ; Immunoglobulin Light Chains/chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Sequence Analysis, DNA
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  • 47
    Publication Date: 2011-01-06
    Description: Self-incompatibility (SI)--intraspecific pollen recognition systems that allow plants to avoid inbreeding--in the Solanaceae (the nightshade family) is controlled by a polymorphic S locus where "self" pollen is rejected on pistils with matching S alleles. In contrast, unilateral interspecific incompatibility (UI) prevents hybridization between related species, most commonly when the pollen donor is self-compatible (SC) and the recipient is SI. We observed that in Solanum, a pollen-expressed Cullin1 gene with high similarity to Petunia SI factors interacts genetically with a gene at or near the S locus to control UI. Cultivated tomato and related red- or orange-fruited species (all SC) exhibit the same loss-of-function mutation in this gene, whereas the green-fruited species (mostly SI) contain a functional allele; hence, similar biochemical mechanisms underlie the rejection of both "self" and interspecific pollen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Wentao -- Chetelat, Roger T -- New York, N.Y. -- Science. 2010 Dec 24;330(6012):1827-30. doi: 10.1126/science.1197908.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Sciences, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21205670" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Crosses, Genetic ; Cullin Proteins/*genetics/metabolism ; Flowers/physiology ; *Genes, Plant ; Hybridization, Genetic ; Introns ; Lycopersicon esculentum/*genetics/*physiology ; Molecular Sequence Data ; Plant Proteins/*genetics/metabolism ; Plants, Genetically Modified ; Pollen/*genetics/physiology ; Pollination ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Ribonucleases/genetics/metabolism ; Sequence Deletion ; Solanum/*genetics/physiology
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  • 48
    Publication Date: 2011-01-22
    Description: Intracellular pathogens such as Listeria monocytogenes subvert cellular functions through the interaction of bacterial effectors with host components. Here we found that a secreted listerial virulence factor, LntA, could target the chromatin repressor BAHD1 in the host cell nucleus to activate interferon (IFN)-stimulated genes (ISGs). IFN-lambda expression was induced in response to infection of epithelial cells with bacteria lacking LntA; however, the BAHD1-chromatin associated complex repressed downstream ISGs. In contrast, in cells infected with lntA-expressing bacteria, LntA prevented BAHD1 recruitment to ISGs and stimulated their expression. Murine listeriosis decreased in BAHD1(+/-) mice or when lntA was constitutively expressed. Thus, the LntA-BAHD1 interplay may modulate IFN-lambda-mediated immune response to control bacterial colonization of the host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lebreton, Alice -- Lakisic, Goran -- Job, Viviana -- Fritsch, Lauriane -- Tham, To Nam -- Camejo, Ana -- Mattei, Pierre-Jean -- Regnault, Beatrice -- Nahori, Marie-Anne -- Cabanes, Didier -- Gautreau, Alexis -- Ait-Si-Ali, Slimane -- Dessen, Andrea -- Cossart, Pascale -- Bierne, Helene -- 233348/European Research Council/International -- New York, N.Y. -- Science. 2011 Mar 11;331(6022):1319-21. doi: 10.1126/science.1200120. Epub 2011 Jan 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Pasteur, Unite des Interactions Bacteries Cellules, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21252314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Chromatin/*metabolism ; Chromosomal Proteins, Non-Histone/*metabolism ; Down-Regulation ; Gene Expression Profiling ; Gene Expression Regulation ; Host-Pathogen Interactions ; Humans ; Interferons/genetics/immunology/*metabolism ; Interleukins/genetics/immunology/*metabolism ; Listeria monocytogenes/genetics/metabolism/*pathogenicity ; Listeriosis/*immunology/microbiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Molecular Sequence Data ; Signal Transduction ; Virulence Factors/chemistry/genetics/*metabolism
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  • 49
    Publication Date: 2011-09-03
    Description: Recent studies suggest that unidentified prokaryotes fix inorganic carbon at globally significant rates in the immense dark ocean. Using single-cell sorting and whole-genome amplification of prokaryotes from two subtropical gyres, we obtained genomic DNA from 738 cells representing most cosmopolitan lineages. Multiple cells of Deltaproteobacteria cluster SAR324, Gammaproteobacteria clusters ARCTIC96BD-19 and Agg47, and some Oceanospirillales from the lower mesopelagic contained ribulose-1,5-bisphosphate carboxylase-oxygenase and sulfur oxidation genes. These results corroborated community DNA and RNA profiling from diverse geographic regions. The SAR324 genomes also suggested C(1) metabolism and a particle-associated life-style. Microautoradiography and fluorescence in situ hybridization confirmed bicarbonate uptake and particle association of SAR324 cells. Our study suggests potential chemolithoautotrophy in several uncultured Proteobacteria lineages that are ubiquitous in the dark oxygenated ocean and provides new perspective on carbon cycling in the ocean's largest habitat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swan, Brandon K -- Martinez-Garcia, Manuel -- Preston, Christina M -- Sczyrba, Alexander -- Woyke, Tanja -- Lamy, Dominique -- Reinthaler, Thomas -- Poulton, Nicole J -- Masland, E Dashiell P -- Gomez, Monica Lluesma -- Sieracki, Michael E -- DeLong, Edward F -- Herndl, Gerhard J -- Stepanauskas, Ramunas -- New York, N.Y. -- Science. 2011 Sep 2;333(6047):1296-300. doi: 10.1126/science.1203690.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bigelow Laboratory for Ocean Sciences, 180 McKown Point Road, Post Office Box 475, West Boothbay Harbor, ME 04575, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21885783" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/genetics/metabolism ; Carbon Cycle ; Carbon Dioxide/metabolism ; *Chemoautotrophic Growth ; Darkness ; Deltaproteobacteria/classification/genetics/growth & development/*metabolism ; Gammaproteobacteria/classification/genetics/growth & development/*metabolism ; Genes, Bacterial ; Genome, Bacterial ; Metagenome ; Molecular Sequence Data ; Oceans and Seas ; Oxidation-Reduction ; Phylogeny ; Ribulose-Bisphosphate Carboxylase/genetics ; Seawater/*microbiology ; Sulfur/metabolism ; Sulfur Compounds/metabolism
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  • 50
    Publication Date: 2011-04-09
    Description: Maternally inherited bacterial symbionts of arthropods are common, yet symbiont invasions of host populations have rarely been observed. Here, we show that Rickettsia sp. nr. bellii swept into a population of an invasive agricultural pest, the sweet potato whitefly, Bemisia tabaci, in just 6 years. Compared with uninfected whiteflies, Rickettsia-infected whiteflies produced more offspring, had higher survival to adulthood, developed faster, and produced a higher proportion of daughters. The symbiont thus functions as both mutualist and reproductive manipulator. The observed increased performance and sex-ratio bias of infected whiteflies are sufficient to explain the spread of Rickettsia across the southwestern United States. Symbiont invasions such as this represent a sudden evolutionary shift for the host, with potentially large impacts on its ecology and invasiveness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Himler, Anna G -- Adachi-Hagimori, Tetsuya -- Bergen, Jacqueline E -- Kozuch, Amaranta -- Kelly, Suzanne E -- Tabashnik, Bruce E -- Chiel, Elad -- Duckworth, Victoria E -- Dennehy, Timothy J -- Zchori-Fein, Einat -- Hunter, Martha S -- 1K 12 GM00708/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Apr 8;332(6026):254-6. doi: 10.1126/science.1199410.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Insect Science, The University of Arizona, Post Office Box 210106, Tucson, AZ 85721-0106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21474763" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Female ; *Genetic Fitness ; Hemiptera/genetics/*microbiology/*physiology ; Male ; Molecular Sequence Data ; Reproduction ; Rickettsia/genetics/*physiology ; Sex Ratio ; Southwestern United States ; *Symbiosis
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  • 51
    Publication Date: 2011-02-05
    Description: Bacterial type III protein secretion systems deliver effector proteins into eukaryotic cells in order to modulate cellular processes. Central to the function of these protein-delivery machines is their ability to recognize and secrete substrates in a defined order. Here, we describe a mechanism by which a type III secretion system from the bacterial enteropathogen Salmonella enterica serovar Typhimurium can sort its substrates before secretion. This mechanism involves a cytoplasmic sorting platform that is sequentially loaded with the appropriate secreted proteins. The sequential loading of this platform, facilitated by customized chaperones, ensures the hierarchy in type III protein secretion. Given the presence of these machines in many important pathogens, these findings can serve as the bases for the development of novel antimicrobial strategies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859126/" 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/PMC3859126/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lara-Tejero, Maria -- Kato, Junya -- Wagner, Samuel -- Liu, Xiaoyun -- Galan, Jorge E -- AI30492/AI/NIAID NIH HHS/ -- R01 AI030492/AI/NIAID NIH HHS/ -- U54 AI0157158/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2011 Mar 4;331(6021):1188-91. doi: 10.1126/science.1201476. Epub 2011 Feb 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21292939" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Bacterial/chemistry/metabolism ; Bacterial Proteins/chemistry/*metabolism ; Bacterial Secretion Systems/*physiology ; Cytoplasm/metabolism ; Membrane Proteins/chemistry/*metabolism ; Molecular Chaperones/chemistry/*metabolism ; Molecular Sequence Data ; Multiprotein Complexes/metabolism ; Mutation ; Protein Binding ; Protein Transport ; Salmonella typhimurium/genetics/*metabolism/*pathogenicity
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  • 52
    Publication Date: 2011-06-28
    Description: Free-living cells of the social amoebae Dictyostelium discoideum can aggregate and develop into multicellular fruiting bodies in which many die altruistically as they become stalk cells that support the surviving spores. Dictyostelium cells exhibit kin discrimination--a potential defense against cheaters, which sporulate without contributing to the stalk. Kin discrimination depends on strain relatedness, and the polymorphic genes tgrB1 and tgrC1 are potential components of that mechanism. Here, we demonstrate a direct role for these genes in kin discrimination. We show that a matching pair of tgrB1 and tgrC1 alleles is necessary and sufficient for attractive self-recognition, which is mediated by differential cell-cell adhesion. We propose that TgrB1 and TgrC1 proteins mediate this adhesion through direct binding. This system is a genetically tractable ancient model of eukaryotic self-recognition.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3142563/" 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/PMC3142563/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirose, Shigenori -- Benabentos, Rocio -- Ho, Hsing-I -- Kuspa, Adam -- Shaulsky, Gad -- F31 GM086131/GM/NIGMS NIH HHS/ -- R01 GM084992/GM/NIGMS NIH HHS/ -- R01 GM084992-03/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Jul 22;333(6041):467-70. doi: 10.1126/science.1203903. Epub 2011 Jun 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21700835" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; *Cell Adhesion ; Cell Aggregation ; Dictyostelium/*genetics/*physiology ; Gene Deletion ; *Genes, Protozoan ; Molecular Sequence Data ; Protein Binding ; Protozoan Proteins/*metabolism ; Spores, Protozoan/physiology
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  • 53
    Publication Date: 2011-07-02
    Description: Viruses may very well be the most abundant biological entities on the planet. Yet neither metagenomic studies nor classical phage isolation techniques have shed much light on the identity of the hosts of most viruses. We used a microfluidic digital polymerase chain reaction (PCR) approach to physically link single bacterial cells harvested from a natural environment with a viral marker gene. When we implemented this technique on the microbial community residing in the termite hindgut, we found genus-wide infection patterns displaying remarkable intragenus selectivity. Viral marker allelic diversity revealed restricted mixing of alleles between hosts, indicating limited lateral gene transfer of these alleles despite host proximity. Our approach does not require culturing hosts or viruses and provides a method for examining virus-bacterium interactions in many environments.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3261838/" 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/PMC3261838/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tadmor, Arbel D -- Ottesen, Elizabeth A -- Leadbetter, Jared R -- Phillips, Rob -- DP1 OD000217/OD/NIH HHS/ -- DP1 OD000217-05/OD/NIH HHS/ -- R01 GM085286/GM/NIGMS NIH HHS/ -- R01 GM085286-01S/GM/NIGMS NIH HHS/ -- R01 GM098465/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Jul 1;333(6038):58-62. doi: 10.1126/science.1200758.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, California Institute of Technology, Pasadena, CA 91125, USA. arbel@caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21719670" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Bacteriophages/classification/genetics/*physiology ; Ecosystem ; Endodeoxyribonucleases/genetics ; Genes, Viral ; Genes, rRNA ; Genetic Variation ; Intestines/microbiology ; Isoptera/*microbiology ; *Microbial Interactions ; *Microfluidic Analytical Techniques ; Molecular Sequence Data ; Phylogeny ; Polymerase Chain Reaction/*methods ; Prophages/genetics ; Sequence Alignment ; Treponema/classification/genetics/*virology
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  • 54
    Publication Date: 2011-07-09
    Description: Current flu vaccines provide only limited coverage against seasonal strains of influenza viruses. The identification of V(H)1-69 antibodies that broadly neutralize almost all influenza A group 1 viruses constituted a breakthrough in the influenza field. Here, we report the isolation and characterization of a human monoclonal antibody CR8020 with broad neutralizing activity against most group 2 viruses, including H3N2 and H7N7, which cause severe human infection. The crystal structure of Fab CR8020 with the 1968 pandemic H3 hemagglutinin (HA) reveals a highly conserved epitope in the HA stalk distinct from the epitope recognized by the V(H)1-69 group 1 antibodies. Thus, a cocktail of two antibodies may be sufficient to neutralize most influenza A subtypes and, hence, enable development of a universal flu vaccine and broad-spectrum antibody therapies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3210727/" 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/PMC3210727/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ekiert, Damian C -- Friesen, Robert H E -- Bhabha, Gira -- Kwaks, Ted -- Jongeneelen, Mandy -- Yu, Wenli -- Ophorst, Carla -- Cox, Freek -- Korse, Hans J W M -- Brandenburg, Boerries -- Vogels, Ronald -- Brakenhoff, Just P J -- Kompier, Ronald -- Koldijk, Martin H -- Cornelissen, Lisette A H M -- Poon, Leo L M -- Peiris, Malik -- Koudstaal, Wouter -- Wilson, Ian A -- Goudsmit, Jaap -- GM080209/GM/NIGMS NIH HHS/ -- HHSN272200900060C/PHS HHS/ -- T32 GM080209/GM/NIGMS NIH HHS/ -- T32 GM080209-03/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):843-50. doi: 10.1126/science.1204839. Epub 2011 Jul 7.〈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.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21737702" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology/isolation & purification ; Antibodies, Neutralizing/*immunology/isolation & purification ; Antibodies, Viral/*immunology/isolation & purification ; Antibody Specificity ; Antigens, Viral/chemistry/genetics/*immunology ; Binding Sites, Antibody ; Conserved Sequence ; Crystallography, X-Ray ; Epitopes/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/genetics/*immunology ; Humans ; Influenza A Virus, H3N2 Subtype/immunology ; Influenza A Virus, H7N7 Subtype/genetics/immunology ; Influenza A virus/*immunology ; Influenza Vaccines/immunology ; Influenza, Human/immunology/prevention & control/therapy ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neutralization Tests ; Orthomyxoviridae Infections/immunology/prevention & control ; Protein Conformation
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  • 55
    Publication Date: 2011-10-25
    Description: Modern survivors of previously more diverse lineages are regarded as living fossils, particularly when characterized by morphological stasis. Cycads are often cited as a classic example, reaching their greatest diversity during the Jurassic-Cretaceous (199.6 to 65.5 million years ago) then dwindling to their present diversity of ~300 species as flowering plants rose to dominance. Using fossil-calibrated molecular phylogenies, we show that cycads underwent a near synchronous global rediversification beginning in the late Miocene, followed by a slowdown toward the Recent. Although the cycad lineage is ancient, our timetrees indicate that living cycad species are not much older than ~12 million years. These data reject the hypothesized role of dinosaurs in generating extant diversity and the designation of today's cycad species as living fossils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nagalingum, N S -- Marshall, C R -- Quental, T B -- Rai, H S -- Little, D P -- Mathews, S -- New York, N.Y. -- Science. 2011 Nov 11;334(6057):796-9. doi: 10.1126/science.1209926. Epub 2011 Oct 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arnold Arboretum of Harvard University, 22 Divinity Avenue, Cambridge, MA 02138, USA. nathalie.nagalingum@rbgsyd.nsw.gov.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22021670" target="_blank"〉PubMed〈/a〉
    Keywords: Bayes Theorem ; *Biological Evolution ; Climate Change ; *Cycadophyta/anatomy & histology/classification/genetics ; Extinction, Biological ; *Fossils ; Genes, Plant ; *Genetic Speciation ; Molecular Sequence Data ; Phylogeny
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  • 56
    Publication Date: 2011-09-17
    Description: Transcription by eukaryotic RNA polymerases (Pols) II and III and archaeal Pol requires structurally related general transcription factors TFIIB, Brf1, and TFB, respectively, which are essential for polymerase recruitment and initiation events. A TFIIB-like protein was not evident in the Pol I basal transcription machinery. We report that TAF1B, a subunit of human Pol I basal transcription factor SL1, is structurally related to TFIIB/TFIIB-like proteins, through predicted amino-terminal zinc ribbon and cyclin-like fold domains. SL1, essential for Pol I recruitment to the ribosomal RNA gene promoter, also has an essential postpolymerase recruitment role, operating through TAF1B. Therefore, a TFIIB-related protein is implicated in preinitiation complex assembly and postpolymerase recruitment events in Pol I transcription, underscoring the parallels between eukaryotic Pol I, II, and III and archaeal transcription machineries.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3566551/" 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/PMC3566551/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naidu, Srivatsava -- Friedrich, J Karsten -- Russell, Jackie -- Zomerdijk, Joost C B M -- 085441/Wellcome Trust/United Kingdom -- 085441/Z/08/Z/Wellcome Trust/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1640-2. doi: 10.1126/science.1207656.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21921199" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA, Ribosomal ; Humans ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Mutation ; Pol1 Transcription Initiation Complex Proteins/*chemistry/genetics/*metabolism ; Promoter Regions, Genetic ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; RNA Polymerase I/*metabolism ; Transcription Factor TFIIB/*chemistry/metabolism ; *Transcription, Genetic
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  • 57
    Publication Date: 2011-11-05
    Description: The RNA polymerase II (RNAP II) largest subunit contains a C-terminal domain (CTD) with up to 52 Tyr(1)-Ser(2)-Pro(3)-Thr(4)-Ser(5)-Pro(6)-Ser(7) consensus repeats. Serines 2, 5, and 7 are known to be phosphorylated, and these modifications help to orchestrate the interplay between transcription and processing of messenger RNA (mRNA) precursors. Here, we provide evidence that phosphorylation of CTD Thr(4) residues is required specifically for histone mRNA 3' end processing, functioning to facilitate recruitment of 3' processing factors to histone genes. Like Ser(2), Thr(4) phosphorylation requires the CTD kinase CDK9 and is evolutionarily conserved from yeast to human. Our data thus illustrate how a CTD modification can play a highly specific role in facilitating efficient gene expression.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3678764/" 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/PMC3678764/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsin, Jing-Ping -- Sheth, Amit -- Manley, James L -- R01 GM028983/GM/NIGMS NIH HHS/ -- R01 GM28983/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Nov 4;334(6056):683-6. doi: 10.1126/science.1206034.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22053051" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Survival ; Chickens ; Cleavage And Polyadenylation Specificity Factor/metabolism ; Cyclin-Dependent Kinase 9/metabolism ; Histones/*genetics ; Humans ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; *RNA 3' End Processing ; RNA Polymerase II/chemistry/*metabolism ; RNA, Messenger/*metabolism ; Threonine/*metabolism ; mRNA Cleavage and Polyadenylation Factors/metabolism
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  • 58
    Publication Date: 2011-07-23
    Description: Mimicry--whereby warning signals in different species evolve to look similar--has long served as a paradigm of convergent evolution. Little is known, however, about the genes that underlie the evolution of mimetic phenotypes or to what extent the same or different genes drive such convergence. Here, we characterize one of the major genes responsible for mimetic wing pattern evolution in Heliconius butterflies. Mapping, gene expression, and population genetic work all identify a single gene, optix, that controls extreme red wing pattern variation across multiple species of Heliconius. Our results show that the cis-regulatory evolution of a single transcription factor can repeatedly drive the convergent evolution of complex color patterns in distantly related species, thus blurring the distinction between convergence and homology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reed, Robert D -- Papa, Riccardo -- Martin, Arnaud -- Hines, Heather M -- Counterman, Brian A -- Pardo-Diaz, Carolina -- Jiggins, Chris D -- Chamberlain, Nicola L -- Kronforst, Marcus R -- Chen, Rui -- Halder, Georg -- Nijhout, H Frederik -- McMillan, W Owen -- New York, N.Y. -- Science. 2011 Aug 26;333(6046):1137-41. doi: 10.1126/science.1208227. Epub 2011 Jul 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of California, Irvine, CA 92697, USA. rreed@uci.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21778360" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; Butterflies/anatomy & histology/*genetics/growth & development ; Evolution, Molecular ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; *Genes, Insect ; Genetic Variation ; Genome, Insect ; Homeodomain Proteins/*genetics ; Insect Proteins/*genetics ; Linkage Disequilibrium ; Molecular Sequence Data ; Moths/genetics ; Phenotype ; Pigmentation/*genetics ; Regulatory Elements, Transcriptional ; Selection, Genetic ; Species Specificity ; Transcription Factors/genetics ; Transcription, Genetic ; Wings, Animal/*anatomy & histology/growth & development
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  • 59
    Publication Date: 2011-11-26
    Description: Different types of cell behavior, including growth, motility, and navigation, require actin proteins to assemble into filaments. Here, we describe a biochemical process that was able to disassemble actin filaments and limit their reassembly. Actin was a specific substrate of the multidomain oxidation-reduction enzyme, Mical, a poorly understood actin disassembly factor that directly responds to Semaphorin/Plexin extracellular repulsive cues. Actin filament subunits were directly modified by Mical on their conserved pointed-end, which is critical for filament assembly. Mical posttranslationally oxidized the methionine 44 residue within the D-loop of actin, simultaneously severing filaments and decreasing polymerization. This mechanism underlying actin cytoskeletal collapse may have broad physiological and pathological ramifications.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612955/" 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/PMC3612955/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hung, Ruei-Jiun -- Pak, Chi W -- Terman, Jonathan R -- DK 091074/DK/NIDDK NIH HHS/ -- F32 DK091074/DK/NIDDK NIH HHS/ -- NS073968/NS/NINDS NIH HHS/ -- R01 NS073968/NS/NINDS NIH HHS/ -- R01 NS073968-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2011 Dec 23;334(6063):1710-3. doi: 10.1126/science.1211956. Epub 2011 Nov 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Neuroscience and Pharmacology and Neuroscience Graduate Program, The University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22116028" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry/*metabolism ; Actins/chemistry/genetics/*metabolism ; Amino Acid Sequence ; Animals ; Cell Adhesion Molecules/metabolism ; DNA-Binding Proteins/*metabolism ; Drosophila ; Drosophila Proteins/chemistry/genetics/*metabolism ; Methionine/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; NADP/metabolism ; Nerve Tissue Proteins/metabolism ; Oxidation-Reduction ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Rabbits ; Semaphorins/metabolism ; Substrate Specificity
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  • 60
    Publication Date: 2011-08-27
    Description: Whole genome comparisons identified introgression from archaic to modern humans. Our analysis of highly polymorphic human leukocyte antigen (HLA) class I, vital immune system components subject to strong balancing selection, shows how modern humans acquired the HLA-B*73 allele in west Asia through admixture with archaic humans called Denisovans, a likely sister group to the Neandertals. Virtual genotyping of Denisovan and Neandertal genomes identified archaic HLA haplotypes carrying functionally distinctive alleles that have introgressed into modern Eurasian and Oceanian populations. These alleles, of which several encode unique or strong ligands for natural killer cell receptors, now represent more than half the HLA alleles of modern Eurasians and also appear to have been later introduced into Africans. Thus, adaptive introgression of archaic alleles has significantly shaped modern human immune systems.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677943/" 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/PMC3677943/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abi-Rached, Laurent -- Jobin, Matthew J -- Kulkarni, Subhash -- McWhinnie, Alasdair -- Dalva, Klara -- Gragert, Loren -- Babrzadeh, Farbod -- Gharizadeh, Baback -- Luo, Ma -- Plummer, Francis A -- Kimani, Joshua -- Carrington, Mary -- Middleton, Derek -- Rajalingam, Raja -- Beksac, Meral -- Marsh, Steven G E -- Maiers, Martin -- Guethlein, Lisbeth A -- Tavoularis, Sofia -- Little, Ann-Margaret -- Green, Richard E -- Norman, Paul J -- Parham, Peter -- AI031168/AI/NIAID NIH HHS/ -- HHSN261200800001E/PHS HHS/ -- R01 AI031168/AI/NIAID NIH HHS/ -- RR000165/RR/NCRR NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Oct 7;334(6052):89-94. doi: 10.1126/science.1209202. Epub 2011 Aug 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21868630" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; African Continental Ancestry Group/genetics ; Alleles ; Animals ; Asian Continental Ancestry Group/genetics ; Continental Population Groups/*genetics ; European Continental Ancestry Group/genetics ; Evolution, Molecular ; *Genes, MHC Class I ; Genetic Variation ; HLA-A Antigens/*genetics/immunology/metabolism ; HLA-B Antigens/*genetics/immunology/metabolism ; HLA-C Antigens/*genetics/immunology ; Haplotypes ; Hominidae/*genetics/*immunology ; Humans ; *Hybridization, Genetic ; Killer Cells, Natural/immunology ; Ligands ; Linkage Disequilibrium ; Molecular Sequence Data ; Oceanic Ancestry Group/genetics ; Receptors, KIR/immunology/metabolism ; Selection, Genetic
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  • 61
    Publication Date: 2011-07-19
    Description: Fanconi anemia is a cancer predisposition syndrome caused by defects in the repair of DNA interstrand cross-links (ICLs). Central to this pathway is the Fanconi anemia I-Fanconi anemia D2 (FANCI-FANCD2) (ID) complex, which is activated by DNA damage-induced phosphorylation and monoubiquitination. The 3.4 angstrom crystal structure of the ~300 kilodalton ID complex reveals that monoubiquitination and regulatory phosphorylation sites map to the I-D interface, suggesting that they occur on monomeric proteins or an opened-up complex and that they may serve to stabilize I-D heterodimerization. The 7.8 angstrom electron-density map of FANCI-DNA crystals and in vitro data show that each protein has binding sites for both single- and double-stranded DNA, suggesting that the ID complex recognizes DNA structures that result from the encounter of replication forks with an ICL.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3310437/" 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/PMC3310437/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joo, Woo -- Xu, Guozhou -- Persky, Nicole S -- Smogorzewska, Agata -- Rudge, Derek G -- Buzovetsky, Olga -- Elledge, Stephen J -- Pavletich, Nikola P -- R01 GM044664/GM/NIGMS NIH HHS/ -- R01 GM044664-10/GM/NIGMS NIH HHS/ -- R37 GM044664/GM/NIGMS NIH HHS/ -- T32 CA009216/CA/NCI NIH HHS/ -- T32 CA009216-32/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Jul 15;333(6040):312-6. doi: 10.1126/science.1205805.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21764741" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; *DNA Repair ; DNA, Single-Stranded/chemistry/metabolism ; Fanconi Anemia/genetics ; Fanconi Anemia Complementation Group D2 Protein/*chemistry/metabolism ; Fanconi Anemia Complementation Group Proteins/*chemistry/metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Static Electricity ; Ubiquitin/chemistry ; Ubiquitination
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  • 62
    Publication Date: 2011-07-30
    Description: The ocean is an important global source of nitrous oxide (N(2)O), a greenhouse gas that contributes to stratospheric ozone destruction. Bacterial nitrification and denitrification are thought to be the primary sources of marine N(2)O, but the isotopic signatures of N(2)O produced by these processes are not consistent with the marine contribution to the global N(2)O budget. Based on enrichment cultures, we report that archaeal ammonia oxidation also produces N(2)O. Natural-abundance stable isotope measurements indicate that the produced N(2)O had bulk delta(15)N and delta(18)O values higher than observed for ammonia-oxidizing bacteria but similar to the delta(15)N and delta(18)O values attributed to the oceanic N(2)O source to the atmosphere. Our results suggest that ammonia-oxidizing archaea may be largely responsible for the oceanic N(2)O source.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santoro, Alyson E -- Buchwald, Carolyn -- McIlvin, Matthew R -- Casciotti, Karen L -- New York, N.Y. -- Science. 2011 Sep 2;333(6047):1282-5. doi: 10.1126/science.1208239. Epub 2011 Jul 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Marine Chemistry and Geochemistry, Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA. asantoro@umces.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21798895" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonia/*metabolism ; Archaea/enzymology/*metabolism ; Bacteria/metabolism ; Culture Media ; Denitrification ; Linear Models ; Molecular Sequence Data ; Nitrification ; Nitrogen Isotopes ; Nitrous Oxide/*metabolism ; Oxidation-Reduction ; Oxygen Isotopes ; Pacific Ocean ; Seawater/*microbiology
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-04-02
    Description: Bacteria and their viruses (phages) undergo rapid coevolution in test tubes, but the relevance to natural environments is unclear. By using a "mark-recapture" approach, we showed rapid coevolution of bacteria and phages in a soil community. Unlike coevolution in vitro, which is characterized by increases in infectivity and resistance through time (arms race dynamics), coevolution in soil resulted in hosts more resistant to their contemporary than past and future parasites (fluctuating selection dynamics). Fluctuating selection dynamics, which can potentially continue indefinitely, can be explained by fitness costs constraining the evolution of high levels of resistance in soil. These results suggest that rapid coevolution between bacteria and phage is likely to play a key role in structuring natural microbial communities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gomez, Pedro -- Buckling, Angus -- New York, N.Y. -- Science. 2011 Apr 1;332(6025):106-9. doi: 10.1126/science.1198767.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, Oxford OX1 3PS, UK. pedro.gomezlopez@zoo.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21454789" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Biological Evolution ; Molecular Sequence Data ; Pseudomonas Phages/*physiology ; Pseudomonas fluorescens/physiology/*virology ; *Soil Microbiology
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  • 64
    Publication Date: 2011-07-30
    Description: The isolation of broadly neutralizing antibodies against influenza A viruses has been a long-sought goal for therapeutic approaches and vaccine design. Using a single-cell culture method for screening large numbers of human plasma cells, we isolated a neutralizing monoclonal antibody that recognized the hemagglutinin (HA) glycoprotein of all 16 subtypes and neutralized both group 1 and group 2 influenza A viruses. Passive transfer of this antibody conferred protection to mice and ferrets. Complexes with HAs from the group 1 H1 and the group 2 H3 subtypes analyzed by x-ray crystallography showed that the antibody bound to a conserved epitope in the F subdomain. This antibody may be used for passive protection and to inform vaccine design because of its broad specificity and neutralization potency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corti, Davide -- Voss, Jarrod -- Gamblin, Steven J -- Codoni, Giosiana -- Macagno, Annalisa -- Jarrossay, David -- Vachieri, Sebastien G -- Pinna, Debora -- Minola, Andrea -- Vanzetta, Fabrizia -- Silacci, Chiara -- Fernandez-Rodriguez, Blanca M -- Agatic, Gloria -- Bianchi, Siro -- Giacchetto-Sasselli, Isabella -- Calder, Lesley -- Sallusto, Federica -- Collins, Patrick -- Haire, Lesley F -- Temperton, Nigel -- Langedijk, Johannes P M -- Skehel, John J -- Lanzavecchia, Antonio -- G0600369/Medical Research Council/United Kingdom -- MC_U117584222/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2011 Aug 12;333(6044):850-6. doi: 10.1126/science.1205669. Epub 2011 Jul 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Research in Biomedicine, 6500 Bellinzona, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21798894" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Neutralizing/*immunology/isolation & purification ; Antibodies, Viral/*immunology/isolation & purification ; Antibody Specificity ; Antigens, Viral/*immunology ; Cells, Cultured ; Cross Reactions ; Crystallography, X-Ray ; Epitopes/immunology ; Ferrets ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus/*immunology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Immunization, Passive ; Immunoglobulin Variable Region/immunology ; Influenza A Virus, H1N1 Subtype/immunology ; Influenza A virus/*immunology ; Influenza B virus/immunology ; Influenza, Human/immunology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Orthomyxoviridae Infections/immunology/prevention & control/therapy ; Plasma Cells/immunology ; Protein Multimerization ; Protein Structure, Secondary
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  • 65
    Publication Date: 2011-02-05
    Description: We describe the draft genome of the microcrustacean Daphnia pulex, which is only 200 megabases and contains at least 30,907 genes. The high gene count is a consequence of an elevated rate of gene duplication resulting in tandem gene clusters. More than a third of Daphnia's genes have no detectable homologs in any other available proteome, and the most amplified gene families are specific to the Daphnia lineage. The coexpansion of gene families interacting within metabolic pathways suggests that the maintenance of duplicated genes is not random, and the analysis of gene expression under different environmental conditions reveals that numerous paralogs acquire divergent expression patterns soon after duplication. Daphnia-specific genes, including many additional loci within sequenced regions that are otherwise devoid of annotations, are the most responsive genes to ecological challenges.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3529199/" 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/PMC3529199/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colbourne, John K -- Pfrender, Michael E -- Gilbert, Donald -- Thomas, W Kelley -- Tucker, Abraham -- Oakley, Todd H -- Tokishita, Shinichi -- Aerts, Andrea -- Arnold, Georg J -- Basu, Malay Kumar -- Bauer, Darren J -- Caceres, Carla E -- Carmel, Liran -- Casola, Claudio -- Choi, Jeong-Hyeon -- Detter, John C -- Dong, Qunfeng -- Dusheyko, Serge -- Eads, Brian D -- Frohlich, Thomas -- Geiler-Samerotte, Kerry A -- Gerlach, Daniel -- Hatcher, Phil -- Jogdeo, Sanjuro -- Krijgsveld, Jeroen -- Kriventseva, Evgenia V -- Kultz, Dietmar -- Laforsch, Christian -- Lindquist, Erika -- Lopez, Jacqueline -- Manak, J Robert -- Muller, Jean -- Pangilinan, Jasmyn -- Patwardhan, Rupali P -- Pitluck, Samuel -- Pritham, Ellen J -- Rechtsteiner, Andreas -- Rho, Mina -- Rogozin, Igor B -- Sakarya, Onur -- Salamov, Asaf -- Schaack, Sarah -- Shapiro, Harris -- Shiga, Yasuhiro -- Skalitzky, Courtney -- Smith, Zachary -- Souvorov, Alexander -- Sung, Way -- Tang, Zuojian -- Tsuchiya, Dai -- Tu, Hank -- Vos, Harmjan -- Wang, Mei -- Wolf, Yuri I -- Yamagata, Hideo -- Yamada, Takuji -- Ye, Yuzhen -- Shaw, Joseph R -- Andrews, Justen -- Crease, Teresa J -- Tang, Haixu -- Lucas, Susan M -- Robertson, Hugh M -- Bork, Peer -- Koonin, Eugene V -- Zdobnov, Evgeny M -- Grigoriev, Igor V -- Lynch, Michael -- Boore, Jeffrey L -- P42 ES004699/ES/NIEHS NIH HHS/ -- P42 ES004699-25/ES/NIEHS NIH HHS/ -- P42ES004699/ES/NIEHS NIH HHS/ -- R01 ES019324/ES/NIEHS NIH HHS/ -- R24 GM078274/GM/NIGMS NIH HHS/ -- R24 GM078274-01A1/GM/NIGMS NIH HHS/ -- R24GM07827401/GM/NIGMS NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Feb 4;331(6017):555-61. doi: 10.1126/science.1197761.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Genomics and Bioinformatics, Indiana University, 915 East Third Street, Bloomington, IN 47405, USA. jcolbour@indiana.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21292972" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Daphnia/*genetics/physiology ; *Ecosystem ; Environment ; Evolution, Molecular ; Gene Conversion ; Gene Duplication ; Gene Expression ; Gene Expression Profiling ; Gene Expression Regulation ; Genes ; Genes, Duplicate ; *Genome ; Metabolic Networks and Pathways/genetics ; Molecular Sequence Annotation ; Molecular Sequence Data ; Multigene Family ; Phylogeny ; Sequence Analysis, DNA
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  • 66
    Publication Date: 2011-11-19
    Description: Many prokaryotic species generate hydrogen sulfide (H(2)S) in their natural environments. However, the biochemistry and physiological role of this gas in nonsulfur bacteria remain largely unknown. Here we demonstrate that inactivation of putative cystathionine beta-synthase, cystathionine gamma-lyase, or 3-mercaptopyruvate sulfurtransferase in Bacillus anthracis, Pseudomonas aeruginosa, Staphylococcus aureus, and Escherichia coli suppresses H(2)S production, rendering these pathogens highly sensitive to a multitude of antibiotics. Exogenous H(2)S suppresses this effect. Moreover, in bacteria that normally produce H(2)S and nitric oxide, these two gases act synergistically to sustain growth. The mechanism of gas-mediated antibiotic resistance relies on mitigation of oxidative stress imposed by antibiotics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shatalin, Konstantin -- Shatalina, Elena -- Mironov, Alexander -- Nudler, Evgeny -- New York, N.Y. -- Science. 2011 Nov 18;334(6058):986-90. doi: 10.1126/science.1209855.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, New York University School of Medicine, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22096201" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/*pharmacology ; Antioxidants/metabolism ; Bacillus anthracis/drug effects/growth & development/metabolism ; Bacteria/*drug effects/growth & development/*metabolism ; Cystathionine beta-Synthase/antagonists & inhibitors/genetics/metabolism ; Cystathionine gamma-Lyase/antagonists & inhibitors/genetics/metabolism ; DNA Breaks, Double-Stranded ; Drug Resistance, Bacterial ; *Drug Resistance, Multiple, Bacterial ; Escherichia coli/drug effects/growth & development/metabolism ; Hydrogen Sulfide/*metabolism/pharmacology ; Molecular Sequence Data ; Nitric Oxide/metabolism ; Oxidative Stress ; Pseudomonas aeruginosa/drug effects/growth & development/metabolism ; Staphylococcus aureus/drug effects/growth & development/metabolism ; Sulfurtransferases/antagonists & inhibitors/genetics/metabolism
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  • 67
    Publication Date: 2011-01-08
    Description: Methane was the most abundant hydrocarbon released during the 2010 Deepwater Horizon oil spill in the Gulf of Mexico. Beyond relevancy to this anthropogenic event, this methane release simulates a rapid and relatively short-term natural release from hydrates into deep water. Based on methane and oxygen distributions measured at 207 stations throughout the affected region, we find that within ~120 days from the onset of release ~3.0 x 10(10) to 3.9 x 10(10) moles of oxygen were respired, primarily by methanotrophs, and left behind a residual microbial community containing methanotrophic bacteria. We suggest that a vigorous deepwater bacterial bloom respired nearly all the released methane within this time, and that by analogy, large-scale releases of methane from hydrate in the deep ocean are likely to be met by a similarly rapid methanotrophic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kessler, John D -- Valentine, David L -- Redmond, Molly C -- Du, Mengran -- Chan, Eric W -- Mendes, Stephanie D -- Quiroz, Erik W -- Villanueva, Christie J -- Shusta, Stephani S -- Werra, Lindsay M -- Yvon-Lewis, Shari A -- Weber, Thomas C -- New York, N.Y. -- Science. 2011 Jan 21;331(6015):312-5. doi: 10.1126/science.1199697. Epub 2011 Jan 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oceanography, Texas A&M University, College Station, TX 77843-3146, USA. jkessler@ocean.tamu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21212320" target="_blank"〉PubMed〈/a〉
    Keywords: Atlantic Ocean ; Bacteria/classification/growth & development/*metabolism ; Biodegradation, Environmental ; *Environmental Pollution ; Hydrocarbons/analysis ; Methane/analysis/*metabolism ; Molecular Sequence Data ; Oxidation-Reduction ; Oxygen/*analysis ; Oxygen Consumption ; *Petroleum ; Phylogeny ; Seawater/chemistry/*microbiology
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  • 68
    Publication Date: 2011-02-19
    Description: The mechanistic basis of resistance of vertebrate populations to contaminants, including Atlantic tomcod from the Hudson River (HR) to polychlorinated biphenyls (PCBs), is unknown. HR tomcod exhibited variants in the aryl hydrocarbon receptor 2 (AHR2) that were nearly absent elsewhere. In ligand-binding assays, AHR2-1 protein (common in the HR) was impaired as compared to widespread AHR2-2 in binding TCDD (2,3,7,8-tetrachlorodibenzo-p-dioxin) and in driving expression in reporter gene assays in AHR-deficient cells treated with TCDD or PCB126. We identified a six-base deletion in AHR2 as the basis of resistance and suggest that the HR population has undergone rapid evolution, probably due to contaminant exposure. This mechanistic basis of resistance in a vertebrate population provides evidence of evolutionary change due to selective pressure at a single locus.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3246799/" 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/PMC3246799/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wirgin, Isaac -- Roy, Nirmal K -- Loftus, Matthew -- Chambers, R Christopher -- Franks, Diana G -- Hahn, Mark E -- ES00260/ES/NIEHS NIH HHS/ -- P30 ES000260/ES/NIEHS NIH HHS/ -- P30 ES000260-47S2/ES/NIEHS NIH HHS/ -- P42 ES007381/ES/NIEHS NIH HHS/ -- P42 ES007381-15S5/ES/NIEHS NIH HHS/ -- P42 ES010344/ES/NIEHS NIH HHS/ -- P42 ES010344-05S2/ES/NIEHS NIH HHS/ -- P42ES007381/ES/NIEHS NIH HHS/ -- R01 ES015447-03/ES/NIEHS NIH HHS/ -- R01ES015447/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2011 Mar 11;331(6022):1322-5. doi: 10.1126/science.1197296. Epub 2011 Feb 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Medicine, New York University School of Medicine,Tuxedo, NY 10987, USA. Isaac.wirgin@nyumc.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21330491" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line, Tumor ; DNA, Mitochondrial/genetics ; Drug Resistance ; Evolution, Molecular ; Gadiformes/*genetics/*metabolism ; Gene Expression ; Gene Frequency ; Genes, Reporter ; Haplotypes ; Ligands ; Mice ; Molecular Sequence Data ; New York ; Polychlorinated Biphenyls/metabolism/*toxicity ; Polymorphism, Genetic ; Polymorphism, Single Nucleotide ; Receptors, Aryl Hydrocarbon/chemistry/*genetics/*metabolism ; Rivers ; Selection, Genetic ; Sequence Deletion ; Tetrachlorodibenzodioxin/metabolism/*toxicity ; Water Pollutants, Chemical/metabolism/*toxicity
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  • 69
    Publication Date: 2011-09-24
    Description: Previous analyses of relations, divergence times, and diversification patterns among extant mammalian families have relied on supertree methods and local molecular clocks. We constructed a molecular supermatrix for mammalian families and analyzed these data with likelihood-based methods and relaxed molecular clocks. Phylogenetic analyses resulted in a robust phylogeny with better resolution than phylogenies from supertree methods. Relaxed clock analyses support the long-fuse model of diversification and highlight the importance of including multiple fossil calibrations that are spread across the tree. Molecular time trees and diversification analyses suggest important roles for the Cretaceous Terrestrial Revolution and Cretaceous-Paleogene (KPg) mass extinction in opening up ecospace that promoted interordinal and intraordinal diversification, respectively. By contrast, diversification analyses provide no support for the hypothesis concerning the delayed rise of present-day mammals during the Eocene Period.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meredith, Robert W -- Janecka, Jan E -- Gatesy, John -- Ryder, Oliver A -- Fisher, Colleen A -- Teeling, Emma C -- Goodbla, Alisha -- Eizirik, Eduardo -- Simao, Taiz L L -- Stadler, Tanja -- Rabosky, Daniel L -- Honeycutt, Rodney L -- Flynn, John J -- Ingram, Colleen M -- Steiner, Cynthia -- Williams, Tiffani L -- Robinson, Terence J -- Burk-Herrick, Angela -- Westerman, Michael -- Ayoub, Nadia A -- Springer, Mark S -- Murphy, William J -- New York, N.Y. -- Science. 2011 Oct 28;334(6055):521-4. doi: 10.1126/science.1211028. Epub 2011 Sep 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, Riverside, CA 92521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21940861" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Evolution, Molecular ; *Extinction, Biological ; *Fossils ; *Mammals/classification/genetics ; Molecular Sequence Data ; *Phylogeny
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  • 70
    Publication Date: 2011-11-05
    Description: Protein synthesis in all organisms is catalyzed by ribosomes. In comparison to their prokaryotic counterparts, eukaryotic ribosomes are considerably larger and are subject to more complex regulation. The large ribosomal subunit (60S) catalyzes peptide bond formation and contains the nascent polypeptide exit tunnel. We present the structure of the 60S ribosomal subunit from Tetrahymena thermophila in complex with eukaryotic initiation factor 6 (eIF6), cocrystallized with the antibiotic cycloheximide (a eukaryotic-specific inhibitor of protein synthesis), at a resolution of 3.5 angstroms. The structure illustrates the complex functional architecture of the eukaryotic 60S subunit, which comprises an intricate network of interactions between eukaryotic-specific ribosomal protein features and RNA expansion segments. It reveals the roles of eukaryotic ribosomal protein elements in the stabilization of the active site and the extent of eukaryotic-specific differences in other functional regions of the subunit. Furthermore, it elucidates the molecular basis of the interaction with eIF6 and provides a structural framework for further studies of ribosome-associated diseases and the role of the 60S subunit in the initiation of protein synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klinge, Sebastian -- Voigts-Hoffmann, Felix -- Leibundgut, Marc -- Arpagaus, Sofia -- Ban, Nenad -- New York, N.Y. -- Science. 2011 Nov 18;334(6058):941-8. doi: 10.1126/science.1211204. Epub 2011 Nov 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22052974" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-Bacterial Agents/metabolism ; Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Cycloheximide/metabolism ; Eukaryotic Initiation Factors/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Peptide Chain Initiation, Translational ; Protein Conformation ; Protein Structure, Secondary ; Protozoan Proteins/chemistry/metabolism ; RNA, Protozoan/chemistry/metabolism ; RNA, Ribosomal/chemistry/metabolism ; RNA, Ribosomal, 5.8S/chemistry/metabolism ; Ribosomal Proteins/*chemistry/metabolism ; Ribosome Subunits, Large, Eukaryotic/*chemistry/metabolism/ultrastructure ; Tetrahymena thermophila/*chemistry/metabolism
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  • 71
    Publication Date: 2011-10-15
    Description: Intestinal bacteria aid host health and limit bacterial pathogen colonization. However, the influence of bacteria on enteric viruses is largely unknown. We depleted the intestinal microbiota of mice with antibiotics before inoculation with poliovirus, an enteric virus. Antibiotic-treated mice were less susceptible to poliovirus disease and supported minimal viral replication in the intestine. Exposure to bacteria or their N-acetylglucosamine-containing surface polysaccharides, including lipopolysaccharide and peptidoglycan, enhanced poliovirus infectivity. We found that poliovirus binds lipopolysaccharide, and exposure of poliovirus to bacteria enhanced host cell association and infection. The pathogenesis of reovirus, an unrelated enteric virus, also was more severe in the presence of intestinal microbes. These results suggest that antibiotic-mediated microbiota depletion diminishes enteric virus infection and that enteric viruses exploit intestinal microbes for replication and transmission.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3222156/" 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/PMC3222156/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuss, Sharon K -- Best, Gavin T -- Etheredge, Chris A -- Pruijssers, Andrea J -- Frierson, Johnna M -- Hooper, Lora V -- Dermody, Terence S -- Pfeiffer, Julie K -- AI38296/AI/NIAID NIH HHS/ -- F32 NS071986/NS/NINDS NIH HHS/ -- P30 CA68485/CA/NCI NIH HHS/ -- P60 DK20593/DK/NIDDK NIH HHS/ -- R01 AI074668/AI/NIAID NIH HHS/ -- R01 AI074668-04/AI/NIAID NIH HHS/ -- R01 AI74668/AI/NIAID NIH HHS/ -- R01 DK070855/DK/NIDDK NIH HHS/ -- R01 DK070855-06/DK/NIDDK NIH HHS/ -- T32 AI007520/AI/NIAID NIH HHS/ -- T32 AI07611/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Oct 14;334(6053):249-52. doi: 10.1126/science.1211057.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21998395" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/pharmacology ; *Bacterial Physiological Phenomena ; Cells, Cultured ; Feces/microbiology/virology ; HeLa Cells ; Humans ; Intestines/*microbiology/virology ; Lipopolysaccharides/metabolism ; Mammalian orthoreovirus 3/*physiology ; *Metagenome ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Poliomyelitis/*virology ; Poliovirus/metabolism/pathogenicity/*physiology ; Reoviridae Infections/*virology ; *Virus Replication ; Virus Shedding
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  • 72
    Publication Date: 2011-09-24
    Description: Most flowering plants establish mutualistic associations with insect pollinators to facilitate sexual reproduction. However, the evolutionary processes that gave rise to these associations remain poorly understood. We reconstructed the times of divergence, diversification patterns, and interaction networks of a diverse group of specialized orchids and their bee pollinators. In contrast to a scenario of coevolution by race formation, we show that fragrance-producing orchids originated at least three times independently after their fragrance-collecting bee mutualists. Whereas orchid diversification has apparently tracked the diversification of orchids' bee pollinators, bees appear to have depended on the diverse chemical environment of neotropical forests. We corroborated this apparent asymmetrical dependency by simulating co-extinction cascades in real interaction networks that lacked reciprocal specialization. These results suggest that the diversification of insect-pollinated angiosperms may have been facilitated by the exploitation of preexisting sensory biases of insect pollinators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramirez, Santiago R -- Eltz, Thomas -- Fujiwara, Mikiko K -- Gerlach, Gunter -- Goldman-Huertas, Benjamin -- Tsutsui, Neil D -- Pierce, Naomi E -- New York, N.Y. -- Science. 2011 Sep 23;333(6050):1742-6. doi: 10.1126/science.1209175.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museum of Comparative Zoology, Harvard University, Cambridge, MA 02138, USA. sramirez@post.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21940893" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bees/anatomy & histology/classification/*genetics/*physiology ; *Biological Evolution ; Ecosystem ; Extinction, Biological ; Female ; Flowers/*anatomy & histology ; Fossils ; Genetic Speciation ; Male ; Molecular Sequence Data ; Odors ; Orchidaceae/anatomy & histology/classification/*genetics/*physiology ; Phylogeny ; *Pollination ; Selection, Genetic ; *Symbiosis
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  • 73
    Publication Date: 2011-05-10
    Description: Whole-genome shotgun sequence data from three individual cells isolated from seawater, followed by analysis of ribosomal DNA, indicated that the cells represented three divergent clades of picobiliphytes. In contrast with the recent description of this phylum, we found no evidence of plastid DNA nor of nuclear-encoded plastid-targeted proteins, which suggests that these picobiliphytes are heterotrophs. Genome data from one cell were dominated by sequences from a widespread single-stranded DNA virus. This virus was absent from the other two cells, both of which contained non-eukaryote DNA derived from marine Bacteroidetes and large DNA viruses. By using shotgun sequencing of uncultured marine picobiliphytes, we revealed the distinct interactions of individual cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoon, Hwan Su -- Price, Dana C -- Stepanauskas, Ramunas -- Rajah, Veeran D -- Sieracki, Michael E -- Wilson, William H -- Yang, Eun Chan -- Duffy, Siobain -- Bhattacharya, Debashish -- New York, N.Y. -- Science. 2011 May 6;332(6030):714-7. doi: 10.1126/science.1203163.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bigelow Laboratory for Ocean Sciences, West Boothbay Harbor, ME 04575, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21551060" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquatic Organisms/classification/*genetics/*physiology/virology ; Bacteria/classification/genetics/isolation & purification ; Cell Communication ; Cell Separation ; DNA Viruses/classification/genetics/isolation & purification ; DNA, Bacterial/analysis/genetics ; DNA, Ribosomal/genetics ; DNA, Single-Stranded ; DNA, Viral/analysis/genetics ; Eukaryota/classification/*genetics/*physiology/virology ; *Genome ; Heterotrophic Processes ; Likelihood Functions ; Molecular Sequence Data ; Phylogeny ; Plankton/classification/genetics/physiology/virology ; Plastids/genetics/metabolism ; Proteins/chemistry/genetics ; *Seawater ; Single-Cell Analysis
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  • 74
    Publication Date: 2011-01-29
    Description: The paucity of enzymes that efficiently deconstruct plant polysaccharides represents a major bottleneck for industrial-scale conversion of cellulosic biomass into biofuels. Cow rumen microbes specialize in degradation of cellulosic plant material, but most members of this complex community resist cultivation. To characterize biomass-degrading genes and genomes, we sequenced and analyzed 268 gigabases of metagenomic DNA from microbes adherent to plant fiber incubated in cow rumen. From these data, we identified 27,755 putative carbohydrate-active genes and expressed 90 candidate proteins, of which 57% were enzymatically active against cellulosic substrates. We also assembled 15 uncultured microbial genomes, which were validated by complementary methods including single-cell genome sequencing. These data sets provide a substantially expanded catalog of genes and genomes participating in the deconstruction of cellulosic biomass.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hess, Matthias -- Sczyrba, Alexander -- Egan, Rob -- Kim, Tae-Wan -- Chokhawala, Harshal -- Schroth, Gary -- Luo, Shujun -- Clark, Douglas S -- Chen, Feng -- Zhang, Tao -- Mackie, Roderick I -- Pennacchio, Len A -- Tringe, Susannah G -- Visel, Axel -- Woyke, Tanja -- Wang, Zhong -- Rubin, Edward M -- New York, N.Y. -- Science. 2011 Jan 28;331(6016):463-7. doi: 10.1126/science.1200387.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy, Joint Genome Institute, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21273488" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteria/enzymology/*genetics/isolation & purification/metabolism ; Bacterial Proteins/chemistry/genetics/metabolism ; *Biomass ; Carbohydrate Metabolism ; Cattle/*microbiology ; Cellulase/genetics/metabolism ; Cellulases/chemistry/*genetics/metabolism ; Cellulose/*metabolism ; Cellulose 1,4-beta-Cellobiosidase/genetics/metabolism ; Genes, Bacterial ; Genome, Bacterial ; *Metagenome ; Metagenomics/methods ; Molecular Sequence Annotation ; Molecular Sequence Data ; Poaceae/microbiology ; Rumen/metabolism/*microbiology ; Sequence Analysis, DNA
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  • 75
    Publication Date: 2011-10-25
    Description: Inhibitor of apoptosis (IAP) proteins are negative regulators of cell death. IAP family members contain RING domains that impart E3 ubiquitin ligase activity. Binding of endogenous or small-molecule antagonists to select baculovirus IAP repeat (BIR) domains within cellular IAP (cIAP) proteins promotes autoubiquitination and proteasomal degradation and so releases inhibition of apoptosis mediated by cIAP. Although the molecular details of antagonist-BIR domain interactions are well understood, it is not clear how this binding event influences the activity of the RING domain. Here biochemical and structural studies reveal that the unliganded, multidomain cIAP1 sequesters the RING domain within a compact, monomeric structure that prevents RING dimerization. Antagonist binding induces conformational rearrangements that enable RING dimerization and formation of the active E3 ligase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dueber, Erin C -- Schoeffler, Allyn J -- Lingel, Andreas -- Elliott, J Michael -- Fedorova, Anna V -- Giannetti, Anthony M -- Zobel, Kerry -- Maurer, Brigitte -- Varfolomeev, Eugene -- Wu, Ping -- Wallweber, Heidi J A -- Hymowitz, Sarah G -- Deshayes, Kurt -- Vucic, Domagoj -- Fairbrother, Wayne J -- P41RR001209/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2011 Oct 21;334(6054):376-80. doi: 10.1126/science.1207862.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Early Discovery Biochemistry, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22021857" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Line, Tumor ; Cloning, Molecular ; Humans ; Hydrophobic and Hydrophilic Interactions ; Inhibitor of Apoptosis Proteins/*antagonists & inhibitors/*chemistry/metabolism ; Mice ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Proteasome Endopeptidase Complex/metabolism ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Secondary ; Scattering, Small Angle ; Ubiquitin-Protein Ligases/chemistry/metabolism ; Ubiquitinated Proteins/chemistry/metabolism ; Ubiquitination
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  • 76
    Publication Date: 2011-11-26
    Description: Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3584687/" 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/PMC3584687/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soon, Fen-Fen -- Ng, Ley-Moy -- Zhou, X Edward -- West, Graham M -- Kovach, Amanda -- Tan, M H Eileen -- Suino-Powell, Kelly M -- He, Yuanzheng -- Xu, Yong -- Chalmers, Michael J -- Brunzelle, Joseph S -- Zhang, Huiming -- Yang, Huaiyu -- Jiang, Hualiang -- Li, Jun -- Yong, Eu-Leong -- Cutler, Sean -- Zhu, Jian-Kang -- Griffin, Patrick R -- Melcher, Karsten -- Xu, H Eric -- GM084041/GM/NIGMS NIH HHS/ -- R01 GM059138/GM/NIGMS NIH HHS/ -- S10 RR027270/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2012 Jan 6;335(6064):85-8. doi: 10.1126/science.1215106. Epub 2011 Nov 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue NE, Grand Rapids, MI 49503, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22116026" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/chemistry/*metabolism ; Amino Acid Sequence ; Arabidopsis/chemistry/*metabolism ; Arabidopsis Proteins/antagonists & inhibitors/*chemistry/*metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Activation ; Models, Molecular ; *Molecular Mimicry ; Molecular Sequence Data ; Phosphoprotein Phosphatases/*chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/*chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Signal Transduction
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