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  • Articles  (30)
  • Base Sequence
  • 2000-2004  (30)
  • 1980-1984
  • 2002  (30)
  • Biology  (30)
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  • Articles  (30)
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  • 2000-2004  (30)
  • 1980-1984
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  • 1
    Publication Date: 2002-10-05
    Description: The detection of single-nucleotide polymorphisms in pathogenic microorganisms has normally been carried out by trial and error. Here we show that DNA hybridization with high-density oligonucleotide arrays provides rapid and convenient detection of single-nucleotide polymorphisms in Plasmodium falciparum, despite its exceptionally high adenine-thymine (AT) content (82%). A disproportionate number of polymorphisms are found in genes encoding proteins associated with the cell membrane. These genes are targets for only 22% of the oligonucleotide probes but account for 69% of the polymorphisms. Genetic variation is also enriched in subtelomeric regions, which account for 22% of the chromosome but 76% of the polymorphisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, Sarah K -- Hartl, Daniel L -- Wirth, Dyann F -- Nielsen, Kaare M -- Choi, Mehee -- Batalov, Serge -- Zhou, Yingyao -- Plouffe, David -- Le Roch, Karine G -- Abagyan, Ruben -- Winzeler, Elizabeth A -- GM61351/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):216-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes/genetics ; DNA, Protozoan/genetics ; *Genes, Protozoan ; Genetic Variation ; Genome, Protozoan ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Plasmodium falciparum/*genetics ; *Polymorphism, Single Nucleotide ; Protozoan Proteins/*genetics ; Sequence Analysis, DNA
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2002-04-06
    Description: Higher order chromatin structure presents a barrier to the recognition and repair of DNA damage. Double-strand breaks (DSBs) induce histone H2AX phosphorylation, which is associated with the recruitment of repair factors to damaged DNA. To help clarify the physiological role of H2AX, we targeted H2AX in mice. Although H2AX is not essential for irradiation-induced cell-cycle checkpoints, H2AX-/- mice were radiation sensitive, growth retarded, and immune deficient, and mutant males were infertile. These pleiotropic phenotypes were associated with chromosomal instability, repair defects, and impaired recruitment of Nbs1, 53bp1, and Brca1, but not Rad51, to irradiation-induced foci. Thus, H2AX is critical for facilitating the assembly of specific DNA-repair complexes on damaged DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721576/" 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/PMC4721576/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celeste, Arkady -- Petersen, Simone -- Romanienko, Peter J -- Fernandez-Capetillo, Oscar -- Chen, Hua Tang -- Sedelnikova, Olga A -- Reina-San-Martin, Bernardo -- Coppola, Vincenzo -- Meffre, Eric -- Difilippantonio, Michael J -- Redon, Christophe -- Pilch, Duane R -- Olaru, Alexandru -- Eckhaus, Michael -- Camerini-Otero, R Daniel -- Tessarollo, Lino -- Livak, Ferenc -- Manova, Katia -- Bonner, William M -- Nussenzweig, Michel C -- Nussenzweig, Andre -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):922-7. Epub 2002 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934988" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology/physiology ; Base Sequence ; Cell Aging ; Cell Cycle ; Cells, Cultured ; *Chromosome Aberrations ; DNA Damage ; *DNA Repair ; Female ; Gene Targeting ; Histones/chemistry/*genetics/*physiology ; Immunoglobulin Class Switching ; Infertility, Male/genetics/physiopathology ; Lymphocyte Count ; Male ; Meiosis ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; Phosphorylation ; *Recombination, Genetic ; Spermatocytes/physiology ; T-Lymphocytes/immunology/physiology
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  • 3
    Publication Date: 2002-06-22
    Description: Positive-strand RNA viruses such as poliovirus replicate their genomes on intracellular membranes of their eukaryotic hosts. Electron microscopy has revealed that purified poliovirus RNA-dependent RNA polymerase forms planar and tubular oligomeric arrays. The structural integrity of these arrays correlates with cooperative RNA binding and RNA elongation and is sensitive to mutations that disrupt intermolecular contacts predicted by the polymerase structure. Membranous vesicles isolated from poliovirus-infected cells contain structures consistent with the presence of two-dimensional polymerase arrays on their surfaces during infection. Therefore, host cytoplasmic membranes may function as physical foundations for two-dimensional polymerase arrays, conferring the advantages of surface catalysis to viral RNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyle, John M -- Bullitt, Esther -- Bienz, Kurt -- Kirkegaard, Karla -- AI-42119/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2218-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077417" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Inclusion Bodies, Viral/metabolism/ultrastructure ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Poliovirus/*enzymology/physiology ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; RNA Replicase/*chemistry/isolation & purification/*metabolism/ultrastructure ; RNA, Viral/biosynthesis/*metabolism ; Viral Core Proteins/metabolism ; Virus Replication
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  • 4
    Publication Date: 2002-01-05
    Description: The recently released human genome sequences provide us with reference data to conduct comparative genomic research on primates, which will be important to understand what genetic information makes us human. Here we present a first-generation human-chimpanzee comparative genome map and its initial analysis. The map was constructed through paired alignment of 77,461 chimpanzee bacterial artificial chromosome end sequences with publicly available human genome sequences. We detected candidate positions, including two clusters on human chromosome 21 that suggest large, nonrandom regions of difference between the two genomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujiyama, Asao -- Watanabe, Hidemi -- Toyoda, Atsushi -- Taylor, Todd D -- Itoh, Takehiko -- Tsai, Shih-Feng -- Park, Hong-Seog -- Yaspo, Marie-Laure -- Lehrach, Hans -- Chen, Zhu -- Fu, Gang -- Saitou, Naruya -- Osoegawa, Kazutoyo -- de Jong, Pieter J -- Suto, Yumiko -- Hattori, Masahira -- Sakaki, Yoshiyuki -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):131-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan. afujiyam@gsc.riken.go.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778049" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes, Artificial, Bacterial ; Chromosomes, Human, Pair 21/genetics ; Cloning, Molecular ; Contig Mapping ; Female ; Gene Library ; *Genome ; *Genome, Human ; Humans ; Male ; Pan troglodytes/*genetics ; *Physical Chromosome Mapping ; Sequence Alignment ; Sequence Analysis, DNA ; Sequence Tagged Sites ; X Chromosome/genetics ; Y Chromosome/genetics
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  • 5
    Publication Date: 2002-08-10
    Description: Primate-specific segmental duplications are considered important in human disease and evolution. The inability to distinguish between allelic and duplication sequence overlap has hampered their characterization as well as assembly and annotation of our genome. We developed a method whereby each public sequence is analyzed at the clone level for overrepresentation within a whole-genome shotgun sequence. This test has the ability to detect duplications larger than 15 kilobases irrespective of copy number, location, or high sequence similarity. We mapped 169 large regions flanked by highly similar duplications. Twenty-four of these hot spots of genomic instability have been associated with genetic disease. Our analysis indicates a highly nonrandom chromosomal and genic distribution of recent segmental duplications, with a likely role in expanding protein diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bailey, Jeffrey A -- Gu, Zhiping -- Clark, Royden A -- Reinert, Knut -- Samonte, Rhea V -- Schwartz, Stuart -- Adams, Mark D -- Myers, Eugene W -- Li, Peter W -- Eichler, Evan E -- CA094816/CA/NCI NIH HHS/ -- GM58815/GM/NIGMS NIH HHS/ -- HG002318/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1003-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Center for Computational Genomics, and Center for Human Genetics, Case Western Reserve University School of Medicine and University Hospitals of Cleveland, Cleveland, OH 44106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169732" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Biological Evolution ; Chromosomes, Human/genetics ; Computational Biology ; Databases, Nucleic Acid ; Exons ; Expressed Sequence Tags ; *Gene Duplication ; Gene Rearrangement ; *Genes, Duplicate ; Genetic Diseases, Inborn/genetics ; *Genome, Human ; Humans ; Models, Genetic ; Polymorphism, Single Nucleotide ; Proteome ; Recombination, Genetic ; Sequence Alignment
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  • 6
    Publication Date: 2002-04-27
    Description: Little is known of how plant disease resistance (R) proteins recognize pathogens and activate plant defenses. Rcr3 is specifically required for the function of Cf-2, a Lycopersicon pimpinellifolium gene bred into cultivated tomato (Lycopersicon esculentum) for resistance to Cladosporium fulvum. Rcr3 encodes a secreted papain-like cysteine endoprotease. Genetic analysis shows Rcr3 is allelic to the L. pimpinellifolium Ne gene, which suppresses the Cf-2-dependent autonecrosis conditioned by its L. esculentum allele, ne (necrosis). Rcr3 alleles from these two species encode proteins that differ by only seven amino acids. Possible roles of Rcr3 in Cf-2-dependent defense and autonecrosis are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kruger, Julia -- Thomas, Colwyn M -- Golstein, Catherine -- Dixon, Mark S -- Smoker, Matthew -- Tang, Saijun -- Mulder, Lonneke -- Jones, Jonathan D G -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):744-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976458" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Cladosporium/*physiology ; Cloning, Molecular ; Cysteine Endopeptidases/chemistry/*genetics/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Gene Expression Regulation, Plant ; *Genes, Plant ; Immunity, Innate ; Leucine/analogs & derivatives/pharmacology ; Lycopersicon esculentum/*enzymology/genetics/*microbiology/physiology ; Molecular Sequence Data ; Mutation ; Phenotype ; *Plant Diseases ; Plant Leaves/enzymology ; Plant Proteins/*metabolism ; Plants, Genetically Modified ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/chemistry/metabolism ; Tobacco/genetics ; Transgenes
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  • 7
    Publication Date: 2002-05-25
    Description: The sulfated peptide phytosulfokine (PSK) is an intercellular signal that plays a key role in cellular dedifferentiation and proliferation in plants. Using ligand-based affinity chromatography, we purified a 120-kilodalton membrane protein, specifically interacting with PSK, from carrot microsomal fractions. The corresponding complementary DNA encodes a 1021-amino acid receptor kinase that contains extracellular leucine-rich repeats, a single transmembrane domain, and a cytoplasmic kinase domain. Overexpression of this receptor kinase in carrot cells caused enhanced callus growth in response to PSK and a substantial increase in the number of tritium-labeled PSK binding sites, suggesting that PSK and this receptor kinase act as a ligand-receptor pair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsubayashi, Yoshikatsu -- Ogawa, Mari -- Morita, Akiko -- Sakagami, Youji -- New York, N.Y. -- Science. 2002 May 24;296(5572):1470-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Bio-Agricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan. matsu@agr.nagoya-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029134" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Cell Line ; Chromatography, Affinity ; DNA, Complementary ; Daucus carota/cytology/*enzymology/genetics/growth & development ; Genes, Plant ; Glycosylation ; Leucine ; Ligands ; Microsomes/enzymology ; Molecular Sequence Data ; Molecular Weight ; Peptide Hormones ; *Plant Growth Regulators ; Plant Proteins/*chemistry/genetics/isolation & purification/*metabolism ; Plants, Genetically Modified ; Polymerase Chain Reaction ; Protein Structure, Tertiary ; Receptors, Cell Surface/*chemistry/genetics/isolation & purification/*metabolism ; Repetitive Sequences, Amino Acid
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  • 8
    Publication Date: 2002-01-05
    Description: Many human cancers originate from defects in the DNA damage response (DDR). Although much is known about this process, it is likely that additional DDR genes remain to be discovered. To identify such genes, we used a strategy that combines protein-protein interaction mapping and large-scale phenotypic analysis in Caenorhabditis elegans. Together, these approaches identified 12 worm DDR orthologs and 11 novel DDR genes. One of these is the putative ortholog of hBCL3, a gene frequently altered in chronic lymphocytic leukemia. Thus, the combination of functional genomic mapping approaches in model organisms may facilitate the identification and characterization of genes involved in cancer and, perhaps, other human diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boulton, Simon J -- Gartner, Anton -- Reboul, Jerome -- Vaglio, Philippe -- Dyson, Nick -- Hill, David E -- Vidal, Marc -- 5R01HG01715-02/HG/NHGRI NIH HHS/ -- 7 R33 CA81658-02/CA/NCI NIH HHS/ -- P01CA80111-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):127-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778048" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Base Sequence ; Caenorhabditis elegans/*genetics/metabolism/physiology ; Caenorhabditis elegans Proteins/genetics/*physiology ; *Chromosome Mapping ; Computational Biology ; DNA Damage/*genetics ; DNA Repair/*genetics ; DNA Replication ; Gamma Rays ; Gene Silencing ; *Genes, Helminth ; Genome ; Humans ; Open Reading Frames ; Phenotype ; Proteome ; Proto-Oncogene Proteins/genetics ; Recombination, Genetic ; Transcription Factors ; Two-Hybrid System Techniques
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  • 9
    Publication Date: 2002-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meegaskumbura, M -- Bossuyt, F -- Pethiyagoda, R -- Manamendra-Arachchi, K -- Bahir, M -- Milinkovitch, M C -- Schneider, C J -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):379.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Boston University, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12376694" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura/anatomy & histology/*classification/genetics/physiology ; Base Sequence ; Biological Evolution ; DNA, Mitochondrial/genetics ; *Ecosystem ; Embryonic Development ; Female ; Male ; Molecular Sequence Data ; Oviposition ; Ovum/physiology ; *Phylogeny ; Sri Lanka ; Trees
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  • 10
    Publication Date: 2002-12-14
    Description: The first chordates appear in the fossil record at the time of the Cambrian explosion, nearly 550 million years ago. The modern ascidian tadpole represents a plausible approximation to these ancestral chordates. To illuminate the origins of chordate and vertebrates, we generated a draft of the protein-coding portion of the genome of the most studied ascidian, Ciona intestinalis. The Ciona genome contains approximately 16,000 protein-coding genes, similar to the number in other invertebrates, but only half that found in vertebrates. Vertebrate gene families are typically found in simplified form in Ciona, suggesting that ascidians contain the basic ancestral complement of genes involved in cell signaling and development. The ascidian genome has also acquired a number of lineage-specific innovations, including a group of genes engaged in cellulose metabolism that are related to those in bacteria and fungi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dehal, Paramvir -- Satou, Yutaka -- Campbell, Robert K -- Chapman, Jarrod -- Degnan, Bernard -- De Tomaso, Anthony -- Davidson, Brad -- Di Gregorio, Anna -- Gelpke, Maarten -- Goodstein, David M -- Harafuji, Naoe -- Hastings, Kenneth E M -- Ho, Isaac -- Hotta, Kohji -- Huang, Wayne -- Kawashima, Takeshi -- Lemaire, Patrick -- Martinez, Diego -- Meinertzhagen, Ian A -- Necula, Simona -- Nonaka, Masaru -- Putnam, Nik -- Rash, Sam -- Saiga, Hidetoshi -- Satake, Masanobu -- Terry, Astrid -- Yamada, Lixy -- Wang, Hong-Gang -- Awazu, Satoko -- Azumi, Kaoru -- Boore, Jeffrey -- Branno, Margherita -- Chin-Bow, Stephen -- DeSantis, Rosaria -- Doyle, Sharon -- Francino, Pilar -- Keys, David N -- Haga, Shinobu -- Hayashi, Hiroko -- Hino, Kyosuke -- Imai, Kaoru S -- Inaba, Kazuo -- Kano, Shungo -- Kobayashi, Kenji -- Kobayashi, Mari -- Lee, Byung-In -- Makabe, Kazuhiro W -- Manohar, Chitra -- Matassi, Giorgio -- Medina, Monica -- Mochizuki, Yasuaki -- Mount, Steve -- Morishita, Tomomi -- Miura, Sachiko -- Nakayama, Akie -- Nishizaka, Satoko -- Nomoto, Hisayo -- Ohta, Fumiko -- Oishi, Kazuko -- Rigoutsos, Isidore -- Sano, Masako -- Sasaki, Akane -- Sasakura, Yasunori -- Shoguchi, Eiichi -- Shin-i, Tadasu -- Spagnuolo, Antoinetta -- Stainier, Didier -- Suzuki, Miho M -- Tassy, Olivier -- Takatori, Naohito -- Tokuoka, Miki -- Yagi, Kasumi -- Yoshizaki, Fumiko -- Wada, Shuichi -- Zhang, Cindy -- Hyatt, P Douglas -- Larimer, Frank -- Detter, Chris -- Doggett, Norman -- Glavina, Tijana -- Hawkins, Trevor -- Richardson, Paul -- Lucas, Susan -- Kohara, Yuji -- Levine, Michael -- Satoh, Nori -- Rokhsar, Daniel S -- HD-37105/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2157-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481130" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Apoptosis ; Base Sequence ; Cellulose/metabolism ; Central Nervous System/physiology ; Ciona intestinalis/anatomy & histology/classification/*genetics/physiology ; Computational Biology ; Endocrine System/physiology ; Gene Dosage ; Gene Duplication ; Genes ; Genes, Homeobox ; *Genome ; Heart/embryology/physiology ; Immunity/genetics ; Molecular Sequence Data ; Multigene Family ; Muscle Proteins/genetics ; Organizers, Embryonic/physiology ; Phylogeny ; Polymorphism, Genetic ; Proteins/genetics/physiology ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Species Specificity ; Thyroid Gland/physiology ; Urochordata/genetics ; Vertebrates/anatomy & histology/classification/genetics/physiology
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  • 11
    Publication Date: 2002-03-16
    Description: A 20-variable instance of the NP-complete three-satisfiability (3-SAT) problem was solved on a simple DNA computer. The unique answer was found after an exhaustive search of more than 1 million (2(20)) possibilities. This computational problem may be the largest yet solved by nonelectronic means. Problems of this size appear to be beyond the normal range of unaided human computation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Braich, Ravinderjit S -- Chelyapov, Nickolas -- Johnson, Cliff -- Rothemund, Paul W K -- Adleman, Leonard -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):499-502. Epub 2002 Mar 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Southern California, Laboratory for Molecular Science, Los Angeles, CA 90089-1340, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896237" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; *Computers ; *Computing Methodologies ; *Dna ; DNA, Single-Stranded ; Electrophoresis, Polyacrylamide Gel ; Gene Library ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction
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  • 12
    Publication Date: 2002-09-21
    Description: Micro-RNAs (miRNAs) are regulatory molecules that mediate effects by interacting with messenger RNA (mRNA) targets. Here we show that Arabidopsis thaliana miRNA 39 (also known as miR171), a 21-ribonucleotide species that accumulates predominantly in inflorescence tissues, is produced from an intergenic region in chromosome III and functionally interacts with mRNA targets encoding several members of the Scarecrow-like (SCL) family of putative transcription factors. miRNA 39 is complementary to an internal region of three SCL mRNAs. The interaction results in specific cleavage of target mRNA within the region of complementarity, indicating that this class of miRNA functions like small interfering RNA associated with RNA silencing to guide sequence-specific cleavage in a developmentally controlled manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Llave, Cesar -- Xie, Zhixin -- Kasschau, Kristin D -- Carrington, James C -- AI27832/AI/NIAID NIH HHS/ -- AI43288/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2053-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Gene Research and Biotechnology, and Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR 97331, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242443" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/metabolism ; Arabidopsis Proteins/*genetics/metabolism ; Base Pair Mismatch ; Base Sequence ; DNA, Intergenic ; Gene Silencing ; MicroRNAs ; Plant Leaves/genetics/metabolism ; Plant Stems/genetics/metabolism ; Plant Structures/genetics/metabolism ; RNA, Antisense/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; RNA, Plant/genetics/metabolism ; RNA, Small Interfering ; RNA, Untranslated/genetics/*metabolism ; Transcription Factors/*genetics/metabolism
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  • 13
    Publication Date: 2002-09-28
    Description: Insecticide resistance is one of the most widespread genetic changes caused by human activity, but we still understand little about the origins and spread of resistant alleles in global populations of insects. Here, via microarray analysis of all P450s in Drosophila melanogaster, we show that DDT-R, a gene conferring resistance to DDT, is associated with overtranscription of a single cytochrome P450 gene, Cyp6g1. Transgenic analysis of Cyp6g1 shows that overtranscription of this gene alone is both necessary and sufficient for resistance. Resistance and up-regulation in Drosophila populations are associated with a single Cyp6g1 allele that has spread globally. This allele is characterized by the insertion of an Accord transposable element into the 5' end of the Cyp6g1 gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daborn, P J -- Yen, J L -- Bogwitz, M R -- Le Goff, G -- Feil, E -- Jeffers, S -- Tijet, N -- Perry, T -- Heckel, D -- Batterham, P -- Feyereisen, R -- Wilson, T G -- ffrench-Constant, R H -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2253-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351787" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Animals, Genetically Modified ; Base Sequence ; Chromosome Mapping ; Cytochrome P-450 Enzyme System/*genetics/metabolism ; *Ddt ; Drosophila Proteins/*genetics/metabolism ; Drosophila melanogaster/enzymology/*genetics ; Gene Expression Profiling ; Gene Expression Regulation, Enzymologic ; *Genes, Insect ; Insecticide Resistance/*genetics ; *Insecticides/metabolism ; Introns ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Phylogeny ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, DNA ; Substrate Specificity ; Transcription, Genetic ; Transgenes
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  • 14
    Publication Date: 2002-10-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):735-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399566" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Y/*genetics ; Costs and Cost Analysis ; Gene Dosage ; *Genes, Duplicate ; Humans ; Male ; *Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA/economics/instrumentation/methods
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  • 15
    Publication Date: 2002-03-23
    Description: One role of messenger RNA (mRNA) degradation is to maintain the fidelity of gene expression by degrading aberrant transcripts. Recent results show that mRNAs without translation termination codons are unstable in eukaryotic cells. We used yeast mutants to demonstrate that these "nonstop" mRNAs are degraded by the exosome in a 3'-to-5' direction. The degradation of nonstop transcripts requires the exosome-associated protein Ski7p. Ski7p is closely related to the translation elongation factor EF1A and the translation termination factor eRF3. This suggests that the recognition of nonstop mRNAs involves the binding of Ski7p to an empty aminoacyl-(RNA-binding) site (A site) on the ribosome, thereby bringing the exosome to a mRNA with a ribosome stalled near the 3' end. This system efficiently degrades mRNAs that are prematurely polyadenylated within the coding region and prevents their expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van Hoof, Ambro -- Frischmeyer, Pamela A -- Dietz, Harry C -- Parker, Roy -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2262-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, 4000 Jones Bridge Road, Chevy Chase, MD 20815, USA. : ambro@u.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910110" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Alleles ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Codon, Terminator/*genetics ; Fungal Proteins/chemistry/genetics/*metabolism ; *GTP-Binding Proteins ; Gene Expression Regulation, Fungal ; Genes, Fungal/genetics ; Half-Life ; Molecular Sequence Data ; Polyadenylation ; Protein Binding ; Protein Biosynthesis ; RNA 3' End Processing ; *RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/*genetics/*metabolism ; Ribosomes/metabolism ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Sequence Alignment ; Sequence Deletion/*genetics
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  • 16
    Publication Date: 2002-07-13
    Description: Arabidopsis VRN genes mediate vernalization, the process by which a long period of cold induces a mitotically stable state that leads to accelerated flowering during later development. VRN1 encodes a protein that binds DNA in vitro in a non-sequence-specific manner and functions in stable repression of the major target of the vernalization pathway, the floral repressor FLC. Overexpression of VRN1 reveals a vernalization-independent function for VRN1, mediated predominantly through the floral pathway integrator FT, and demonstrates that VRN1 requires vernalization-specific factors to target FLC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, Yaron Y -- Mesnage, Stephane -- Mylne, Joshua S -- Gendall, Anthony R -- Dean, Caroline -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114624" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/anatomy & histology/*genetics/growth & development/*physiology ; Arabidopsis Proteins/chemistry/*genetics/metabolism/*physiology ; Base Sequence ; Cloning, Molecular ; DNA, Plant/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics/*physiology ; Down-Regulation ; Gene Expression Regulation, Plant ; Genes, Plant ; MADS Domain Proteins/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Photoperiod ; Plant Proteins/genetics/metabolism ; Plant Structures/anatomy & histology/physiology ; Plants, Genetically Modified ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; *Repressor Proteins ; Temperature
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  • 17
    Publication Date: 2002-05-23
    Description: The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (alpha2betabeta'omegasigmaA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the sigma subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the sigma subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced -10 and -35 elements and provides the basis for models of the closed and open promoter complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murakami, Katsuhiko S -- Masuda, Shoko -- Campbell, Elizabeth A -- Muzzin, Oriana -- Darst, Seth A -- GM20470/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- GM61898/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 17;296(5571):1285-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016307" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA, Bacterial/*chemistry/genetics/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Holoenzymes/chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; *Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Subunits ; Sigma Factor/*chemistry/metabolism ; Templates, Genetic ; Thermus/*enzymology ; *Transcription, Genetic
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  • 18
    Publication Date: 2002-06-29
    Description: Globally, human immunodeficiency virus-type 1 (HIV-1) is extraordinarily variable, and this diversity poses a major obstacle to AIDS vaccine development. Currently, candidate vaccines are derived from isolates, with the hope that they will be sufficiently cross-reactive to protect against circulating viruses. This may be overly optimistic, however, given that HIV-1 envelope proteins can differ in more than 30% of their amino acids. To contend with the diversity, country-specific vaccines are being considered, but evolutionary relationships may be more useful than regional considerations. Consensus or ancestor sequences could be used in vaccine design to minimize the genetic differences between vaccine strains and contemporary isolates, effectively reducing the extent of diversity by half.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaschen, Brian -- Taylor, Jesse -- Yusim, Karina -- Foley, Brian -- Gao, Feng -- Lang, Dorothy -- Novitsky, Vladimir -- Haynes, Barton -- Hahn, Beatrice H -- Bhattacharya, Tanmoy -- Korber, Bette -- N01 AI 85338/AI/NIAID NIH HHS/ -- P20 AI 27767/AI/NIAID NIH HHS/ -- R01 AI 05397/AI/NIAID NIH HHS/ -- R01 AI 35351/AI/NIAID NIH HHS/ -- R01 AI 40951/AI/NIAID NIH HHS/ -- YI AI 1500-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2354-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Los Alamos National Laboratory, Los Alamos, NM 87545, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089434" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/immunology ; Base Sequence ; Consensus Sequence ; Cross Reactions ; Evolution, Molecular ; Gene Products, env/chemistry/genetics/immunology ; *Genetic Variation ; Genome, Viral ; HIV Antibodies/biosynthesis/immunology ; HIV Antigens/genetics/immunology ; HIV Infections/epidemiology/prevention & control/virology ; HIV-1/classification/*genetics/*immunology ; Humans ; Likelihood Functions ; *Phylogeny
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):174-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bioterrorism ; DNA, Viral/*chemical synthesis ; Databases, Nucleic Acid ; Mice ; Poliomyelitis/prevention & control/virology ; *Poliovirus/genetics/pathogenicity/physiology ; RNA, Viral/*chemical synthesis/*genetics ; Vaccination ; Variola virus ; Virulence ; Virus Assembly ; Virus Replication
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  • 20
    Publication Date: 2002-06-18
    Description: Activation-induced cytidine deaminase (AID), a putative RNA-editing enzyme, is indispensable for somatic hypermutation (SHM), class switch recombination, and gene conversion of immunoglobulin genes, which indicates a common molecular mechanism for these phenomena. Here we show that ectopic expression of AID alone can induce hypermutation in an artificial GFP substrate in NIH 3T3 murine fibroblast cells. The frequency of mutations was closely correlated with the level of transcription of the target gene, and the distribution of mutations in NIH 3T3 cells was similar to those of SHM in B lymphocytes. These results indicate that AID is sufficient for the generation of SHM in an actively transcribed gene in fibroblasts, as well as B cells, and that any of the required cofactors must be present in these fibroblasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshikawa, Kiyotsugu -- Okazaki, Il-Mi -- Eto, Tomonori -- Kinoshita, Kazuo -- Muramatsu, Masamichi -- Nagaoka, Hitoshi -- Honjo, Tasuku -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2033-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Chemistry and Molecular Biology, Graduate School of Medicine, Kyoto University, Yoshida Konoe-cho, Sakyo-ku, Kyoto, 606-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065838" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; B-Lymphocytes/physiology ; Base Sequence ; Cytidine Deaminase/genetics/*metabolism ; DNA/chemistry/genetics ; Genes, Reporter ; Green Fluorescent Proteins ; Luminescent Proteins/genetics/metabolism ; Mice ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Conformation ; Point Mutation ; Recombinant Proteins/metabolism ; Somatic Hypermutation, Immunoglobulin ; Transcription, Genetic ; Transfection
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-10-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):719-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399553" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; Computational Biology ; DNA/*genetics ; *Genome ; *Genome, Human ; Humans ; Oligonucleotide Array Sequence Analysis ; Pan troglodytes/*genetics ; Polymorphism, Single Nucleotide ; Sequence Analysis, DNA ; Sequence Deletion ; Sequence Homology, Nucleic Acid ; Software ; Species Specificity
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  • 22
    Publication Date: 2002-05-11
    Description: Comparison of the whole-genome sequence of Bacillus anthracis isolated from a victim of a recent bioterrorist anthrax attack with a reference reveals 60 new markers that include single nucleotide polymorphisms (SNPs), inserted or deleted sequences, and tandem repeats. Genome comparison detected four high-quality SNPs between the two sequenced B. anthracis chromosomes and seven differences among different preparations of the reference genome. These markers have been tested on a collection of anthrax isolates and were found to divide these samples into distinct families. These results demonstrate that genome-based analysis of microbial pathogens will provide a powerful new tool for investigation of infectious disease outbreaks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Read, Timothy D -- Salzberg, Steven L -- Pop, Mihai -- Shumway, Martin -- Umayam, Lowell -- Jiang, Lingxia -- Holtzapple, Erik -- Busch, Joseph D -- Smith, Kimothy L -- Schupp, James M -- Solomon, Daniel -- Keim, Paul -- Fraser, Claire M -- R01-LM06845/LM/NLM NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2028-33. Epub 2002 May 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA., Department of Biological Sciences, Northern Arizona University, Flagstaff, AZ 86011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004073" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/microbiology ; Bacillus anthracis/classification/*genetics/isolation & ; purification/pathogenicity ; Bacterial Typing Techniques ; Base Sequence ; Bioterrorism ; Chromosome Inversion ; Computational Biology ; Disease Outbreaks ; Genetic Markers ; *Genetic Variation ; *Genome, Bacterial ; Genomics ; Humans ; Minisatellite Repeats ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Plasmids ; *Polymorphism, Single Nucleotide ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Sequence Deletion ; Species Specificity ; Transposases/genetics ; Virulence/genetics
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-08-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinhart, Brenda J -- Bartel, David P -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1831. Epub 2002 Aug 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193644" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Centromere/*chemistry ; Cloning, Molecular ; Gene Expression Regulation, Fungal ; Gene Silencing ; Heterochromatin/*chemistry ; MicroRNAs ; Protein Biosynthesis ; RNA, Antisense/*chemistry/metabolism ; RNA, Double-Stranded/metabolism ; RNA, Fungal/chemistry/genetics/metabolism ; RNA, Small Interfering ; RNA, Untranslated/*chemistry/metabolism ; Repetitive Sequences, Nucleic Acid ; Schizosaccharomyces/*genetics ; Transcription, Genetic
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  • 24
    Publication Date: 2002-09-21
    Description: Somatically mutated high-affinity autoantibodies are a hallmark of some autoimmune diseases, including systemic lupus erythematosus. It has long been presumed that germinal centers (GCs) are critical in autoantibody production, because they are the only sites currently believed to sustain a high rate of somatic hypermutation. Contrary to this idea, we found that splenic autoreactive B cells in autoimmune MRL.Fas(lpr) mice proliferated and underwent active somatic hypermutation at the T zone-red pulp border rather than in GCs. Our results implicate this region as an important site for hypermutation and the loss of B cell self-tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉William, Jacqueline -- Euler, Chad -- Christensen, Sean -- Shlomchik, Mark J -- P01-A36529/PHS HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2066-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine, Section of Immunobiology, Yale University School of Medicine, Box 208035, New Haven, CT 06520-8035, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242446" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Anti-Idiotypic/immunology ; Autoantibodies/*biosynthesis ; Autoimmune Diseases/immunology ; *Autoimmunity ; B-Lymphocytes/*immunology ; Base Sequence ; Dendritic Cells, Follicular/immunology ; Genes, Immunoglobulin ; Germinal Center/*immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mice, Inbred MRL lpr ; Mice, Transgenic ; Molecular Sequence Data ; Rheumatoid Factor/*biosynthesis ; Self Tolerance ; *Somatic Hypermutation, Immunoglobulin ; Spleen/*immunology ; T-Lymphocytes/immunology
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  • 25
    Publication Date: 2002-03-23
    Description: Translation is an important mechanism to monitor the quality of messenger RNAs (mRNAs), as exemplified by the translation-dependent recognition and degradation of transcripts harboring premature termination codons (PTCs) by the nonsense-mediated mRNA decay (NMD) pathway. We demonstrate in yeast that mRNAs lacking all termination codons are as labile as nonsense transcripts. Decay of "nonstop" transcripts in yeast requires translation but is mechanistically distinguished from NMD and the major mRNA turnover pathway that requires deadenylation, decapping, and 5'-to-3' exonucleolytic decay. These data suggest that nonstop decay is initiated when the ribosome reaches the 3' terminus of the message. We demonstrate multiple physiologic sources of nonstop transcripts and conservation of their accelerated decay in mammalian cells. This process regulates the stability and expression of mRNAs that fail to signal translational termination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frischmeyer, Pamela A -- van Hoof, Ambro -- O'Donnell, Kathryn -- Guerrerio, Anthony L -- Parker, Roy -- Dietz, Harry C -- GM55239/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2258-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetic Medicine, Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910109" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions/chemistry/genetics/metabolism ; Base Sequence ; Cell Line ; Codon, Terminator/*genetics ; Databases, Genetic ; Genes, Fungal/genetics ; Glucuronidase/genetics ; Half-Life ; Humans ; Polyadenylation ; *Protein Biosynthesis ; RNA 3' End Processing ; *RNA Processing, Post-Transcriptional ; RNA Stability ; RNA, Messenger/chemistry/*genetics/*metabolism ; Saccharomyces cerevisiae/*genetics ; Sequence Deletion/*genetics
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  • 26
    Publication Date: 2002-05-25
    Description: Pyrrolysine is a lysine derivative encoded by the UAG codon in methylamine methyltransferase genes of Methanosarcina barkeri. Near a methyltransferase gene cluster is the pylT gene, which encodes an unusual transfer RNA (tRNA) with a CUA anticodon. The adjacent pylS gene encodes a class II aminoacyl-tRNA synthetase that charges the pylT-derived tRNA with lysine but is not closely related to known lysyl-tRNA synthetases. Homologs of pylS and pylT are found in a Gram-positive bacterium. Charging a tRNA(CUA) with lysine is a likely first step in translating UAG amber codons as pyrrolysine in certain methanogens. Our results indicate that pyrrolysine is the 22nd genetically encoded natural amino acid.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srinivasan, Gayathri -- James, Carey M -- Krzycki, Joseph A -- New York, N.Y. -- Science. 2002 May 24;296(5572):1459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Ohio State University, Columbus, OH 43210, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029131" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/chemistry/*genetics/metabolism ; Anticodon ; Archaeal Proteins ; Base Sequence ; Catalytic Domain ; *Codon ; Codon, Terminator ; Kinetics ; Lysine/analogs & derivatives/chemistry/*genetics/metabolism ; Methanosarcina barkeri/chemistry/enzymology/*genetics ; Methyltransferases/genetics/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Biosynthesis ; RNA, Archaeal/chemistry/genetics/metabolism ; RNA, Transfer/chemistry/*genetics/metabolism ; Recombinant Proteins/metabolism ; Sequence Alignment
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  • 27
    Publication Date: 2002-11-26
    Description: The DJ-1 gene encodes a ubiquitous, highly conserved protein. Here, we show that DJ-1 mutations are associated with PARK7, a monogenic form of human parkinsonism. The function of the DJ-1 protein remains unknown, but evidence suggests its involvement in the oxidative stress response. Our findings indicate that loss of DJ-1 function leads to neurodegeneration. Elucidating the physiological role of DJ-1 protein may promote understanding of the mechanisms of brain neuronal maintenance and pathogenesis of Parkinson's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonifati, Vincenzo -- Rizzu, Patrizia -- van Baren, Marijke J -- Schaap, Onno -- Breedveld, Guido J -- Krieger, Elmar -- Dekker, Marieke C J -- Squitieri, Ferdinando -- Ibanez, Pablo -- Joosse, Marijke -- van Dongen, Jeroen W -- Vanacore, Nicola -- van Swieten, John C -- Brice, Alexis -- Meco, Giuseppe -- van Duijn, Cornelia M -- Oostra, Ben A -- Heutink, Peter -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):256-9. Epub 2002 Nov 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetic-Epidemiologic Unit, Department of Clinical Genetics, Department of Epidemiology and Biostatistics, Erasmus Medical Center Rotterdam, Post Office Box 1738, 3000 DR Rotterdam, Netherlands. bonifati@kgen.fgg.eur.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446870" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Base Sequence ; Brain/metabolism ; COS Cells ; Cell Nucleus/metabolism ; Chromosomes, Human, Pair 1 ; Cloning, Molecular ; Cytoplasm/metabolism ; DNA, Complementary ; Exons ; Genes, Recessive ; Humans ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; *Mutation ; Oncogene Proteins/chemistry/*genetics/metabolism ; Oxidative Stress ; PC12 Cells ; Parkinsonian Disorders/*genetics/metabolism ; Pedigree ; Physical Chromosome Mapping ; Point Mutation ; Protein Structure, Secondary ; Rats ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Deletion ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 28
    Publication Date: 2002-07-27
    Description: Most human cancer cells show signs of genome instability, ranging from elevated mutation rates to gross chromosomal rearrangements and alterations in chromosome number. Little is known about the molecular mechanisms that generate this instability or how it is suppressed in normal cells. Recent studies of the yeast Saccharomyces cerevisiae have begun to uncover the extensive and redundant pathways that keep the rate of genome rearrangements at very low levels. These studies, which we review here, have implicated more than 50 genes in the suppression of genome instability, including genes that function in S-phase checkpoints, recombination pathways, and telomere maintenance. Human homologs of several of these genes have well-established roles as tumor suppressors, consistent with the hypothesis that the mechanisms preserving genome stability in yeast are the same mechanisms that go awry in cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolodner, Richard D -- Putnam, Christopher D -- Myung, Kyungjae -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):552-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ludwig Institute for Cancer Research, Cancer Center and Department of Medicine, CMME3058, 9500 Gilman Drive, University of California-San Diego School of Medicine, La Jolla, CA 92093, USA. rkolodner@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142524" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosome Aberrations ; DNA Replication ; *Genes, Fungal ; *Genome, Fungal ; Models, Genetic ; *Mutation ; Neoplasms/genetics ; Recombination, Genetic ; S Phase ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Telomere/metabolism/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 29
    Publication Date: 2002-03-23
    Description: The climatic and environmental changes associated with the last glaciation (90,000 to 10,000 years before the present; 90 to 10 ka B.P.) are an important example of the effects of global climate change on biological diversity. These effects were particularly marked in Beringia (northeastern Siberia, northwestern North America, and the exposed Bering Strait) during the late Pleistocene. To investigate the evolutionary impact of these events, we studied genetic change in the brown bear, Ursus arctos, in eastern Beringia over the past 60,000 years using DNA preserved in permafrost remains. A marked degree of genetic structure is observed in populations throughout this period despite local extinctions, reinvasions, and potential interspecies competition with the short-faced bear, Arctodus simus. The major phylogeographic changes occurred 35 to 21 ka B.P., before the glacial maximum, and little change is observed after this time. Late Pleistocene histories of mammalian taxa may be more complex than those that might be inferred from the fossil record or contemporary DNA sequences alone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, I -- Matheus, P -- Shapiro, B -- Jensen, D -- Cooper, A -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2267-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biological Anthropology, University of Oxford, Oxford OX2 6QS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Climate ; DNA, Mitochondrial/genetics/isolation & purification ; Diet ; *Ecosystem ; *Evolution, Molecular ; Fossils ; Founder Effect ; Haplotypes/genetics ; Ice ; Molecular Sequence Data ; Phylogeny ; Siberia ; Species Specificity ; Time Factors ; Ursidae/*genetics/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-08-03
    Description: In animals, the double-stranded RNA-specific endonuclease Dicer produces two classes of functionally distinct, tiny RNAs: microRNAs (miRNAs) and small interfering RNAs (siRNAs). miRNAs regulate mRNA translation, whereas siRNAs direct RNA destruction via the RNA interference (RNAi) pathway. Here we show that, in human cell extracts, the miRNA let-7 naturally enters the RNAi pathway, which suggests that only the degree of complementarity between a miRNA and its RNA target determines its function. Human let-7 is a component of a previously identified, miRNA-containing ribonucleoprotein particle, which we show is an RNAi enzyme complex. Each let-7-containing complex directs multiple rounds of RNA cleavage, which explains the remarkable efficiency of the RNAi pathway in human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hutvagner, Gyorgy -- Zamore, Phillip D -- GM62862-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2056-60. Epub 2002 Aug 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Lazare Research Building, Room 825, 364 Plantation Street, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12154197" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Argonaute Proteins ; Base Pairing ; Base Sequence ; Cell Extracts ; Cytoplasm/metabolism ; DEAD Box Protein 20 ; DEAD-box RNA Helicases ; Drosophila melanogaster/genetics ; Endoribonucleases/metabolism ; Eukaryotic Initiation Factor-2 ; *Eukaryotic Initiation Factors ; *Gene Silencing ; HeLa Cells ; Humans ; MicroRNAs ; Models, Genetic ; Nuclear Proteins/metabolism ; Peptide Initiation Factors/metabolism ; Protein Biosynthesis ; RNA Helicases/metabolism ; RNA, Antisense/chemistry/*metabolism ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Messenger/chemistry/*metabolism ; RNA, Small Interfering ; RNA, Untranslated/chemistry/*metabolism ; RNA-Induced Silencing Complex ; Ribonuclease III ; Ribonucleoproteins/metabolism ; Ribonucleoproteins, Small Nuclear
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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