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  • Genes
  • Structure-Activity Relationship
  • American Association for the Advancement of Science (AAAS)  (225)
  • International Union of Crystallography (IUCr)
  • 2005-2009  (53)
  • 1980-1984  (172)
  • 1955-1959
  • 1925-1929
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  • 1
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    Genetics. Genomes highlight plant pathogens' powerful arsenal (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1217.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946041" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/genetics/physiology ; Biological Evolution ; DNA, Algal/*genetics ; Genes ; Genetic Variation ; *Genome ; Phytophthora/*genetics/*pathogenicity ; Plant Diseases/microbiology ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-03-11
    Description: Nisin is a posttranslationally modified antimicrobial peptide that is widely used as a food preservative. It contains five cyclic thioethers of varying sizes that are installed by a single enzyme, NisC. Reported here are the in vitro reconstitution of the cyclization process and the x-ray crystal structure of the NisC enzyme. The structure reveals similarities in fold and substrate activation with mammalian farnesyl transferases, suggesting that human homologs of NisC posttranslationally modify a cysteine of a protein substrate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Bo -- Yu, John Paul J -- Brunzelle, Joseph S -- Moll, Gert N -- van der Donk, Wilfred A -- Nair, Satish K -- GM58822/GM/NIGMS NIH HHS/ -- R01 GM079038/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527981" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/*biosynthesis/chemistry ; Carbon-Sulfur Lyases/chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Farnesyltranstransferase/chemistry ; Humans ; Lactococcus lactis/*enzymology ; Models, Molecular ; Molecular Sequence Data ; Nisin/*biosynthesis/chemistry ; Protein Conformation ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
    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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  • 3
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    Engineering cooperativity in biomotor-protein assemblies (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-03-11
    Description: A biosynthetic approach was developed to control and probe cooperativity in multiunit biomotor assemblies by linking molecular motors to artificial protein scaffolds. This approach provides precise control over spatial and elastic coupling between motors. Cooperative interactions between monomeric kinesin-1 motors attached to protein scaffolds enhance hydrolysis activity and microtubule gliding velocity. However, these interactions are not influenced by changes in the elastic properties of the scaffold, distinguishing multimotor transport from that powered by unorganized monomeric motors. These results highlight the role of supramolecular architecture in determining mechanisms of collective transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diehl, Michael R -- Zhang, Kechun -- Lee, Heun Jin -- Tirrell, David A -- New York, N.Y. -- Science. 2006 Mar 10;311(5766):1468-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. diehl@rice.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527982" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/chemistry ; Amino Acid Sequence ; Elasticity ; Elastin/chemistry ; Hydrolysis ; Kinesin/chemistry ; Microtubules/physiology ; Models, Biological ; Molecular Motor Proteins/*physiology ; Molecular Sequence Data ; Protein Engineering ; Protein Structure, Tertiary ; Proteins/chemistry/*physiology ; Recombinant Proteins/chemistry ; Structure-Activity Relationship
    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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  • 4
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    Structural basis for double-stranded RNA processing by Dicer (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-01-18
    Description: The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macrae, Ian J -- Zhou, Kaihong -- Li, Fei -- Repic, Adrian -- Brooks, Angela N -- Cande, W Zacheus -- Adams, Paul D -- Doudna, Jennifer A -- New York, N.Y. -- Science. 2006 Jan 13;311(5758):195-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16410517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Conserved Sequence ; Crystallography, X-Ray ; Giardia lamblia/enzymology ; Humans ; Lanthanoid Series Elements/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Tertiary ; RNA Interference ; RNA, Double-Stranded/*metabolism ; RNA, Protozoan/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Ribonuclease III/*chemistry/metabolism ; Schizosaccharomyces/genetics ; Structure-Activity Relationship
    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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  • 5
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    Phytophthora genome sequences uncover evolutionary origins and mechanisms of pathogenesis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-02
    Description: Draft genome sequences have been determined for the soybean pathogen Phytophthora sojae and the sudden oak death pathogen Phytophthora ramorum. Oomycetes such as these Phytophthora species share the kingdom Stramenopila with photosynthetic algae such as diatoms, and the presence of many Phytophthora genes of probable phototroph origin supports a photosynthetic ancestry for the stramenopiles. Comparison of the two species' genomes reveals a rapid expansion and diversification of many protein families associated with plant infection such as hydrolases, ABC transporters, protein toxins, proteinase inhibitors, and, in particular, a superfamily of 700 proteins with similarity to known oomycete avirulence genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tyler, Brett M -- Tripathy, Sucheta -- Zhang, Xuemin -- Dehal, Paramvir -- Jiang, Rays H Y -- Aerts, Andrea -- Arredondo, Felipe D -- Baxter, Laura -- Bensasson, Douda -- Beynon, Jim L -- Chapman, Jarrod -- Damasceno, Cynthia M B -- Dorrance, Anne E -- Dou, Daolong -- Dickerman, Allan W -- Dubchak, Inna L -- Garbelotto, Matteo -- Gijzen, Mark -- Gordon, Stuart G -- Govers, Francine -- Grunwald, Niklaus J -- Huang, Wayne -- Ivors, Kelly L -- Jones, Richard W -- Kamoun, Sophien -- Krampis, Konstantinos -- Lamour, Kurt H -- Lee, Mi-Kyung -- McDonald, W Hayes -- Medina, Monica -- Meijer, Harold J G -- Nordberg, Eric K -- Maclean, Donald J -- Ospina-Giraldo, Manuel D -- Morris, Paul F -- Phuntumart, Vipaporn -- Putnam, Nicholas H -- Rash, Sam -- Rose, Jocelyn K C -- Sakihama, Yasuko -- Salamov, Asaf A -- Savidor, Alon -- Scheuring, Chantel F -- Smith, Brian M -- Sobral, Bruno W S -- Terry, Astrid -- Torto-Alalibo, Trudy A -- Win, Joe -- Xu, Zhanyou -- Zhang, Hongbin -- Grigoriev, Igor V -- Rokhsar, Daniel S -- Boore, Jeffrey L -- BB/C509123/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1261-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Virginia Bioinformatics Institute, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA. bmtyler@vt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946064" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/genetics/physiology ; *Biological Evolution ; DNA, Algal/*genetics ; Genes ; *Genome ; Hydrolases/genetics/metabolism ; Photosynthesis/genetics ; Phylogeny ; Physical Chromosome Mapping ; Phytophthora/classification/*genetics/*pathogenicity/physiology ; Plant Diseases/microbiology ; Polymorphism, Single Nucleotide ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA ; Symbiosis ; Toxins, Biological/genetics
    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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  • 6
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    Structural insight into pre-B cell receptor function (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-04-14
    Description: The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bankovich, Alexander J -- Raunser, Stefan -- Juo, Z Sean -- Walz, Thomas -- Davis, Mark M -- Garcia, K Christopher -- T32 AI007290/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 13;316(5822):291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in 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/17431183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Complementarity Determining Regions/chemistry/physiology ; Crystallography, X-Ray ; Humans ; Immunoglobulin Heavy Chains/chemistry/physiology ; Immunoglobulin Light Chains/chemistry/physiology ; Immunoglobulin Light Chains, Surrogate ; Membrane Glycoproteins/*chemistry/physiology/ultrastructure ; Mice ; Models, Molecular ; Pre-B Cell Receptors ; Protein Conformation ; Receptors, Antigen, B-Cell/*chemistry/physiology/ultrastructure ; Recombinant Proteins ; Structure-Activity Relationship
    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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  • 7
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    Ecology. Plant wannabes (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1229.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946048" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chloroplasts/*physiology ; Digestive System/anatomy & histology/microbiology ; Digestive System Physiological Phenomena ; Eukaryota/*physiology ; Gastropoda/genetics/microbiology/*physiology ; Genes ; Photosynthesis ; *Symbiosis
    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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  • 8
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    Genomics. Sea anemone provides a new view of animal evolution (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):27.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Genes ; *Genome ; Genome, Human ; Genomics ; Humans ; Introns ; Sea Anemones/*genetics ; Sequence Analysis, DNA
    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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  • 9
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    The Chlamydomonas genome reveals the evolution of key animal and plant functions (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-10-13
    Description: Chlamydomonas reinhardtii is a unicellular green alga whose lineage diverged from land plants over 1 billion years ago. It is a model system for studying chloroplast-based photosynthesis, as well as the structure, assembly, and function of eukaryotic flagella (cilia), which were inherited from the common ancestor of plants and animals, but lost in land plants. We sequenced the approximately 120-megabase nuclear genome of Chlamydomonas and performed comparative phylogenomic analyses, identifying genes encoding uncharacterized proteins that are likely associated with the function and biogenesis of chloroplasts or eukaryotic flagella. Analyses of the Chlamydomonas genome advance our understanding of the ancestral eukaryotic cell, reveal previously unknown genes associated with photosynthetic and flagellar functions, and establish links between ciliopathy and the composition and function of flagella.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2875087/" 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/PMC2875087/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Merchant, Sabeeha S -- Prochnik, Simon E -- Vallon, Olivier -- Harris, Elizabeth H -- Karpowicz, Steven J -- Witman, George B -- Terry, Astrid -- Salamov, Asaf -- Fritz-Laylin, Lillian K -- Marechal-Drouard, Laurence -- Marshall, Wallace F -- Qu, Liang-Hu -- Nelson, David R -- Sanderfoot, Anton A -- Spalding, Martin H -- Kapitonov, Vladimir V -- Ren, Qinghu -- Ferris, Patrick -- Lindquist, Erika -- Shapiro, Harris -- Lucas, Susan M -- Grimwood, Jane -- Schmutz, Jeremy -- Cardol, Pierre -- Cerutti, Heriberto -- Chanfreau, Guillaume -- Chen, Chun-Long -- Cognat, Valerie -- Croft, Martin T -- Dent, Rachel -- Dutcher, Susan -- Fernandez, Emilio -- Fukuzawa, Hideya -- Gonzalez-Ballester, David -- Gonzalez-Halphen, Diego -- Hallmann, Armin -- Hanikenne, Marc -- Hippler, Michael -- Inwood, William -- Jabbari, Kamel -- Kalanon, Ming -- Kuras, Richard -- Lefebvre, Paul A -- Lemaire, Stephane D -- Lobanov, Alexey V -- Lohr, Martin -- Manuell, Andrea -- Meier, Iris -- Mets, Laurens -- Mittag, Maria -- Mittelmeier, Telsa -- Moroney, James V -- Moseley, Jeffrey -- Napoli, Carolyn -- Nedelcu, Aurora M -- Niyogi, Krishna -- Novoselov, Sergey V -- Paulsen, Ian T -- Pazour, Greg -- Purton, Saul -- Ral, Jean-Philippe -- Riano-Pachon, Diego Mauricio -- Riekhof, Wayne -- Rymarquis, Linda -- Schroda, Michael -- Stern, David -- Umen, James -- Willows, Robert -- Wilson, Nedra -- Zimmer, Sara Lana -- Allmer, Jens -- Balk, Janneke -- Bisova, Katerina -- Chen, Chong-Jian -- Elias, Marek -- Gendler, Karla -- Hauser, Charles -- Lamb, Mary Rose -- Ledford, Heidi -- Long, Joanne C -- Minagawa, Jun -- Page, M Dudley -- Pan, Junmin -- Pootakham, Wirulda -- Roje, Sanja -- Rose, Annkatrin -- Stahlberg, Eric -- Terauchi, Aimee M -- Yang, Pinfen -- Ball, Steven -- Bowler, Chris -- Dieckmann, Carol L -- Gladyshev, Vadim N -- Green, Pamela -- Jorgensen, Richard -- Mayfield, Stephen -- Mueller-Roeber, Bernd -- Rajamani, Sathish -- Sayre, Richard T -- Brokstein, Peter -- Dubchak, Inna -- Goodstein, David -- Hornick, Leila -- Huang, Y Wayne -- Jhaveri, Jinal -- Luo, Yigong -- Martinez, Diego -- Ngau, Wing Chi Abby -- Otillar, Bobby -- Poliakov, Alexander -- Porter, Aaron -- Szajkowski, Lukasz -- Werner, Gregory -- Zhou, Kemin -- Grigoriev, Igor V -- Rokhsar, Daniel S -- Grossman, Arthur R -- GM07185/GM/NIGMS NIH HHS/ -- GM42143/GM/NIGMS NIH HHS/ -- R01 GM032843/GM/NIGMS NIH HHS/ -- R01 GM042143/GM/NIGMS NIH HHS/ -- R01 GM042143-09/GM/NIGMS NIH HHS/ -- R01 GM060992/GM/NIGMS NIH HHS/ -- R01 GM062915-06/GM/NIGMS NIH HHS/ -- R37 GM030626/GM/NIGMS NIH HHS/ -- R37 GM042143/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 12;318(5848):245-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17932292" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/*genetics/*physiology ; Animals ; *Biological Evolution ; Chlamydomonas reinhardtii/*genetics/physiology ; Chloroplasts/metabolism ; Computational Biology ; DNA, Algal/genetics ; Flagella/metabolism ; Genes ; *Genome ; Genomics ; Membrane Transport Proteins/genetics/physiology ; Molecular Sequence Data ; Multigene Family ; Photosynthesis/genetics ; Phylogeny ; Plants/genetics ; Proteome ; Sequence Analysis, DNA
    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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  • 10
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    Physiology. Still pondering an age-old question (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-11-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flatt, Thomas -- Promislow, Daniel E L -- New York, N.Y. -- Science. 2007 Nov 23;318(5854):1255-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Brown University, Providence, RI 02912, USA. thomas_flatt@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18033874" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/*physiology ; Animals ; Biological Evolution ; Fertility ; Genes ; Humans ; Longevity/genetics ; Mutation ; Reproduction ; Selection, Genetic
    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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  • 11
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    Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-07-07
    Description: Sea anemones are seemingly primitive animals that, along with corals, jellyfish, and hydras, constitute the oldest eumetazoan phylum, the Cnidaria. Here, we report a comparative analysis of the draft genome of an emerging cnidarian model, the starlet sea anemone Nematostella vectensis. The sea anemone genome is complex, with a gene repertoire, exon-intron structure, and large-scale gene linkage more similar to vertebrates than to flies or nematodes, implying that the genome of the eumetazoan ancestor was similarly complex. Nearly one-fifth of the inferred genes of the ancestor are eumetazoan novelties, which are enriched for animal functions like cell signaling, adhesion, and synaptic transmission. Analysis of diverse pathways suggests that these gene "inventions" along the lineage leading to animals were likely already well integrated with preexisting eukaryotic genes in the eumetazoan progenitor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Putnam, Nicholas H -- Srivastava, Mansi -- Hellsten, Uffe -- Dirks, Bill -- Chapman, Jarrod -- Salamov, Asaf -- Terry, Astrid -- Shapiro, Harris -- Lindquist, Erika -- Kapitonov, Vladimir V -- Jurka, Jerzy -- Genikhovich, Grigory -- Grigoriev, Igor V -- Lucas, Susan M -- Steele, Robert E -- Finnerty, John R -- Technau, Ulrich -- Martindale, Mark Q -- Rokhsar, Daniel S -- 5 P41 LM006252-09/LM/NLM NIH HHS/ -- THL007279F/PHS HHS/ -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):86-94.〈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/17615350" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Cell Adhesion ; Evolution, Molecular ; Genes ; Genetic Linkage ; *Genome ; Genome, Human ; Genomics ; Humans ; Introns ; Metabolic Networks and Pathways ; Multigene Family ; Muscles/physiology ; Nervous System Physiological Phenomena ; Phylogeny ; Sea Anemones/*genetics/metabolism ; Sequence Analysis, DNA ; Signal Transduction ; Synteny
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 12
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    Patterning mechanisms of branched organs (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-12-06
    Description: Branching morphogenesis is one of the earliest events essential for the success of metazoans. By branching out and forming cellular or tissue extensions, cells can maximize their surface area and overcome space constraints posed by organ size. Over the past decade, tremendous progress has been made toward understanding the branching mechanisms of various invertebrate and vertebrate organ systems. Despite their distinct origins, morphologies and functions, different cell and tissue types use a remarkably conserved set of tools to undergo branching morphogenesis. Recent studies have shed important light on the basis of molecular conservation in the formation of branched structures in diverse organs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2645229/" 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/PMC2645229/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lu, Pengfei -- Werb, Zena -- CA057621/CA/NCI NIH HHS/ -- ES012801/ES/NIEHS NIH HHS/ -- R01 CA057621/CA/NCI NIH HHS/ -- R01 CA057621-16A1/CA/NCI NIH HHS/ -- U01 ES012801-06/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2008 Dec 5;322(5907):1506-9. doi: 10.1126/science.1162783.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Program in Developmental Biology, University of California at San Francisco, San Francisco, CA 94143-0452, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19056977" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Vessels/embryology/physiology ; *Body Patterning ; Cell Differentiation ; Epithelium/embryology/physiology ; Genes ; Mesoderm/embryology/physiology ; *Morphogenesis ; Nervous System/embryology ; Neurons/cytology ; *Organogenesis ; Regeneration ; Signal Transduction ; Stem Cells/physiology ; Stromal Cells/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein (2008)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2008-05-10
    Description: Energy-dependent quenching of excess absorbed light energy (qE) is a vital mechanism for regulating photosynthetic light harvesting in higher plants. All of the physiological characteristics of qE have been positively correlated with charge transfer between coupled chlorophyll and zeaxanthin molecules in the light-harvesting antenna of photosystem II (PSII). We found evidence for charge-transfer quenching in all three of the individual minor antenna complexes of PSII (CP29, CP26, and CP24), and we conclude that charge-transfer quenching in CP29 involves a delocalized state of an excitonically coupled chlorophyll dimer. We propose that reversible conformational changes in CP29 can "tune" the electronic coupling between the chlorophylls in this dimer, thereby modulating the energy of the chlorophyll-zeaxanthin charge-transfer state and switching on and off the charge-transfer quenching during qE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahn, Tae Kyu -- Avenson, Thomas J -- Ballottari, Matteo -- Cheng, Yuan-Chung -- Niyogi, Krishna K -- Bassi, Roberto -- Fleming, Graham R -- New York, N.Y. -- Science. 2008 May 9;320(5877):794-7. doi: 10.1126/science.1154800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18467588" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis Proteins/chemistry/genetics/*physiology ; Chlorophyll/physiology ; Chlorophyll Binding Proteins ; Chloroplast Proteins ; Electron Transport ; Electrophysiology ; Light ; Light-Harvesting Protein Complexes/chemistry/genetics/*physiology ; Lutein/metabolism ; Models, Molecular ; Photosystem II Protein Complex/chemistry/genetics/*physiology ; Protein Conformation ; Recombinant Proteins/metabolism ; Ribonucleoproteins ; Structure-Activity Relationship ; Xanthophylls/metabolism ; Zeaxanthins
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    Haploid genetic screens in human cells identify host factors used by pathogens (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: Loss-of-function genetic screens in model organisms have elucidated numerous biological processes, but the diploid genome of mammalian cells has precluded large-scale gene disruption. We used insertional mutagenesis to develop a screening method to generate null alleles in a human cell line haploid for all chromosomes except chromosome 8. Using this approach, we identified host factors essential for infection with influenza and genes encoding important elements of the biosynthetic pathway of diphthamide, which are required for the cytotoxic effects of diphtheria toxin and exotoxin A. We also identified genes needed for the action of cytolethal distending toxin, including a cell-surface protein that interacts with the toxin. This approach has both conceptual and practical parallels with genetic approaches in haploid yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carette, Jan E -- Guimaraes, Carla P -- Varadarajan, Malini -- Park, Annie S -- Wuethrich, Irene -- Godarova, Alzbeta -- Kotecki, Maciej -- Cochran, Brent H -- Spooner, Eric -- Ploegh, Hidde L -- Brummelkamp, Thijn R -- New York, N.Y. -- Science. 2009 Nov 27;326(5957):1231-5. doi: 10.1126/science.1178955.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉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/19965467" target="_blank"〉PubMed〈/a〉
    Keywords: ADP Ribose Transferases/metabolism/toxicity ; Adenosine Diphosphate Ribose/metabolism ; Amino Acid Sequence ; Antigens, Bacterial/metabolism/toxicity ; Bacterial Toxins/*metabolism/toxicity ; Biosynthetic Pathways ; Cell Line, Tumor ; Diphtheria Toxin/metabolism/toxicity ; Exotoxins/metabolism/toxicity ; Genes ; *Genetic Testing ; *Haploidy ; Histidine/analogs & derivatives/biosynthesis ; *Host-Pathogen Interactions ; Humans ; Influenza A Virus, H1N1 Subtype/*pathogenicity ; Molecular Sequence Data ; Monosaccharide Transport Proteins/genetics/metabolism ; Mutagenesis, Insertional ; N-Acylneuraminate Cytidylyltransferase/genetics/metabolism ; Peptide Elongation Factor 2/metabolism ; Proteins/chemistry/genetics/metabolism ; Virulence Factors/metabolism/toxicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Profile: Ruth Ley. Gut reactions (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-05-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2009 May 29;324(5931):1136-7. doi: 10.1126/science.324_1136.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19478161" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/classification/genetics/*isolation & purification ; Diet ; Digestive System/*microbiology ; Ecology/history ; Genes ; Genes, Bacterial ; Genomics/history ; History, 20th Century ; History, 21st Century ; Humans ; Interdisciplinary Communication ; *Metagenome ; *Microbiology/history ; United States
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Green evolution and dynamic adaptations revealed by genomes of the marine picoeukaryotes Micromonas (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-04-11
    Description: Picoeukaryotes are a taxonomically diverse group of organisms less than 2 micrometers in diameter. Photosynthetic marine picoeukaryotes in the genus Micromonas thrive in ecosystems ranging from tropical to polar and could serve as sentinel organisms for biogeochemical fluxes of modern oceans during climate change. These broadly distributed primary producers belong to an anciently diverged sister clade to land plants. Although Micromonas isolates have high 18S ribosomal RNA gene identity, we found that genomes from two isolates shared only 90% of their predicted genes. Their independent evolutionary paths were emphasized by distinct riboswitch arrangements as well as the discovery of intronic repeat elements in one isolate, and in metagenomic data, but not in other genomes. Divergence appears to have been facilitated by selection and acquisition processes that actively shape the repertoire of genes that are mutually exclusive between the two isolates differently than the core genes. Analyses of the Micromonas genomes offer valuable insights into ecological differentiation and the dynamic nature of early plant evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worden, Alexandra Z -- Lee, Jae-Hyeok -- Mock, Thomas -- Rouze, Pierre -- Simmons, Melinda P -- Aerts, Andrea L -- Allen, Andrew E -- Cuvelier, Marie L -- Derelle, Evelyne -- Everett, Meredith V -- Foulon, Elodie -- Grimwood, Jane -- Gundlach, Heidrun -- Henrissat, Bernard -- Napoli, Carolyn -- McDonald, Sarah M -- Parker, Micaela S -- Rombauts, Stephane -- Salamov, Aasf -- Von Dassow, Peter -- Badger, Jonathan H -- Coutinho, Pedro M -- Demir, Elif -- Dubchak, Inna -- Gentemann, Chelle -- Eikrem, Wenche -- Gready, Jill E -- John, Uwe -- Lanier, William -- Lindquist, Erika A -- Lucas, Susan -- Mayer, Klaus F X -- Moreau, Herve -- Not, Fabrice -- Otillar, Robert -- Panaud, Olivier -- Pangilinan, Jasmyn -- Paulsen, Ian -- Piegu, Benoit -- Poliakov, Aaron -- Robbens, Steven -- Schmutz, Jeremy -- Toulza, Eve -- Wyss, Tania -- Zelensky, Alexander -- Zhou, Kemin -- Armbrust, E Virginia -- Bhattacharya, Debashish -- Goodenough, Ursula W -- Van de Peer, Yves -- Grigoriev, Igor V -- New York, N.Y. -- Science. 2009 Apr 10;324(5924):268-72. doi: 10.1126/science.1167222.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monterey Bay Aquarium Research Institute, Moss Landing, CA 95039 USA. azworden@mbari.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19359590" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; *Biological Evolution ; Chlorophyta/classification/cytology/*genetics/physiology ; DNA Transposable Elements ; Ecosystem ; Gene Expression Regulation ; Genes ; Genetic Variation ; *Genome ; Introns ; Meiosis/genetics ; Molecular Sequence Data ; Oceans and Seas ; Photosynthesis/genetics ; Phylogeny ; Phytoplankton/classification/genetics ; Plants/*genetics ; RNA, Untranslated ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA ; Transcription Factors/genetics
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    AIDS vaccine research. HIV natural resistance field finally overcomes resistance (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2009 Dec 11;326(5959):1476-7. doi: 10.1126/science.326.5959.1476.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20007880" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; CD4-Positive T-Lymphocytes/*immunology/virology ; Female ; Genes ; HIV/immunology/physiology ; HIV Infections/*immunology ; Hemophilia A ; Homosexuality, Male ; Humans ; *Immunity, Innate ; Killer Cells, Natural/immunology ; Lymphocyte Activation ; Male ; Prostitution ; T-Lymphocytes, Regulatory/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    The molecular requirements for cytokinesis (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-03-19
    Description: After anaphase onset, animal cells build an actomyosin contractile ring that constricts the plasma membrane to generate two daughter cells connected by a cytoplasmic bridge. The bridge is ultimately severed to complete cytokinesis. Myriad techniques have been used to identify proteins that participate in cytokinesis in vertebrates, insects, and nematodes. A conserved core of about 20 proteins are individually involved with cytokinesis in most animal cells. These components are found in the contractile ring, on the central spindle, within the RhoA pathway, and on vesicles that expand the membrane and sever the bridge. Cytokinesis involves additional proteins, but they, or their requirement in cytokinesis, are not conserved among animal cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glotzer, Michael -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1735-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology, Dr. BohrGasse 7, A-1030 Vienna, Austria. mglotzer@imp.univie.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15774750" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/physiology ; Actins/metabolism ; Animals ; Biological Evolution ; Cell Cycle Proteins/*metabolism ; *Cytokinesis/genetics ; Cytoskeletal Proteins/*metabolism ; Genes ; Membrane Fusion/physiology ; Microtubules/physiology ; Models, Biological ; Myosins/metabolism ; Proteins/*metabolism ; Spindle Apparatus/physiology ; rhoA GTP-Binding Protein/metabolism
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    SLC24A5, a putative cation exchanger, affects pigmentation in zebrafish and humans (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: Lighter variations of pigmentation in humans are associated with diminished number, size, and density of melanosomes, the pigmented organelles of melanocytes. Here we show that zebrafish golden mutants share these melanosomal changes and that golden encodes a putative cation exchanger slc24a5 (nckx5) that localizes to an intracellular membrane, likely the melanosome or its precursor. The human ortholog is highly similar in sequence and functional in zebrafish. The evolutionarily conserved ancestral allele of a human coding polymorphism predominates in African and East Asian populations. In contrast, the variant allele is nearly fixed in European populations, is associated with a substantial reduction in regional heterozygosity, and correlates with lighter skin pigmentation in admixed populations, suggesting a key role for the SLC24A5 gene in human pigmentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lamason, Rebecca L -- Mohideen, Manzoor-Ali P K -- Mest, Jason R -- Wong, Andrew C -- Norton, Heather L -- Aros, Michele C -- Jurynec, Michael J -- Mao, Xianyun -- Humphreville, Vanessa R -- Humbert, Jasper E -- Sinha, Soniya -- Moore, Jessica L -- Jagadeeswaran, Pudur -- Zhao, Wei -- Ning, Gang -- Makalowska, Izabela -- McKeigue, Paul M -- O'donnell, David -- Kittles, Rick -- Parra, Esteban J -- Mangini, Nancy J -- Grunwald, David J -- Shriver, Mark D -- Canfield, Victor A -- Cheng, Keith C -- CA73935/CA/NCI NIH HHS/ -- EY11308/EY/NEI NIH HHS/ -- HD37572/HD/NICHD NIH HHS/ -- HD40179/HD/NICHD NIH HHS/ -- HG002154/HG/NHGRI NIH HHS/ -- HL077910/HL/NHLBI NIH HHS/ -- RR017441/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jake Gittlen Cancer Research Foundation, Department of Pathology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357253" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; African Continental Ancestry Group/genetics ; Alanine/genetics ; Alleles ; Amino Acid Sequence ; Animals ; Antiporters/chemistry/*genetics/physiology ; Asian Continental Ancestry Group/genetics ; Biological Evolution ; Calcium/metabolism ; European Continental Ancestry Group/genetics ; Gene Frequency ; Genes ; Genetic Variation ; Haplotypes ; Heterozygote ; Humans ; Ion Transport ; Melanins/analysis ; Melanosomes/chemistry/ultrastructure ; Mice ; Molecular Sequence Data ; Multifactorial Inheritance ; Mutation ; Pigment Epithelium of Eye/chemistry/ultrastructure ; Polymorphism, Single Nucleotide ; Selection, Genetic ; Skin Pigmentation/*genetics ; Threonine/genetics ; Zebrafish/embryology/*genetics/metabolism ; Zebrafish Proteins/chemistry/*genetics/physiology
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    Diversity. Summers's comments draw attention to gender, racial gaps (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, Andrew -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):492-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681345" target="_blank"〉PubMed〈/a〉
    Keywords: *Career Choice ; Career Mobility ; *Engineering ; Female ; Genes ; Humans ; Male ; *Prejudice ; *Science ; *Sex Characteristics
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  • 21
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    Structural roles for human translation factor eIF3 in initiation of protein synthesis (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-12-03
    Description: Protein synthesis in mammalian cells requires initiation factor eIF3, a approximately 750-kilodalton complex that controls assembly of 40S ribosomal subunits on messenger RNAs (mRNAs) bearing either a 5'-cap or an internal ribosome entry site (IRES). Cryo-electron microscopy reconstructions show that eIF3, a five-lobed particle, interacts with the hepatitis C virus (HCV) IRES RNA and the 5'-cap binding complex eIF4F via the same domain. Detailed modeling of eIF3 and eIF4F onto the 40S ribosomal subunit reveals that eIF3 uses eIF4F or the HCV IRES in structurally similar ways to position the mRNA strand near the exit site of 40S, promoting initiation complex assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siridechadilok, Bunpote -- Fraser, Christopher S -- Hall, Richard J -- Doudna, Jennifer A -- Nogales, Eva -- New York, N.Y. -- Science. 2005 Dec 2;310(5753):1513-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16322461" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Eukaryotic Initiation Factor-3/chemistry/*physiology/ultrastructure ; Eukaryotic Initiation Factor-4F/metabolism ; HeLa Cells ; Hepacivirus/genetics ; Humans ; Models, Molecular ; Protein Binding ; Protein Biosynthesis/*physiology ; Protein Conformation ; RNA, Messenger/metabolism ; RNA, Viral/metabolism ; Ribosomes/metabolism ; Structure-Activity Relationship
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    A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-06-04
    Description: Fluoroquinolones are gaining increasing importance in the treatment of tuberculosis. The expression of MfpA, a member of the pentapeptide repeat family of proteins from Mycobacterium tuberculosis, causes resistance to ciprofloxacin and sparfloxacin. This protein binds to DNA gyrase and inhibits its activity. Its three-dimensional structure reveals a fold, which we have named the right-handed quadrilateral beta helix, that exhibits size, shape, and electrostatic similarity to B-form DNA. This represents a form of DNA mimicry and explains both its inhibitory effect on DNA gyrase and fluoroquinolone resistance resulting from the protein's expression in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hegde, Subray S -- Vetting, Matthew W -- Roderick, Steven L -- Mitchenall, Lesley A -- Maxwell, Anthony -- Takiff, Howard E -- Blanchard, John S -- AI33696/AI/NIAID NIH HHS/ -- AI60899/AI/NIAID NIH HHS/ -- T32 AI007501/AI/NIAID NIH HHS/ -- T32 AI07501/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1480-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933203" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antitubercular Agents/chemistry/*pharmacology ; Bacterial Proteins/chemistry/*physiology ; Ciprofloxacin/pharmacology ; Crystallography, X-Ray ; DNA Gyrase/metabolism ; DNA, Bacterial/*chemistry ; DNA, Superhelical/chemistry ; *Drug Resistance, Bacterial ; Drug Resistance, Microbial/*physiology ; Enzyme Inhibitors/chemistry ; Escherichia coli/enzymology ; Fluoroquinolones/antagonists & inhibitors/chemistry/*pharmacology ; Models, Molecular ; *Molecular Mimicry ; Molecular Sequence Data ; Monomeric GTP-Binding Proteins ; Mycobacterium tuberculosis/drug effects/*physiology ; Protein Conformation ; Protein Folding ; Structure-Activity Relationship ; Topoisomerase II Inhibitors
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    Fewer genes, more noncoding RNA (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-09-06
    Description: Recent studies showing that most "messenger" RNAs do not encode proteins finally explain the long-standing discrepancy between the small number of protein-coding genes found in vertebrate genomes and the much larger and ever-increasing number of polyadenylated transcripts identified by tag-sampling or microarray-based methods. Exploring the role and diversity of these numerous noncoding RNAs now constitutes a main challenge in transcription research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Claverie, Jean-Michel -- New York, N.Y. -- Science. 2005 Sep 2;309(5740):1529-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural and Genomics Information Laboratory, CNRS UPR 2589, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, Marseille 13402, France. jean-michel.claverie@igs.cnrs-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16141064" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Genes ; *Genome, Human ; Genomics ; Humans ; Mice ; Proteins/genetics ; RNA, Untranslated/*biosynthesis/physiology ; *Transcription, Genetic
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    Comparative metagenomics of microbial communities (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-23
    Description: The species complexity of microbial communities and challenges in culturing representative isolates make it difficult to obtain assembled genomes. Here we characterize and compare the metabolic capabilities of terrestrial and marine microbial communities using largely unassembled sequence data obtained by shotgun sequencing DNA isolated from the various environments. Quantitative gene content analysis reveals habitat-specific fingerprints that reflect known characteristics of the sampled environments. The identification of environment-specific genes through a gene-centric comparative analysis presents new opportunities for interpreting and diagnosing environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tringe, Susannah Green -- von Mering, Christian -- Kobayashi, Arthur -- Salamov, Asaf A -- Chen, Kevin -- Chang, Hwai W -- Podar, Mircea -- Short, Jay M -- Mathur, Eric J -- Detter, John C -- Bork, Peer -- Hugenholtz, Philip -- Rubin, Edward M -- New York, N.Y. -- Science. 2005 Apr 22;308(5721):554-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy (DOE) 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/15845853" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Archaea/classification/genetics/metabolism ; Bacteria/classification/*genetics/metabolism ; Bacterial Proteins/genetics/metabolism ; Biodiversity ; Biofilms ; Bone and Bones/microbiology ; Computational Biology ; *Ecosystem ; Energy Metabolism ; Eukaryotic Cells/metabolism ; Gene Library ; Genes ; Genes, Bacterial ; *Genome ; Genome, Bacterial ; *Genomics ; Molecular Sequence Data ; Operon ; Phylogeny ; Polymerase Chain Reaction ; Proteins/genetics/metabolism ; Proteome ; Seawater/*microbiology ; Sequence Analysis, DNA ; *Soil Microbiology ; Whales/*microbiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Breast cancer. Dissecting a hidden breast cancer risk (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-09-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1664-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16150987" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Anticarcinogenic Agents/therapeutic use ; Breast/*anatomy & histology/chemistry/pathology ; Breast Neoplasms/*etiology/genetics/pathology/prevention & control ; Collagen/analysis ; Connective Tissue/anatomy & histology ; DNA/analysis ; Epithelial Cells/cytology ; Ethics, Clinical ; Female ; Fibroblasts/cytology/physiology ; Genes ; Humans ; Mammography ; Middle Aged ; Models, Statistical ; Risk Factors ; Tamoxifen/therapeutic use
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Chemistry. The renaissance of natural products as drug candidates (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paterson, Ian -- Anderson, Edward A -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):451-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. ip100@cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239465" target="_blank"〉PubMed〈/a〉
    Keywords: Alkanes/chemical synthesis/chemistry/pharmacology ; Anti-Infective Agents/chemical synthesis/*chemistry/pharmacology ; Antineoplastic Agents/chemical synthesis/*chemistry/pharmacology ; Biological Products/*chemistry ; Bryostatins ; Carbamates/chemical synthesis/chemistry/pharmacology ; Clinical Trials as Topic ; Combinatorial Chemistry Techniques ; *Drug Design ; *Drug Evaluation, Preclinical ; Drug Screening Assays, Antitumor ; Evolution, Molecular ; Furans/chemistry/pharmacology ; Genetic Engineering ; Ketones/chemistry/pharmacology ; Lactones/chemical synthesis/chemistry/pharmacology ; Macrolides/chemistry/pharmacology ; Molecular Structure ; Pyrones/chemical synthesis/chemistry/pharmacology ; Structure-Activity Relationship
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    What determines species diversity? (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2005 Jul 1;309(5731):90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15994536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Biological Evolution ; *Ecosystem ; Environment ; Forecasting ; Genes ; Phylogeny ; Plants
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Altered TCR signaling from geometrically repatterned immunological synapses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: The immunological synapse is a specialized cell-cell junction that is defined by large-scale spatial patterns of receptors and signaling molecules yet remains largely enigmatic in terms of formation and function. We used supported bilayer membranes and nanometer-scale structures fabricated onto the underlying substrate to impose geometric constraints on immunological synapse formation. Analysis of the resulting alternatively patterned synapses revealed a causal relation between the radial position of T cell receptors (TCRs) and signaling activity, with prolonged signaling from TCR microclusters that had been mechanically trapped in the peripheral regions of the synapse. These results are consistent with a model of the synapse in which spatial translocation of TCRs represents a direct mechanism of signal regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mossman, Kaspar D -- Campi, Gabriele -- Groves, Jay T -- Dustin, Michael L -- GM64900/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1191-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Graduate Group, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293763" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Antigen-Presenting Cells/metabolism ; Cells, Cultured ; Lipid Bilayers ; Mice ; Models, Immunological ; Receptors, Antigen, T-Cell/chemistry/*metabolism ; *Signal Transduction ; Structure-Activity Relationship ; T-Lymphocytes/immunology/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Genetics. Zebrafish researchers hook gene for human skin color (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1754-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16357234" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; African Continental Ancestry Group/genetics ; Alanine/genetics ; Alleles ; Animals ; Antiporters/chemistry/*genetics/physiology ; Asian Continental Ancestry Group/genetics ; European Continental Ancestry Group/genetics ; Genes ; Genetic Variation ; Humans ; Mutation ; Selection, Genetic ; Skin Pigmentation/*genetics ; Threonine/genetics ; Zebrafish/*genetics ; Zebrafish Proteins/chemistry/*genetics/physiology
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    Animal evolution and the molecular signature of radiations compressed in time (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-24
    Description: The phylogenetic relationships among most metazoan phyla remain uncertain. We obtained large numbers of gene sequences from metazoans, including key understudied taxa. Despite the amount of data and breadth of taxa analyzed, relationships among most metazoan phyla remained unresolved. In contrast, the same genes robustly resolved phylogenetic relationships within a major clade of Fungi of approximately the same age as the Metazoa. The differences in resolution within the two kingdoms suggest that the early history of metazoans was a radiation compressed in time, a finding that is in agreement with paleontological inferences. Furthermore, simulation analyses as well as studies of other radiations in deep time indicate that, given adequate sequence data, the lack of resolution in phylogenetic trees is a signature of closely spaced series of cladogenetic events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rokas, Antonis -- Kruger, Dirk -- Carroll, Sean B -- New York, N.Y. -- Science. 2005 Dec 23;310(5756):1933-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Laboratory of Molecular Biology, R. M. Bock Labs, University of Wisconsin-Madison, 1525 Linden Drive, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16373569" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Computer Simulation ; DNA, Complementary ; Fungi/classification ; Genes ; Humans ; Invertebrates/classification/genetics ; Models, Biological ; Phylogeny ; Sequence Analysis, DNA ; Time
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    A molecular phylogeny for bats illuminates biogeography and the fossil record (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-01
    Description: Bats make up more than 20% of extant mammals, yet their evolutionary history is largely unknown because of a limited fossil record and conflicting or incomplete phylogenies. Here, we present a highly resolved molecular phylogeny for all extant bat families. Our results support the hypothesis that megabats are nested among four major microbat lineages, which originated in the early Eocene [52 to 50 million years ago (Mya)], coincident with a significant global rise in temperature, increase in plant diversity and abundance, and the zenith of Tertiary insect diversity. Our data suggest that bats originated in Laurasia, possibly in North America, and that three of the major microbat lineages are Laurasian in origin, whereas the fourth is Gondwanan. Combining principles of ghost lineage analysis with molecular divergence dates, we estimate that the bat fossil record underestimates (unrepresented basal branch length, UBBL) first occurrences by, on average, 73% and that the sum of missing fossil history is 61%.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teeling, Emma C -- Springer, Mark S -- Madsen, Ole -- Bates, Paul -- O'brien, Stephen J -- Murphy, William J -- N01-CO-12400/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):580-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genomic Diversity, Basic Research Program, SAIC-Frederick, Inc., National Cancer Institute, Frederick, MD 21702, USA. emma.teeling@ucd.ie〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681385" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Asia ; Bayes Theorem ; Biodiversity ; Biological Evolution ; Chiroptera/anatomy & histology/*classification/*genetics/physiology ; Echolocation ; Europe ; Flight, Animal ; *Fossils ; Genes ; Geography ; Likelihood Functions ; North America ; *Phylogeny ; Plants ; Sequence Analysis, DNA ; South America ; Temperature ; Time
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    From individual dispersal to species ranges: perspectives for a changing world (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-12
    Description: Dispersal is often risky to the individual, yet the long-term survival of populations depends on having a sufficient number of individuals that move, find each other, and locate suitable breeding habitats. This tension has consequences that rarely meet our conservation or management goals. This is particularly true in changing environments, which makes the study of dispersal urgently topical in a world plagued with habitat loss, climate change, and species introductions. Despite the difficulty of tracking mobile individuals over potentially vast ranges, recent research has revealed a multitude of ways in which dispersal evolution can either constrain, or accelerate, species' responses to environmental changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kokko, Hanna -- Lopez-Sepulcre, Andres -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Ecological and Evolutionary Dynamics, Department of Biological and Environmental Science, University of Helsinki, Post Office Box 65 (Viikinkaari 1), FIN-00014 Helsinki, Finland. hanna.kokko@helsinki.fi〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902127" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; *Animal Migration ; Animals ; Behavior, Animal ; Biological Evolution ; Cues ; *Ecosystem ; *Environment ; Genes ; Homing Behavior ; Humans ; *Movement ; Population Dynamics ; Reproduction ; Selection, Genetic
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    Voltage sensor of Kv1.2: structural basis of electromechanical coupling (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-09
    Description: Voltage-dependent ion channels contain voltage sensors that allow them to switch between nonconductive and conductive states over the narrow range of a few hundredths of a volt. We investigated the mechanism by which these channels sense cell membrane voltage by determining the x-ray crystal structure of a mammalian Shaker family potassium ion (K+) channel. The voltage-dependent K+ channel Kv1.2 grew three-dimensional crystals, with an internal arrangement that left the voltage sensors in an apparently native conformation, allowing us to reach three important conclusions. First, the voltage sensors are essentially independent domains inside the membrane. Second, they perform mechanical work on the pore through the S4-S5 linker helices, which are positioned to constrict or dilate the S6 inner helices of the pore. Third, in the open conformation, two of the four conserved Arg residues on S4 are on a lipid-facing surface and two are buried in the voltage sensor. The structure offers a simple picture of how membrane voltage influences the open probability of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, Stephen B -- Campbell, Ernest B -- Mackinnon, Roderick -- GM43949/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Aug 5;309(5736):903-8. Epub 2005 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, 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/16002579" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry ; Crystallography, X-Ray ; Electrochemistry ; Ion Channel Gating/physiology ; Membrane Potentials ; Models, Biological ; Models, Molecular ; Potassium Channels/*chemistry/*physiology ; Protein Conformation ; Protein Structure, Tertiary ; Structure-Activity Relationship
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    Biochemistry. Protein that mimics DNA helps tuberculosis bacteria resist antibiotics (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-06-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferber, Dan -- New York, N.Y. -- Science. 2005 Jun 3;308(5727):1393.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15933168" target="_blank"〉PubMed〈/a〉
    Keywords: Antitubercular Agents/antagonists & inhibitors/metabolism/*pharmacology ; Bacterial Proteins/chemistry/*physiology ; DNA Gyrase/metabolism ; DNA, Bacterial/*chemistry/metabolism ; *Drug Resistance, Bacterial ; Drug Resistance, Microbial/*physiology ; Enzyme Inhibitors ; Fluoroquinolones/antagonists & inhibitors/metabolism/*pharmacology ; *Molecular Mimicry ; Monomeric GTP-Binding Proteins ; Mycobacterium smegmatis/drug effects/genetics ; Mycobacterium tuberculosis/drug effects/*physiology ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; *Topoisomerase II Inhibitors
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    Structural bioinformatics-based design of selective, irreversible kinase inhibitors (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-28
    Description: The active sites of 491 human protein kinase domains are highly conserved, which makes the design of selective inhibitors a formidable challenge. We used a structural bioinformatics approach to identify two selectivity filters, a threonine and a cysteine, at defined positions in the active site of p90 ribosomal protein S6 kinase (RSK). A fluoromethylketone inhibitor, designed to exploit both selectivity filters, potently and selectively inactivated RSK1 and RSK2 in mammalian cells. Kinases with only one selectivity filter were resistant to the inhibitor, yet they became sensitized after genetic introduction of the second selectivity filter. Thus, two amino acids that distinguish RSK from other protein kinases are sufficient to confer inhibitor sensitivity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3641834/" 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/PMC3641834/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Michael S -- Zhang, Chao -- Shokat, Kevan M -- Taunton, Jack -- R01 GM071434-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 27;308(5726):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Chemistry and Chemical Biology, and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-2280, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919995" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; COS Cells ; *Computational Biology ; Cysteine/chemistry/metabolism ; Cytidine Deaminase/antagonists & inhibitors/chemistry/metabolism ; Enzyme Inhibitors/*chemistry/metabolism/*pharmacology ; Epidermal Growth Factor/pharmacology ; Heterocyclic Compounds, 2-Ring/chemistry/metabolism/*pharmacology ; Histones/metabolism ; Hydrophobic and Hydrophilic Interactions ; Molecular Structure ; Mutation ; Phosphorylation ; Protein Structure, Tertiary ; Ribosomal Protein S6 Kinases, 90-kDa/*antagonists & ; inhibitors/*chemistry/metabolism ; Sequence Alignment ; Serine/metabolism ; Structure-Activity Relationship ; Threonine/chemistry/metabolism
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    Cell biology. Lessons in rational drug design for protein kinases (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-05-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahn, Natalie G -- Resing, Katheryn A -- New York, N.Y. -- Science. 2005 May 27;308(5726):1266-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA. natalie.ahn@colorado.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15919981" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Alkylation ; Binding Sites ; *Computational Biology ; Cysteine/chemistry/metabolism ; *Drug Design ; Drug Resistance/genetics ; Enzyme Inhibitors/*chemistry/metabolism/*pharmacology ; Hydrophobic and Hydrophilic Interactions ; Models, Chemical ; Mutation ; Ribosomal Protein S6 Kinases, 90-kDa/*antagonists & ; inhibitors/*chemistry/metabolism ; Structure-Activity Relationship
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    Differential targeting of Gbetagamma-subunit signaling with small molecules (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-04-22
    Description: G protein betagamma subunits have potential as a target for therapeutic treatment of a number of diseases. We performed virtual docking of a small-molecule library to a site on Gbetagamma subunits that mediates protein interactions. We hypothesized that differential targeting of this surface could allow for selective modulation of Gbetagamma subunit functions. Several compounds bound to Gbetagamma subunits with affinities from 0.1 to 60 muM and selectively modulated functional Gbetagamma-protein-protein interactions in vitro, chemotactic peptide signaling pathways in HL-60 leukocytes, and opioid receptor-dependent analgesia in vivo. These data demonstrate an approach for modulation of G protein-coupled receptor signaling that may represent an important therapeutic strategy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonacci, Tabetha M -- Mathews, Jennifer L -- Yuan, Chujun -- Lehmann, David M -- Malik, Sundeep -- Wu, Dianqing -- Font, Jose L -- Bidlack, Jean M -- Smrcka, Alan V -- GM60286/GM/NIGMS NIH HHS/ -- HL-T3207949/HL/NHLBI NIH HHS/ -- HL080706/HL/NHLBI NIH HHS/ -- K05-DA00360/DA/NIDA NIH HHS/ -- R01 CA132317/CA/NCI NIH HHS/ -- R01 GM054597/GM/NIGMS NIH HHS/ -- R01 GM054597-09/GM/NIGMS NIH HHS/ -- R01 HL080706/HL/NHLBI NIH HHS/ -- R01 HL080706-10/HL/NHLBI NIH HHS/ -- R01 HL080706-11/HL/NHLBI NIH HHS/ -- T32DA07232/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):443-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627746" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics/pharmacology ; Animals ; Binding Sites ; Binding, Competitive ; Cell Line ; Computer Simulation ; Cyclohexanes/chemistry/*metabolism/*pharmacology ; Drug Evaluation, Preclinical/*methods ; Enzyme-Linked Immunosorbent Assay ; G-Protein-Coupled Receptor Kinase 2 ; GTP-Binding Protein alpha Subunits/metabolism ; GTP-Binding Protein beta Subunits/chemistry/*metabolism ; GTP-Binding Protein gamma Subunits/chemistry/*metabolism ; HL-60 Cells ; Humans ; Isoenzymes/metabolism ; Mice ; Mice, Inbred ICR ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Structure ; Morphine/pharmacology ; N-Formylmethionine Leucyl-Phenylalanine/metabolism ; Peptide Library ; Peptides/*metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Phospholipase C beta ; Protein Binding ; Protein Interaction Mapping ; *Signal Transduction ; Software ; Structure-Activity Relationship ; Type C Phospholipases/metabolism ; Xanthenes/chemistry/*metabolism/*pharmacology ; beta-Adrenergic Receptor Kinases/metabolism
    Print ISSN: 0036-8075
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    The genome of the sea urchin Strongylocentrotus purpuratus (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-11
    Description: We report the sequence and analysis of the 814-megabase genome of the sea urchin Strongylocentrotus purpuratus, a model for developmental and systems biology. The sequencing strategy combined whole-genome shotgun and bacterial artificial chromosome (BAC) sequences. This use of BAC clones, aided by a pooling strategy, overcame difficulties associated with high heterozygosity of the genome. The genome encodes about 23,300 genes, including many previously thought to be vertebrate innovations or known only outside the deuterostomes. This echinoderm genome provides an evolutionary outgroup for the chordates and yields insights into the evolution of deuterostomes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3159423/" 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/PMC3159423/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sea Urchin Genome Sequencing Consortium -- Sodergren, Erica -- Weinstock, George M -- Davidson, Eric H -- Cameron, R Andrew -- Gibbs, Richard A -- Angerer, Robert C -- Angerer, Lynne M -- Arnone, Maria Ina -- Burgess, David R -- Burke, Robert D -- Coffman, James A -- Dean, Michael -- Elphick, Maurice R -- Ettensohn, Charles A -- Foltz, Kathy R -- Hamdoun, Amro -- Hynes, Richard O -- Klein, William H -- Marzluff, William -- McClay, David R -- Morris, Robert L -- Mushegian, Arcady -- Rast, Jonathan P -- Smith, L Courtney -- Thorndyke, Michael C -- Vacquier, Victor D -- Wessel, Gary M -- Wray, Greg -- Zhang, Lan -- Elsik, Christine G -- Ermolaeva, Olga -- Hlavina, Wratko -- Hofmann, Gretchen -- Kitts, Paul -- Landrum, Melissa J -- Mackey, Aaron J -- Maglott, Donna -- Panopoulou, Georgia -- Poustka, Albert J -- Pruitt, Kim -- Sapojnikov, Victor -- Song, Xingzhi -- Souvorov, Alexandre -- Solovyev, Victor -- Wei, Zheng -- Whittaker, Charles A -- Worley, Kim -- Durbin, K James -- Shen, Yufeng -- Fedrigo, Olivier -- Garfield, David -- Haygood, Ralph -- Primus, Alexander -- Satija, Rahul -- Severson, Tonya -- Gonzalez-Garay, Manuel L -- Jackson, Andrew R -- Milosavljevic, Aleksandar -- Tong, Mark -- Killian, Christopher E -- Livingston, Brian T -- Wilt, Fred H -- Adams, Nikki -- Belle, Robert -- Carbonneau, Seth -- Cheung, Rocky -- Cormier, Patrick -- Cosson, Bertrand -- Croce, Jenifer -- Fernandez-Guerra, Antonio -- Geneviere, Anne-Marie -- Goel, Manisha -- Kelkar, Hemant -- Morales, Julia -- Mulner-Lorillon, Odile -- Robertson, Anthony J -- Goldstone, Jared V -- Cole, Bryan -- Epel, David -- Gold, Bert -- Hahn, Mark E -- Howard-Ashby, Meredith -- Scally, Mark -- Stegeman, John J -- Allgood, Erin L -- Cool, Jonah -- Judkins, Kyle M -- McCafferty, Shawn S -- Musante, Ashlan M -- Obar, Robert A -- Rawson, Amanda P -- Rossetti, Blair J -- Gibbons, Ian R -- Hoffman, Matthew P -- Leone, Andrew -- Istrail, Sorin -- Materna, Stefan C -- Samanta, Manoj P -- Stolc, Viktor -- Tongprasit, Waraporn -- Tu, Qiang -- Bergeron, Karl-Frederik -- Brandhorst, Bruce P -- Whittle, James -- Berney, Kevin -- Bottjer, David J -- Calestani, Cristina -- Peterson, Kevin -- Chow, Elly -- Yuan, Qiu Autumn -- Elhaik, Eran -- Graur, Dan -- Reese, Justin T -- Bosdet, Ian -- Heesun, Shin -- Marra, Marco A -- Schein, Jacqueline -- Anderson, Michele K -- Brockton, Virginia -- Buckley, Katherine M -- Cohen, Avis H -- Fugmann, Sebastian D -- Hibino, Taku -- Loza-Coll, Mariano -- Majeske, Audrey J -- Messier, Cynthia -- Nair, Sham V -- Pancer, Zeev -- Terwilliger, David P -- Agca, Cavit -- Arboleda, Enrique -- Chen, Nansheng -- Churcher, Allison M -- Hallbook, F -- Humphrey, Glen W -- Idris, Mohammed M -- Kiyama, Takae -- Liang, Shuguang -- Mellott, Dan -- Mu, Xiuqian -- Murray, Greg -- Olinski, Robert P -- Raible, Florian -- Rowe, Matthew -- Taylor, John S -- Tessmar-Raible, Kristin -- Wang, D -- Wilson, Karen H -- Yaguchi, Shunsuke -- Gaasterland, Terry -- Galindo, Blanca E -- Gunaratne, Herath J -- Juliano, Celina -- Kinukawa, Masashi -- Moy, Gary W -- Neill, Anna T -- Nomura, Mamoru -- Raisch, Michael -- Reade, Anna -- Roux, Michelle M -- Song, Jia L -- Su, Yi-Hsien -- Townley, Ian K -- Voronina, Ekaterina -- Wong, Julian L -- Amore, Gabriele -- Branno, Margherita -- Brown, Euan R -- Cavalieri, Vincenzo -- Duboc, Veronique -- Duloquin, Louise -- Flytzanis, Constantin -- Gache, Christian -- Lapraz, Francois -- Lepage, Thierry -- Locascio, Annamaria -- Martinez, Pedro -- Matassi, Giorgio -- Matranga, Valeria -- Range, Ryan -- Rizzo, Francesca -- Rottinger, Eric -- Beane, Wendy -- Bradham, Cynthia -- Byrum, Christine -- Glenn, Tom -- Hussain, Sofia -- Manning, Gerard -- Miranda, Esther -- Thomason, Rebecca -- Walton, Katherine -- Wikramanayke, Athula -- Wu, Shu-Yu -- Xu, Ronghui -- Brown, C Titus -- Chen, Lili -- Gray, Rachel F -- Lee, Pei Yun -- Nam, Jongmin -- Oliveri, Paola -- Smith, Joel -- Muzny, Donna -- Bell, Stephanie -- Chacko, Joseph -- Cree, Andrew -- Curry, Stacey -- Davis, Clay -- Dinh, Huyen -- Dugan-Rocha, Shannon -- Fowler, Jerry -- Gill, Rachel -- Hamilton, Cerrissa -- Hernandez, Judith -- Hines, Sandra -- Hume, Jennifer -- Jackson, Laronda -- Jolivet, Angela -- Kovar, Christie -- Lee, Sandra -- Lewis, Lora -- Miner, George -- Morgan, Margaret -- Nazareth, Lynne V -- Okwuonu, Geoffrey -- Parker, David -- Pu, Ling-Ling -- Thorn, Rachel -- Wright, Rita -- 2P42 ESO7381/PHS HHS/ -- 5 U54 HG003273/HG/NHGRI NIH HHS/ -- EY11930/EY/NEI NIH HHS/ -- F32 ESO12794/PHS HHS/ -- F32 HD047136/HD/NICHD NIH HHS/ -- F32 HD047136-02/HD/NICHD NIH HHS/ -- F32 HD047136-03/HD/NICHD NIH HHS/ -- F32-HD47136/HD/NICHD NIH HHS/ -- GM058231/GM/NIGMS NIH HHS/ -- GM070840/GM/NIGMS NIH HHS/ -- GM61005/GM/NIGMS NIH HHS/ -- GM61464/GM/NIGMS NIH HHS/ -- HD-37105/HD/NICHD NIH HHS/ -- HD039948/HD/NICHD NIH HHS/ -- HD14483/HD/NICHD NIH HHS/ -- HD66219/HD/NICHD NIH HHS/ -- P30-CA14051/CA/NCI NIH HHS/ -- R01 ES006272/ES/NIEHS NIH HHS/ -- R01 ES006272-13/ES/NIEHS NIH HHS/ -- R01 GM070840/GM/NIGMS NIH HHS/ -- R01 HD028152/HD/NICHD NIH HHS/ -- R01ES006272/ES/NIEHS NIH HHS/ -- R37-HD12896/HD/NICHD NIH HHS/ -- RR-15044/RR/NCRR NIH HHS/ -- S19916/Biotechnology and Biological Sciences Research Council/United Kingdom -- T32 GM007601/GM/NIGMS NIH HHS/ -- U54 HG003273/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):941-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095691" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcification, Physiologic ; Cell Adhesion Molecules/genetics/physiology ; Complement Activation/genetics ; Computational Biology ; Embryonic Development/genetics ; Evolution, Molecular ; Gene Expression Regulation, Developmental ; Genes ; *Genome ; Immunity, Innate/genetics ; Immunologic Factors/genetics/physiology ; Male ; Nervous System Physiological Phenomena ; Proteins/genetics/physiology ; *Sequence Analysis, DNA ; Signal Transduction ; Strongylocentrotus purpuratus/embryology/*genetics/immunology/physiology ; Transcription Factors/genetics
    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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    The late Miocene radiation of modern Felidae: a genetic assessment (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-01-10
    Description: Modern felid species descend from relatively recent (〈11 million years ago) divergence and speciation events that produced successful predatory carnivores worldwide but that have confounded taxonomic classifications. A highly resolved molecular phylogeny with divergence dates for all living cat species, derived from autosomal, X-linked, Y-linked, and mitochondrial gene segments (22,789 base pairs) and 16 fossil calibrations define eight principal lineages produced through at least 10 intercontinental migrations facilitated by sea-level fluctuations. A ghost lineage analysis indicates that available felid fossils underestimate (i.e., unrepresented basal branch length) first occurrence by an average of 76%, revealing a low representation of felid lineages in paleontological remains. The phylogenetic performance of distinct gene classes showed that Y-chromosome segments are appreciably more informative than mitochondrial DNA, X-linked, or autosomal genes in resolving the rapid Felidae species radiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Warren E -- Eizirik, Eduardo -- Pecon-Slattery, Jill -- Murphy, William J -- Antunes, Agostinho -- Teeling, Emma -- O'Brien, Stephen J -- N01-CO-12400/CO/NCI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):73-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genomic Diversity, National Cancer Institute, Frederick, MD 21702-1201, USA. johnsonw@ncifcrf.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400146" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Americas ; Animals ; Asia ; *Biological Evolution ; Cats/classification/genetics ; DNA/genetics ; DNA, Mitochondrial/genetics ; Europe ; Felidae/*classification/*genetics ; Felis/classification/genetics ; Fossils ; Genes ; *Genetic Speciation ; Lynx/classification/genetics ; Panthera/classification/genetics ; Phylogeny ; Puma/classification/genetics ; X Chromosome/genetics ; Y Chromosome/genetics
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    Evolution. Spider genes and fossils spin tales of the original worldwide web (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1730.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794049" target="_blank"〉PubMed〈/a〉
    Keywords: *Amber ; Animals ; *Biological Evolution ; DNA, Complementary ; Fibroins/*genetics ; *Fossils ; Genes ; *Silk/genetics ; *Spiders/genetics/physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Pharmacology. Hitting the hot spots of cell signaling cascades (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tesmer, John Joseph Grubb -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):377-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109, USA. tesmerjj@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627730" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Site ; Animals ; Binding Sites ; Computer Simulation ; Drug Design ; Drug Evaluation, Preclinical/*methods ; GTP-Binding Protein alpha Subunits/metabolism ; GTP-Binding Protein beta Subunits/chemistry/*metabolism ; GTP-Binding Protein gamma Subunits/chemistry/*metabolism ; Models, Molecular ; Peptide Library ; Peptides/*metabolism ; Protein Binding ; *Signal Transduction ; Software ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 42
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    Evolution. Two rapidly evolving genes spell trouble for hybrids (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1238-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124304" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Copepoda/genetics ; Crosses, Genetic ; Drosophila/*genetics ; Drosophila melanogaster/genetics ; *Evolution, Molecular ; Genes ; Genes, Insect ; Genes, Plant ; *Genetic Speciation ; *Hybridization, Genetic ; Mimulus/genetics ; Mutation ; *Selection, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 43
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    Sponge paleogenomics reveals an ancient role for carbonic anhydrase in skeletogenesis (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-06-02
    Description: Sponges (phylum Porifera) were prolific reef-building organisms during the Paleozoic and Mesozoic approximately 542 to 65 million years ago. These ancient animals inherited components of the first multicellular skeletogenic toolkit from the last common ancestor of the Metazoa. Using a paleogenomics approach, including gene- and protein-expression techniques and phylogenetic reconstruction, we show that a molecular component of this toolkit was the precursor to the alpha-carbonic anhydrases (alpha-CAs), a gene family used by extant animals in a variety of fundamental physiological processes. We used the coralline demosponge Astrosclera willeyana, a "living fossil" that has survived from the Mesozoic, to provide insight into the evolution of the ability to biocalcify, and show that the alpha-CA family expanded from a single ancestral gene through several independent gene-duplication events in sponges and eumetazoans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jackson, Daniel J -- Macis, Luciana -- Reitner, Joachim -- Degnan, Bernard M -- Worheide, Gert -- New York, N.Y. -- Science. 2007 Jun 29;316(5833):1893-5. Epub 2007 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geoscience Centre Gottingen, Department of Geobiology, Goldschmidtstrasse 3, D-37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540861" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bicarbonates/metabolism ; *Calcification, Physiologic ; Calcium Carbonate/analysis/metabolism ; Carbonic Anhydrases/chemistry/*genetics/*metabolism ; Computational Biology ; Evolution, Molecular ; Gene Duplication ; Genes ; Genomics ; Molecular Sequence Data ; Porifera/anatomy & histology/enzymology/*genetics/*physiology ; Recombinant Proteins/chemistry/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-11-03
    Description: Quinoxalinedione compounds such as 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) are the most commonly used alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor antagonists. However, we find that in the presence of transmembrane AMPA receptor regulatory proteins (TARPs), which are AMPA receptor auxiliary subunits, CNQX acts as a partial agonist. CNQX induced small depolarizing currents in neurons of the central nervous system, and reconstitution of this agonist activity required coexpression of TARPs. A crystal structure of CNQX bound to the TARP-less AMPA receptor ligand-binding domain showed that, although CNQX induces partial domain closure, this movement is not transduced into linker separation, suggesting that TARPs may increase agonist efficacy by strengthening the coupling between domain closure and channel opening. Our results demonstrate that the presence of an auxiliary subunit can determine whether a compound functions as an agonist or antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Menuz, Karen -- Stroud, Robert M -- Nicoll, Roger A -- Hays, Franklin A -- GM078754/GM/NIGMS NIH HHS/ -- P50 GM73210/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 2;318(5851):815-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17975069" target="_blank"〉PubMed〈/a〉
    Keywords: 6-Cyano-7-nitroquinoxaline-2,3-dione/chemistry/*pharmacology ; Animals ; Benzodiazepines/pharmacology ; Binding, Competitive ; Cell Line ; Cerebellum/cytology ; Crystallography, X-Ray ; *Drug Partial Agonism ; Hippocampus/cytology ; Humans ; In Vitro Techniques ; Interneurons/drug effects ; Mice ; Models, Molecular ; Patch-Clamp Techniques ; Protein Conformation ; Protein Subunits/*physiology ; Pyramidal Cells/drug effects/metabolism ; Quinoxalines/pharmacology ; Receptors, AMPA/*agonists/*antagonists & inhibitors ; Structure-Activity Relationship ; Synaptic Transmission/drug effects ; Trichlormethiazide/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Buddenbrockia is a cnidarian worm (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-07-07
    Description: A major evolutionary divide occurs in the animal kingdom between the so-called radially symmetric animals, which includes the cnidarians, and the bilaterally symmetric animals, which includes all worm phyla. Buddenbrockia plumatellae is an active, muscular, parasitic worm that belongs to the phylum Myxozoa, a group of morphologically simplified microscopic endoparasites that has proved difficult to place phylogenetically. Phylogenetic analyses of multiple protein-coding genes demonstrate that Buddenbrockia is a cnidarian. This active muscular worm increases the known diversity in cnidarian body plans and demonstrates that a muscular, wormlike form can evolve in the absence of overt bilateral symmetry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jimenez-Guri, Eva -- Philippe, Herve -- Okamura, Beth -- Holland, Peter W H -- New York, N.Y. -- Science. 2007 Jul 6;317(5834):116-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, South Parks Road, Oxford OX1 3PS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17615357" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Cnidaria/anatomy & histology/*classification/*genetics/physiology ; DNA, Ribosomal/genetics ; Genes ; Genes, Homeobox ; Locomotion ; Molecular Sequence Data ; Muscles/anatomy & histology/ultrastructure ; *Phylogeny ; Polymerase Chain Reaction ; Proteins/genetics
    Print ISSN: 0036-8075
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    Cell biology: Shinya Yamanaka: modest researcher, results to brag about (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2008 Feb 1;319(5863):562. doi: 10.1126/science.319.5863.562.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18239101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biomedical Research/economics ; *Cellular Reprogramming ; Embryonic Stem Cells/cytology/physiology ; Genes ; History, 21st Century ; Humans ; Japan ; Mice ; *Pluripotent Stem Cells/cytology/physiology ; Research Support as Topic ; Skin/cytology
    Print ISSN: 0036-8075
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    Chemistry. An enlightening structure-function relationship (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armitage, Bruce A -- Berget, Peter B -- New York, N.Y. -- Science. 2008 Feb 29;319(5867):1195-6. doi: 10.1126/science.1155093.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Molecular Biosensor and Imaging Center (MBIC), Carnegie Mellon University, Pittsburgh, PA 15213, USA. army@cmu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18309067" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Antibodies, Monoclonal/*chemistry/genetics ; Antigen-Antibody Complex ; Binding Sites, Antibody ; Crystallization ; Fluorescence ; Fluorescent Dyes ; Hydrophobic and Hydrophilic Interactions ; Luminescence ; Molecular Structure ; Mutation ; Protein Conformation ; Spectrometry, Fluorescence ; Stilbenes/*chemistry/immunology ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
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    The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-10-04
    Description: The adenosine class of heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) mediates the important role of extracellular adenosine in many physiological processes and is antagonized by caffeine. We have determined the crystal structure of the human A2A adenosine receptor, in complex with a high-affinity subtype-selective antagonist, ZM241385, to 2.6 angstrom resolution. Four disulfide bridges in the extracellular domain, combined with a subtle repacking of the transmembrane helices relative to the adrenergic and rhodopsin receptor structures, define a pocket distinct from that of other structurally determined GPCRs. The arrangement allows for the binding of the antagonist in an extended conformation, perpendicular to the membrane plane. The binding site highlights an integral role for the extracellular loops, together with the helical core, in ligand recognition by this class of GPCRs and suggests a role for ZM241385 in restricting the movement of a tryptophan residue important in the activation mechanism of the class A receptors.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2586971/" 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/PMC2586971/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaakola, Veli-Pekka -- Griffith, Mark T -- Hanson, Michael A -- Cherezov, Vadim -- Chien, Ellen Y T -- Lane, J Robert -- Ijzerman, Adriaan P -- Stevens, Raymond C -- GM075915/GM/NIGMS NIH HHS/ -- P50 GM073197/GM/NIGMS NIH HHS/ -- P50 GM073197-04/GM/NIGMS NIH HHS/ -- R01 GM089857/GM/NIGMS NIH HHS/ -- U54 GM074961/GM/NIGMS NIH HHS/ -- U54 GM074961-04/GM/NIGMS NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Nov 21;322(5905):1211-7. doi: 10.1126/science.1164772. Epub 2008 Oct 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037 USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18832607" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine A2 Receptor Antagonists ; Animals ; Binding Sites ; Crystallography, X-Ray ; Humans ; Ligands ; Protein Binding ; Protein Conformation ; Receptor, Adenosine A2A/*chemistry ; Structure-Activity Relationship ; Triazines/chemistry ; Triazoles/chemistry ; Tryptophan/chemistry ; Turkeys
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    Genome sequence, comparative analysis, and population genetics of the domestic horse (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-11-07
    Description: We report a high-quality draft sequence of the genome of the horse (Equus caballus). The genome is relatively repetitive but has little segmental duplication. Chromosomes appear to have undergone few historical rearrangements: 53% of equine chromosomes show conserved synteny to a single human chromosome. Equine chromosome 11 is shown to have an evolutionary new centromere devoid of centromeric satellite DNA, suggesting that centromeric function may arise before satellite repeat accumulation. Linkage disequilibrium, showing the influences of early domestication of large herds of female horses, is intermediate in length between dog and human, and there is long-range haplotype sharing among breeds.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3785132/" 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/PMC3785132/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wade, C M -- Giulotto, E -- Sigurdsson, S -- Zoli, M -- Gnerre, S -- Imsland, F -- Lear, T L -- Adelson, D L -- Bailey, E -- Bellone, R R -- Blocker, H -- Distl, O -- Edgar, R C -- Garber, M -- Leeb, T -- Mauceli, E -- MacLeod, J N -- Penedo, M C T -- Raison, J M -- Sharpe, T -- Vogel, J -- Andersson, L -- Antczak, D F -- Biagi, T -- Binns, M M -- Chowdhary, B P -- Coleman, S J -- Della Valle, G -- Fryc, S -- Guerin, G -- Hasegawa, T -- Hill, E W -- Jurka, J -- Kiialainen, A -- Lindgren, G -- Liu, J -- Magnani, E -- Mickelson, J R -- Murray, J -- Nergadze, S G -- Onofrio, R -- Pedroni, S -- Piras, M F -- Raudsepp, T -- Rocchi, M -- Roed, K H -- Ryder, O A -- Searle, S -- Skow, L -- Swinburne, J E -- Syvanen, A C -- Tozaki, T -- Valberg, S J -- Vaudin, M -- White, J R -- Zody, M C -- Broad Institute Genome Sequencing Platform -- Broad Institute Whole Genome Assembly Team -- Lander, E S -- Lindblad-Toh, K -- 098051/Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Nov 6;326(5954):865-7. doi: 10.1126/science.1178158.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Broad Institute, 7 Cambridge Center, Cambridge, MA 02142, USA. c.wade@usyd.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19892987" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic/genetics ; Centromere/genetics ; Chromosome Mapping ; Chromosomes, Mammalian/*genetics ; Computational Biology ; DNA Copy Number Variations ; Dogs ; Evolution, Molecular ; Female ; Genes ; *Genome ; Haplotypes ; Horses/*genetics ; Humans ; Molecular Sequence Data ; Phylogeny ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Synteny
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    Understanding human origins (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-10-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alberts, Bruce -- New York, N.Y. -- Science. 2009 Oct 2;326(5949):17. doi: 10.1126/science.1182387.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19797627" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Genes ; *Hominidae/genetics ; Humans
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    Genomics. Green evolution, green revolution (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Archibald, John M -- New York, N.Y. -- Science. 2009 Apr 10;324(5924):191-2. doi: 10.1126/science.1172972.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Canadian Institute for Advanced Research, Program in Integrated Microbial Biodiversity, Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada. john.archibald@dal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19359572" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Chlorophyta/classification/cytology/*genetics/physiology ; Gene Transfer, Horizontal ; Genes ; *Genome ; Introns ; Meiosis/genetics ; Photosynthesis/*genetics ; Plants/*genetics ; Sequence Analysis, DNA ; Transcription Factors/genetics
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    Genomic footprints of a cryptic plastid endosymbiosis in diatoms (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-06-27
    Description: Diatoms and other chromalveolates are among the dominant phytoplankters in the world's oceans. Endosymbiosis was essential to the success of chromalveolates, and it appears that the ancestral plastid in this group had a red algal origin via an ancient secondary endosymbiosis. However, recent analyses have turned up a handful of nuclear genes in chromalveolates that are of green algal derivation. Using a genome-wide approach to estimate the "green" contribution to diatoms, we identified 〉1700 green gene transfers, constituting 16% of the diatom nuclear coding potential. These genes were probably introduced into diatoms and other chromalveolates from a cryptic endosymbiont related to prasinophyte-like green algae. Chromalveolates appear to have recruited genes from the two major existing algal groups to forge a highly successful, species-rich protist lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moustafa, Ahmed -- Beszteri, Bank -- Maier, Uwe G -- Bowler, Chris -- Valentin, Klaus -- Bhattacharya, Debashish -- R01ES013679/ES/NIEHS NIH HHS/ -- T32 GM98629/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Jun 26;324(5935):1724-6. doi: 10.1126/science.1172983.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Interdisciplinary Program in Genetics, University of Iowa, Iowa City, IA 52242, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19556510" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Evolution ; Cell Nucleus/genetics ; Chlorophyta/classification/*genetics/physiology ; Diatoms/classification/*genetics/physiology ; Gene Transfer, Horizontal ; Genes ; *Genome ; Phylogeny ; Plastids/*genetics ; Rhodophyta/classification/*genetics/physiology ; *Symbiosis
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    Evidence for ecological speciation and its alternative (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-02-07
    Description: Natural selection commonly drives the origin of species, as Darwin initially claimed. Mechanisms of speciation by selection fall into two broad categories: ecological and mutation-order. Under ecological speciation, divergence is driven by divergent natural selection between environments, whereas under mutation-order speciation, divergence occurs when different mutations arise and are fixed in separate populations adapting to similar selection pressures. Tests of parallel evolution of reproductive isolation, trait-based assortative mating, and reproductive isolation by active selection have demonstrated that ecological speciation is a common means by which new species arise. Evidence for mutation-order speciation by natural selection is more limited and has been best documented by instances of reproductive isolation resulting from intragenomic conflict. However, we still have not identified all aspects of selection, and identifying the underlying genes for reproductive isolation remains challenging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schluter, Dolph -- New York, N.Y. -- Science. 2009 Feb 6;323(5915):737-41. doi: 10.1126/science.1160006.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodiversity Research Centre and Zoology Department, University of British Columbia, Vancouver, BC V6T 1Z4, Canada. schluter@zoology.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19197053" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; Biological Evolution ; *Ecosystem ; Genes ; *Genetic Speciation ; Genetic Variation ; Models, Biological ; Models, Genetic ; *Mutation ; Phenotype ; Plants/genetics ; Quantitative Trait Loci ; Reproduction ; *Selection, Genetic
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
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    Three-dimensional molecular modeling and drug design (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-06-27
    Description: A discussion of drug-receptor theory is used to show that the three-dimensional structure, or shape, of molecules is important for biological activity. The computer-assisted molecular modeling system at Merck is described, and it is shown that this system is useful for generating and storing molecular structures, determining preferred conformation, comparing molecular shapes, and computing molecular properties. Applications of the system to the study of anti-inflammatory drugs, somatostatin-like compounds, and dihydrofolate reductase inhibitors are summarized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gund, P -- Andose, J D -- Rhodes, J B -- Smith, G M -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1425-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6104357" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonic Acids ; Binding Sites ; Computers ; Cyclooxygenase Inhibitors ; Humans ; Indomethacin ; *Models, Molecular ; *Models, Structural ; *Molecular Conformation ; *Pharmaceutical Preparations ; Receptors, Drug/metabolism ; Somatostatin/analogs & derivatives ; Structure-Activity Relationship
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    Allele increasing susceptibility to human breast cancer may be linked to the glutamate-pyruvate transaminase locus (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-04-25
    Description: The patterns of the occurrence of breast cancer in 11 high-risk families were evaluated by segregation and linkage analysis. These patterns were consistent with the hypothesis that increased susceptibility to breast cancer was inherited as an autosomal dominant allele with high penetrance in women. The postulated susceptibility allele in these families may be chromosomally linked to the glutamate-pyruvate transaminase (E.C. 2.6.1.2, alanine aminotransferase) locus. Confirmation of this linkage in other families would establish the existence of a gene increasing susceptibility to breast cancer. Since there is no association in the general population between a woman's glutamate-pyruvate transaminase genotype and her cancer risk, the glutamate-pyruvate transaminase linkage cannot be used as a screening test for breast cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, M C -- Go, R C -- Elston, R C -- Lynch, H T -- Petrakis, N L -- New York, N.Y. -- Science. 1980 Apr 25;208(4442):406-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367867" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine Transaminase/*genetics ; Alleles ; Breast Neoplasms/*genetics/transmission ; Female ; Genes ; Genetic Linkage ; Humans ; Pedigree ; X Chromosome
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    Tooth induction in chick epithelium: expression of quiescent genes for enamel synthesis (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-02-29
    Description: Intraocular grafts of chick epithelium combined with mouse molar mesenchyme produced a variety of dental structures including perfectly formed crowns with differentiated ameloblasts depositing enamel matrix. The results suggest that the loss of teeth in Aves did not result from a loss of genetic coding for enamel synthesis in the oral epithelium but from an alteration in the tissue interactions requisite for odontogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kollar, E J -- Fisher, C -- New York, N.Y. -- Science. 1980 Feb 29;207(4434):993-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352302" target="_blank"〉PubMed〈/a〉
    Keywords: *Amelogenesis ; Animals ; Chick Embryo/*cytology ; Culture Techniques ; Dental Enamel Proteins/*biosynthesis/genetics ; Embryonic Induction ; Epithelial Cells ; Genes ; Mandible/cytology ; Mesoderm/cytology ; Mice ; *Odontogenesis
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    Immunoglobulin gene rearrangement in immature B cells (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Two types of immature B cells, namely fetal liver hybridomas and the leukemic cell line 70Z/3, both of which have cytoplasmic mu chains but no light chains, were examined for DNA rearrangements of their light chain and heavy chain immunoglobulin genes. In the fetal liver hybridomas, which were constructed from fetal liver cells and a tumor cell, no light chain gene rearrangement was observed, whereas in the 70Z/3 cell line a kappa light chain rearrangement probably occurred. The results suggest that, although the lack of light chain synthesis can be due to a lack of gene rearrangement, there may also be transcriptional regulation, which may also be important for the expression of light chain immunoglobulins in immature B cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maki, R -- Kearney, J -- Paige, C -- Tonegawa, S -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1366-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6774416" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Genes ; Hybrid Cells/immunology ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin kappa-Chains/*genetics ; Immunoglobulin mu-Chains/*genetics ; Leukemia, Experimental/*immunology ; Liver/*embryology ; Mice ; Recombination, Genetic ; Transcription, Genetic
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    Vesicle targeting: timed release and specificity for leukocytes in mice by subcutaneous injection (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-01-18
    Description: When unilamellar vesicles were administered subcutaneously in mice, the half-time for the destruction of the vesicles varied from 12 to 600 hours, depending on their composition. The vesicles tested consisted of distearoyl phosphatidylcholine, cholesterol, and certain sugar and amino-sugar derivatives of cholesterol. Vesicle with amino-sugar derivatives showed the greatest longevity and became localized with high specificity in aggregates of polymorphonuclear leukocytes. A substantial delay between the time that the vesicles broke open and the time that labels contained in the vesicles were excreted suggests that the vesicles undergo endocytosis before destruction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mauk, M R -- Gamble, R C -- Baldeschwieler, J D -- New York, N.Y. -- Science. 1980 Jan 18;207(4428):309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7350660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cholesterol/analogs & derivatives ; Endocytosis ; Liposomes/*therapeutic use ; Lysosomes/metabolism ; Metabolic Clearance Rate ; Mice ; Neutrophils/*metabolism ; Phosphatidylcholines ; Structure-Activity Relationship
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    Regression of tumors in guinea pigs after treatment with synthetic muramyl dipeptides and trehalose dimycolate (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-04-25
    Description: A high incidence of tumor regression was observed in guinea pigs bearing transplantable, line-10 hepatocellular carcinomas when synthetic muramyl dipeptides combined with trehalose dimycolate in oil-in-water emulsions were injected directly into the tumors. These compounds are promising candidates to replace viable bacillus Calmette-Guerin in cancer immunotherapy in humans and animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McLaughlin, C A -- Schwartzman, S M -- Horner, B L -- Jones, G H -- Moffatt, J G -- Nestor, J J Jr -- Tegg, D -- New York, N.Y. -- Science. 1980 Apr 25;208(4442):415-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7189295" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylmuramyl-Alanyl-Isoglutamine/administration & dosage/*therapeutic use ; Animals ; Cord Factors/administration & dosage/*therapeutic use ; Drug Combinations ; Emulsions ; Glycolipids/*therapeutic use ; Glycopeptides/*therapeutic use ; Immunotherapy ; Liver Neoplasms, Experimental/*therapy ; Lymphatic Metastasis ; Structure-Activity Relationship
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    J genes for heavy chain immunoglobulins of mouse (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-05
    Description: A 15,8-kilobase pair fragment of BALB/c mouse liver DNA, cloned in the Charon 4A lambda phage vector system, was shown to contain the mu heavy chain constant region (CHmu) gene for the mouse immunoglobulin M. In addition, this fragment of DNA contains at least two J genes, used to code for the carboxyl terminal portion of heavy chain variable regions. These genes are located in genomic DNA about eight kilobase pairs to the 5' side of the CHmu gene. The complete nucleotide sequence of a 1120-base pair stretch of DNA that includes the two J genes has been determined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newell, N -- Richards, J E -- Tucker, P W -- Blattner, F R -- New York, N.Y. -- Science. 1980 Sep 5;209(4461):1128-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6250219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites, Antibody/*genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; Genes ; Genetic Linkage ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulin mu-Chains/*genetics ; Mice
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    Gene affecting superoxide dismutase activity linked to the histocompatibility complex in H-2 congenic mice (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-01-04
    Description: The activity of cyanide-sensitive, Cu-Zn superoxide dismutase (SOD) was studied in liver sytosols from H-2 congenic strains of mice. Higher SOD activity was found in livers of mice having H-2b/A.BY, B10, and C3H.SW/haplotypes than in those of H-2a, H-2k and H-2d haplotypes. Segregation studies supported these correlations. In H-2 recombinant strains of mice, the genes influencing the liver SOD activity occur, as ascertained by mapping techniques, at or near the H-2d region of the major histocompatibility complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Novak, R -- Bosze, Z -- Matkovics, B -- Fachet, J -- New York, N.Y. -- Science. 1980 Jan 4;207(4426):86-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7350646" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Genes ; Genes, Regulator ; Genetic Linkage ; H-2 Antigens/*genetics ; Liver/enzymology ; *Major Histocompatibility Complex ; Mice ; Superoxide Dismutase/*genetics
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    Altering genotype and phenotype by DNA-mediated gene transfer (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: Transformation, or DNA-mediated gene transfer, permits the introduction of new genetic information into a cell and frequently results in a change in phenotype. The transforming DNA is ultimately integrated into a recipient cell chromosome. No unique chromosomal locations are apparent, different lines contain the transforming DNA on different chromosomes. Expression of transformed genes frequently results in the synthesis of new polypeptide products which restore appropriate mutant cells to the wild-type phenotype. Thus transformation provides an in vivo assay for the functional role of DNA sequence organization about specific genes. Transforming genes coding for selectable functions, such as adenine phosphoribosyltransferase or thymidine kinase, have now been isolated by utilizing transformation in concert with molecular cloning. Finally, transformation may provide a general approach to the analysis of complex heritable phenotypes by permitting the distinction between phenotypic changes without concomitant changes in DNA and functional genetic rearrangements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellicer, A -- Robins, D -- Wold, B -- Sweet, R -- Jackson, J -- Lowy, I -- Roberts, J M -- Sim, G K -- Silverstein, S -- Axel, R -- CA 16346/CA/NCI NIH HHS/ -- CA 17477/CA/NCI NIH HHS/ -- CA 23767/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1414-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7414320" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Phosphoribosyltransferase/*genetics ; Cloning, Molecular/methods ; DNA/*genetics ; *DNA, Recombinant ; Genes ; Genotype ; Mutation ; Pentosyltransferases/*genetics ; Phenotype ; Recombination, Genetic ; Selection, Genetic ; Thymidine Kinase/*genetics ; *Transformation, Genetic
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    Regional assignment of genes for human esterase D and retinoblastoma to chromosome band 13q14 (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-30
    Description: The expression of human esterase D was evaluated quantitatively and qualitatively in five persons with partial deletions or duplications of chromosome 13. The results showed that the locus of this enzyme is at band 13q14. Deletion of this same band in other subjects has been found previously to indicate a predisposition to the development of retinoblastoma, which was present in the four individuals in this study who had partial deletions of chromosome 13. Because of this close synteny, esterase D evaluation should aid in the diagnosis and genetic counseling of retinoblastoma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sparkes, R S -- Sparkes, M C -- Wilson, M G -- Towner, J W -- Benedict, W -- Murphree, A L -- Yunis, J J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1042-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375916" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Deletion ; Chromosome Mapping ; *Chromosomes, Human, 13-15 ; Esterases/*genetics ; Female ; Genes ; Humans ; Intellectual Disability/enzymology/genetics ; Male ; Retinoblastoma/enzymology/*genetics
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    Stereospecific nicotine receptors on rat brain membranes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-07
    Description: A stereospecific binding site for nicotine has been detected on rat brain membranes. Competition studies with cholinergic agonists suggest that this site is a nicotinic cholinergic receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romano, C -- Goldstein, A -- DA-1938/DA/NIDA NIH HHS/ -- DA-7063/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):647-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7433991" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Brain/*metabolism ; Ligands ; Male ; Nicotine/metabolism ; Rats ; Receptors, Cholinergic/*metabolism ; Receptors, Nicotinic/*metabolism ; Stereoisomerism ; Structure-Activity Relationship ; Synaptic Membranes/metabolism
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    Directed deletion of a yeast transfer RNA intervening sequence (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Many eukaryotic genes contain intevening sequences, segments of DNA that interrupt the continuity of the gene. They are removed from RNA transcripts of the gene by a process known as splicing. The intervening sequence in a yeast tyrosine transfer RNA (tRNA Tyr) suppressor gene was deleted in order to test its role in the expression of the gene. The altered gene and its parent were introduced into yeast by transformation. Both genes exhibited suppressor function, showing that the intervening sequence is not absolutely essential for the expression of this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, R B -- Johnson, P F -- Tanaka, S -- Schold, M -- Itakura, K -- Abelson, J -- CA10984/CA/NCI NIH HHS/ -- GM 26391/GM/NIGMS NIH HHS/ -- GM 35658/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1396-400.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6997991" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; DNA, Recombinant ; Genes ; Mutation ; Nucleic Acid Precursors/genetics ; Plasmids ; RNA, Fungal/*genetics ; RNA, Transfer/*genetics ; Saccharomyces cerevisiae/genetics ; Suppression, Genetic ; Tyrosine
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    GABA analogues activate channels of different duration on cultured mouse spinal neurons (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-04-17
    Description: Voltage-clamp recordings from mouse spinal neurons grown in culture were used to study the membrane current fluctuations induced by 12 substances structurally similar to gamma-aminobutyric acid (GABA). Fluctuation analysis provided estimates of the electrical properties of the elementary events underlying these responses. Estimates of the mean conductance of channels activated by all of the substances except glycine did not differ significantly from that estimated for GABA, whereas mean durations of agonist-activated channels all differed significantly from that found for GABA. The results indicate that all of the substances tested except glycine activate channels of similar conductance but of different durations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, J L -- Mathers, D A -- New York, N.Y. -- Science. 1981 Apr 17;212(4492):358-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6259733" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/drug effects ; Ion Channels/*drug effects ; Membrane Potentials/drug effects ; Mice ; Neurons/drug effects ; Receptors, Cell Surface/metabolism ; Receptors, GABA-A ; Spinal Nerves/*drug effects ; Structure-Activity Relationship ; Time Factors ; gamma-Aminobutyric Acid/*analogs & derivatives/pharmacology
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    The major histocompatibility complex in man (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-09-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dausset, J -- New York, N.Y. -- Science. 1981 Sep 25;213(4515):1469-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6792704" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Surface/genetics ; Forecasting ; Genes ; Genes, MHC Class II ; Genetic Linkage ; HLA Antigens/genetics ; Humans ; Immune Tolerance ; Immunity, Cellular ; *Major Histocompatibility Complex ; Polymorphism, Genetic ; Transplantation Immunology
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    Multiple opiate receptors: alcohol selectively inhibits binding to delta receptors (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-23
    Description: The addition of ethanol or other aliphatic alcohols to rat brain membranes strongly inhibits binding of enkephalins at concentrations at which little inhibition of opiate alkaloids is seen. Inhibition is reversible, and potency increases with chain length of the alcohol. The results suggest that delta receptors are considerably more sensitive to alcohols than mu receptors. This is the first demonstration of selective inhibition of one of the postulated classes of opiate receptors by a reagent that is not a ligand for the receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hiller, J M -- Angel, L M -- Simon, E J -- DA-00017/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):468-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6270788" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohols/*pharmacology ; Animals ; Brain/metabolism ; Cells, Cultured ; In Vitro Techniques ; Neuroblastoma/metabolism ; Rats ; Receptors, Opioid/classification/*drug effects/metabolism ; Structure-Activity Relationship
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    Insulin as a potent, specific growth factor in a rat hepatoma cell line (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-02-27
    Description: A line or rat hepatoma cells in culture which, in response to serum starvation, become arrested in the early G1 phase of growth, can be stimulated by insulin alone to enter the cell cycle and traverse S phase. A half-maximum response is observed at 30 to 70 picomolar concentrations and the maximum response is essentially identical to that found with optimum serum concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koontz, J W -- Iwahashi, M -- AM 24047/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Feb 27;211(4485):947-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7008195" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle/drug effects ; Cell Division/drug effects ; Cell Line ; *Growth Substances ; Insulin/*pharmacology ; Liver Neoplasms, Experimental/*pathology ; Mitosis/drug effects ; Proinsulin/pharmacology ; Rats ; Structure-Activity Relationship
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    Rational approaches to chemotherapy: antisickling agents (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klotz, I M -- Haney, D N -- King, L C -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):724-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256275" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*drug therapy ; Aspirin/analogs & derivatives/therapeutic use ; Chemical Phenomena ; Chemistry ; *Hemoglobin, Sickle ; Humans ; Protein Binding/drug effects ; Protein Conformation ; Salicylates/*therapeutic use ; Solubility ; Structure-Activity Relationship
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    Do jumping genes make evolutionary leaps? (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):634-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256261" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; DNA/*genetics ; Genes ; Recombination, Genetic
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    Asbestos surface charge heterogeneity and biological effects (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-09-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Light, W G -- New York, N.Y. -- Science. 1981 Sep 25;213(4515):1534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7280676" target="_blank"〉PubMed〈/a〉
    Keywords: *Asbestos ; Humans ; Occupational Diseases/chemically induced ; Structure-Activity Relationship
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    Growth inhibition by adenosine 3',5-monophosphate derivatives does not require 3',5' phosphodiester linkage (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-09-04
    Description: Analogs of adenosine 3',5'-monophosphate (cyclic AMP) inhibit the growth of cultured cell lines. The effects of 8-bromo- and N6-butyryl-substituted analogs of cyclic and noncyclic AMP on six cell lines were examined and were equally inhibitory. Variant cell lines with altered cyclic AMP-dependent protein kinase were more resistant to both cyclic and noncyclic nucleotides. We conclude that growth inhibition by analogs of cyclic AMP (i) does not require a 3',5' phosphodiester bond and (ii) may be mediated by a pathway involving endogenous cyclic AMP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, T F -- Kowalchyk, J A -- AM 25861/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Sep 4;213(4512):1120-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6267695" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/*drug effects ; Cell Line ; Cricetinae ; Cyclic AMP/*pharmacology ; DNA/biosynthesis ; Growth Inhibitors/*pharmacology ; Mice ; Phosphodiesterase Inhibitors/pharmacology ; Structure-Activity Relationship
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    A new wave of antibiotics builds (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H -- New York, N.Y. -- Science. 1981 Dec 11;214(4526):1225-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7302591" target="_blank"〉PubMed〈/a〉
    Keywords: *Cephalosporins/therapeutic use ; Humans ; Research ; Structure-Activity Relationship ; United States
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    Thymosin stimulates secretion of luteinizing hormone-releasing factor (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-11-06
    Description: Partially purified thymosin fraction 5 and one of its synthetic peptide components, thymosin beta 4, but not thymosin alpha 1, stimulated secretion of luteinizing hormone--releasing factor from superfused medial basal hypothalami from random cycling female rats. In addition, luteinizing hormone was released from pituitary glands superfused in sequence with hypothalami. No release of luteinizing hormone in response to thymosin was observed from pituitaries superfused alone. These data provide the first evidence of a direct effect of the endocrine thymus on the hypothalamus and suggest a potentially important role for thymic peptides in reproductive function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rebar, R W -- Miyake, A -- Low, T L -- Goldstein, A L -- AG-01531/AG/NIA NIH HHS/ -- HD-12303/HD/NICHD NIH HHS/ -- HD-14362/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1981 Nov 6;214(4521):669-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7027442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Gonadotropin-Releasing Hormone/*secretion ; Hormones/pharmacology ; Hypothalamo-Hypophyseal System/drug effects ; Hypothalamus/*drug effects ; Peptide Fragments/pharmacology ; Rats ; Structure-Activity Relationship ; Thymosin/*pharmacology ; Thymus Hormones/*pharmacology
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    Didemnins: antiviral and antitumor depsipeptides from a caribbean tunicate (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-05-22
    Description: Extracts of samples of a Caribbean tunicate (ascidian, sea squirt) of the family Didemnidae inhibit in vitro at low concentrations the growth of DNA and RNA viruses as well as L1210 leukemic cells. The active compounds isolated from the tunicate, didemnins A, B, and C, are depsipeptides, and didemnin B (a derivative of didemnin A) is the component active at the lowest concentration in inhibiting viral replication in vitro and P388 leukemia in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rinehart, K L Jr -- Gloer, J B -- Hughes, R G Jr -- Renis, H E -- McGovren, J P -- Swynenberg, E B -- Stringfellow, D A -- Kuentzel, S L -- Li, L H -- AI 04769/AI/NIAID NIH HHS/ -- GM 27029/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 May 22;212(4497):933-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7233187" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibiotics, Antineoplastic/*isolation & purification ; Antiviral Agents/*isolation & purification ; *Depsipeptides ; Leukemia, Experimental/*drug therapy ; Peptides, Cyclic/*isolation & purification/therapeutic use ; Structure-Activity Relationship ; Urochordata/*analysis
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    Changes in DNA during meiosis in a repair-deficient mutant (rad 52) of yeast (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-05-01
    Description: The kinetic patterns of DNA synthesis in wild-type (RAD+) and rad 52 mutants of yeast, which exhibit high levels of synchrony during meiosis, are comparable. However, RAD 52 mutants accumulate single-strand breaks in parental DNA during the DNA synthesis period. Thus, the product of the RAD 52 gene has a role in meiotic DNA metabolism, as well as in the repair of DNA damage during mitotic growth. The observed breaks may be unresolved recombination intermediates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Resnick, M A -- Kasimos, J N -- Game, J C -- Braun, R J -- Roth, R M -- 5 R01 GM17317-11/GM/NIGMS NIH HHS/ -- S07-RR07027/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):543-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010606" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; DNA, Single-Stranded/genetics ; Genes ; *Meiosis ; Molecular Weight ; Mutation ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics
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    Two classes of single-stranded regions in DNA from sea urchin embryos (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-02-06
    Description: Native DNA from sea urchin embryos contains single-stranded regions (gaps) of up to 3000 nucleotides. The longer gaps (more than 1400 nucleotides) are nonrandomly distributed and are rich in histone gene sequences, other moderately repetitive sequences, and polypyrimidines. The shorter gaps are associated with DNA replication. A method for isolation of the two classes of single-stranded DNA pieces is reported.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wortzman, M S -- Baker, R F -- New York, N.Y. -- Science. 1981 Feb 6;211(4482):588-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7455698" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; *DNA Replication ; DNA, Single-Stranded/*analysis/genetics ; Genes ; Histones/*genetics ; Recombination, Genetic ; Sea Urchins/*genetics
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    Micromolar affinity benzodiazepine receptors: identification and characterization in central nervous system (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-06-11
    Description: Receptors that selectively bind micromolar concentrations of benzodiazepines are present in rat brain membrane. These micromolar receptors exhibit saturable, stereospecific binding, and the potency of benzodiazepine binding to these receptors is correlated with the ability of the benzodiazepines to inhibit maximum electric shock-induced convulsions. Benzodiazepine receptors with nanomolar affinity differ from the micromolar receptors in their binding, kinetic, and pharmacologic characteristics. The micromolar receptors also bind phenytoin, a non-benzodiazepine anticonvulsant. These results provide evidence for a distinct class of clinically relevant benzodiazepine receptors that may regulate neuronal excitability and anticonvulsant activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowling, A C -- DeLorenzo, R J -- NS 1352/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1982 Jun 11;216(4551):1247-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6281893" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzodiazepines/*metabolism/pharmacology ; Benzodiazepinones/metabolism ; Brain/*metabolism ; Calmodulin/antagonists & inhibitors ; Diazepam/metabolism ; Kinetics ; Ligands ; Protein Kinase Inhibitors ; Rats ; Receptors, Drug/*metabolism ; Receptors, GABA-A ; Structure-Activity Relationship
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    Artificial enzymes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-11-05
    Description: Simple chemical catalysts have been designed to achieve some desirable features of enzymes. These novel catalysts are not proteins, but they may incorporate the typical enzyme catalytic groups and they achieve selectivity in their reactions by use of geometric control, as do enzymes. Catalysts that carry out geometrically controlled chlorinations of aromatic rings and steroids have been constructed. Other catalysts achieve the selective synthesis of amino acids, and still others imitate ribonuclease in detailed mechanism and hydrolyze RNA. Optimization of geometries has led to a rate acceleration of over 10(8) in one instance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breslow, R -- New York, N.Y. -- Science. 1982 Nov 5;218(4572):532-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123255" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Cyclodextrins ; *Enzymes ; Kinetics ; Models, Chemical ; Ribonucleases ; Structure-Activity Relationship ; Substrate Specificity ; Transaminases
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  • 82
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    Stereoisomers of N-allylnormetazocine: phencyclidine-like behavioral effects in squirrel monkeys and rats (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-01-08
    Description: (+/-)-N-Allylnormetazocine is a benzomorphan opioid with psychotomimetic effects. The pure stereoisomers of this compound, as well as the racemic mixture, were compared to phencyclidine for their behavioral effects on squirrel monkeys and rats trained to discriminate phencyclidine from saline. Dose-response determinations were made for responses to phencyclidine, to a racemic mixture of N-allylnormetazocine, and to the pure levo and dextro isomers of N-allylnormetazocine. In both rats and monkeys, the dextro isomer and the racemic mixture produced dose-dependent responses appropriate for phencyclidine; the levo isomer did not produce the responses appropriate for phencyclidine at any of the doses tested. In both species, the levo isomer was more potent than the dextro isomer in decreasing the rate of responding. Thus racemic N-allylnormetazocine is a mixture of compounds that produce different behavioral effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brady, K T -- Balster, R L -- May, E L -- DA-00490/DA/NIDA NIH HHS/ -- DA-01442/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1982 Jan 8;215(4529):178-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6274022" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/*drug effects ; Male ; Naloxone/pharmacology ; Phenazocine/*analogs & derivatives/pharmacology ; Phencyclidine/pharmacology ; Rats ; Rats, Inbred Strains ; Receptors, Opioid/drug effects ; Saimiri ; Stereoisomerism ; Structure-Activity Relationship
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  • 83
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    Alpha-substituted gamma-butyrolactones: new class of anticonvulsant drugs (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-10
    Description: Alkyl-Substituted gamma-butyrolactones were synthesized and tested for their convulsant and anticonvulsant actions in mice and guinea pigs. The alpha-substituted compounds, alpha, alpha-dimethyl-, and alpha-ethyl-alpha-methyl-gamma-butyrolactone were anticonvulsant compounds with a spectrum of activity similar to that of ethosuximide. In contrast, beta-substituted compounds were convulsant agents similar to picrotoxinin. The alpha-substituted-gama-butyrolactones represent a new class of anticonvulsant drug with experimental and clinical potential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klunk, W E -- McKeon, A -- Covey, D F -- Ferrendelli, J A -- GM-07200/GM/NIGMS NIH HHS/ -- GM-24483/GM/NIGMS NIH HHS/ -- NS-14834/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1982 Sep 10;217(4564):1040-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6810462" target="_blank"〉PubMed〈/a〉
    Keywords: *4-Butyrolactone/analogs & derivatives/*therapeutic use/toxicity ; Animals ; *Anticonvulsants ; Chemical Phenomena ; Chemistry ; Convulsants ; Drug Evaluation, Preclinical ; Electroencephalography ; Epilepsy, Absence/drug therapy ; Ethosuximide/pharmacology ; *Furans/*therapeutic use ; Guinea Pigs ; Mice ; Structure-Activity Relationship ; Trimethadione/pharmacology
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  • 84
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    Human immunoglobulin heavy chain genes map to a region of translocations in malignant B lymphocytes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kirsch, I R -- Morton, C C -- Nakahara, K -- Leder, P -- New York, N.Y. -- Science. 1982 Apr 16;216(4543):301-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6801764" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/*physiology ; Chromosome Mapping ; Genes ; Humans ; Immunoglobulin Heavy Chains/*genetics ; Leukemia/*genetics ; Recombination, Genetic ; Translocation, Genetic
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  • 85
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    Purinergic regulation of food intake (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-02
    Description: Inosine peripherally administered to rats markedly suppressed spontaneous food intake and food intake induced by diazepam, muscimol, insulin, and food deprivation. The purines 2-deoxyguanosine and 2-deoxyinosine also suppressed food deprivation-induced feeding, whereas 7-methylinosine, which does not bind to the benzodiazepine binding site in vitro, had no effect on food intake when compared with controls. These results suggest that purines may represent endogenous substances that regulate food intake through interactions with the benzodiazepine receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levine, A S -- Morley, J E -- New York, N.Y. -- Science. 1982 Jul 2;217(4554):77-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7046046" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Appetite/*drug effects ; Deoxyguanosine/pharmacology ; Diazepam/pharmacology ; Eating/*drug effects ; Food Deprivation ; Inosine/analogs & derivatives/pharmacology ; Insulin/pharmacology ; Male ; Muscimol/pharmacology ; Purines/*pharmacology ; Rats ; Rats, Inbred Strains ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 86
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    Spectral character of sunlight modulates photosynthesis of previtamin D3 and its photoisomers in human skin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-05-28
    Description: The photosynthesis of previtamin D3 from 7-dehydrocholesterol in human skin was determined after exposure to narrow-band radiation or simulated solar radiation. The optimum wavelengths for the production of previtamin D3 were determined to be between 295 and 300 nanometers. When human skin was exposed to 295-nanometer radiation, up to 65 percent of the original 7-dehydrocholesterol content was converted to previtamin D3. In comparison, when adjacent skin was exposed to simulated solar radiation, the maximum formation of previtamin D3 was about 20 percent. Major differences in the formation of lumisterol3, and tachysterol3 from previtamin D3 were also observed. It is concluded that the spectral character of natural sunlight has a profound effect on the photochemistry of 7-dehydrocholesterol in human skin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacLaughlin, J A -- Anderson, R R -- Holick, M F -- AM 27334/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 May 28;216(4549):1001-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6281884" target="_blank"〉PubMed〈/a〉
    Keywords: Cholecalciferol/*biosynthesis/metabolism ; Dehydrocholesterols/radiation effects ; Ergosterol/metabolism ; Humans ; In Vitro Techniques ; Isomerism ; Photochemistry ; Skin/*metabolism ; Spectrum Analysis ; Structure-Activity Relationship ; Ultraviolet Rays
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  • 87
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    Identification of the constant chromosome regions involved in human hematologic malignant disease (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-05-14
    Description: Specific consistent chromosome translocations are regularly observed in certain human leukemias and lymphomas. For the myeloid leukemias, the constant recombinants are: the long arm of 9 to chromosome 22 in chronic myeloid leukemia, the long arm of 21 to chromosome 8 in acute myeloblastic leukemia, and the long arm of 17 to chromosome 15 in acute promyelocytic leukemia. Three related translocations are seen in Burkitt lymphoma and B cell acute lymphocytic leukemia; in each one, chromosome 8 is involved with chromosome 2, 14, or 22. Analysis of a complex translocation affecting chromosomes 8 and 14 indicates that the translocation of chromosome 8 to chromosome 14 is the critical constant rearrangement. The analysis of the DNA at the translocation sites of these chromosomes, rather than the reciprocal of each translocation, appears to be the most productive focus for initial study. The various immunoglobulin loci are located in chromosomes 2, 14, and 22, the chromosomes regularly involved in translocations in Burkitt lymphoma and B cell acute lymphocytic leukemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rowley, J D -- CA 16910/CA/NCI NIH HHS/ -- CA 19266/CA/NCI NIH HHS/ -- CA 25568/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1982 May 14;216(4547):749-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7079737" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosome Aberrations ; Chromosomes, Human, 13-15 ; Chromosomes, Human, 16-18 ; Chromosomes, Human, 21-22 and Y ; Chromosomes, Human, 6-12 and X ; Genes ; Humans ; Immunoglobulins/*genetics ; Leukemia/*genetics ; Lymphoma/*genetics ; Translocation, Genetic
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  • 88
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    Somatic mutation in genes for the variable portion of the immunoglobulin heavy chain (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-04-16
    Description: The size of the gene pool potentially encoding antibodies to p-azophenyl arsonate has been examined. A heavy chain-specific full-length complementary DNA clone has been constructed with the use of messenger RNA from a hybridoma that produces antibodies to the arsonate hapten and bears nearly a full complement of the determinants comprising the cross-reactive idiotype (CRI). The sequences of both the complementary DNA clone and the corresponding immunoglobulin heavy chain have been independently determined. A probe for the variable region gene was prepared from the original heavy chain complementary DNA clone and used to analyze, by Southern filter hybridization, genomic DNA from both A/J (CRI positive) and BALB/c (CRI negative) mice. Approximately 20 to 25 restriction fragments containing "germline" variable region gene segments were detected in both strains, and many are shared by both, Since 35 CRI-positive heavy chains have been partially sequenced thus far and 31 are different, the results of the hybridization analysis suggest that somatic mutation events involving the variable region gene segments of the heavy chain play a role in the origin of the amino acid sequence diversity seen in this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J -- Rabbitts, T H -- Estess, P -- Slaughter, C -- Tucker, P W -- Capra, J D -- A112127/PHS HHS/ -- AI-06020/AI/NIAID NIH HHS/ -- AI18016/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Apr 16;216(4543):309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6801765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites, Antibody/*genetics ; Genes ; Haptens ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Idiotypes/genetics ; Immunoglobulin Variable Region/*genetics ; Mice ; *Mutation
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  • 89
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    Oxytocin induces maternal behavior in virgin female rats (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-05-07
    Description: Intracerebroventricular administration of oxytocin to virgin female rats that had been ovariectomized and primed with estrogen 48 hours previously induced a rapid onset of full maternal behavior. The maternal behavior persisted and its incidence was dose-related. Tocinoic acid, the ring structure of oxytocin, also rapidly induced the onset of persistent, full maternal behavior. Arginine vasopressin induced persistent maternal behavior, but this behavior had a later onset. Prostaglandin F2 alpha induced strong partial maternal behavior, which showed early onset but did not persist. Many other peptides, ovarian steroids, and prostaglandin E2 were no more effective than saline. These findings suggest that the release of oxytocin and prostaglandin F2 alpha during labor may promote maternal behavior in rats.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pedersen, C A -- Ascher, J A -- Monroe, Y L -- Prange, A J Jr -- MH-22536/MH/NIMH NIH HHS/ -- MH-32316/MH/NIMH NIH HHS/ -- MH-34933/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1982 May 7;216(4546):648-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7071605" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine Vasopressin/pharmacology ; Brain/physiology ; Female ; Injections, Intraventricular ; *Maternal Behavior ; Oxytocin/administration & dosage/*pharmacology ; Rats ; Structure-Activity Relationship
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  • 90
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    Translational efficiency of transfer RNA's: uses of an extended anticodon (1982)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1982-11-12
    Description: Transfer RNA's are probably very strongly selected for translational efficiency. In this article, the argument is presented that the coding performance of the triplet anticodon is enhanced by selection of a matching anticodon loop and stem sequence. the anticodon plus these nearby sequence features (the extended anticodon) therefore contains more coding information than the anticodon alone and can perform more efficiently and accurately at the ribosome. This idea successfully accounts for the relative efficiencies of many transfer RNA's.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarus, M -- New York, N.Y. -- Science. 1982 Nov 12;218(4573):646-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6753149" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/genetics ; Kinetics ; Nucleic Acid Conformation ; *Protein Biosynthesis ; RNA, Transfer/*genetics ; Ribosomes/metabolism ; Structure-Activity Relationship ; Suppression, Genetic
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  • 91
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    Splice junctions: association with variation in protein structure (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
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  • 92
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    Myoglobin gene is a big surprise. The first analysis of a myoglobin gene reveals some striking similarities and some unexpected differences from hemoglobin genes (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-03-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1983 Mar 18;219(4590):1312.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6828858" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Genes ; Humans ; Myoglobin/*genetics
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  • 93
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    Z-DNA moves toward "real biology" (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):495-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623088" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Dna ; Eukaryota/genetics ; Humans ; *Nucleic Acid Conformation ; Species Specificity ; Structure-Activity Relationship
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  • 94
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    Antibodies that react with predetermined sites on proteins (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-02-11
    Description: Contrary to previous predictions, relatively short synthetic peptides that mimic part of a protein sequence are routinely capable of eliciting an antiserum that reacts with the partially mimicked protein. Peptides capable of eliciting protein-reactive serums are frequently represented in the primary sequence of a protein, can be characterized by a set of simple chemical rules, and are confined neither to immunodominant regions of intact proteins nor to the amino or carboxyl terminals. As such, synthetic peptide immunogens are valuable for eliciting reagents with predetermined specificity that can be used for basic research. In addition, some synthetic peptides are capable of mimicking regions of virus proteins and eliciting immune responses in animals that are protective against the viral agents. Such peptides may thus serve as the basis for safe, chemically defined synthetic vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sutcliffe, J G -- Shinnick, T M -- Green, N -- Lerner, R A -- R01 AI 18509/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):660-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186024" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibody Specificity ; Cross Reactions ; *Epitopes ; Peptides/immunology ; Proteins/*immunology ; Structure-Activity Relationship ; Vaccines/immunology
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  • 95
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; Structure-Activity Relationship
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  • 96
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    Protein engineering (1983)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1983-02-11
    Description: The prospects for protein engineering, including the roles of x-ray crystallography, chemical synthesis of DNA, and computer modelling of protein structure and folding, are discussed. It is now possible to attempt to modify many different properties of proteins by combining information on crystal structure and protein chemistry with artificial gene synthesis. Such techniques offer the potential for altering protein structure and function in ways not possible by any other method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, K M -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):666-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6572017" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; X-Ray Diffraction
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  • 97
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    Benzoquinolinediones: activity as insect teratogens (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-10-28
    Description: Morphological abnormalities including extra compound eyes, extra heads, and distally duplicated legs were generated in cricket embryos by treating eggs with single doses of either benz[g]isoquinoline-5,10-dione or benzo[h]quinoline-5,6-dione. Slight structural modifications of the molecules resulted in a loss of teratogenic activity, although embryotoxicity occurred. These potent insect teratogens can be used for analysis of developmental events during embryogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walton, B T -- Ho, C -- Ma, C Y -- O'Neill, E G -- Kao, G L -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):422-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623081" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Isoquinolines/*toxicity ; Orthoptera/*embryology ; Quinolines/*toxicity ; *Quinolones ; Structure-Activity Relationship ; *Teratogens
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 98
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    Inhibition of dihydropteridine reductase by novel 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Hydroxylated derivatives of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), a nigrostriatal neurotoxin in humans and primates, noncompetitively inhibited dihydropteridine reductase from human liver and rat striatal synaptosomes in vitro at micromolar concentrations. In contrast, MPTP and its chloro- and norderivatives did not inhibit this enzyme at lower than millimolar concentrations. Dihydropteridine reductase converts dihydrobiopterin to tetrahydrobiopterin, the required cofactor for the hydroxylation of aromatic amino acids during the synthesis of dopamine and serotonin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abell, C W -- Shen, R S -- Gessner, W -- Brossi, A -- HD 14635/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):405-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6608790" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine ; Animals ; Corpus Striatum/enzymology ; Dihydropteridine Reductase/*antagonists & inhibitors ; Humans ; Hydroxylation ; Liver/enzymology ; NAD/metabolism ; NADH, NADPH Oxidoreductases/*antagonists & inhibitors ; Pyridines/*pharmacology ; Rats ; Structure-Activity Relationship ; Synaptosomes/enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 99
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    Homology of genome of AIDS-associated virus with genomes of human T-cell leukemia viruses (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-31
    Description: A T lymphotropic virus found in patients with the acquired immune deficiency syndrome (AIDS) or lymphadenopathy syndrome has been postulated to be the cause of AIDS. Immunological analysis of this retrovirus and its biological properties suggest that it is a member of the family of human T-lymphotropic retroviruses known as HTLV. Accordingly, it has been named HTLV-III. In the present report it is shown by nucleic acid hybridization that sequences of the genome of HTLV-III are homologous to the structural genes (gag, pol, and env) of both HTLV-I and HTLV-II and to a potential coding region called pX located between the env gene and the long terminal repeating sequence that is unique to the HTLV family of retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Gallo, R C -- Hahn, B H -- Shaw, G M -- Popovic, M -- Salahuddin, S Z -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):927-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089333" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; Cloning, Molecular ; Dna ; DNA, Viral ; Deltaretrovirus/classification/*genetics ; Genes ; *Genes, Viral ; Humans ; *Nucleic Acid Hybridization ; RNA, Viral ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 100
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    Genes of the major histocompatibility complex in mouse and man (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: The genes of the major histocompatibility complex code for cell-surface molecules that play an important role in the generation of the immune response. These genes and molecules have been studied intensively over the last five decades by geneticists, biochemists, and immunologists, but only recently has the isolation of the genes by molecular biologists facilitated their precise characterization. Many surprising findings have been made concerning their structure, multiplicity, organization, function, and evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinmetz, M -- Hood, L -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):727-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356354" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chromosome Mapping ; Genes ; H-2 Antigens/*genetics ; HLA Antigens/*genetics ; Histocompatibility Antigens/genetics ; Humans ; *Major Histocompatibility Complex ; Mice ; Polymorphism, Genetic ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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