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  • Nucleic Acid Hybridization
  • American Association for the Advancement of Science (AAAS)  (420)
  • American Association for the Advancement of Science
  • American Chemical Society (ACS)
  • Blackwell Publishing Ltd
  • PANGAEA
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Keywords
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  • American Association for the Advancement of Science (AAAS)  (420)
  • American Association for the Advancement of Science
  • American Chemical Society (ACS)
  • Blackwell Publishing Ltd
  • PANGAEA
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  • 1
    Publication Date: 2015-02-24
    Description: For over half a century, the biological roles of nucleic acids as catalytic enzymes, intracellular regulatory molecules, and the carriers of genetic information have been studied extensively. More recently, the sequence-specific binding properties of DNA have been exploited to direct the assembly of materials at the nanoscale. Integral to any methodology focused on assembling matter from smaller pieces is the idea that final structures have well-defined spacings, orientations, and stereo-relationships. This requirement can be met by using DNA-based constructs that present oriented nanoscale bonding elements from rigid core units. Here, we draw analogy between such building blocks and the familiar chemical concepts of "bonds" and "valency" and review two distinct but related strategies that have used this design principle in constructing new configurations of matter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Matthew R -- Seeman, Nadrian C -- Mirkin, Chad A -- New York, N.Y. -- Science. 2015 Feb 20;347(6224):1260901. doi: 10.1126/science.1260901.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering, Northwestern University, Evanston, IL 60208, USA. ; Department of Chemistry, New York University, New York, NY 10003, USA. chadnano@northwestern.edu ned.seeman@nyu.edu. ; Department of Materials Science and Engineering, Northwestern University, Evanston, IL 60208, USA. Department of Chemistry and International Institute for Nanotechnology, Northwestern University, Evanston, IL 60208, USA. chadnano@northwestern.edu ned.seeman@nyu.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25700524" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*chemistry ; Nanostructures/*chemistry ; Nucleic Acid Conformation ; Nucleic Acid Hybridization
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  • 2
    Publication Date: 2011-10-15
    Description: A current limitation in nanoparticle superlattice engineering is that the identities of the particles being assembled often determine the structures that can be synthesized. Therefore, specific crystallographic symmetries or lattice parameters can only be achieved using specific nanoparticles as building blocks (and vice versa). We present six design rules that can be used to deliberately prepare nine distinct colloidal crystal structures, with control over lattice parameters on the 25- to 150-nanometer length scale. These design rules outline a strategy to independently adjust each of the relevant crystallographic parameters, including particle size (5 to 60 nanometers), periodicity, and interparticle distance. As such, this work represents an advance in synthesizing tailorable macroscale architectures comprising nanoscale materials in a predictable fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macfarlane, Robert J -- Lee, Byeongdu -- Jones, Matthew R -- Harris, Nadine -- Schatz, George C -- Mirkin, Chad A -- New York, N.Y. -- Science. 2011 Oct 14;334(6053):204-8. doi: 10.1126/science.1210493.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21998382" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallization ; Crystallography ; DNA/*chemistry ; Engineering ; Metal Nanoparticles/*chemistry ; Microscopy, Electron, Transmission ; Nucleic Acid Hybridization ; Oligonucleotides/chemistry ; Particle Size ; Scattering, Small Angle ; Thermodynamics
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  • 3
    Publication Date: 2010-05-08
    Description: It is now possible to perform whole-genome shotgun sequencing as well as capture of specific genomic regions for extinct organisms. However, targeted resequencing of large parts of nuclear genomes has yet to be demonstrated for ancient DNA. Here we show that hybridization capture on microarrays can successfully recover more than a megabase of target regions from Neandertal DNA even in the presence of approximately 99.8% microbial DNA. Using this approach, we have sequenced approximately 14,000 protein-coding positions inferred to have changed on the human lineage since the last common ancestor shared with chimpanzees. By generating the sequence of one Neandertal and 50 present-day humans at these positions, we have identified 88 amino acid substitutions that have become fixed in humans since our divergence from the Neandertals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3140021/" 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/PMC3140021/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burbano, Hernan A -- Hodges, Emily -- Green, Richard E -- Briggs, Adrian W -- Krause, Johannes -- Meyer, Matthias -- Good, Jeffrey M -- Maricic, Tomislav -- Johnson, Philip L F -- Xuan, Zhenyu -- Rooks, Michelle -- Bhattacharjee, Arindam -- Brizuela, Leonardo -- Albert, Frank W -- de la Rasilla, Marco -- Fortea, Javier -- Rosas, Antonio -- Lachmann, Michael -- Hannon, Gregory J -- Paabo, Svante -- P01 CA013106/CA/NCI NIH HHS/ -- P01 CA013106-38/CA/NCI NIH HHS/ -- P01 CA013106-39/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 May 7;328(5979):723-5. doi: 10.1126/science.1188046.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Evolutionary Anthropology, D-04103 Leipzig, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20448179" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Fossils ; Genes ; *Genome ; *Genome, Human ; Hominidae/*genetics ; Humans ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis/*methods ; Pan troglodytes/genetics ; Proteins/chemistry/genetics ; Sequence Alignment ; Sequence Analysis, DNA/*methods
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2009-04-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, William -- New York, N.Y. -- Science. 2009 Apr 3;324(5923):46-7. doi: 10.1126/science.1172136.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Functional Nanomaterials, Brookhaven National Laboratory, Upton, NY 11973, USA. wsherman@bnl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19342576" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA/chemistry ; Furocoumarins/chemistry ; Hot Temperature ; Nanotechnology/*methods ; Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Ultraviolet Rays
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  • 5
    Publication Date: 2009-05-16
    Description: During transcription initiation in vitro, prokaryotic and eukaryotic RNA polymerase (RNAP) can engage in abortive initiation-the synthesis and release of short (2 to 15 nucleotides) RNA transcripts-before productive initiation. It has not been known whether abortive initiation occurs in vivo. Using hybridization with locked nucleic acid probes, we directly detected abortive transcripts in bacteria. In addition, we show that in vivo abortive initiation shows characteristics of in vitro abortive initiation: Abortive initiation increases upon stabilizing interactions between RNAP and either promoter DNA or sigma factor, and also upon deleting elongation factor GreA. Abortive transcripts may have functional roles in regulating gene expression in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718712/" 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/PMC2718712/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, Seth R -- Ebright, Richard H -- Nickels, Bryce E -- GM41376/GM/NIGMS NIH HHS/ -- R01 GM041376/GM/NIGMS NIH HHS/ -- R01 GM041376-19/GM/NIGMS NIH HHS/ -- R01 GM041376-20/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 May 15;324(5929):927-8. doi: 10.1126/science.1169237.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19443781" target="_blank"〉PubMed〈/a〉
    Keywords: DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/*genetics/metabolism ; Escherichia coli Proteins/genetics/metabolism ; Gene Expression Regulation, Bacterial ; Nucleic Acid Hybridization ; Nucleic Acid Probes ; Plasmids ; Promoter Regions, Genetic ; RNA, Bacterial/*genetics/metabolism ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2009-04-04
    Description: A substantial challenge in engineering molecular motors is designing mechanisms to coordinate the motion between multiple domains of the motor so as to bias random thermal motion. For bipedal motors, this challenge takes the form of coordinating the movement of the biped's legs so that they can move in a synchronized fashion. To address this problem, we have constructed an autonomous DNA bipedal walker that coordinates the action of its two legs by cyclically catalyzing the hybridization of metastable DNA fuel strands. This process leads to a chemically ratcheted walk along a directionally polar DNA track. By covalently cross-linking aliquots of the walker to its track in successive walking states, we demonstrate that this Brownian motor can complete a full walking cycle on a track whose length could be extended for longer walks. We believe that this study helps to uncover principles behind the design of unidirectional devices that can function without intervention. This device should be able to fulfill roles that entail the performance of useful mechanical work on the nanometer scale.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3470906/" 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/PMC3470906/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Omabegho, Tosan -- Sha, Ruojie -- Seeman, Nadrian C -- R37 GM029554/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Apr 3;324(5923):67-71. doi: 10.1126/science.1170336.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19342582" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/*chemistry ; DNA, Single-Stranded/*chemistry ; Furocoumarins/chemistry ; Inverted Repeat Sequences ; Nanotechnology/methods ; Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Ultraviolet Rays
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  • 7
    Publication Date: 2008-11-15
    Description: The reverse transcriptase (RT) of human immunodeficiency virus (HIV) catalyzes a series of reactions to convert single-stranded viral RNA into double-stranded DNA for host cell integration. This process requires a variety of enzymatic activities, including DNA polymerization, RNA cleavage, strand transfer, and strand displacement synthesis. We used single-molecule fluorescence resonance energy transfer to probe the interactions between RT and nucleic acid substrates in real time. RT was observed to slide on nucleic acid duplexes, rapidly shuttling between opposite termini of the duplex. Upon reaching the DNA 3' terminus, RT can spontaneously flip into a polymerization orientation. Sliding kinetics were regulated by cognate nucleotides and anti-HIV drugs, which stabilized and destabilized the polymerization mode, respectively. These long-range translocation activities facilitate multiple stages of the reverse transcription pathway, including normal DNA polymerization and strand displacement synthesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717043/" 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/PMC2717043/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Shixin -- Abbondanzieri, Elio A -- Rausch, Jason W -- Le Grice, Stuart F J -- Zhuang, Xiaowei -- GM 068518/GM/NIGMS NIH HHS/ -- R01 GM068518/GM/NIGMS NIH HHS/ -- R01 GM068518-05/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2008 Nov 14;322(5904):1092-7. doi: 10.1126/science.1163108.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19008444" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbocyanines ; DNA Primers/metabolism ; DNA, Viral/biosynthesis/*metabolism ; Fluorescence Resonance Energy Transfer ; Fluorescent Dyes ; HIV Reverse Transcriptase/chemistry/*metabolism ; HIV-1/*enzymology ; Kinetics ; Models, Molecular ; Nevirapine/metabolism/pharmacology ; Nucleic Acid Hybridization ; Nucleotides/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Viral/*metabolism ; Reverse Transcriptase Inhibitors/metabolism/pharmacology ; Reverse Transcription ; Ribonuclease H/chemistry/metabolism
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2008-07-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackelprang, Rachel -- Rubin, Edward M -- New York, N.Y. -- Science. 2008 Jul 11;321(5886):211-2. doi: 10.1126/science.1161890.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18621660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone and Bones ; DNA/chemistry/*genetics ; DNA Damage ; *Genetic Techniques ; Genomics/*methods ; Hominidae/*genetics ; Humans ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; *Paleontology ; Polymerase Chain Reaction/methods ; Sequence Analysis, DNA
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  • 9
    Publication Date: 2007-11-17
    Description: Artificial biochemical circuits are likely to play as large a role in biological engineering as electrical circuits have played in the engineering of electromechanical devices. Toward that end, nucleic acids provide a designable substrate for the regulation of biochemical reactions. However, it has been difficult to incorporate signal amplification components. We introduce a design strategy that allows a specified input oligonucleotide to catalyze the release of a specified output oligonucleotide, which in turn can serve as a catalyst for other reactions. This reaction, which is driven forward by the configurational entropy of the released molecule, provides an amplifying circuit element that is simple, fast, modular, composable, and robust. We have constructed and characterized several circuits that amplify nucleic acid signals, including a feedforward cascade with quadratic kinetics and a positive feedback circuit with exponential growth kinetics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, David Yu -- Turberfield, Andrew J -- Yurke, Bernard -- Winfree, Erik -- New York, N.Y. -- Science. 2007 Nov 16;318(5853):1121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Computation and Neural Systems, California Institute of Technology, MC 136-93, 1200 East California Boulevard, Pasadena, CA91125, USA. dzhang@dna.caltech.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18006742" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalysis ; Chemical Engineering ; *Computers, Molecular ; DNA/*chemistry ; Entropy ; Equipment Design ; Feedback, Physiological ; Mice ; Nanotechnology ; Nucleic Acid Hybridization ; Rabbits
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  • 10
    Publication Date: 2007-02-10
    Description: Extensive studies are currently being performed to associate disease susceptibility with one form of genetic variation, namely, single-nucleotide polymorphisms (SNPs). In recent years, another type of common genetic variation has been characterized, namely, structural variation, including copy number variants (CNVs). To determine the overall contribution of CNVs to complex phenotypes, we have performed association analyses of expression levels of 14,925 transcripts with SNPs and CNVs in individuals who are part of the International HapMap project. SNPs and CNVs captured 83.6% and 17.7% of the total detected genetic variation in gene expression, respectively, but the signals from the two types of variation had little overlap. Interrogation of the genome for both types of variants may be an effective way to elucidate the causes of complex phenotypes and disease in humans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2665772/" 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/PMC2665772/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stranger, Barbara E -- Forrest, Matthew S -- Dunning, Mark -- Ingle, Catherine E -- Beazley, Claude -- Thorne, Natalie -- Redon, Richard -- Bird, Christine P -- de Grassi, Anna -- Lee, Charles -- Tyler-Smith, Chris -- Carter, Nigel -- Scherer, Stephen W -- Tavare, Simon -- Deloukas, Panagiotis -- Hurles, Matthew E -- Dermitzakis, Emmanouil T -- 065535/Wellcome Trust/United Kingdom -- 076113/Wellcome Trust/United Kingdom -- 077009/Wellcome Trust/United Kingdom -- 077014/Wellcome Trust/United Kingdom -- 077046/Wellcome Trust/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):848-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17289997" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Female ; Gene Deletion ; *Gene Dosage ; Gene Duplication ; *Gene Expression Regulation ; *Genetic Variation ; Genetics, Population ; *Genome, Human ; Genomics/methods ; Haplotypes ; Humans ; Linkage Disequilibrium ; Male ; Mutation ; Nucleic Acid Hybridization ; Phenotype ; *Polymorphism, Single Nucleotide ; Regression Analysis
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  • 11
    Publication Date: 2007-03-17
    Description: We tested the hypothesis that de novo copy number variation (CNV) is associated with autism spectrum disorders (ASDs). We performed comparative genomic hybridization (CGH) on the genomic DNA of patients and unaffected subjects to detect copy number variants not present in their respective parents. Candidate genomic regions were validated by higher-resolution CGH, paternity testing, cytogenetics, fluorescence in situ hybridization, and microsatellite genotyping. Confirmed de novo CNVs were significantly associated with autism (P = 0.0005). Such CNVs were identified in 12 out of 118 (10%) of patients with sporadic autism, in 2 out of 77 (3%) of patients with an affected first-degree relative, and in 2 out of 196 (1%) of controls. Most de novo CNVs were smaller than microscopic resolution. Affected genomic regions were highly heterogeneous and included mutations of single genes. These findings establish de novo germline mutation as a more significant risk factor for ASD than previously recognized.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2993504/" 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/PMC2993504/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sebat, Jonathan -- Lakshmi, B -- Malhotra, Dheeraj -- Troge, Jennifer -- Lese-Martin, Christa -- Walsh, Tom -- Yamrom, Boris -- Yoon, Seungtai -- Krasnitz, Alex -- Kendall, Jude -- Leotta, Anthony -- Pai, Deepa -- Zhang, Ray -- Lee, Yoon-Ha -- Hicks, James -- Spence, Sarah J -- Lee, Annette T -- Puura, Kaija -- Lehtimaki, Terho -- Ledbetter, David -- Gregersen, Peter K -- Bregman, Joel -- Sutcliffe, James S -- Jobanputra, Vaidehi -- Chung, Wendy -- Warburton, Dorothy -- King, Mary-Claire -- Skuse, David -- Geschwind, Daniel H -- Gilliam, T Conrad -- Ye, Kenny -- Wigler, Michael -- MH076431/MH/NIMH NIH HHS/ -- MH61009/MH/NIMH NIH HHS/ -- MH64547/MH/NIMH NIH HHS/ -- R01 MH076431/MH/NIMH NIH HHS/ -- R01 MH076431-01/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):445-9. Epub 2007 Mar 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA. sebat@cshl.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17363630" target="_blank"〉PubMed〈/a〉
    Keywords: Asperger Syndrome/genetics ; Autistic Disorder/*genetics ; Case-Control Studies ; Child ; Cytogenetic Analysis ; Female ; Gene Deletion ; *Gene Dosage ; Gene Duplication ; Genetic Predisposition to Disease ; *Genome, Human ; Germ-Line Mutation ; Humans ; In Situ Hybridization, Fluorescence ; Male ; Markov Chains ; Microsatellite Repeats ; *Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; Parents ; Siblings
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  • 12
    Publication Date: 2006-11-11
    Description: The sea urchin Strongylocentrotus purpuratus is a model organism for study of the genomic control circuitry underlying embryonic development. We examined the complete repertoire of genes expressed in the S. purpuratus embryo, up to late gastrula stage, by means of high-resolution custom tiling arrays covering the whole genome. We detected complete spliced structures even for genes known to be expressed at low levels in only a few cells. At least 11,000 to 12,000 genes are used in embryogenesis. These include most of the genes encoding transcription factors and signaling proteins, as well as some classes of general cytoskeletal and metabolic proteins, but only a minor fraction of genes encoding immune functions and sensory receptors. Thousands of small asymmetric transcripts of unknown function were also detected in intergenic regions throughout the genome. The tiling array data were used to correct and authenticate several thousand gene models during the genome annotation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Samanta, Manoj P -- Tongprasit, Waraporn -- Istrail, Sorin -- Cameron, R Andrew -- Tu, Qiang -- Davidson, Eric H -- Stolc, Viktor -- HD-37105/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):960-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Systemix Institute, Los Altos, CA 94024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095694" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastula/metabolism ; Computational Biology ; Embryo, Nonmammalian/*metabolism ; Embryonic Development/*genetics ; Gastrula/metabolism ; Gene Expression Profiling ; *Gene Expression Regulation, Developmental ; *Genome ; Intracellular Signaling Peptides and Proteins/genetics/metabolism ; Molecular Probe Techniques ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; RNA, Messenger/genetics/metabolism ; RNA, Untranslated/genetics/metabolism ; Signal Transduction/genetics ; Strongylocentrotus purpuratus/*embryology/*genetics/growth & development ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic
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  • 13
    Publication Date: 2006-03-11
    Description: A central challenge of genomics is to detect, simply and inexpensively, all differences in sequence among the genomes of individual members of a species. We devised a system to detect all single-nucleotide differences between genomes with the use of data from a single hybridization to a whole-genome DNA microarray. This allowed us to detect a variety of spontaneous single-base pair substitutions, insertions, and deletions, and most (〉90%) of the approximately 30,000 known single-nucleotide polymorphisms between two Saccharomyces cerevisiae strains. We applied this approach to elucidate the genetic basis of phenotypic variants and to identify the small number of single-base pair changes accumulated during experimental evolution of yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gresham, David -- Ruderfer, Douglas M -- Pratt, Stephen C -- Schacherer, Joseph -- Dunham, Maitreya J -- Botstein, David -- Kruglyak, Leonid -- P50 GM071508/GM/NIGMS NIH HHS/ -- R01 GM046406/GM/NIGMS NIH HHS/ -- R37 MH059520/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 31;311(5769):1932-6. Epub 2006 Mar 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544, USA. dgresham@genomics.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16527929" target="_blank"〉PubMed〈/a〉
    Keywords: Directed Molecular Evolution ; Genes, Fungal ; *Genome, Fungal ; Genomics ; Mutation ; Nucleic Acid Hybridization ; *Oligonucleotide Array Sequence Analysis ; Phenotype ; Point Mutation ; *Polymorphism, Single Nucleotide ; Saccharomyces cerevisiae/*genetics/physiology ; Sequence Deletion ; Suppression, Genetic
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  • 14
    Publication Date: 2005-12-13
    Description: Practical components for three-dimensional molecular nanofabrication must be simple to produce, stereopure, rigid, and adaptable. We report a family of DNA tetrahedra, less than 10 nanometers on a side, that can self-assemble in seconds with near-quantitative yield of one diastereomer. They can be connected by programmable DNA linkers. Their triangulated architecture confers structural stability; by compressing a DNA tetrahedron with an atomic force microscope, we have measured the axial compressibility of DNA and observed the buckling of the double helix under high loads.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodman, R P -- Schaap, I A T -- Tardin, C F -- Erben, C M -- Berry, R M -- Schmidt, C F -- Turberfield, A J -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1661-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339440" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; Chemistry, Physical ; DNA/*chemistry ; Dimerization ; Elasticity ; Microscopy, Atomic Force ; Models, Molecular ; Molecular Structure ; *Nanostructures ; *Nanotechnology ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry ; Physicochemical Phenomena ; Stereoisomerism
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  • 15
    Publication Date: 2005-08-06
    Description: We describe a DNA sequencing technology in which a commonly available, inexpensive epifluorescence microscope is converted to rapid nonelectrophoretic DNA sequencing automation. We apply this technology to resequence an evolved strain of Escherichia coli at less than one error per million consensus bases. A cell-free, mate-paired library provided single DNA molecules that were amplified in parallel to 1-micrometer beads by emulsion polymerase chain reaction. Millions of beads were immobilized in a polyacrylamide gel and subjected to automated cycles of sequencing by ligation and four-color imaging. Cost per base was roughly one-ninth as much as that of conventional sequencing. Our protocols were implemented with off-the-shelf instrumentation and reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shendure, Jay -- Porreca, Gregory J -- Reppas, Nikos B -- Lin, Xiaoxia -- McCutcheon, John P -- Rosenbaum, Abraham M -- Wang, Michael D -- Zhang, Kun -- Mitra, Robi D -- Church, George M -- New York, N.Y. -- Science. 2005 Sep 9;309(5741):1728-32. Epub 2005 Aug 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA. shendure@alumni.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16081699" target="_blank"〉PubMed〈/a〉
    Keywords: Acrylic Resins ; Algorithms ; Automation ; Costs and Cost Analysis ; DNA Ligases/metabolism ; DNA Primers ; DNA, Bacterial/*genetics ; Escherichia coli/*genetics ; *Evolution, Molecular ; Fluorescent Dyes ; Gels ; Gene Library ; *Genome, Bacterial ; Microscopy, Fluorescence ; Microspheres ; Mutation ; Nucleic Acid Hybridization ; Point Mutation ; Polymerase Chain Reaction ; Sequence Analysis, DNA/economics/instrumentation/*methods
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  • 16
    Publication Date: 2004-02-14
    Description: The structure of an RNA polymerase II-transcribing complex has been determined in the posttranslocation state, with a vacancy at the growing end of the RNA-DNA hybrid helix. At the opposite end of the hybrid helix, the RNA separates from the template DNA. This separation of nucleic acid strands is brought about by interaction with a set of proteins loops in a strand/loop network. Formation of the network must occur in the transition from abortive initiation to promoter escape.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westover, Kenneth D -- Bushnell, David A -- Kornberg, Roger D -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):1014-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963331" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Crystallization ; Crystallography, X-Ray ; DNA, Single-Stranded/*chemistry/metabolism ; Models, Molecular ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligoribonucleotides/chemistry/metabolism ; Promoter Regions, Genetic ; Protein Conformation ; RNA Polymerase II/*chemistry/*metabolism ; RNA, Complementary/*chemistry/metabolism ; Saccharomyces cerevisiae/enzymology ; Templates, Genetic ; Transcription Factor TFIIB/metabolism ; *Transcription, Genetic
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  • 17
    Publication Date: 2004-11-13
    Description: Elucidating the transcribed regions of the genome constitutes a fundamental aspect of human biology, yet this remains an outstanding problem. To comprehensively identify coding sequences, we constructed a series of high-density oligonucleotide tiling arrays representing sense and antisense strands of the entire nonrepetitive sequence of the human genome. Transcribed sequences were located across the genome via hybridization to complementary DNA samples, reverse-transcribed from polyadenylated RNA obtained from human liver tissue. In addition to identifying many known and predicted genes, we found 10,595 transcribed sequences not detected by other methods. A large fraction of these are located in intergenic regions distal from previously annotated genes and exhibit significant homology to other mammalian proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bertone, Paul -- Stolc, Viktor -- Royce, Thomas E -- Rozowsky, Joel S -- Urban, Alexander E -- Zhu, Xiaowei -- Rinn, John L -- Tongprasit, Waraporn -- Samanta, Manoj -- Weissman, Sherman -- Gerstein, Mark -- Snyder, Michael -- P50 HG02357/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2242-6. Epub 2004 Nov 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539566" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Computational Biology ; Conserved Sequence ; CpG Islands ; DNA, Complementary ; DNA, Intergenic ; Databases, Genetic ; Exons ; *Genome, Human ; Humans ; Introns ; Mice ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis/*methods ; Oligonucleotide Probes ; Proteins/chemistry/genetics ; RNA, Messenger/genetics ; Reproducibility of Results ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid ; *Transcription, Genetic
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  • 18
    Publication Date: 2004-04-17
    Description: Pathway optimization is difficult to achieve owing to complex, nonlinear, and largely unknown interactions of enzymes, regulators, and metabolites. We report a pathway reconstruction using RNA display-derived messenger RNA-enzyme fusion molecules. These chimeras are immobilized by hybridization of their messenger RNA end with homologous capture DNA spotted on a substrate surface. Enzymes thus immobilized retain activity proportional to the amount of capture DNA, allowing modulation of the relative activity of pathway enzymes. Entire pathways can thus be reconstructed and optimized in vitro from genomic information. We provide concept validation with the sequential reactions catalyzed by luciferase and nucleoside diphosphate kinase and further illustrate this method with the optimization of the five-step pathway for trehalose synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jung, Gyoo Yeol -- Stephanopoulos, Gregory -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):428-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Massachusetts Institute of Technology, Room 56-469, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087547" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; DNA/genetics/metabolism ; Enzymes, Immobilized/genetics/*metabolism ; Gene Expression ; *Gene Expression Profiling ; *Genetic Engineering ; Glucose/metabolism ; Glucosyltransferases/genetics/metabolism ; Hexokinase/genetics/metabolism ; Kinetics ; Luciferases/genetics/metabolism ; *Metabolism ; Nucleic Acid Hybridization ; Nucleoside-Diphosphate Kinase/genetics/metabolism ; Oligonucleotide Array Sequence Analysis ; Phosphoglucomutase/genetics/metabolism ; Phosphoric Monoester Hydrolases/genetics/metabolism ; *Protein Array Analysis ; Protein Biosynthesis ; RNA, Messenger/*metabolism ; Trehalose/*biosynthesis ; UTP-Glucose-1-Phosphate Uridylyltransferase/genetics/metabolism
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  • 19
    Publication Date: 2004-02-14
    Description: The structure of the general transcription factor IIB (TFIIB) in a complex with RNA polymerase II reveals three features crucial for transcription initiation: an N-terminal zinc ribbon domain of TFIIB that contacts the "dock" domain of the polymerase, near the path of RNA exit from a transcribing enzyme; a "finger" domain of TFIIB that is inserted into the polymerase active center; and a C-terminal domain, whose interaction with both the polymerase and with a TATA box-binding protein (TBP)-promoter DNA complex orients the DNA for unwinding and transcription. TFIIB stabilizes an early initiation complex, containing an incomplete RNA-DNA hybrid region. It may interact with the template strand, which sets the location of the transcription start site, and may interfere with RNA exit, which leads to abortive initiation or promoter escape. The trajectory of promoter DNA determined by the C-terminal domain of TFIIB traverses sites of interaction with TFIIE, TFIIF, and TFIIH, serving to define their roles in the transcription initiation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bushnell, David A -- Westover, Kenneth D -- Davis, Ralph E -- Kornberg, Roger D -- AI21144/AI/NIAID NIH HHS/ -- GM49985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):983-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963322" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Nucleic Acid Hybridization ; Promoter Regions, Genetic ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/chemistry/metabolism ; RNA Polymerase II/*chemistry/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism ; TATA Box ; TATA-Box Binding Protein/chemistry/metabolism ; Templates, Genetic ; Transcription Factor TFIIB/*chemistry/metabolism ; Transcription Factors, TFII/chemistry/metabolism ; *Transcription, Genetic ; Zinc/chemistry
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  • 20
    Publication Date: 2003-07-19
    Description: Direct quantification of biomolecular interaction by single-molecule force spectroscopy has evolved into a powerful tool for materials and life sciences. We introduce an approach in which the unbinding forces required to break intermolecular bonds are measured in a differential format by comparison with a known reference bond (here, a short DNA duplex). In addition to a marked increase in sensitivity and force resolution, which enabled us to resolve single-base pair mismatches, this concept allows for highly specific parallel assays. This option was exploited to overcome cross-reactions of antibodies in a protein biochip application.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albrecht, Christian -- Blank, Kerstin -- Lalic-Multhaler, Mio -- Hirler, Siegfried -- Mai, Thao -- Gilbert, Ilka -- Schiffmann, Susanne -- Bayer, Tom -- Clausen-Schaumann, Hauke -- Gaub, Hermann E -- New York, N.Y. -- Science. 2003 Jul 18;301(5631):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nanotype GmbH, Lochhamer Schlag 12, 82166 Grafelfing, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12869761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; *Base Pair Mismatch ; *Biosensing Techniques ; Carbocyanines ; Cross Reactions ; *DNA/chemistry/genetics/metabolism ; Dimethylpolysiloxanes ; Fluorescence ; Fluorescent Dyes ; Glass ; Humans ; Immunoassay ; Interleukin-5/analysis/immunology ; Mice ; Microscopy, Atomic Force ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Oligonucleotide Array Sequence Analysis ; *Protein Array Analysis ; Protein Binding ; Silicones ; Temperature ; Thermodynamics
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  • 21
    Publication Date: 2003-11-01
    Description: Functional analysis of a genome requires accurate gene structure information and a complete gene inventory. A dual experimental strategy was used to verify and correct the initial genome sequence annotation of the reference plant Arabidopsis. Sequencing full-length cDNAs and hybridizations using RNA populations from various tissues to a set of high-density oligonucleotide arrays spanning the entire genome allowed the accurate annotation of thousands of gene structures. We identified 5817 novel transcription units, including a substantial amount of antisense gene transcription, and 40 genes within the genetically defined centromeres. This approach resulted in completion of approximately 30% of the Arabidopsis ORFeome as a resource for global functional experimentation of the plant proteome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamada, Kayoko -- Lim, Jun -- Dale, Joseph M -- Chen, Huaming -- Shinn, Paul -- Palm, Curtis J -- Southwick, Audrey M -- Wu, Hank C -- Kim, Christopher -- Nguyen, Michelle -- Pham, Paul -- Cheuk, Rosa -- Karlin-Newmann, George -- Liu, Shirley X -- Lam, Bao -- Sakano, Hitomi -- Wu, Troy -- Yu, Guixia -- Miranda, Molly -- Quach, Hong L -- Tripp, Matthew -- Chang, Charlie H -- Lee, Jeong M -- Toriumi, Mitsue -- Chan, Marie M H -- Tang, Carolyn C -- Onodera, Courtney S -- Deng, Justine M -- Akiyama, Kenji -- Ansari, Yasser -- Arakawa, Takahiro -- Banh, Jenny -- Banno, Fumika -- Bowser, Leah -- Brooks, Shelise -- Carninci, Piero -- Chao, Qimin -- Choy, Nathan -- Enju, Akiko -- Goldsmith, Andrew D -- Gurjal, Mani -- Hansen, Nancy F -- Hayashizaki, Yoshihide -- Johnson-Hopson, Chanda -- Hsuan, Vickie W -- Iida, Kei -- Karnes, Meagan -- Khan, Shehnaz -- Koesema, Eric -- Ishida, Junko -- Jiang, Paul X -- Jones, Ted -- Kawai, Jun -- Kamiya, Asako -- Meyers, Cristina -- Nakajima, Maiko -- Narusaka, Mari -- Seki, Motoaki -- Sakurai, Tetsuya -- Satou, Masakazu -- Tamse, Racquel -- Vaysberg, Maria -- Wallender, Erika K -- Wong, Cecilia -- Yamamura, Yuki -- Yuan, Shiaulou -- Shinozaki, Kazuo -- Davis, Ronald W -- Theologis, Athanasios -- Ecker, Joseph R -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):842-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Gene Expression Center, Albany, CA 94710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593172" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics ; Chromosome Mapping ; Chromosomes, Plant/genetics ; Cloning, Molecular ; Computational Biology ; DNA, Complementary/genetics ; DNA, Intergenic ; Expressed Sequence Tags ; Gene Expression Profiling ; Genes, Plant ; *Genome, Plant ; Genomics ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; Open Reading Frames ; RNA, Messenger/*genetics ; RNA, Plant/*genetics ; Reverse Transcriptase Polymerase Chain Reaction ; *Transcription, Genetic
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  • 22
    Publication Date: 2003-11-01
    Description: We describe a new molecular class of genetic-pairing system that has a native DNA backbone but has all four base pairs replaced by new, larger pairs. The base pairs include size-expanded analogs of thymine and of adenine, both extended by the width of a benzene ring (2.4 A). The expanded-diameter double helices are more thermodynamically stable than the Watson-Crick helix, likely because of enhanced base stacking. Structural data confirm a right-handed, double-stranded, and base-paired helical form. Because of the larger base size, all the pairs of this helical system are fluorescent, which suggests practical applications in detection of natural DNA and RNA. Our findings establish that there is no apparent structural or thermodynamic prohibition against genetic systems having sizes different from the natural one.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Haibo -- Gao, Jianmin -- Lynch, Stephen R -- Saito, Y David -- Maynard, Lystranne -- Kool, Eric T -- GM52956/GM/NIGMS NIH HHS/ -- GM63587/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593180" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/*analogs & derivatives/chemistry ; *Base Pairing ; Base Sequence ; Benzene/chemistry ; Circular Dichroism ; Hydrogen Bonding ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; *Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/*chemistry ; Temperature ; Thermodynamics ; Thymine/*analogs & derivatives/chemistry
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  • 23
    Publication Date: 2003-06-14
    Description: Comparison of the gene-expression profiles between adults of Drosophila melanogaster and Drosophila simulans has uncovered the evolution of genes that exhibit sex-dependent regulation. Approximately half the genes showed differences in expression between the species, and among these, approximately 83% involved a gain, loss, increase, decrease, or reversal of sex-biased expression. Most of the interspecific differences in messenger RNA abundance affect male-biased genes. Genes that differ in expression between the species showed functional clustering only if they were sex-biased. Our results suggest that sex-dependent selection may drive changes in expression of many of the most rapidly evolving genes in the Drosophila transcriptome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranz, Jose M -- Castillo-Davis, Cristian I -- Meiklejohn, Colin D -- Hartl, Daniel L -- New York, N.Y. -- Science. 2003 Jun 13;300(5626):1742-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organismic and Evolutionary Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805547" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bayes Theorem ; Drosophila/*genetics ; Drosophila melanogaster/*genetics ; *Evolution, Molecular ; Female ; *Gene Expression ; Gene Expression Profiling ; Genes, Insect ; *Genome ; Male ; Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; RNA, Messenger/genetics/metabolism ; Selection, Genetic ; Sex Characteristics ; Species Specificity ; *Transcription, Genetic ; X Chromosome/genetics
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  • 24
    Publication Date: 2002-10-05
    Description: The detection of single-nucleotide polymorphisms in pathogenic microorganisms has normally been carried out by trial and error. Here we show that DNA hybridization with high-density oligonucleotide arrays provides rapid and convenient detection of single-nucleotide polymorphisms in Plasmodium falciparum, despite its exceptionally high adenine-thymine (AT) content (82%). A disproportionate number of polymorphisms are found in genes encoding proteins associated with the cell membrane. These genes are targets for only 22% of the oligonucleotide probes but account for 69% of the polymorphisms. Genetic variation is also enriched in subtelomeric regions, which account for 22% of the chromosome but 76% of the polymorphisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, Sarah K -- Hartl, Daniel L -- Wirth, Dyann F -- Nielsen, Kaare M -- Choi, Mehee -- Batalov, Serge -- Zhou, Yingyao -- Plouffe, David -- Le Roch, Karine G -- Abagyan, Ruben -- Winzeler, Elizabeth A -- GM61351/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):216-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes/genetics ; DNA, Protozoan/genetics ; *Genes, Protozoan ; Genetic Variation ; Genome, Protozoan ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Plasmodium falciparum/*genetics ; *Polymorphism, Single Nucleotide ; Protozoan Proteins/*genetics ; Sequence Analysis, DNA
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  • 25
    Publication Date: 2002-03-16
    Description: A 20-variable instance of the NP-complete three-satisfiability (3-SAT) problem was solved on a simple DNA computer. The unique answer was found after an exhaustive search of more than 1 million (2(20)) possibilities. This computational problem may be the largest yet solved by nonelectronic means. Problems of this size appear to be beyond the normal range of unaided human computation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Braich, Ravinderjit S -- Chelyapov, Nickolas -- Johnson, Cliff -- Rothemund, Paul W K -- Adleman, Leonard -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):499-502. Epub 2002 Mar 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Southern California, Laboratory for Molecular Science, Los Angeles, CA 90089-1340, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896237" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; *Computers ; *Computing Methodologies ; *Dna ; DNA, Single-Stranded ; Electrophoresis, Polyacrylamide Gel ; Gene Library ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-04-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reif, John H -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):478-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Computer Science Department, Duke University, Durham, NC 27708, USA. reif@cs.duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964464" target="_blank"〉PubMed〈/a〉
    Keywords: Automation ; Biotechnology ; Computers ; *Computing Methodologies ; *Dna ; DNA Restriction Enzymes ; DNA, Recombinant ; Nucleic Acid Hybridization ; Rna
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  • 27
    Publication Date: 2002-06-08
    Description: The use of direct-write dip-pen nanolithography (DPN) to generate covalently anchored, nanoscale patterns of oligonucleotides on both metallic and insulating substrates is described. Modification of DNA with hexanethiol groups allowed patterning on gold, and oligonucleotides bearing 5'-terminal acrylamide groups could be patterned on derivatized silica. Feature sizes ranging from many micrometers to less than 100 nanometers were achieved, and the resulting patterns exhibited the sequence-specific binding properties of the DNA from which they were composed. The patterns can be used to direct the assembly of individual oligonucleotide-modified particles on a surface, and the deposition of multiple DNA sequences in a single array is demonstrated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Demers, L M -- Ginger, D S -- Park, S-J -- Li, Z -- Chung, S-W -- Mirkin, C A -- 1 F32 HG02463/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1836-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Center for Nanofabrication and Molecular Self-Assembly, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052950" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; *DNA/chemistry ; *Gold ; Humidity ; *Microscopy, Atomic Force ; *Nanotechnology ; Nucleic Acid Hybridization ; *Oligodeoxyribonucleotides/chemistry ; Oligonucleotide Array Sequence Analysis ; *Oxides ; Silanes ; *Silicon Compounds ; Sulfhydryl Compounds ; Surface Properties ; Temperature
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  • 28
    Publication Date: 2002-07-06
    Description: Recent advances in the realization of individual molecular-scale electronic devices emphasize the need for novel tools and concepts capable of assembling such devices into large-scale functional circuits. We demonstrated sequence-specific molecular lithography on substrate DNA molecules by harnessing homologous recombination by RecA protein. In a sequence-specific manner, we patterned the coating of DNA with metal, localized labeled molecular objects and grew metal islands on specific sites along the DNA substrate, and generated molecularly accurate stable DNA junctions for patterning the DNA substrate connectivity. In our molecular lithography, the information encoded in the DNA molecules replaces the masks used in conventional microelectronics, and the RecA protein serves as the resist. The molecular lithography works with high resolution over a broad range of length scales from nanometers to many micrometers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keren, Kinneret -- Krueger, Michael -- Gilad, Rachel -- Ben-Yoseph, Gdalyahu -- Sivan, Uri -- Braun, Erez -- New York, N.Y. -- Science. 2002 Jul 5;297(5578):72-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Solid State Institute, Technion-Israel Institute of Technology, Haifa 32000, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12098693" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies ; Biopolymers ; Biotin ; DNA/chemistry/genetics/*metabolism ; DNA, Single-Stranded/*metabolism ; Electric Conductivity ; *Electronics ; Glutaral ; Gold ; Microscopy, Atomic Force ; Microscopy, Electron, Scanning ; *Nanotechnology ; Nucleic Acid Hybridization ; Rec A Recombinases/chemistry/immunology/*metabolism ; Recombination, Genetic ; Silver ; Streptavidin ; Templates, Genetic
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  • 29
    Publication Date: 2001-12-18
    Description: The duplication of the mammalian genome is an organized event, but there is limited information about the precision of the duplication program at specific genetic loci. We developed an approach that allows DNA replication events to be visualized in individual DNA molecules. Studying the latent replication of Epstein-Barr virus episomes, we show that different initiation sites are used to commence DNA replication from a specific portion of the viral genome (zone), whereas termination does not seem to be genomically defined. We conclude that initiation zones and pausing sites are major organizers of the duplication program, but initiation, fork progression, and termination of replication can vary in each molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norio, P -- Schildkraut, C L -- GM45751/GM/NIGMS NIH HHS/ -- P30CA13330/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2361-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. norio@aecom.yu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743204" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Replication ; DNA, Viral/biosynthesis/genetics ; Electrophoresis, Gel, Pulsed-Field ; Electrophoresis, Gel, Two-Dimensional ; Fluorescent Antibody Technique ; Genes, Viral ; *Genome, Viral ; Herpesvirus 4, Human/*genetics/*physiology ; Humans ; Microscopy, Fluorescence ; Nucleic Acid Hybridization ; *Plasmids ; Replication Origin ; Tumor Cells, Cultured ; Virus Replication
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  • 30
    Publication Date: 2001-11-10
    Description: We describe a microarray-based screen performed by imposing different genetic selections on thousands of yeast mutants in parallel, representing most genes in the yeast genome. The presence or absence of mutants was detected by oligonucleotide arrays that hybridize to 20-nucleotide "barcodes." We used this method to screen for components of the nonhomologous end-joining (NHEJ) pathway. Known components of the pathway were identified, as well as a gene not previously known to be involved in NHEJ, NEJ1. Nej1 protein interacts with the amino terminus of LIF1/XRCC4, a recently recognized "guardian of the genome" against cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ooi, S L -- Shoemaker, D D -- Boeke, J D -- GM36481/GM/NIGMS NIH HHS/ -- HG01627/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2552-6. Epub 2001 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, 617 Hunterian Building, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701889" target="_blank"〉PubMed〈/a〉
    Keywords: CCAAT-Binding Factor/genetics/metabolism ; DNA Ligases/genetics/metabolism ; *DNA Repair ; DNA-Binding Proteins/chemistry/genetics/metabolism ; Fungal Proteins/genetics/metabolism ; *Genes, Fungal ; Genetic Complementation Test ; *Mutation ; Nucleic Acid Hybridization ; *Oligonucleotide Array Sequence Analysis ; Plasmids ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics/physiology ; Saccharomyces cerevisiae Proteins/*genetics/metabolism ; Transcription Factors/genetics/metabolism ; Transformation, Genetic ; Two-Hybrid System Techniques
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jain, K K -- New York, N.Y. -- Science. 2001 Oct 19;294(5542):621-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11641502" target="_blank"〉PubMed〈/a〉
    Keywords: Computational Biology ; DNA Probes ; DNA, Complementary ; Diagnosis ; *Gene Expression Profiling ; Genetic Testing ; Genetics, Medical ; Genome, Human ; Genomics ; Humans ; Miniaturization ; Nucleic Acid Hybridization ; *Oligonucleotide Array Sequence Analysis/instrumentation/methods ; Pharmacogenetics ; Polymorphism, Single Nucleotide ; RNA, Messenger/genetics/metabolism ; Software
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  • 32
    Publication Date: 2001-10-06
    Description: Oligonucleotide microarrays were used to map the detailed topography of chromosome replication in the budding yeast Saccharomyces cerevisiae. The times of replication of thousands of sites across the genome were determined by hybridizing replicated and unreplicated DNAs, isolated at different times in S phase, to the microarrays. Origin activations take place continuously throughout S phase but with most firings near mid-S phase. Rates of replication fork movement vary greatly from region to region in the genome. The two ends of each of the 16 chromosomes are highly correlated in their times of replication. This microarray approach is readily applicable to other organisms, including humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raghuraman, M K -- Winzeler, E A -- Collingwood, D -- Hunt, S -- Wodicka, L -- Conway, A -- Lockhart, D J -- Davis, R W -- Brewer, B J -- Fangman, W L -- New York, N.Y. -- Science. 2001 Oct 5;294(5540):115-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Department of Mathematics, University of Washington, Seattle, WA 98195, USA. raghu@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11588253" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Sequence ; Centromere/metabolism ; Chromosomes, Fungal/genetics/*metabolism ; *DNA Replication ; DNA, Fungal/*biosynthesis/genetics/metabolism ; DNA, Intergenic ; Fourier Analysis ; *Genome, Fungal ; Kinetics ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; *Replication Origin ; *S Phase ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; Telomere/metabolism ; Transcription, Genetic
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  • 33
    Publication Date: 2001-09-15
    Description: We have assembled data from Caenorhabditis elegans DNA microarray experiments involving many growth conditions, developmental stages, and varieties of mutants. Co-regulated genes were grouped together and visualized in a three-dimensional expression map that displays correlations of gene expression profiles as distances in two dimensions and gene density in the third dimension. The gene expression map can be used as a gene discovery tool to identify genes that are co-regulated with known sets of genes (such as heat shock, growth control genes, germ line genes, and so forth) or to uncover previously unknown genetic functions (such as genomic instability in males and sperm caused by specific transposons).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, S K -- Lund, J -- Kiraly, M -- Duke, K -- Jiang, M -- Stuart, J M -- Eizinger, A -- Wylie, B N -- Davidson, G S -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2087-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology and Genetics, Stanford University Medical School, Stanford, CA 94305, USA. kim@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11557892" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Caenorhabditis elegans/*genetics/physiology ; *Computational Biology ; DNA Transposable Elements ; DNA, Complementary ; Databases, Factual ; Female ; *Gene Expression ; *Gene Expression Profiling ; Gene Expression Regulation ; *Genes, Helminth ; Genome ; *Genomics ; Helminth Proteins/biosynthesis/genetics ; Intestines/physiology ; Male ; Muscles/physiology ; Neurons/physiology ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; Oocytes/physiology ; RNA, Helminth/genetics ; Software ; Spermatozoa/physiology
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  • 34
    Publication Date: 2000-08-01
    Description: The path of the nucleic acids through a transcription elongation complex was tracked by mapping cross-links between bacterial RNA polymerase (RNAP) and transcript RNA or template DNA onto the x-ray crystal structure. In the resulting model, the downstream duplex DNA is nestled in a trough formed by the beta' subunit and enclosed on top by the beta subunit. In the RNAP channel, the RNA/DNA hybrid extends from the enzyme active site, along a region of the beta subunit harboring rifampicin resistance mutations, to the beta' subunit "rudder." The single-stranded RNA is then extruded through another channel formed by the beta-subunit flap domain. The model provides insight into the functional properties of the transcription complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korzheva, N -- Mustaev, A -- Kozlov, M -- Malhotra, A -- Nikiforov, V -- Goldfarb, A -- Darst, S A -- GM30717/GM/NIGMS NIH HHS/ -- GM49242/GM/NIGMS NIH HHS/ -- GM53759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 28;289(5479):619-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Public Health Research Institute, 455 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10915625" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cross-Linking Reagents ; Crystallography, X-Ray ; DNA/chemistry/genetics/*metabolism ; DNA Primers ; DNA-Directed RNA Polymerases/*chemistry/genetics/metabolism ; Models, Molecular ; Mutation ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/chemistry/metabolism ; Oligoribonucleotides/chemistry/metabolism ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Messenger/chemistry/genetics/*metabolism ; Templates, Genetic ; Thermus/enzymology ; *Transcription, Genetic
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: A human cytomegalovirus gene array was used to identify a previously unidentified class of viral transcripts. These transcripts, termed virion RNAs, were packaged within infectious virions and were delivered to the host cell on infection. This mechanism of herpesvirus gene expression allows for viral genes to be expressed within an infected cell immediately after virus entry and in the absence of transcription from the viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bresnahan, W A -- Shenk, T -- CA85786/CA/NCI NIH HHS/ -- F32 AI010448/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875924" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; Cells, Cultured ; Cytomegalovirus/*genetics/*physiology ; Dactinomycin/pharmacology ; Gene Expression ; Genes, Viral ; Genome, Viral ; Golgi Apparatus/metabolism ; Humans ; Nucleic Acid Hybridization ; Nucleic Acid Synthesis Inhibitors/pharmacology ; Oligonucleotide Array Sequence Analysis ; RNA, Messenger/*genetics/isolation & purification/metabolism ; RNA, Viral/*genetics/isolation & purification/metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription, Genetic ; Viral Proteins/genetics/metabolism ; Virion/*genetics/physiology ; Virus Assembly
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-03-31
    Description: All cellular organisms use specialized RNA polymerases called "primases" to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the "toprim" fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keck, J L -- Roche, D D -- Lynch, A S -- Berger, J M -- New York, N.Y. -- Science. 2000 Mar 31;287(5462):2482-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, no. 3206, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10741967" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Catalytic Domain ; Crystallography, X-Ray ; DNA Helicases/chemistry/metabolism ; DNA Primase/*chemistry/*metabolism ; DNA Replication ; DNA, Bacterial/metabolism ; DNA, Single-Stranded/*metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Escherichia coli/*enzymology/metabolism ; Metals/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA/biosynthesis ; Recombinant Proteins/chemistry/metabolism ; Templates, Genetic
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walt, D R -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):451-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Tufts University, Medford, MA 02155, USA. david.walt@tufts.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10671175" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Probes ; *Fiber Optic Technology ; Fluorescent Dyes ; Gene Expression Profiling/*methods ; Image Processing, Computer-Assisted ; Microspheres ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis/*methods ; Optical Fibers
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-08
    Description: A method for analyzing combinatorial DNA arrays using oligonucleotide-modified gold nanoparticle probes and a conventional flatbed scanner is described here. Labeling oligonucleotide targets with nanoparticle rather than fluorophore probes substantially alters the melting profiles of the targets from an array substrate. This difference permits the discrimination of an oligonucleotide sequence from targets with single nucleotide mismatches with a selectivity that is over three times that observed for fluorophore-labeled targets. In addition, when coupled with a signal amplification method based on nanoparticle-promoted reduction of silver(I), the sensitivity of this scanometric array detection system exceeds that of the analogous fluorophore system by two orders of magnitude.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taton, T A -- Mirkin, C A -- Letsinger, R L -- GM 57356/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1757-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Center for Nanofabrication and Molecular Self-Assembly, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10976070" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pair Mismatch ; Base Pairing ; Carbocyanines ; Fluorescent Dyes ; Gold ; Microscopy, Confocal ; Microscopy, Fluorescence ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis/instrumentation/*methods ; *Oligonucleotide Probes ; Sensitivity and Specificity ; Temperature
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  • 39
    Publication Date: 1999-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, S J -- Eisenberg, J F -- Miyamoto, M -- Hedges, S B -- Kumar, S -- Wilson, D E -- Menotti-Raymond, M -- Murphy, W J -- Nash, W G -- Lyons, L A -- Menninger, J C -- Stanyon, R -- Wienberg, J -- Copeland, N G -- Jenkins, N A -- Gellin, J -- Yerle, M -- Andersson, L -- Womack, J -- Broad, T -- Postlethwait, J -- Serov, O -- Bailey, E -- James, M R -- Marshall Graves, J A -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):463-78.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, Frederick, MD, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10577209" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Chromosome Mapping ; Chromosome Painting ; *Genome ; *Genome, Human ; Humans ; Mammals/*genetics ; Nucleic Acid Hybridization ; Phylogeny
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-11-27
    Description: In the S locus-controlled self-incompatibility system of Brassica, recognition of self-related pollen at the surface of stigma epidermal cells leads to inhibition of pollen tube development. The female (stigmatic) determinant of this recognition reaction is a polymorphic transmembrane receptor protein kinase encoded at the S locus. Another highly polymorphic, anther-expressed gene, SCR, also encoded at the S locus, fulfills the requirements for the hypothesized pollen determinant. Loss-of-function and gain-of-function studies prove that the SCR gene product is necessary and sufficient for determining pollen self-incompatibility specificity, possibly by acting as a ligand for the stigmatic receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schopfer, C R -- Nasrallah, M E -- Nasrallah, J B -- GM57527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1697-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576728" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Brassica/genetics/*physiology ; Cysteine/chemistry ; *Genes, Plant ; Germination ; Glycoproteins/genetics/metabolism ; Haplotypes ; Ligands ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plant Proteins/chemistry/*genetics/metabolism/*physiology ; Plant Structures/genetics/physiology ; Pollen/genetics/*physiology ; Polymorphism, Genetic ; Protein Kinases/genetics/metabolism ; Sequence Alignment ; Transformation, Genetic
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, T -- New York, N.Y. -- Science. 1999 Jul 16;285(5426):316-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10438292" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crigler-Najjar Syndrome/therapy ; DNA/chemistry/metabolism ; *DNA Repair ; Genes, Plant ; *Genetic Engineering ; Genetic Therapy/*methods ; Humans ; Mutagenesis ; Nucleic Acid Hybridization ; Oligonucleotides/metabolism ; Plants/genetics ; RNA/chemistry/metabolism ; Recombination, Genetic
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  • 42
    Publication Date: 1999-05-29
    Description: Bacille Calmette-Guerin (BCG) vaccines are live attenuated strains of Mycobacterium bovis administered to prevent tuberculosis. To better understand the differences between M. tuberculosis, M. bovis, and the various BCG daughter strains, their genomic compositions were studied by performing comparative hybridization experiments on a DNA microarray. Regions deleted from BCG vaccines relative to the virulent M. tuberculosis H37Rv reference strain were confirmed by sequencing across the missing segment of the H37Rv genome. Eleven regions (encompassing 91 open reading frames) of H37Rv were found that were absent from one or more virulent strains of M. bovis. Five additional regions representing 38 open reading frames were present in M. bovis but absent from some or all BCG strains; this is evidence for the ongoing evolution of BCG strains since their original derivation. A precise understanding of the genetic differences between closely related Mycobacteria suggests rational approaches to the design of improved diagnostics and vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Behr, M A -- Wilson, M A -- Gill, W P -- Salamon, H -- Schoolnik, G K -- Rane, S -- Small, P M -- New York, N.Y. -- Science. 1999 May 28;284(5419):1520-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, Department of Medicine, McGill University Health Centre, Montreal H3G 1A4, Canada. mbgq@musica.mcgill.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10348738" target="_blank"〉PubMed〈/a〉
    Keywords: BCG Vaccine/*genetics/immunology ; DNA, Bacterial/genetics ; Evolution, Molecular ; *Gene Deletion ; Genetic Variation ; *Genome, Bacterial ; Humans ; Mycobacterium bovis/*genetics/immunology/pathogenicity ; Mycobacterium tuberculosis/*genetics/immunology/pathogenicity ; Nucleic Acid Hybridization ; *Oligonucleotide Array Sequence Analysis ; Open Reading Frames ; Polymerase Chain Reaction ; Vaccines, Attenuated ; Virulence
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-04-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sikorski, R -- Peters, R -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1967.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9537907" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; DNA/*chemistry ; *Electric Conductivity ; Electrochemistry ; *Electrodes ; Miniaturization ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/*chemistry ; Silver/chemistry
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1998 Jun 12;280(5370):1692-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9660707" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Base Sequence ; Chromosome Inversion ; DNA/*genetics ; Evolution, Molecular ; *Genome, Human ; Humans ; *Multigene Family ; Nucleic Acid Hybridization ; *Polymorphism, Genetic ; RNA, Fungal/genetics ; RNA, Small Nuclear/*genetics ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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  • 45
    Publication Date: 1998-06-06
    Description: Single-nucleotide polymorphisms (SNPs) are the most frequent type of variation in the human genome, and they provide powerful tools for a variety of medical genetic studies. In a large-scale survey for SNPs, 2.3 megabases of human genomic DNA was examined by a combination of gel-based sequencing and high-density variation-detection DNA chips. A total of 3241 candidate SNPs were identified. A genetic map was constructed showing the location of 2227 of these SNPs. Prototype genotyping chips were developed that allow simultaneous genotyping of 500 SNPs. The results provide a characterization of human diversity at the nucleotide level and demonstrate the feasibility of large-scale identification of human SNPs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, D G -- Fan, J B -- Siao, C J -- Berno, A -- Young, P -- Sapolsky, R -- Ghandour, G -- Perkins, N -- Winchester, E -- Spencer, J -- Kruglyak, L -- Stein, L -- Hsie, L -- Topaloglou, T -- Hubbell, E -- Robinson, E -- Mittmann, M -- Morris, M S -- Shen, N -- Kilburn, D -- Rioux, J -- Nusbaum, C -- Rozen, S -- Hudson, T J -- Lipshutz, R -- Chee, M -- Lander, E S -- HG00098/HG/NHGRI NIH HHS/ -- HG01323/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1998 May 15;280(5366):1077-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582121" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Alleles ; Chromosome Mapping/*methods ; DNA, Complementary ; Databases, Factual ; Deoxyribonucleotides/*genetics ; Dinucleoside Phosphates ; Gene Expression ; Genetic Markers ; *Genetic Techniques ; Genetic Variation ; *Genome, Human ; *Genotype ; Heterozygote ; Homozygote ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; *Polymorphism, Genetic ; Reproducibility of Results ; Sequence Analysis, DNA ; Sequence Tagged Sites
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, R -- Sikorski, R -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1230.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9508693" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/analysis/*genetics ; Heterozygote ; Humans ; Monophenol Monooxygenase/*genetics ; Nucleic Acid Hybridization ; *Nucleic Acid Probes ; Peptides ; *Polymorphism, Genetic ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/*methods
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  • 47
    Publication Date: 1998-08-26
    Description: As more genomes are sequenced, the identification and characterization of the causes of heritable variation within a species will be increasingly important. It is demonstrated that allelic variation in any two isolates of a species can be scanned, mapped, and scored directly and efficiently without allele-specific polymerase chain reaction, without creating new strains or constructs, and without knowing the specific nature of the variation. A total of 3714 biallelic markers, spaced about every 3.5 kilobases, were identified by analyzing the patterns obtained when total genomic DNA from two different strains of yeast was hybridized to high-density oligonucleotide arrays. The markers were then used to simultaneously map a multidrug-resistance locus and four other loci with high resolution (11 to 64 kilobases).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winzeler, E A -- Richards, D R -- Conway, A R -- Goldstein, A L -- Kalman, S -- McCullough, M J -- McCusker, J H -- Stevens, D A -- Wodicka, L -- Lockhart, D J -- Davis, R W -- 1R01 HG01633/HG/NHGRI NIH HHS/ -- HG00185-01/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1998 Aug 21;281(5380):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. winzeler@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9712584" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Chromosome Mapping/*methods ; Cycloheximide/pharmacology ; Drug Resistance, Microbial/genetics ; Drug Resistance, Multiple/genetics ; Gene Deletion ; Genes, Fungal ; Genetic Linkage ; Genetic Markers ; *Genetic Techniques ; *Genetic Variation ; *Genome, Fungal ; Genotype ; Nucleic Acid Hybridization ; Phenotype ; Recombination, Genetic ; Saccharomyces cerevisiae/*genetics
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  • 48
    Publication Date: 1995-07-21
    Description: An insertional mutagenesis system that uses transposons carrying unique DNA sequence tags was developed for the isolation of bacterial virulence genes. The tags from a mixed population of bacterial mutants representing the inoculum and bacteria recovered from infected hosts were detected by amplification, radiolabeling, and hybridization analysis. When applied to a murine model of typhoid fever caused by Salmonella typhimurium, mutants with attenuated virulence were revealed by use of tags that were present in the inoculum but not in bacteria recovered from infected mice. This approach resulted in the identification of new virulence genes, some of which are related to, but functionally distinct from, the inv/spa family of S. typhimurium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hensel, M -- Shea, J E -- Gleeson, C -- Jones, M D -- Dalton, E -- Holden, D W -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):400-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Infectious Diseases and Bacteriology, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618105" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *DNA Transposable Elements ; *Genes, Bacterial ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; *Mutagenesis, Insertional ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Salmonella Infections, Animal/*microbiology ; Salmonella typhimurium/genetics/*pathogenicity ; Sequence Tagged Sites ; Virulence/genetics
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  • 49
    Publication Date: 1995-10-20
    Description: A high-capacity system was developed to monitor the expression of many genes in parallel. Microarrays prepared by high-speed robotic printing of complementary DNAs on glass were used for quantitative expression measurements of the corresponding genes. Because of the small format and high density of the arrays, hybridization volumes of 2 microliters could be used that enabled detection of rare transcripts in probe mixtures derived from 2 micrograms of total cellular messenger RNA. Differential expression measurements of 45 Arabidopsis genes were made by means of simultaneous, two-color fluorescence hybridization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schena, M -- Shalon, D -- Davis, R W -- Brown, P O -- R21HG00450/HG/NHGRI NIH HHS/ -- R37AG00198/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):467-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Beckman Center, Stanford University Medical Center, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569999" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics ; *Arabidopsis Proteins ; DNA, Complementary/*genetics ; DNA, Plant/genetics ; DNA-Binding Proteins ; *Gene Expression ; *Genes, Plant ; *Genetic Techniques ; Genome, Human ; Homeodomain Proteins ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plant Leaves/genetics ; Plant Roots/genetics ; Plants, Genetically Modified ; Polymerase Chain Reaction ; RNA Probes ; RNA, Messenger/genetics ; RNA, Plant/genetics ; Transcription Factors
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-14
    Description: Zinc finger proteins of the Cys2His2 type represent a large class of proteins that have been assumed to function by means of specific interactions with DNA. Experiments motivated by structural characteristics of zinc finger protein-DNA complexes revealed that certain zinc finger proteins bound DNA-RNA hybrids with affinities comparable to or greater than those for DNA duplexes. The interactions between the zinc finger proteins and the DNA-RNA hybrids were dependent on which strand was RNA and were sequence-specific. Thus, interactions with DNA-RNA hybrids should be considered with regard to the biological roles of zinc finger proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, Y -- Berg, J M -- GM46257/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):282-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7536342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/chemistry/*metabolism ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA/chemistry/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Sp1 Transcription Factor/metabolism ; Zinc Fingers/*physiology
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  • 51
    Publication Date: 1995-06-23
    Description: A gene, ATM, that is mutated in the autosomal recessive disorder ataxia telangiectasia (AT) was identified by positional cloning on chromosome 11q22-23. AT is characterized by cerebellar degeneration, immunodeficiency, chromosomal instability, cancer predisposition, radiation sensitivity, and cell cycle abnormalities. The disease is genetically heterogeneous, with four complementation groups that have been suspected to represent different genes. ATM, which has a transcript of 12 kilobases, was found to be mutated in AT patients from all complementation groups, indicating that it is probably the sole gene responsible for this disorder. A partial ATM complementary DNA clone of 5.9 kilobases encoded a putative protein that is similar to several yeast and mammalian phosphatidylinositol-3' kinases that are involved in mitogenic signal transduction, meiotic recombination, and cell cycle control. The discovery of ATM should enhance understanding of AT and related syndromes and may allow the identification of AT heterozygotes, who are at increased risk of cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savitsky, K -- Bar-Shira, A -- Gilad, S -- Rotman, G -- Ziv, Y -- Vanagaite, L -- Tagle, D A -- Smith, S -- Uziel, T -- Sfez, S -- Ashkenazi, M -- Pecker, I -- Frydman, M -- Harnik, R -- Patanjali, S R -- Simmons, A -- Clines, G A -- Sartiel, A -- Gatti, R A -- Chessa, L -- Sanal, O -- Lavin, M F -- Jaspers, N G -- Taylor, A M -- Arlett, C F -- Miki, T -- Weissman, S M -- Lovett, M -- Collins, F S -- Shiloh, Y -- HG00882/HG/NHGRI NIH HHS/ -- NS31763/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1749-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Sackler School of Medicine, Tel Aviv University, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792600" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ataxia Telangiectasia/*genetics ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle ; Cell Cycle Proteins ; Chromosome Mapping ; Chromosomes, Artificial, Yeast ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; DNA, Complementary/genetics ; DNA-Binding Proteins ; Female ; Genetic Complementation Test ; Genetic Predisposition to Disease ; Heterozygote ; Humans ; Male ; Meiosis ; Molecular Sequence Data ; Neoplasms/genetics ; Nucleic Acid Hybridization ; Phosphatidylinositol 3-Kinases ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/*genetics/physiology ; *Protein-Serine-Threonine Kinases ; Proteins/chemistry/*genetics/physiology ; Radiation Tolerance ; Sequence Deletion ; Signal Transduction ; Tumor Suppressor Proteins
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  • 52
    Publication Date: 1995-10-20
    Description: A physical map of Arabidopsis thaliana chromosome 4 was constructed in yeast artificial chromosome clones and used to analyze the organization of the chromosome. Mapping of the nucleolar organizing region and the centromere integrated the physical and cytogenetic maps. Detailed comparison of physical with genetic distances showed that the frequency of recombination varied substantially, with relative hot and cold spots occurring along the whole chromosome. Eight repeated DNA sequence families were found in a complex arrangement across the centromeric region and nowhere else on the chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmidt, R -- West, J -- Love, K -- Lenehan, Z -- Lister, C -- Thompson, H -- Bouchez, D -- Dean, C -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):480-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, Biotechnology, John Innes Centre, Colney, Norwich, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570002" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics ; Centromere/genetics ; *Chromosome Mapping ; Chromosome Walking ; Chromosomes/*genetics ; Chromosomes, Artificial, Yeast ; DNA, Plant/genetics ; DNA, Ribosomal/genetics ; *Genes, Plant ; Genetic Markers ; Genome, Plant ; Nucleic Acid Hybridization ; Nucleolus Organizer Region/genetics ; Polymorphism, Restriction Fragment Length ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):368-9, 371.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569988" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics ; Colon/metabolism ; Colonic Neoplasms/genetics ; DNA, Complementary/genetics ; *Gene Expression ; Genes, Fungal ; Genes, Plant ; *Genetic Techniques ; Humans ; Nucleic Acid Hybridization ; Pancreas/metabolism ; RNA, Messenger/genetics ; Saccharomyces cerevisiae/genetics ; Sequence Analysis, DNA
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  • 54
    Publication Date: 1994-12-16
    Description: Representational difference analysis was used to isolate unique sequences present in more than 90 percent of Kaposi's sarcoma (KS) tissues obtained from patients with acquired immunodeficiency syndrome (AIDS). These sequences were not present in tissue DNA from non-AIDS patients, but were present in 15 percent of non-KS tissue DNA samples from AIDS patients. The sequences are homologous to, but distinct from, capsid and tegument protein genes of the Gammaherpesvirinae, herpesvirus saimiri and Epstein-Barr virus. These KS-associated herpesvirus-like (KSHV) sequences appear to define a new human herpesvirus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Y -- Cesarman, E -- Pessin, M S -- Lee, F -- Culpepper, J -- Knowles, D M -- Moore, P S -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1865-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997879" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*complications ; Amino Acid Sequence ; Base Composition ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA, Viral/*analysis/chemistry/genetics ; Female ; Herpesviridae/*genetics ; Herpesvirus 2, Saimiriine/genetics ; Herpesvirus 4, Human/genetics ; Humans ; Male ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Open Reading Frames ; Polymerase Chain Reaction ; Retrospective Studies ; Sarcoma, Kaposi/etiology/*virology ; Sequence Homology, Amino Acid
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  • 55
    Publication Date: 1994-11-04
    Description: The tomato Cf-9 gene confers resistance to infection by races of the fungus Cladosporium fulvum that carry the avirulence gene Avr9. The Cf-9 gene was isolated by transposon tagging with the maize transposable element Dissociation. The DNA sequence of Cf-9 encodes a putative membrane-anchored extracytoplasmic glycoprotein. The predicted protein shows homology to the receptor domain of several receptor-like protein kinases in Arabidopsis, to antifungal polygalacturonase-inhibiting proteins in plants, and to other members of the leucine-rich repeat family of proteins. This structure is consistent with that of a receptor that could bind Avr9 peptide and activate plant defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, D A -- Thomas, C M -- Hammond-Kosack, K E -- Balint-Kurti, P J -- Jones, J D -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):789-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Developmental Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973631" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cladosporium/genetics/*physiology ; Consensus Sequence ; DNA Primers ; *DNA Transposable Elements ; Fungal Proteins/genetics ; Gene Targeting ; *Genes, Plant ; Glycoproteins/chemistry/*genetics ; Glycosylation ; Lycopersicon esculentum/chemistry/*genetics/microbiology ; Membrane Glycoproteins/chemistry/*genetics ; Molecular Sequence Data ; Multigene Family ; Nucleic Acid Hybridization ; Plant Proteins/chemistry/*genetics ; Plants, Genetically Modified ; Polymerase Chain Reaction ; Sequence Alignment
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2008-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091221" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping/*methods ; Genetic Linkage ; Genetic Markers ; Genetic Predisposition to Disease ; Genetics, Medical/*methods ; Genome, Fungal ; *Genome, Human ; Genotype ; Humans ; Nucleic Acid Hybridization
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, J -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1399-401.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197450" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chemistry, Organic/methods ; Chemistry, Pharmaceutical/*methods ; *Drug Design ; *Genetic Techniques ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Oligonucleotides/chemical synthesis/metabolism ; Peptides/chemical synthesis ; Protein Engineering/methods
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-12
    Description: The folding pathways of large, highly structured RNA molecules are largely unexplored. Insight into both the kinetics of folding and the presence of intermediates was provided in a study of the Mg(2+)-induced folding of the Tetrahymena ribozyme by hybridization of complementary oligodeoxynucleotide probes. This RNA folds via a complex mechanism involving both Mg(2+)-dependent and Mg(2+)-independent steps. A hierarchical model for the folding pathway is proposed in which formation of one helical domain (P4-P6) precedes that of a second helical domain (P3-P7). The overall rate-limiting step is formation of P3-P7, and takes place with an observed rate constant of 0.72 +/- 0.14 minute-1. The folding mechanism of large RNAs appears similar to that of many multidomain proteins in that formation of independently stable substructures precedes their association into the final conformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zarrinkar, P P -- Williamson, J R -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):918-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Introns ; Kinetics ; Magnesium/metabolism/pharmacology ; Models, Chemical ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; RNA, Catalytic/*chemistry/metabolism ; RNA, Protozoan/*chemistry ; Ribonuclease H/metabolism ; Temperature ; Tetrahymena/*genetics
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  • 59
    Publication Date: 1993-04-02
    Description: Point mutations that activate the Ki-ras proto-oncogene are presented in about 50 percent of human colorectal tumors. To study the functional significance of these mutations, the activated Ki-ras genes in two human colon carcinoma cell lines, DLD-1 and HCT 116, were disrupted by homologous recombination. Compared with parental cells, cells disrupted at the activated Ki-ras gene were morphologically altered, lost the capacity for anchorage-independent growth, grew more slowly both in vitro and in nude mice, and showed reduced expression of c-myc. Thus, the activated Ki-ras gene plays a key role in colorectal tumorigenesis through altered cell differentiation and cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shirasawa, S -- Furuse, M -- Yokoyama, N -- Sasazuki, T -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Kyushu University, Fukuoka, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465203" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Differentiation ; Cell Division ; Codon ; Colonic Neoplasms/*genetics/pathology ; Gene Expression Regulation, Neoplastic ; Genes, myc/genetics ; Genes, ras/*genetics ; Humans ; Infant ; Mice ; Mice, Nude ; Molecular Sequence Data ; Mutagenesis, Insertional ; Nucleic Acid Hybridization ; Plasmids ; *Point Mutation ; Polymerase Chain Reaction ; Restriction Mapping ; Transfection ; Tumor Cells, Cultured
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1993-10-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, L M -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):530-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211178" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Primers ; Electrophoresis/methods ; Human Genome Project ; Humans ; Mass Spectrometry ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA/*methods
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  • 61
    Publication Date: 1993-04-02
    Description: Two forms of a member of the POU domain family of transcriptional regulators, highly related to Oct-2, are selectively expressed in terminally differentiating epidermis and hair follicles. One form, referred to as Skn-1i, contains an amino-terminal domain that inhibits DNA binding and can inhibit transactivation by Oct-1. A second form, Skn-1a, contains an alternative amino terminus and serves to activate cytokeratin 10 (K10) gene expression. The pattern of expression of the Skn-1a/i gene products and the effect of the alternative products on the expression of other genes suggest that these factors serve regulatory functions with respect to epidermal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andersen, B -- Schonemann, M D -- Flynn, S E -- Pearse, R V 2nd -- Singh, H -- Rosenfeld, M G -- DK39949/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):78-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Regulatory Biology Program, Howard Hughes Medical Institute, University of California School of Medicine, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7682011" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; DNA/chemistry/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics ; Epidermis/*metabolism ; *Gene Expression/drug effects ; Keratins/genetics ; Leucine Zippers ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Octamer Transcription Factor-2 ; Polymerase Chain Reaction ; *Repressor Proteins ; Sequence Homology, Amino Acid ; Transcription Factors/chemistry/*genetics/metabolism/pharmacology
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  • 62
    Publication Date: 1993-01-08
    Description: Soon after methicillin was introduced into clinical practice in the early 1960s, resistant strains of Staphylococcus aureus (MRSA) appeared, bearing a newly acquired resistance gene, mecA, that encodes a penicillin binding protein, PBP2a. MRSA have spread throughout the world, and an investigation of the clonality of 472 isolates by DNA hybridization was performed. All 472 isolates could be divided into six temporally ordered mecA hybridization patterns, and three of these were subdivided by the chromomosomal transposon Tn554. Each Tn554 pattern occurred in association with one and only one mecA pattern, suggesting that mecA divergence preceded the acquisition of Tn554 in all cases and therefore that mecA may have been acquired just once by S. aureus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kreiswirth, B -- Kornblum, J -- Arbeit, R D -- Eisner, W -- Maslow, J N -- McGeer, A -- Low, D E -- Novick, R P -- AI22159/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):227-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bureau of Laboratories, New York City Department of Health, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8093647" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Proteins ; Biological Evolution ; Carrier Proteins/genetics ; DNA Transposable Elements ; DNA, Bacterial/analysis/genetics ; Deoxyribonucleases, Type II Site-Specific ; *Hexosyltransferases ; Methicillin Resistance/*genetics ; Muramoylpentapeptide Carboxypeptidase/genetics ; Nucleic Acid Hybridization ; Penicillin-Binding Proteins ; *Peptidyl Transferases ; Polymorphism, Restriction Fragment Length ; Staphylococcus aureus/drug effects/*genetics
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-06
    Description: The HM1 gene in maize controls both race-specific resistance to the fungus Cochliobolus carbonum race 1 and expression of the NADPH (reduced form of nicotinamide adenine dinucleotide phosphate)-dependent HC toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus to permit infection. Several HM1 alleles were generated and cloned by transposon-induced mutagenesis. The sequence of wild-type HM1 shares homology with dihydroflavonol-4-reductase genes from maize, petunia, and snap-dragon. Sequence homology is greatest in the beta alpha beta-dinucleotide binding fold that is conserved among NADPH- and NADH (reduced form of nicotinamide adenine dinucleotide)-dependent reductases and dehydrogenases. This indicates that HM1 encodes HCTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johal, G S -- Briggs, S P -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):985-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology Research, Pioneer Hi-Bred International, Inc., Johnston, IA 50131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA/chemistry/genetics ; *Genes, Plant ; *Helminthosporium ; Introns ; Molecular Sequence Data ; NADP/pharmacology ; Nucleic Acid Hybridization ; Oxidoreductases/chemistry/*genetics ; Peptides, Cyclic/antagonists & inhibitors ; *Plant Diseases ; *Plant Proteins ; Polymorphism, Restriction Fragment Length ; RNA Splicing ; RNA, Messenger/genetics ; Zea mays/enzymology/*genetics
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  • 64
    Publication Date: 1992-09-04
    Description: The Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV), which is used for the overexpression of eukaryotic genes and is being engineered for possible use as a viral insecticide, has a circular, supercoiled genome of approximately 128 kilobases. Despite its widespread use, little is known about the mechanism by which AcMNPV replicates. Evidence is presented in this report that AcMNPV origins of DNA replication are repeated sequences each containing several closely related imperfect palindromes that are present in six regions distributed around the genome. Although AcMNPV infection-dependent plasmid replication was initiated by a single complete palindrome, the amount of replication was substantially increased in plasmids containing six or eight palindromes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, M -- Bjornson, R -- Pearson, G -- Rohrmann, G -- AI21973/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1382-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Agricultural Chemistry, Oregon State University, Corvallis 97331.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529337" target="_blank"〉PubMed〈/a〉
    Keywords: Baculoviridae/*genetics ; Base Sequence ; *DNA Replication ; DNA, Superhelical/chemistry/*genetics ; DNA, Viral/chemistry/*genetics ; Genes, Viral/*genetics ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Hybridization ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Transfection ; *Virus Replication
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-20
    Description: A synthetic RNA-DNA bubble duplex construct intended to mimic the nucleic acid framework of a functional transcription elongation complex was designed and assembled. The construct consisted of a double-stranded DNA duplex of variable length (the template and nontemplate strands) containing an internal noncomplementary DNA "bubble" sequence. The 3' end of an RNA oligonucleotide that is partially complementary to the template DNA strand was hybridized within the DNA bubble to form an RNA-DNA duplex with a non-complementary 5'-terminal RNA tail. The addition of either Escherichia coli or T7 RNA polymerase to this construct formed a complex that synthesized RNA with good efficiency from the hybridized RNA primer in a template-directed and processive manner, and displayed other features of a normal promoter-initiated transcription elongation complex. Other such constructs can be designed to examine many of the functional and regulatory properties of transcription systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daube, S S -- von Hippel, P H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1320-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1280856" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology/genetics ; In Vitro Techniques ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Promoter Regions, Genetic ; RNA/genetics ; Structure-Activity Relationship ; Templates, Genetic ; *Transcription, Genetic
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-11-13
    Description: Two DNA strand transfer reactions occur during retroviral reverse transcription. The mechanism of the first, minus strand strong-stop DNA, transfer has been studied in vitro with human immunodeficiency virus 1 reverse transcriptase (HIV-1 RT) and a model template-primer system derived from the HIV-1 genome. The results reveal that HIV-1 RT alone can catalyze DNA strand transfer reactions. Two kinetically distinct ribonuclease (RNase) H activities associated with HIV-1 RT are required for removal of RNA fragments annealed to the nascent DNA strand. Examination of the binding of DNA.RNA duplex and single-stranded RNA to HIV-1 RT during strand transfer supports a model where the enzyme accommodates both the acceptor RNA template and the nascent DNA strand before the transfer event is completed. The polymerase activity incorporated additional bases beyond the 5' end of the RNA template, resulting in a base misincorporation upon DNA strand transfer. Such a process occurring in vivo during retroviral homologous recombination could contribute to the hypermutability of the HIV-1 genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peliska, J A -- Benkovic, S J -- AI08275/AI/NIAID NIH HHS/ -- GM13306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1112-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park 16802.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279806" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; DNA, Viral/biosynthesis/chemistry/*metabolism ; Deoxyribonucleotides ; HIV Reverse Transcriptase ; HIV-1/*enzymology/genetics ; Kinetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; RNA, Transfer/metabolism ; RNA, Viral/chemistry/metabolism ; RNA-Directed DNA Polymerase/genetics/*metabolism ; Ribonuclease H/metabolism ; Templates, Genetic
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  • 67
    Publication Date: 1992-08-21
    Description: A point mutation in the POU-specific portion of the human gene that encodes the tissue-specific POU-domain transcription factor, Pit-1, results in hypopituitarism, with deficiencies of growth hormone, prolactin, and thyroid-stimulating hormone. In two unrelated Dutch families, a mutation in Pit-1 that altered an alanine in the first putative alpha helix of the POU-specific domain to proline was observed. This mutation generated a protein capable of binding to DNA response elements but unable to effectively activate its known target genes, growth hormone and prolactin. The phenotype of the affected individuals suggests that the mutant Pit-1 protein is competent to initiate other programs of gene activation required for normal proliferation of somatotrope, lactotrope, and thyrotrope cell types. Thus, a mutation in the POU-specific domain of Pit-1 has a selective effect on a subset of Pit-1 target genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfaffle, R W -- DiMattia, G E -- Parks, J S -- Brown, M R -- Wit, J M -- Jansen, M -- Van der Nat, H -- Van den Brande, J L -- Rosenfeld, M G -- Ingraham, H A -- HD24960/HD/NICHD NIH HHS/ -- HD2697/HD/NICHD NIH HHS/ -- NIDDK 18477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1118-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509263" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Northern ; DNA/chemistry/metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Growth Hormone/deficiency ; Humans ; Hypopituitarism/*genetics/pathology ; Mice ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Pituitary Gland, Anterior/*pathology ; Pituitary Hormones/*deficiency ; Polymerase Chain Reaction ; Prolactin/deficiency ; Rats ; Sequence Homology, Nucleic Acid ; Thyrotropin/deficiency ; Transcription Factor Pit-1 ; Transcription Factors/*genetics/metabolism ; Transfection
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  • 68
    Publication Date: 1992-06-12
    Description: Glutamate-operated ion channels (GluR channels) of the L-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-kainate subtype are found in both neurons and glial cells of the central nervous system. These channels are assembled from the GluR-A, -B, -C, and -D subunits; channels containing a GluR-B subunit show an outwardly rectifying current-voltage relation and low calcium permeability, whereas channels lacking the GluR-B subunit are characterized by a doubly rectifying current-voltage relation and high calcium permeability. Most cell types in the central nervous system coexpress several subunits, including GluR-B. However, Bergmann glia in rat cerebellum do not express GluR-B subunit genes. In a subset of cultured cerebellar glial cells, likely derived from Bergmann glial cells. GluR channels exhibit doubly rectifying current-voltage relations and high calcium permeability, whereas GluR channels of cerebellar neurons have low calcium permeability. Thus, differential expression of the GluR-B subunit gene in neurons and glia is one mechanism by which functional properties of native GluR channels are regulated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnashev, N -- Khodorova, A -- Jonas, P -- Helm, P J -- Wisden, W -- Monyer, H -- Seeburg, P H -- Sakmann, B -- New York, N.Y. -- Science. 1992 Jun 12;256(5063):1566-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Medizinische Forschung, Abteilung Zellphysiologie, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317970" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cell Membrane Permeability ; Cells, Cultured ; Cerebellum/*physiology ; Gene Expression ; Glutamates/physiology ; In Vitro Techniques ; Ion Channel Gating ; Neuroglia/*physiology ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Rats ; Receptors, Kainic Acid ; Receptors, Neurotransmitter/*physiology
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  • 69
    Publication Date: 1992-06-19
    Description: A triple helix is formed upon binding of an oligodeoxynucleotide to the major groove of duplex DNA. A benzo[e]pyridoindole derivative (BePI) strongly stabilized this structure and showed preferential binding to a triplex rather than to a duplex. Energy transfer experiments suggest that BePI intercalates within the triple helix. Sequence-specific inhibition of transcription initiation of a specific gene by Escherichia coli RNA polymerase by a triplex-forming oligodeoxynucleotide is strongly enhanced when the triplex is stabilized by BePI. Upon irradiation with ultraviolet light, BePI induces covalent modifications of the target within the triple helix structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mergny, J L -- Duval-Valentin, G -- Nguyen, C H -- Perrouault, L -- Faucon, B -- Rougee, M -- Montenay-Garestier, T -- Bisagni, E -- Helene, C -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1681-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biophysique, Institut National de la Sante et de la Recherche Medicale, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1609278" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Carbolines/metabolism ; DNA/genetics/*metabolism ; DNA-Directed RNA Polymerases/genetics/metabolism ; Escherichia coli/*genetics ; Hot Temperature ; In Vitro Techniques ; *Ligands ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Transcription, Genetic
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-05-01
    Description: A eukaryotic chromosomal origin of replication was identified in the yeast Saccharomyces cerevisiae. By several criteria, including map position, deletion analysis, and a synthetic form of saturation mutagenesis, the origin co-localized with the HMR-E silencer, which is a DNA element that represses transcription of the adjacent genes. A specific site within the silencer was required for both initiation of chromosomal replication and for repression of transcription. This analysis directly demonstrates that initiation of eukaryotic chromosomal replication is dependent on specific sequence elements and that a particular element can act in both initiation of chromosomal replication and regulation of transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivier, D H -- Rine, J -- ES07075/ES/NIEHS NIH HHS/ -- GM 31105/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 1;256(5057):659-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585179" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; *DNA Replication ; DNA, Fungal/biosynthesis ; *Gene Expression Regulation, Fungal ; Genes, Fungal ; Mutagenesis ; Nucleic Acid Hybridization ; *Regulatory Sequences, Nucleic Acid ; Saccharomyces cerevisiae/*genetics ; *Transcription, Genetic
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  • 71
    Publication Date: 1992-09-04
    Description: The folding of chromatin in interphase cell nuclei was studied by fluorescent in situ sequences chromatin according to a random walk model. This model provides the basis for calculating the spacing of sequences along the linear DNA molecule from interphase distance measurements. An interphase mapping strategy based on this model was tested with 13 probes from a 4-megabase pair (Mbp) region of chromosome 4 containing the Huntington disease locus. The results confirmed the locations of the probes and showed that the remaining gap in the published maps of this region is negligible in size. Interphase distance measurements should facilitate construction of chromosome maps with an average marker density of one per 100 kbp, approximately ten times greater than that achieved by hybridization to metaphase chromosome. achieved by hybridization to metaphase chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van den Engh, G -- Sachs, R -- Trask, B J -- HG00256/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1410-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Genome Center, Lawrence Livermore National Laboratory, Livermore, CA 94550.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1388286" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/*chemistry ; Chromatin/*chemistry ; Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Cosmids ; DNA/*chemistry ; DNA Probes ; Humans ; Huntington Disease/genetics ; *Interphase ; Metaphase ; Nucleic Acid Hybridization
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  • 72
    Publication Date: 1992-03-06
    Description: Myotonic dystrophy (DM) is the most common inherited neuromuscular disease in adults, with a global incidence of 1 in 8000 individuals. DM is an autosomal dominant, multisystemic disorder characterized primarily by myotonia and progressive muscle weakness. Genomic and complementary DNA probes that map to a 10-kilobase Eco RI genomic fragment from human chromosome 19q13.3 have been used to detect a variable length polymorphism in individuals with DM. Increases in the size of the allele in patients with DM are now shown to be due to an increased number of trinucleotide CTG repeats in the 3' untranslated region of a DM candidate gene. An increase in the severity of the disease in successive generations (genetic anticipation) is accompanied by an increase in the number of trinucleotide repeats. Nearly all cases of DM (98 percent or 253 of 258 individuals) displayed expansion of the CTG repeat region. These results suggest that DM is primarily caused by mutations that generate an amplification of a specific CTG repeat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahadevan, M -- Tsilfidis, C -- Sabourin, L -- Shutler, G -- Amemiya, C -- Jansen, G -- Neville, C -- Narang, M -- Barcelo, J -- O'Hoy, K -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1253-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Ottawa, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546325" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosomes, Human, Pair 19 ; Codon ; DNA/*chemistry ; Deoxyribonuclease EcoRI ; Humans ; Molecular Sequence Data ; *Mutation ; Myotonic Dystrophy/*genetics ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping
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  • 73
    Publication Date: 1992-03-20
    Description: The suprachiasmatic nuclei (SCN) of the hypothalamus comprise the primary pacemaker responsible for generation of circadian rhythms in mammals. Light stimuli that synchronize this circadian clock induce expression of the c-fos gene in rodent SCN, which suggests a possible role for Fos in circadian entrainment. Appropriate light stimuli also induce the expression of jun-B messenger RNA in the SCN of golden hamsters but only slightly elevate c-jun messenger RNA levels. In addition, light increases the amount of a protein complex in the SCN that binds specifically to sites on DNA known to mediate regulation by the AP-1 transcription factor. The photic regulation of both jun-B messenger RNA expression and AP-1 binding activity is dependent on circadian phase: only light stimuli that shift behavioral rhythms induce jun-B and AP-1 expression. Thus, light and the circadian pacemaker interact to regulate a specific set of immediate-early genes in the SCN that may participate in entrainment of the circadian clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kornhauser, J M -- Nelson, D E -- Mayo, K E -- Takahashi, J S -- New York, N.Y. -- Science. 1992 Mar 20;255(5051):1581-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Neuroscience, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1549784" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cricetinae ; *Gene Expression Regulation ; Genes, fos/physiology ; Genes, jun/*physiology ; *Light ; Molecular Sequence Data ; Nucleic Acid Hybridization ; *Periodicity ; Proto-Oncogene Proteins c-jun/*biosynthesis ; RNA Probes ; RNA, Messenger/*biosynthesis ; Suprachiasmatic Nucleus/physiology ; Time Factors ; Transcription, Genetic
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  • 74
    Publication Date: 1992-03-16
    Description: Synthetic oligonucleotides containing GC-rich triplet sequences were used in a scanning strategy to identify unstable genetic sequences at the myotonic dystrophy (DM) locus. A highly polymorphic GCT repeat was identified and found to be unstable, with an increased number of repeats occurring in DM patients. In the case of severe congenital DM, the paternal triplet allele was inherited unaltered while the maternal, DM-associated allele was unstable. These studies suggest that the mutational mechanism leading to DM is triplet amplification, similar to that occurring in the fragile X syndrome. The triplet repeat sequence is within a gene (to be referred to as myotonin-protein kinase), which has a sequence similar to protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, Y H -- Pizzuti, A -- Fenwick, R G Jr -- King, J -- Rajnarayan, S -- Dunne, P W -- Dubel, J -- Nasser, G A -- Ashizawa, T -- de Jong, P -- 5-M01-RR00350/RR/NCRR NIH HHS/ -- P30-HG00210/HG/NHGRI NIH HHS/ -- P50HL42267-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1256-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Genetics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546326" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosomes, Human, Pair 19 ; Cloning, Molecular ; DNA/chemistry ; Humans ; Molecular Sequence Data ; Mutation ; Myotonic Dystrophy/*genetics ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Polymorphism, Genetic ; *Repetitive Sequences, Nucleic Acid
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  • 75
    Publication Date: 1992-08-21
    Description: Complementary DNA clones from the pink-eyed dilution (p) locus of mouse chromosome 7 were isolated from murine melanoma and melanocyte libraries. The transcript from this gene is missing or altered in six independent mutant alleles of the p locus, suggesting that disruption of this gene results in the hypopigmentation phenotype that defines mutant p alleles. Characterization of the human homolog revealed that it is localized to human chromosome 15 at q11.2-q12, a region associated with Prader-Willi and Angelman syndromes, suggesting that altered expression of this gene may be responsible for the hypopigmentation phenotype exhibited by certain individuals with these disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardner, J M -- Nakatsu, Y -- Gondo, Y -- Lee, S -- Lyon, M F -- King, R A -- Brilliant, M H -- CA06927/CA/NCI NIH HHS/ -- GM22167/GM/NIGMS NIH HHS/ -- GM43840/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1121-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509264" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Carrier Proteins ; Chromosomes, Human, Pair 15 ; Cloning, Molecular ; DNA/genetics ; Humans ; Melanocytes/chemistry ; Melanoma, Experimental/chemistry ; *Membrane Proteins ; *Membrane Transport Proteins ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Phenotype ; Pigmentation Disorders/*genetics ; Prader-Willi Syndrome/*genetics ; Proteins/chemistry ; Sequence Homology, Nucleic Acid
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  • 76
    Publication Date: 1992-11-27
    Description: Studies of a series of short oligonucleotide double and triple helices containing either all RNA, all DNA, or a mixture of the two show strand-dependent variation in their stability and structure. The variation in stability for both groups falls over a range of greater than 10 kilocalories per mole. In forming the triple helix, RNA is favored on both pyrimidine strands, whereas DNA is favored on the purine strand. In general, relatively unstable duplexes form particularly stable triplexes and vice versa. Structural data indicate that the strands in hybrid helices adopt a conformation that is intermediate between molecules containing all DNA and all RNA. Thus, RNA-DNA hybrids were not forced into the conformation of the RNA (A-form). The provocative stability of the triplex with an RNA third strand+DNA duplex points to novel antisense strategies and opens the possibility of an in vivo role of these structures. Overall, the data emphasize the fundamental role of sugars in determining the properties of nucleic acid complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, R W -- Crothers, D M -- GAR21966/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1463-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279808" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; Macromolecular Substances ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Oligonucleotides/chemistry ; RNA/*chemistry ; Thermodynamics
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  • 77
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1992-06-12
    Description: The neurohypophyseal hormone oxytocin (OT) is the most potent uterotonic agent known and is used to induce labor. Yet, endogenous circulating OT appears not to participate in the induction of labor. As shown here, the finding of OT messenger RNA and peptide in the uterus suggests a solution for this paradox. During gestation, rat uterus OT messenger RNA increased more than 150-fold and, at term, exceeded hypothalamic OT messenger RNA by 70-fold. Thus, during parturition, OT may act primarily as a local mediator and not as a circulating hormone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lefebvre, D L -- Giaid, A -- Bennett, H -- Lariviere, R -- Zingg, H H -- New York, N.Y. -- Science. 1992 Jun 12;256(5063):1553-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Gene Expression ; Hypothalamus/physiology ; Nucleic Acid Hybridization ; Oxytocin/*genetics ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Rats ; Uterus/*physiology
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  • 78
    Publication Date: 1991-05-03
    Description: Although bladder cancers are very common, little is known about their molecular pathogenesis. In this study, invasive bladder cancers were evaluated for the presence of gene mutations in the p53 suppressor gene. Of 18 tumors evaluated, 11 (61 percent) were found to have genetic alterations of p53. The alterations included ten point mutations resulting in single amino acid substitutions, and one 24-base pair deletion. In all but one case, the mutations were associated with chromosome 17p allelic deletions, leaving the cells with only mutant forms of the p53 gene products. Through the use of the polymerase chain reaction and oligomer-specific hybridization, p53 mutations were identified in 1 to 7 percent of the cells within the urine sediment of each of three patients tested. The p53 mutations are the first genetic alterations demonstrated to occur in a high proportion of primary invasive bladder cancers. Detection of such mutations ex vivo has clinical implications for monitoring individuals whose tumor cells are shed extracorporeally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidransky, D -- Von Eschenbach, A -- Tsai, Y C -- Jones, P -- Summerhayes, I -- Marshall, F -- Paul, M -- Green, P -- Hamilton, S R -- Frost, P -- CA09071/CA/NCI NIH HHS/ -- CA43460/CA/NCI NIH HHS/ -- CA49758/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):706-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024123" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Deletion ; Chromosomes, Human, Pair 17 ; *Genes, p53 ; Humans ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Urinary Bladder Neoplasms/*genetics/urine ; Urine/cytology
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  • 79
    Publication Date: 1991-01-04
    Description: An expression cloning strategy was devised to isolate the keratinocyte growth factor (KGF) receptor complementary DNA. NIH/3T3 fibroblasts, which secrete this epithelial cell-specific mitogen, were transfected with a keratinocyte expression complementary DNA library. Among several transformed foci identified, one demonstrated the acquisition of specific high-affinity KGF binding sites. The pattern of binding competition by related fibroblast growth factors (FGFs) indicated that this receptor had high affinity for acidic FGF as well as KGF. The rescued 4.2-kilobase complementary DNA was shown to encode a predicted membrane-spanning tyrosine kinase related to but distinct from the basic FGF receptor. This expression cloning approach may be generally applicable to the isolation of genes that constitute limiting steps in mitogenic signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miki, T -- Fleming, T P -- Bottaro, D P -- Rubin, J S -- Ron, D -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):72-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846048" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cell Line ; *Cloning, Molecular ; DNA/*genetics ; Fibroblast Growth Factor 10 ; Fibroblast Growth Factor 7 ; Fibroblast Growth Factors/metabolism ; Fibroblasts/metabolism ; *Gene Expression ; Growth Substances/metabolism ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; Receptor, Fibroblast Growth Factor, Type 2 ; Receptors, Cell Surface/*genetics/metabolism ; *Receptors, Fibroblast Growth Factor ; Recombinant Proteins/metabolism ; Transfection ; Transformation, Genetic
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  • 80
    Publication Date: 1991-01-18
    Description: Concerted evolution is the production and maintenance of homogeneity within repeated families of DNA. Two mechanisms--unequal crossing over and biased gene conversion--have been the principal explanations of concerted evolution. Concerted evolution of ribosomal DNA (rDNA) arrays is thought to be largely the result of unequal crossing over. However, concerted evolution of rDNA in parthenogenetic lizards of hybrid origin is strongly biased toward one of two parental sequences, which is consistent with biased gene conversion as the operative mechanism. The apparent gene conversions are independent of initial genome dosage and result in homogenization of rDNA arrays across all nucleolar organizer regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hillis, D M -- Moritz, C -- Porter, C A -- Baker, R J -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):308-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1987647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Blotting, Southern ; DNA, Ribosomal/*genetics ; Gene Conversion ; Karyotyping ; Lizards ; Nucleic Acid Hybridization ; Parthenogenesis ; Restriction Mapping
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  • 81
    Publication Date: 1991-08-02
    Description: Calcium-activated potassium channels mediate many biologically important functions in electrically excitable cells. Despite recent progress in the molecular analysis of voltage-activated K+ channels, Ca(2+)-activated K+ channels have not been similarly characterized. The Drosophila slowpoke (slo) locus, mutations of which specifically abolish a Ca(2+)-activated K+ current in muscles and neurons, provides an opportunity for molecular characterization of these channels. Genomic and complementary DNA clones from the slo locus were isolated and sequenced. The polypeptide predicted by slo is similar to voltage-activated K+ channel polypeptides in discrete domains known to be essential for function. Thus, these results indicate that slo encodes a structural component of Ca(2+)-activated K+ channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Atkinson, N S -- Robertson, G A -- Ganetzky, B -- NS15390/NS/NINDS NIH HHS/ -- T32 GM07131/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):551-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857984" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Chromosome Aberrations ; Chromosome Deletion ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Drosophila/*genetics/physiology ; Exons ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Phenotype ; Potassium Channels/drug effects/*genetics/physiology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Translocation, Genetic
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  • 82
    Publication Date: 1991-03-08
    Description: Yeast artificial chromosomes (YACs) were obtained from a 550-kilobase region that contains three probes previously mapped as very close to the locus of the fragile X syndrome. These YACs spanned the fragile site in Xq27.3 as shown by fluorescent in situ hybridization. An internal 200-kilobase segment contained four chromosomal breakpoints generated by induction of fragile X expression. A single CpG island was identified in the cloned region between markers DXS463 and DXS465 that appears methylated in mentally retarded fragile X males, but not in nonexpressing male carriers of the mutation nor in normal males. This CpG island may indicate the presence of a gene involved in the clinical phenotype of the syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitz, D -- Rousseau, F -- Devys, D -- Saccone, S -- Abderrahim, H -- Le Paslier, D -- Cohen, D -- Vincent, A -- Toniolo, D -- Della Valle, G -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1236-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, Institut de Chimie Biologique, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006411" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Fungal ; Cloning, Molecular ; DNA Probes ; *Dinucleoside Phosphates ; Fragile X Syndrome/*genetics ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Reference Values ; Restriction Mapping ; Saccharomyces cerevisiae/genetics ; *X Chromosome
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  • 83
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-09-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1489.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1896858" target="_blank"〉PubMed〈/a〉
    Keywords: *Base Sequence ; *Computers ; DNA/*genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides ; Sequence Homology, Nucleic Acid
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  • 84
    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is a member of a family of pro-inflammatory cytokines. Although the best characterized activities of IL-8 include the chemoattraction and activation of neutrophils, other members of this family have a wide range of specific actions including the chemotaxis and activation of monocytes, the selective chemotaxis of memory T cells, the inhibition of hematopoietic stem cell proliferation, and the induction of neutrophil infiltration in vivo. A complementary DNA encoding the IL-8 receptor from human neutrophils has now been isolated. The amino acid sequence shows that the receptor is a member of the superfamily of receptors that couple to guanine nucleotide binding proteins (G proteins). The sequence is 29% identical to that of receptors for the other neutrophil chemoattractants, fMet-Leu-Phe and C5a. Mammalian cells transfected with the IL-8 receptor cDNA clone bind IL-8 with high affinity and respond specifically to IL-8 by transiently mobilizing calcium. The IL-8 receptor may be part of a subfamily of related G protein-coupled receptors that transduce signals for the IL-8 family of pro-inflammatory cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lee, J -- Kuang, W J -- Rice, G C -- Wood, W I -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840701" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; DNA Probes ; Humans ; Interleukin-8/*metabolism ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; RNA, Messenger/genetics ; Receptors, Immunologic/*genetics/metabolism ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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  • 85
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-10-04
    Description: DNA sequence analysis is a multistage process that includes the preparation of DNA, its fragmentation and base analysis, and the interpretation of the resulting sequence information. New technological advances have led to the automation of certain steps in this process and have raised the possibility of large-scale DNA sequencing efforts in the near future [for example, 1 million base pairs (Mb) per year]. New sequencing methodologies, fully automated instrumentation, and improvements in sequencing-related computational resources may render genome-size sequencing projects (100 Mb or larger) feasible during the next 5 to 10 years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunkapiller, T -- Kaiser, R J -- Koop, B F -- Hood, L -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):59-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NSF Science and Technology Center for Molecular Biotechnology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925562" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Automation ; *Base Sequence ; DNA/*chemistry ; *Human Genome Project ; Humans ; Mass Spectrometry ; Microscopy/instrumentation ; Nucleic Acid Hybridization ; Robotics
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  • 86
    Publication Date: 1991-05-17
    Description: Some strains of Escherichia coli contain retroelements (retrons) that encode genes for reverse transcriptase and branched, multicopy, single-stranded DNA (msDNA) linked to RNA. However, the origin of retrons is unknown. A P4-like cryptic prophage was found that contains a retroelement (retron Ec73) for msDNA-Ec73 in an E. coli clinical strain. The entire genome of this prophage, named phi R73, is 12.7 kilobase pairs and is flanked by 29-base pair direct repeats derived from the 3' end of the selenocystyl transfer RNA gene (selC). P2 bacteriophage caused excision of the phi R73 prophage and acted as a helper to package phi R73 DNA into an infectious virion. The newly formed phi R73 closely resembled P4 as a virion and in its lytic growth. Retronphage phi R73 lysogenized a new host strain, reintegrating its genome into the selC gene of the host chromosome and enabling the newly formed lysogens to produce msDNA-Ec73. Hence, retron Ec73 can be transferred intercellularly as part of the genome of a helper-dependent retronphage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Sunshine, M G -- Six, E W -- Inouye, M -- AI04043/AI/NIAID NIH HHS/ -- GM44012/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):969-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey at Rutgers, Piscataway 08854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709758" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Coliphages/*genetics/ultrastructure ; DNA, Bacterial/genetics ; DNA, Viral/genetics ; Escherichia coli/*genetics ; *Genes, Bacterial ; *Genes, Viral ; Microscopy, Electron ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Open Reading Frames ; RNA, Transfer/*genetics ; RNA-Directed DNA Polymerase/genetics
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  • 87
    Publication Date: 1991-05-03
    Description: In Saccharopolyspora erythraea, the genes that govern synthesis of the polyketide portion of the macrolide antibiotic erythromycin are organized in six repeated units that encode fatty acid synthase (FAS)-like activities. Each repeated unit is designated a module, and two modules are contained in a single open reading frame. A model for the synthesis of this complex polyketide is proposed, where each module encodes a functional synthase unit and each synthase unit participates specifically in one of the six FAS-like elongation steps required for formation of the polyketide. In addition, genetic organization and biochemical order of events appear to be colinear. Evidence for the model is provided by construction of a selected mutant and by isolation of a polyketide of predicted structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donadio, S -- Staver, M J -- McAlpine, J B -- Swanson, S J -- Katz, L -- New York, N.Y. -- Science. 1991 May 3;252(5006):675-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Corporate Molecular Biology, Abbott Laboratories, Abbott Park, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Bacterial/genetics ; Erythromycin/analogs & derivatives/biosynthesis/chemistry ; Genes, Bacterial ; Gram-Positive Bacteria/enzymology/genetics ; Hydroxylation ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Multienzyme Complexes/*genetics ; Mutation ; Nucleic Acid Hybridization ; Repetitive Sequences, Nucleic Acid
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  • 88
    Publication Date: 1991-05-24
    Description: DNA sequences have been located at the fragile X site by in situ hybridization and by the mapping of breakpoints in two somatic cell hybrids that were constructed to break at the fragile site. These hybrids were found to have breakpoints in a common 5-kilobase Eco RI restriction fragment. When this fragment was used as a probe on the chromosomal DNA of normal and fragile X genotype individuals, alterations in the mobility of the sequences detected by the probe were found only in fragile X genotype DNA. These sequences were of an increased size in all fragile X individuals and varied within families, indicating that the region was unstable. This probe provides a means with which to analyze fragile X pedigrees and is a diagnostic reagent for the fragile X genotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, S -- Pritchard, M -- Kremer, E -- Lynch, M -- Nancarrow, J -- Baker, E -- Holman, K -- Mulley, J C -- Warren, S T -- Schlessinger, D -- New York, N.Y. -- Science. 1991 May 24;252(5009):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cytogenetics and Molecular Genetics, Adelaide Children's Hospital, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031189" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; DNA/*genetics ; Female ; Fragile X Syndrome/*genetics ; Genotype ; Humans ; Hybrid Cells/cytology ; Male ; Nucleic Acid Hybridization ; Reference Values ; Restriction Mapping ; X Chromosome
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  • 89
    Publication Date: 1991-05-10
    Description: In order to identify genes specific for the sensory neurons of Aplysia, a miniaturized differential screening method based on the polymerase chain reaction and applicable to small amounts of tissue was used. One messenger RNA was isolated that is expressed in every mechanoreceptor sensory cluster of the Aplysia central nervous system. This messenger RNA encodes a peptide that seems to function as an inhibitory cotransmitter. The peptide selectively inhibits certain postsynaptic cells but not others and thereby allows the sensory neurons to achieve target-specific synaptic actions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunet, J F -- Shapiro, E -- Foster, S A -- Kandel, E R -- Iino, Y -- New York, N.Y. -- Science. 1991 May 10;252(5007):856-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, New York, NY.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia ; Biomarkers ; Blotting, Northern ; Chromatography, High Pressure Liquid ; In Vitro Techniques ; Neurons, Afferent/*chemistry ; Nucleic Acid Hybridization ; Peptides/*analysis ; Polymerase Chain Reaction ; RNA, Messenger/analysis ; Species Specificity ; Transcription, Genetic
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-17
    Description: Human mitochondrial transcription factor 1 (mtTF1) has been sequenced and is a nucleus-encoded DNA binding protein of 204 amino acids (24,400 daltons). Expression of human mtTF1 in bacteria yields a protein with correct physical properties and the ability to activate mitochondrial DNA promoters. Analysis of the protein's sequence reveals no similarities to any other DNA binding proteins except for the existence of two domains that are characteristic of high mobility group (HMG) proteins. Human mtTF1 is most closely related to a DNA binding HMG-box region in hUBF, a human protein known to be important for transcription by RNA polymerase I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parisi, M A -- Clayton, D A -- GM07365-15/GM/NIGMS NIH HHS/ -- GM33088-20/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):965-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2035027" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; DNA, Mitochondrial/*genetics ; DNA-Binding Proteins/*genetics ; Gene Library ; High Mobility Group Proteins/*genetics ; Humans ; Mitochondria/*metabolism ; *Mitochondrial Proteins ; Molecular Sequence Data ; Molecular Weight ; *Nuclear Proteins ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Open Reading Frames ; Promoter Regions, Genetic ; RNA, Messenger/genetics/isolation & purification ; Sequence Homology, Nucleic Acid ; Transcription Factors/*genetics
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  • 91
    Publication Date: 1991-08-16
    Description: The expression of the V(D)J [variable (diversity) joining elements] recombination activating genes, RAG-1 and RAG-2, has been examined during T cell development in the thymus. In situ hybridization to intact thymus and RNA blot analysis of isolated thymic subpopulations separated on the basis of T cell receptor (TCR) expression demonstrated that both TCR- and TCR+ cortical thymocytes express RAG-1 and RAG-2 messenger RNA's. Within the TCR+ population, RAG expression was observed in immature CD4+CD8+ (double positive) cells, but not in the more mature CD4+CD8- or CD4-CD8+ (single positive) subpopulations. Thus, although cortical thymocytes that bear TCR on their surface continue to express RAG-1 and RAG-2, it appears that the expression of both genes is normally terminated during subsequent thymic maturation. Since thymocyte maturation in vivo is thought to be regulated through the interaction of the TCR complex with self major histocompatibility complex (MHC) antigens, these data suggest that signals transduced by the TCR complex might result in the termination of RAG expression. Consistent with this hypothesis, thymocyte TCR cross-linking in vitro led to rapid termination of RAG-1 and RAG-2 expression, whereas cross-linking of other T cell surface antigens such as CD4, CD8, or HLA class I had no effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turka, L A -- Schatz, D G -- Oettinger, M A -- Chun, J J -- Gorka, C -- Lee, K -- McCormack, W T -- Thompson, C B -- DK-01899/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):778-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1831564" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/physiology ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/physiology ; Cell Differentiation ; Cell Survival ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Gene Expression ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Mice ; Nuclear Proteins ; Nucleic Acid Hybridization ; Proteins/*genetics ; RNA, Messenger/genetics ; Receptor Aggregation ; Receptors, Antigen, T-Cell/*physiology ; Receptors, Interleukin-2/genetics ; T-Lymphocyte Subsets/enzymology/*physiology ; Thymus Gland/cytology/*enzymology ; VDJ Recombinases
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  • 92
    Publication Date: 1991-05-31
    Description: A complementary DNA encoding a G protein-coupled glutamate receptor from rat brain, GluGR, was cloned by functional expression in Xenopus oocytes. The complementary DNA encodes a protein of 1199 amino acids containing a seven-transmembrane motif, flanked by large amino- and carboxyl-terminal domains. This receptor lacks any amino acid sequence similarity with other G protein-coupled receptors, suggesting that it may be a member of a new subfamily. The presence of two introns flanking the central core suggests that GluGR may have evolved by exon shuffling. Expressed in oocytes, GluGR is activated by quisqualate greater than glutamate greater than ibotenate greater than trans-1-aminocyclopentyl-1,3-dicarboxylate, and it is inhibited by 2-amino-3-phosphonopropionate. Activation is blocked by Bordella pertussis toxin. These properties are typical of some metabotropic glutamate receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Houamed, K M -- Kuijper, J L -- Gilbert, T L -- Haldeman, B A -- O'Hara, P J -- Mulvihill, E R -- Almers, W -- Hagen, F S -- AR 17803/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Brain Chemistry ; *Cloning, Molecular ; DNA/genetics ; Exons ; GTP-Binding Proteins/*metabolism ; Humans ; Introns ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Rats ; Receptors, Glutamate ; Receptors, Neurotransmitter/chemistry/*genetics/metabolism ; Sequence Homology, Nucleic Acid
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  • 93
    Publication Date: 1990-07-06
    Description: Oligonucleotides equipped with EDTA-Fe can bind specifically to duplex DNA by triple-helix formation and produce double-strand cleavage at binding sites greater than 12 base pairs in size. To demonstrate that oligonucleotide-directed triple-helix formation is a viable chemical approach for the site-specific cleavage of large genomic DNA, an oligonucleotide with EDTA-Fe at the 5' and 3' ends was targeted to a 20-base pair sequence in the 340-kilobase pair chromosome III of Saccharomyces cerevisiae. Double-strand cleavage products of the correct size and location were observed, indicating that the oligonucleotide bound and cleaved the target site among almost 14 megabase pairs of DNA. Because oligonucleotide-directed triple-helix formation has the potential to be a general solution for DNA recognition, this result has implications for physical mapping of chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strobel, S A -- Dervan, P B -- GM 42966/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 6;249(4964):73-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arnold and Mabel Beckman Laboratories of Chemical Synthesis, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2195655" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Chromosomes, Fungal/*metabolism ; DNA, Fungal/*genetics/metabolism ; Densitometry ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligonucleotides/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics
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  • 94
    Publication Date: 1990-06-22
    Description: The vast repertoire of immunoglobulins and T cell receptors is generated, in part, by V(D)J recombination, a series of genomic rearrangements that occur specifically in developing lymphocytes. The recombination activating gene, RAG-1, which is a gene expressed exclusively in maturing lymphoid cells, was previously isolated. RAG-1 inefficiently induced V(D)J recombinase activity when transfected into fibroblasts, but cotransfection with an adjacent gene, RAG-2, has resulted in at least a 1000-fold increase in the frequency of recombination. The 2.1-kilobase RAG-2 complementary DNA encodes a putative protein of 527 amino acids whose sequence is unrelated to that of RAG-1. Like RAG-1, RAG-2 is conserved between species that carry out V(D)J recombination, and its expression pattern correlates precisely with that of V(D)J recombinase activity. In addition to being located just 8 kilobases apart, these convergently transcribed genes are unusual in that most, if not all, of their coding and 3' untranslated sequences are contained in single exons. RAG-1 and RAG-2 might activate the expression of the V(D)J recombinase but, more likely, they directly participate in the recombination reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oettinger, M A -- Schatz, D G -- Gorka, C -- Baltimore, D -- GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1517-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cell Line ; Chickens ; Cricetinae ; DNA/*genetics ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Dogs ; Female ; *Gene Rearrangement, B-Lymphocyte ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Multigene Family ; Nuclear Proteins ; Nucleic Acid Hybridization ; Opossums ; Proteins/*genetics ; Rabbits ; Recombination, Genetic/*genetics ; Restriction Mapping ; Transfection ; Turtles ; VDJ Recombinases
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  • 95
    Publication Date: 1990-08-17
    Description: Primary and secondary hypertriglyceridemia is common in the general population, but the biochemical basis for this disease is largely unknown. With the use of transgenic technology, two lines of mice were created that express the human apolipoprotein CIII gene. One of these mouse lines with 100 copies of the gene was found to express large amounts of the protein and to be severely hypertriglyceridemic. The other mouse line with one to two copies of the gene expressed low amounts of the protein, but nevertheless manifested mild hypertriglyceridemia. Thus, overexpression of apolipoprotein CIII can be a primary cause of hypertriglyceridemia in vivo and may provide one possible etiology for this common disorder in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ito, Y -- Azrolan, N -- O'Connell, A -- Walsh, A -- Breslow, J L -- HL 36461/HL/NHLBI NIH HHS/ -- HL33435/HL/NHLBI NIH HHS/ -- HL33714/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):790-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2167514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoprotein C-III ; Apolipoproteins C/blood/*genetics ; Chylomicrons/blood ; Cloning, Molecular ; DNA Restriction Enzymes/metabolism ; DNA, Recombinant/metabolism ; *Gene Expression ; Humans ; Hypertriglyceridemia/blood/*genetics ; Lipoproteins, VLDL/blood ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Transgenic ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; Triglycerides/blood
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  • 96
    Publication Date: 1990-01-19
    Description: Interleukin-3 (IL-3) binds to its receptor with high and low affinities, induces tyrosine phosphorylation, and promotes the proliferation and differentiation of hematopoietic cells. A binding component of the IL-3 receptor was cloned. Fibroblasts transfected with the complementary DNA bound IL-3 with a low affinity [dissociation constant (Kd) of 17.9 +/- 3.6 nM]. No consensus sequence for a tyrosine kinase was present in the cytoplasmic domain. Thus, additional components are required for a functional high affinity IL-3 receptor. A sequence comparison of the IL-3 receptor with other cytokine receptors (erythropoietin, IL-4, IL-6, and the beta chain IL-2 receptor) revealed a common motif of a distinct receptor gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Itoh, N -- Yonehara, S -- Schreurs, J -- Gorman, D M -- Maruyama, K -- Ishii, A -- Yahara, I -- Arai, K -- Miyajima, A -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):324-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2404337" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Cloning, Molecular ; DNA/genetics ; DNA Probes ; Escherichia coli/genetics ; Fibroblasts/metabolism ; Interleukin-3/metabolism ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Plasmids ; Protein-Tyrosine Kinases/metabolism ; Receptors, Immunologic/*genetics/metabolism ; Receptors, Interleukin-3 ; Sequence Homology, Nucleic Acid ; Transfection
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  • 97
    Publication Date: 1990-04-27
    Description: Affinity-purified, polyclonal antibodies to the gamma subunit of the dihydropyridine (DHP)-sensitive, voltage-dependent calcium channel have been used to isolate complementary DNAs to the rabbit skeletal muscle protein from an expression library. The deduced primary structure indicates that the gamma subunit is a 25,058-dalton protein that contains four transmembrane domains and two N-linked glycosylation sites, consistent with biochemical analyses showing that the gamma subunit is a glycosylated hydrophobic protein. Nucleic acid hybridization studies indicate that there is a 1200-nucleotide transcript in skeletal muscle but not in brain or heart. The gamma subunit may play a role in assembly, modulation, or the structure of the skeletal muscle calcium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jay, S D -- Ellis, S B -- McCue, A F -- Williams, M E -- Vedvick, T S -- Harpold, M M -- Campbell, K P -- HL-14388/HL/NHLBI NIH HHS/ -- HL-37187/HL/NHLBI NIH HHS/ -- HL-39265/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):490-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2158672" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Calcium Channels/drug effects/physiology ; DNA/isolation & purification ; Dihydropyridines/*pharmacology ; Disulfides ; Electrophoresis, Polyacrylamide Gel ; Immunoassay ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Muscles/*analysis ; Nucleic Acid Hybridization ; Protein Conformation ; RNA, Messenger/analysis ; Rabbits ; Sequence Homology, Nucleic Acid
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  • 98
    Publication Date: 1990-06-15
    Description: Leukocyte adhesion deficiency (LAD) is an inherited disorder of leukocyte function caused by derangements in CD18 expression. The genetic and functional abnormalities in a lymphocyte cell line from a patient with LAD have been corrected by retrovirus-mediated transduction of a functional CD18 gene. Lymphocytes from patients with LAD were exposed to CD18-expressing retrovirus and enriched for cells that express CD11a and CD18 (LFA-1) on the cell surface. Molecular and functional analyses of these cells revealed (i) one copy of proviral sequence per cell, (ii) viral-directed CD18 RNA that exceeded normal endogenous levels, (iii) normal quantities of CD11a and CD18 protein on the cell surface, and (iv) reconstitution of LFA-1-dependent adhesive function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, J M -- Ping, A J -- Krauss, J C -- Mayo-Bond, L -- Rogers, C E -- Anderson, D C -- Todd, R F -- R01 AI19031/AI/NIAID NIH HHS/ -- R01 AI23521/AI/NIAID NIH HHS/ -- R01 CA39064/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1413-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Internal Medicine, Ann Arbor, MI.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1972597" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD ; Antigens, CD18 ; Antigens, Differentiation/genetics/immunology ; Cell Aggregation ; Cell Line ; Cell Line, Transformed ; Gene Expression ; Genetic Therapy ; Genetic Vectors ; Herpesvirus 4, Human ; Humans ; *Leukocyte-Adhesion Deficiency Syndrome ; Lymphocyte Function-Associated Antigen-1 ; Lymphocytes/immunology ; Membrane Glycoproteins ; Mice ; Nucleic Acid Hybridization ; Receptors, Leukocyte-Adhesion/genetics/immunology ; Retroviridae/*genetics ; Tetradecanoylphorbol Acetate/pharmacology ; *Transfection
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  • 99
    Publication Date: 1990-04-13
    Description: Phosphate-methylated DNA hybridizes strongly and specifically to natural DNA and RNA. Hybridization to single-stranded and double-stranded DNA leads to site-selective blocking of replication and transcription. Phosphate-methylated DNA was used to interrupt the life cycle of the human immunodeficiency virus type-1 (HIV-1), the causative agent of acquired immunodeficiency syndrome (AIDS). Both antisense and sense phosphate-methylated DNA 20-nucleotide oligomers, targeted at the transactivator responsive region and the primer binding site, caused complete inhibition of viral infectivity at a low concentration. Hybridization of phosphate-methylated DNA with folded and unfolded RNA was studied by ultraviolet and proton nuclear magnetic resonance spectroscopy. The combined results of hybridization studies and biological experiments suggest that the design of effective antisense phosphate-methylated DNA should focus on hairpin loop structures in the viral RNA. For sense systems, the 5' end of the integrated viral genome is considered to be the important target site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buck, H M -- Koole, L H -- van Genderen, M H -- Smit, L -- Geelen, J L -- Jurriaans, S -- Goudsmit, J -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):208-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organic Chemistry, Eindhoven University of Technology, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2326635" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/genetics ; Base Composition ; Base Sequence ; Cell Line ; Codon/genetics ; *DNA Probes/metabolism ; DNA, Viral/biosynthesis ; HIV-1/*genetics/pathogenicity ; Hydrogen Bonding ; Indicators and Reagents ; Methylation ; Models, Structural ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Organophosphorus Compounds/metabolism ; RNA, Viral/*genetics ; Thermodynamics ; Virulence/genetics
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  • 100
    Publication Date: 1990-08-24
    Description: Fluorescence in situ hybridization makes possible direct visualization of single sequences not only on chromosomes, but within decondensed interphase nuclei, providing a potentially powerful approach for high-resolution (1 Mb and below) gene mapping and the analysis of nuclear organization. Interphase mapping was able to extend the ability to resolve and order sequences up to two orders of magnitude beyond localization on banded or unbanded chromosomes. Sequences within the human dystrophin gene separated by less than 100 kb to 1 Mb were visually resolved at interphase by means of standard microscopy. In contrast, distances in the 1-Mb range could not be ordered on the metaphase chromosome length. Analysis of sequences 100 kb to 1 Mb apart indicates a strong correlation between interphase distance and linear DNA distance, which could facilitate a variety of gene-mapping efforts. Results estimate chromatin condensation up to 1 Mb and indicate a comparable condensation for different cell types prepared by different techniques.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawrence, J B -- Singer, R H -- McNeil, J A -- HD 18066/HD/NICHD NIH HHS/ -- HG 00251/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):928-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2203143" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Banding ; Chromosome Mapping ; *Chromosomes, Human, Pair 1 ; DNA/genetics ; DNA Probes ; Dystrophin ; Fibroblasts/cytology ; *Genes ; Genome, Human ; Humans ; Interphase ; Metaphase ; Muscle Proteins/*genetics ; Nucleic Acid Hybridization
    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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