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  • Articles  (984)
  • Inorganic Chemistry  (773)
  • Molecular Sequence Data  (211)
  • 1995-1999
  • 1990-1994  (984)
  • 1950-1954
  • 1991  (984)
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  • Articles  (984)
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  • 1995-1999
  • 1990-1994  (984)
  • 1950-1954
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  • 1
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    The combination of symbolic and numerical computation for three-dimensional modeling of RNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-13
    Description: Three-dimensional (3-D) structural models of RNA are essential for understanding of the cellular roles played by RNA. Such models have been obtained by a technique based on a constraint satisfaction algorithm that allows for the facile incorporation of secondary and other structural information. The program generates 3-D structures of RNA with atomic-level resolution that can be refined by numerical techniques such as energy minimization. The precision of this technique was evaluated by comparing predicted transfer RNA loop and RNA pseudoknot structures with known or consensus structures. The root-mean-square deviation (2.0 to 3.0 angstroms before minimization) between predicted and control structures reveal this system to be an effective method in modeling RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Major, F -- Turcotte, M -- Gautheret, D -- Lapalme, G -- Fillion, E -- Cedergren, R -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1255-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement d'Informatique et de Recherche Operationnelle, Universite de Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716375" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Anticodon/chemistry ; Base Sequence ; *Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/*chemistry ; RNA, Transfer/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    A multisubunit ribozyme that is a catalyst of and template for complementary strand RNA synthesis (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-29
    Description: Derivatives of the sunY self-splicing intron efficiently catalyzed the synthesis of complementary strand RNA by template-directed assembly of oligonucleotides. These ribozymes were separated into three short RNA fragments that formed active catalytic complexes. One of the multisubunit sunY derivatives catalyzed the synthesis of a strand of RNA complementary to one of its own subunits. These results suggest that prebiotically synthesized oligonucleotides might have been able to assemble into a complex capable of self-replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doudna, J A -- Couture, S -- Szostak, J W -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1605-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1707185" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; *Introns ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/metabolism ; RNA/*biosynthesis/genetics ; RNA Splicing ; RNA, Catalytic/*metabolism ; Templates, Genetic ; Tetrahymena/*genetics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Group I intron self-splicing with adenosine: evidence for a single nucleoside-binding site (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-19
    Description: For self-splicing of Tetrahymena ribosomal RNA precursor, guanosine binding is required for 5' splice-site cleavage and exon ligation. Whether these two reactions use the same or different guanosine-binding sites has been debated. A double mutation in a previously identified guanosine-binding site within the intron resulted in preference for adenosine (or adenosine triphosphate) as the substrate for cleavage at the 5' splice site. However, splicing was blocked in the exon ligation step. Blockage was reversed by a change from guanine to adenine at the 3' splice site. These results indicate that a single determinant specifies nucleoside binding for both steps of splicing. Furthermore, it suggests that RNA could form an active site specific for adenosine triphosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Been, M D -- Perrotta, A T -- GM-40689/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):434-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017681" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*metabolism ; Adenosine Triphosphate/pharmacology ; Animals ; Base Sequence ; Binding Sites ; Exons ; Guanosine/metabolism ; *Introns ; Magnesium/pharmacology ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis ; RNA Precursors/chemistry/genetics ; *RNA Splicing ; RNA, Catalytic/metabolism ; Tetrahymena/genetics
    Print ISSN: 0036-8075
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  • 4
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    Identification of the DNA binding site for NGFI-B by genetic selection in yeast (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-31
    Description: An in vivo selection system for isolating targets of DNA binding proteins in yeast was developed and used to identify the DNA binding site for the NGFI-B protein, a member of the steroid-thyroid hormone receptor superfamily. The feasibility of the technique was verified by selecting DNA fragments that contained binding sites for GCN4, a well-characterized yeast transcriptional activator. The DNA binding domain of NGFI-B, expressed as part of a LexA-NGFI-B-GAL4 chimeric activator, was then used to isolate a rat genomic DNA fragment that contained an NGFI-B binding site. The NGFI-B response element (NBRE) is similar to but functionally distinct from elements recognized by the estrogen and thyroid hormone receptors and the hormone receptor-like proteins COUP-TF, CF1, and H-2RIIBP. Cotransfection experiments in mammalian cells demonstrated that NGFI-B can activate transcription from the NBRE with or without its putative ligand binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Fahrner, T J -- Johnston, M -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 31;252(5010):1296-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925541" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Fungal/*metabolism ; DNA-Binding Proteins/genetics/*metabolism/pharmacology ; Fungal Proteins/metabolism ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Plasmids ; *Protein Kinases ; Rats ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Repressor Proteins ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; *Serine Endopeptidases ; Transcription Factors/genetics/*metabolism/pharmacology ; Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Isolation of an active human transposable element (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-30
    Description: Two de novo insertions of truncated L1 elements into the factor VIII gene on the X chromosome have been identified that produced hemophilia A. A full-length L1 element that is the likely progenitor of one of these insertions was isolated by its sequence identity to the factor VIII insertion. This L1 element contains two open-reading frames and is one of at least four alleles of a locus on chromosome 22 that has been occupied by an L1 element for at least 6 million years.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dombroski, B A -- Mathias, S L -- Nanthakumar, E -- Scott, A F -- Kazazian, H H Jr -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1662412" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosomes, Human, Pair 22 ; *DNA Transposable Elements ; Factor VIII/*genetics ; Genome, Human ; Hemophilia A/*genetics ; Humans ; Molecular Sequence Data ; Open Reading Frames ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; X Chromosome
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Repression of HIV-1 transcription by a cellular protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-22
    Description: A cellular DNA binding protein, LBP-1, sequentially interacts in a concentration-dependent manner with two sites that surround the transcriptional initiation site of the human immunodeficiency virus type 1 (HIV-1) promoter. Although sequences in the downstream site (site I) were found to enhance transcription, purified LBP-1 specifically repressed transcription in vitro by binding to the upstream site (site II), which overlaps the TATA element. The binding of human TATA binding factor (TFIID) to the promoter before LBP-1 blocked repression, suggesting that repression resulted from an inhibition of TFIID binding to the TATA element. Furthermore, mutations that eliminated binding to site II both prevented repression in vitro and increased HIV-1 transcription in stably transformed cells. These findings suggest that a cellular factor regulates HIV-1 transcription in a manner that is characteristic of bacterial repressors and that this factor could be important in HIV-1 latency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kato, H -- Horikoshi, M -- Roeder, R G -- AI27397/AI/NIAID NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1476-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006421" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/genetics ; *Gene Expression Regulation, Viral ; HIV-1/*genetics ; Molecular Sequence Data ; Promoter Regions, Genetic ; Repressor Proteins/*genetics ; Transcription Factor TFIID ; Transcription Factors/metabolism ; Transcription, Genetic
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  • 7
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    A phosphorylation site in the Na+ channel required for modulation by protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-08
    Description: Voltage-gated sodium channels are responsible for generation of action potentials in excitable cells. Activation of protein kinase C slows inactivation of sodium channels and reduces peak sodium currents. Phosphorylation of a single residue, serine 1506, that is located in the conserved intracellular loop between domains III and IV and is involved in inactivation of the sodium channel, is required for both modulatory effects. Mutant sodium channels lacking this phosphorylation site have normal functional properties in unstimulated cells but do not respond to activation of protein kinase C. Phosphorylation of this conserved site in sodium channel alpha subunits may regulate electrical activity in a wide range of excitable cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉West, J W -- Numann, R -- Murphy, B J -- Scheuer, T -- Catterall, W A -- GM07270/GM/NIGMS NIH HHS/ -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):866-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658937" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/physiology ; Cells, Cultured ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Kinase C/*metabolism ; Sodium Channels/metabolism/*physiology
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  • 8
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    Identification of p53 gene mutations in bladder cancers and urine samples (1991)
    American Association for the Advancement of Science (AAAS)
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    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
    Print ISSN: 0036-8075
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  • 9
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    Photoreceptor deactivation and retinal degeneration mediated by a photoreceptor-specific protein kinase C (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: The protein kinase C (PKC) family of serine-threonine kinases has been implicated in the regulation of a variety of signaling cascades. One member of this family, eye-PKC, is expressed exclusively in the Drosophila visual system. The inaC (inactivation-no-afterpotential C) locus was shown to be the structural gene for eye-PKC. Analysis of the light response from inaC mutants showed that this kinase is required for the deactivation and rapid desensitization of the visual cascade. Light adaptation was also defective in inaC mutant flies. In flies carrying the retinal degeneration mutation rdgB, absence of eye-PKC suppressed photoreceptor cell degeneration. These results indicate that eye-PKC functions in the light-dependent regulation of the phototransduction cascade in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, D P -- Ranganathan, R -- Hardy, R W -- Marx, J -- Tsuchida, T -- Zuker, C S -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1478-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Diego, La Jolla.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962207" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological/physiology ; Amino Acid Sequence ; Animals ; Calcium/physiology ; DNA Mutational Analysis ; Drosophila melanogaster/*genetics ; Eye/enzymology ; Genes ; Molecular Sequence Data ; Photoreceptor Cells/*physiology ; Protein Kinase C/chemistry/*physiology ; Restriction Mapping ; Retinal Degeneration/pathology/*physiopathology ; Signal Transduction ; *Vision, Ocular
    Print ISSN: 0036-8075
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  • 10
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    Function of the homeodomain protein GHF1 in pituitary cell proliferation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-12
    Description: Mutations that cause pituitary dwarfism in the mouse reside in the gene encoding the transcription factor growth hormone factor 1 (GHF1 or pit1). These dwarf mice (dw and dwJ) are deficient in growth hormone (GH) and prolactin (PRL) synthesis and exhibit pituitary hypoplasia, suggesting a stem cell defect. With antisense oligonucleotide technology, a cell culture model of this genetic defect was developed. Specific inhibition of GHF1 synthesis by complementary oligonucleotides led to a marked decrease in GH and PRL expression and to a marked decrease in proliferation of somatotrophic cell lines. These results provide direct evidence that the homeodomain protein GHF1 is required not only for the establishment and maintenance of the differentiated phenotype but for cell proliferation as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castrillo, J L -- Theill, L E -- Karin, M -- DK38527/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):197-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1677216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antisense Elements (Genetics) ; Base Sequence ; *Cell Division ; Cells, Cultured ; DNA/biosynthesis ; DNA-Binding Proteins/*physiology ; Dwarfism/genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Growth Hormone/genetics ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Pituitary Gland/*cytology/physiology ; Prolactin/genetics ; Transcription Factor Pit-1 ; Transcription Factors/*physiology
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  • 11
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    Cloning and expression of a cocaine-sensitive rat dopamine transporter (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The action of dopamine and other monoamine neurotransmitters at synapses is terminated predominantly by high-affinity reuptake into presynaptic terminals by specific sodium-dependent neurotransmitter transport proteins. A complementary DNA encoding a rat dopamine transporter has been isolated that exhibits high sequence similarity with the previously cloned norepinephrine and gamma-aminobutyric acid transporters. Transient expression of the complementary DNA in HeLa cells confirms the cocaine sensitivity of this transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kilty, J E -- Lorang, D -- Amara, S G -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cloning, Molecular ; Cocaine/*pharmacology ; Dopamine/*metabolism ; Dopamine Plasma Membrane Transport Proteins ; Gene Expression ; HeLa Cells ; Humans ; Kinetics ; *Membrane Glycoproteins ; *Membrane Transport Proteins ; Molecular Sequence Data ; *Nerve Tissue Proteins ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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  • 12
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    A genetic model for interaction of the homeodomain recognition helix with DNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-25
    Description: The Bicoid homeodomain protein controls anterior development in the Drosophila embryo by binding to DNA and regulating gene expression. With the use of genetic assays in yeast, the interaction between the Bicoid homeodomain and a series of mutated DNA sites was studied. These experiments defined important features of homeodomain binding sites, identified specific amino acid-base pair contacts, and suggested a model for interaction of the recognition alpha-helices of Bicoid and Antennapedia-class homeodomain proteins with DNA. The model is in general agreement with results of crystallographic and magnetic resonance studies, but differs in important details. It is likely that genetic studies of protein-DNA interaction will continue to complement conventional structural approaches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanes, S D -- Brent, R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):426-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1671176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/*metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Drosophila ; Gene Expression Regulation ; Genes, Homeobox/*genetics ; *Homeodomain Proteins ; Insect Hormones/*genetics/metabolism ; *Models, Genetic ; Molecular Sequence Data ; *Trans-Activators ; Transcription, Genetic
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  • 13
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    Visualizing the higher order folding of a catalytic RNA molecule (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-25
    Description: The higher order folding process of the catalytic RNA derived from the self-splicing intron of Tetrahymena thermophila was monitored with the use of Fe(II)-EDTA-induced free radical chemistry. The overall tertiary structure of the RNA molecule forms cooperatively with the uptake of at least three magnesium ions. Local folding transitions display different metal ion dependencies, suggesting that the RNA tertiary structure assembles through a specific folding intermediate before the catalytic core is formed. Enzymatic activity, assayed with an RNA substrate that is complementary to the catalytic RNA active site, coincides with the cooperative structural transition. The higher order RNA foldings produced by Mg(II), Ca(II), and Sr(II) are similar; however, only the Mg(II)-stabilized RNA is catalytically active. Thus, these results directly demonstrate that divalent metal ions participate in general folding of the ribozyme tertiary structure, and further indicate a more specific involvement of Mg(II) in catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celander, D W -- Cech, T R -- New York, N.Y. -- Science. 1991 Jan 25;251(4992):401-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1989074" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Calcium/metabolism ; Densitometry ; Kinetics ; Magnesium/metabolism ; Magnesium Chloride/pharmacology ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/drug effects/metabolism ; Strontium/metabolism ; Tetrahymena
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  • 14
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    Resistance to ddI and sensitivity to AZT induced by a mutation in HIV-1 reverse transcriptase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-27
    Description: Serial human immunodeficiency virus type-1 (HIV-1) isolates were obtained from five individuals with acquired immunodeficiency syndrome (AIDS) who changed therapy to 2',3'-dideoxyinosine (ddI) after at least 12 months of treatment with 3'-azido-3'-deoxythymidine (zidovudine, AZT). The in vitro sensitivity to ddI decreased during the 12 months following ddI initiation, whereas AZT sensitivity increased. Analysis of the reverse transcriptase coding region revealed a mutation associated with reduced sensitivity to ddI. When this mutation was present in the same genome as a mutation known to confer AZT resistance, the isolates showed increased sensitivity to AZT. Analysis of HIV-1 variants confirmed that the ddI resistance mutation alone conferred ddI and 2',3'-dideoxycytidine resistance, and suppressed the effect of the AZT resistance mutation. The use of combination therapy for HIV-1 disease may prevent drug-resistant isolates from emerging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉St Clair, M H -- Martin, J L -- Tudor-Williams, G -- Bach, M C -- Vavro, C L -- King, D M -- Kellam, P -- Kemp, S D -- Larder, B A -- New York, N.Y. -- Science. 1991 Sep 27;253(5027):1557-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Virology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716788" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*drug therapy/microbiology ; Base Sequence ; DNA, Viral/*genetics ; Didanosine/*pharmacology/*therapeutic use ; Drug Resistance, Microbial ; Genotype ; HIV-1/*drug effects/enzymology/isolation & purification ; Humans ; Molecular Sequence Data ; *Mutation ; Oligodeoxyribonucleotides ; RNA-Directed DNA Polymerase/*genetics/metabolism ; Zidovudine/pharmacology/*therapeutic use
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  • 15
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    Related RNA polymerase-binding regions in human RAP30/74 and Escherichia coli sigma 70 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: RAP30/74 is a heteromeric general transcription initiation factor that binds to mammalian RNA polymerase II. The RAP30 subunit contains a region that is similar in amino acid sequence to the RNA polymerase-binding domain of the Escherichia coli transcription initiation factor sigma 70 (sigma 70). Mammalian RNA polymerase II specifically protected a serine residue in the sigma 70-related region of RAP30 from phosphorylation in vitro. In addition, human RAP30/74 bound to Escherichia coli RNA polymerase and was displaced by sigma 70. These results suggest that RAP30 and sigma 70 have functionally related RNA polymerase-binding regions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCracken, S -- Greenblatt, J -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):900-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1652156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Centrifugation, Density Gradient ; Cyanogen Bromide ; Cyclic AMP/pharmacology ; Escherichia coli/*analysis/enzymology ; Humans ; Molecular Sequence Data ; Peptide Fragments/chemistry/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; RNA Polymerase II/*metabolism ; Sigma Factor/chemistry/*metabolism ; Transcription Factors/chemistry/*metabolism ; *Transcription Factors, TFII ; Trypsin
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  • 16
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    Exchange of conduction pathways between two related K+ channels (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-22
    Description: The structure of the ion conduction pathway or pore of voltage-gated ion channels is unknown, although the linker between the membrane spanning segments S5 and S6 has been suggested to form part of the pore in potassium channels. To test whether this region controls potassium channel conduction, a 21-amino acid segment of the S5-S6 linker was transplanted from the voltage-activated potassium channel NGK2 to another potassium channel DRK1, which has very different pore properties. In the resulting chimeric channel, the single channel conductance and blockade by external and internal tetraethylammonium (TEA) ion were characteristic of the donor NGK2 channel. Thus, this 21-amino acid segment controls the essential biophysical properties of the pore and may form the conduction pathway of these potassium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hartmann, H A -- Kirsch, G E -- Drewe, J A -- Taglialatela, M -- Joho, R H -- Brown, A M -- NS08805/NS/NINDS NIH HHS/ -- NS23877/NS/NINDS NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):942-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/physiology ; Chimera ; Cloning, Molecular ; Female ; Ion Channel Gating ; Membrane Potentials ; Molecular Sequence Data ; Oligonucleotide Probes ; Oocytes/physiology ; Polymerase Chain Reaction ; Potassium Channels/drug effects/genetics/*physiology ; Rats ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Tetraethylammonium ; Tetraethylammonium Compounds/pharmacology ; Xenopus
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  • 17
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    Elvis impersonator? (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, P W -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):357-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925586" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Molecular Sequence Data ; *Oligopeptides
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  • 18
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    Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described. The x-ray crystal structure of the complex is the basis of the analysis. The peptide inhibitor, derived from a naturally occurring heat-stable protein kinase inhibitor, contains an amphipathic helix that is followed by a turn and an extended conformation. The extended region occupies the cleft between the two lobes of the enzyme and contains a five-residue consensus recognition sequence common to all substrates and peptide inhibitors of the catalytic subunit. The helical portion of the peptide binds to a hydrophobic groove and conveys high affinity binding. Loops from both domains converge at the active site and contribute to a network of conserved residues at the sites of magnesium adenosine triphosphate binding and catalysis. Amino acids associated with peptide recognition, nonconserved, extend over a large surface area.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Zheng, J H -- Ten Eyck, L F -- Xuong, N H -- Taylor, S S -- Sowadski, J M -- RR01644/RR/NCRR NIH HHS/ -- T32CA09523/CA/NCI NIH HHS/ -- T32DK07233/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):414-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, San Diego, La Jolla 92093-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carrier Proteins/*chemistry/metabolism ; Computer Simulation ; Enzyme Inhibitors/*chemistry ; *Intracellular Signaling Peptides and Proteins ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Kinases/*chemistry/metabolism ; X-Ray Diffraction
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  • 19
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    Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-14
    Description: In the interleukin-2 (IL-2) system, intracellular signal transduction is triggered by the beta chain of the IL-2 receptor (IL-2R beta); however, the responsible signaling mechanism remains unidentified. Evidence for the formation of a stable complex of IL-2R beta and the lymphocyte-specific protein tyrosine kinase p56lck is presented. Specific association sites were identified in the tyrosine kinase catalytic domain of p56lck and in the cytoplasmic domain of IL-2R beta. As a result of interaction, IL-2R beta became phosphorylated in vitro by p56lck. Treatment of T lymphocytes with IL-2 promotes p56lck kinase activity. These data suggest the participation of p56lck as a critical signaling molecule downstream of IL-2R via a novel interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatakeyama, M -- Kono, T -- Kobayashi, N -- Kawahara, A -- Levin, S D -- Perlmutter, R M -- Taniguchi, T -- New York, N.Y. -- Science. 1991 Jun 14;252(5012):1523-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047859" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Antigens, CD/immunology ; Base Sequence ; Binding Sites ; Cell Division/drug effects ; Cell Line ; Humans ; Interleukin-2/pharmacology ; Killer Cells, Natural/cytology/drug effects/immunology ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Lymphocytes/drug effects/*immunology ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Protein-Tyrosine Kinases/genetics/isolation & purification/*metabolism ; Receptors, Interleukin-2/genetics/isolation & purification/*physiology ; *Signal Transduction ; Transfection
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  • 20
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    A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: Methylamine dehydrogenase (MADH), an alpha 2 beta 2 enzyme from numerous methylotrophic soil bacteria, contains a novel quinonoid redox prosthetic group that is covalently bound to its small beta subunit through two amino acyl residues. A comparison of the amino acid sequence deduced from the gene sequence of the small subunit for the enzyme from Methylobacterium extorquens AM1 with the published amino acid sequence obtained by the Edman degradation method, allowed the identification of the amino acyl constituents of the cofactor as two tryptophyl residues. This information was crucial for interpreting 1H and 13C nuclear magnetic resonance, and mass spectral data collected for the semicarbazide- and carboxymethyl-derivatized bis(tripeptidyl)-cofactor of MADH from bacterium W3A1. The cofactor is composed of two cross-linked tryptophyl residues. Although there are many possible isomers, only one is consistent with all the data: The first tryptophyl residue in the peptide sequence exists as an indole-6,7-dione, and is attached at its 4 position to the 2 position of the second, otherwise unmodified, indole side group. Contrary to earlier reports, the cofactor of MADH is not 2,7,9-tricarboxypyrroloquinoline quinone (PQQ), a derivative thereof, or pro-PQQ. This appears to be the only example of two cross-linked, modified amino acyl residues having a functional role in the active site of an enzyme, in the absence of other cofactors or metal ions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McIntire, W S -- Wemmer, D E -- Chistoserdov, A -- Lidstrom, M E -- GM 36296/GM/NIGMS NIH HHS/ -- HL 16251/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 10;252(5007):817-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Veterans Affairs Medical Center, San Francisco, CA 94121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2028257" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Dipeptides/*chemistry ; Gram-Negative Aerobic Bacteria/enzymology ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Molecular Sequence Data ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry ; Quinones/*chemistry ; Tryptophan/chemistry
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  • 21
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    Deregulation of a homeobox gene, HOX11, by the t(10;14) in T cell leukemia (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-05
    Description: Molecular cloning of the t(10;14)(q24;q11) recurrent breakpoint of T cell acute lymphoblastic leukemia has demonstrated a transcript for the candidate gene TCL3. Characterization of this gene from chromosome segment 10q24 revealed it to be a new homeobox, HOX11. The HOX11 homeodomain is most similar to that of the murine gene Hlx and possesses a markedly glycine-rich variable region and an acidic carboxyl terminus. HOX11, while expressed in liver, was not detected in normal thymus or T cells. This lineage-restricted homeobox gene is deregulated upon translocation into the T cell receptor locus where it may act as an oncogene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hatano, M -- Roberts, C W -- Minden, M -- Crist, W M -- Korsmeyer, S J -- 1 PO1 CA49712/CA/NCI NIH HHS/ -- CA 21765/CA/NCI NIH HHS/ -- CA 30969/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1676542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Chromosomes, Human, Pair 10 ; Chromosomes, Human, Pair 14 ; Cloning, Molecular ; *Gene Expression Regulation, Neoplastic ; *Genes, Homeobox ; Humans ; Leukemia-Lymphoma, Adult T-Cell/*genetics ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; *Translocation, Genetic
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  • 22
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    Identification of the 1H-NMR spectra of complex oligosaccharides with artificial neural networks (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-01
    Description: Artificial networks can be used to identify hydrogen nuclear magnetic resonance (1H-NMR) spectra of complex oligosaccharides. Feed-forward neural networks with back-propagation of errors can distinguish between spectra of oligosaccharides that differ by only one glycosyl residue in twenty. The artificial neural networks use features of the strongly overlapping region of the spectra (hump region) as well as features of the resolved regions of the spectra (structural reporter groups) to recognize spectra and efficiently recognized 1H-NMR spectra even when the spectra were perturbed by minor variations in their chemical shifts. Identification of spectra by neural network-based pattern recognition techniques required less than 0.1 second. It is anticipated that artificial neural networks can be used to identify the structures of any complex carbohydrate that has been previously characterized and for which a 1H-NMR spectrum is available.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, B -- Hansen, T -- Nute, D -- Albersheim, P -- Darvill, A -- York, W -- Sellers, J -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):542-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Complex Carbohydrate Research Center, Athens, GA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990429" target="_blank"〉PubMed〈/a〉
    Keywords: *Artificial Intelligence ; Carbohydrate Conformation ; Carbohydrate Sequence ; *Glucans ; Hydrogen ; Magnetic Resonance Spectroscopy/methods ; Molecular Sequence Data ; Oligosaccharides/*chemistry ; Polysaccharides/*chemistry ; *Xylans
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  • 23
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    Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-12
    Description: The most frequently occurring RNA hairpins in 16S and 23S ribosomal RNA contain a tetranucleotide loop that has a GNRA consensus sequence. The solution structures of the GCAA and GAAA hairpins have been determined by nuclear magnetic resonance spectroscopy. Both loops contain an unusual G-A base pair between the first and last residue in the loop, a hydrogen bond between a G base and a phosphate, extensive base stacking, and a hydrogen bond between a sugar 2'-end OH and a base. These interactions explain the high stability of these hairpins and the sequence requirements for the variant and invariant nucleotides in the GNRA tetranucleotide loop family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heus, H A -- Pardi, A -- AI 27026/AI/NIAID NIH HHS/ -- AI 30726/AI/NIAID NIH HHS/ -- RR03283/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):191-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1712983" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Graphics ; Hydrogen Bonding ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry ; RNA/chemistry/*ultrastructure ; Structure-Activity Relationship ; Thermodynamics
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  • 24
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    Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-29
    Description: Interactions between cytotoxic lymphocytes and their targets require the T cell antigen receptor (TCR) and the integrin lymphocyte function-associated molecule-1 (LFA-1, CD11a/CD18). LFA-1 is not constitutively avid for its counter-receptors, intercellular adhesion molecules (ICAMs)-1 and -2. Cross-linking of the TCR transiently converts LFA-1 to a high avidity state and thus provides a mechanism for regulating cellular adhesion and de-adhesion in an antigen-specific manner. Truncation of the cytoplasmic domain of the beta, but not the alpha, subunit of LFA-1 eliminated binding to ICAM-1 and sensitivity to phorbol esters. Thus, LFA-1 binding to ICAM-1 was found to be regulated by the cytoplasmic domain of the beta subunit of LFA-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hibbs, M L -- Xu, H -- Stacker, S A -- Springer, T A -- CA31798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1611-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Blood Research, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1672776" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Cell Adhesion ; Cell Adhesion Molecules/*physiology ; Cell Line ; Flow Cytometry ; Intercellular Adhesion Molecule-1 ; Lymphocyte Function-Associated Antigen-1/genetics/*physiology ; Macromolecular Substances ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/*physiology ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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  • 25
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    A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-22
    Description: Macrophage-like U-937 cells secrete a 22-kilodalton heparin-binding growth factor that is mitogenic for BALB-3T3 fibroblasts and smooth muscle cells, but not endothelial cells. The amino acid sequence predicted from complementary DNA clones indicates that the mitogen is a new member of the epidermal growth factor (EGF) family. This heparin-binding EGF-like growth factor (HB-EGF) binds to EGF receptors on A-431 epidermoid carcinoma cells and smooth muscle cells, but is a far more potent mitogen for smooth muscle cells than is EGF. HB-EGF is also expressed in cultured human macrophages and may be involved in macrophage-mediated cellular proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Higashiyama, S -- Abraham, J A -- Miller, J -- Fiddes, J C -- Klagsbrun, M -- CA37392/CA/NCI NIH HHS/ -- CA45548/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgical Research, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840698" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Division/drug effects ; Cell Line ; Chromatography, Affinity ; Chromatography, High Pressure Liquid ; DNA Replication/drug effects ; Epidermal Growth Factor/genetics/isolation & ; purification/*metabolism/pharmacology ; Growth Substances/*metabolism ; Heparin/*metabolism ; Humans ; Kinetics ; Macrophages/*metabolism ; Molecular Sequence Data ; Protein Binding ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Homology, Nucleic Acid
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  • 26
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    Expression cDNA cloning of the KGF receptor by creation of a transforming autocrine loop (1991)
    American Association for the Advancement of Science (AAAS)
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    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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  • 27
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    Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 amino acids. It consists of a 12-stranded mixed beta sheet surrounded by 14 alpha helices and bears a striking resemblance to several hydrolase structures including dienelactone hydrolase, serine carboxypeptidase-II, three neutral lipases, and haloalkane dehalogenase. The active site is unusual because it contains Glu, not Asp, in the Ser-His-acid catalytic triad and because the relation of the triad to the rest of the protein approximates a mirror image of that seen in the serine proteases. Furthermore, the active site lies near the bottom of a deep and narrow gorge that reaches halfway into the protein. Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sussman, J L -- Harel, M -- Frolow, F -- Oefner, C -- Goldman, A -- Toker, L -- Silman, I -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):872-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1678899" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*metabolism ; Acetylcholinesterase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/enzymology ; Chemistry, Physical ; Crystallization ; Electric Organ/*enzymology ; Glutamates ; Glutamic Acid ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Structure ; Phosphatidylinositols/metabolism ; Physicochemical Phenomena ; Protein Conformation ; Sequence Homology, Nucleic Acid ; *Torpedo ; X-Ray Diffraction
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  • 28
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    Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-09
    Description: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Prive, G G -- Milligan, D L -- Scott, W G -- Yeh, J -- Jancarik, J -- Koshland, D E Jr -- Kim, S H -- AI 30725/AI/NIAID NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1342-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660187" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid/metabolism ; Binding Sites ; Disulfides/analysis ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry/metabolism ; Salmonella typhimurium/metabolism ; X-Ray Diffraction
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  • 29
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    Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-22
    Description: Defensins (molecular weight 3500 to 4000) act in the mammalian immune response by permeabilizing the plasma membranes of a broad spectrum of target organisms, including bacteria, fungi, and enveloped viruses. The high-resolution crystal structure of defensin HNP-3 (1.9 angstrom resolution, R factor 0.19) reveals a dimeric beta sheet that has an architecture very different from other lytic peptides. The dimeric assembly suggests mechanisms by which defensins might bind to and permeabilize the lipid bilayer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hill, C P -- Yee, J -- Selsted, M E -- Eisenberg, D -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1481-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eisenberg, Molecular Biology Institute, Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006422" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blood Proteins/chemistry/*ultrastructure ; Cell Membrane Permeability ; Crystallography ; Defensins ; Guinea Pigs ; Humans ; Macromolecular Substances ; Membrane Proteins/chemistry/ultrastructure ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Conformation ; Rabbits ; Rats ; Structure-Activity Relationship ; X-Ray Diffraction ; *alpha-Defensins
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  • 30
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    Similarity of protein G and ubiquitin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kraulis, P J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):581-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658931" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites, Antibody ; Immunoglobulin G ; Models, Molecular ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/genetics/immunology ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Ubiquitins/*chemistry/genetics
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  • 31
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    Mapping of DNA instability at the fragile X to a trinucleotide repeat sequence p(CCG)n (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The sequence of a Pst I restriction fragment was determined that demonstrate instability in fragile X syndrome pedigrees. The region of instability was localized to a trinucleotide repeat p(CCG)n. The sequence flanking this repeat were identical in normal and affected individuals. The breakpoints in two somatic cell hybrids constructed to break at the fragile site also mapped to this repeat sequence. The repeat exhibits instability both when cloned in a nonhomologous host and after amplification by the polymerase chain reaction. These results suggest variation in the trinucleotide repeat copy number as the molecular basis for the instability and possibly the fragile site. This would account for the observed properties of this region in vivo and in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kremer, E J -- Pritchard, M -- Lynch, M -- Yu, S -- Holman, K -- Baker, E -- Warren, S T -- Schlessinger, D -- Sutherland, G R -- Richards, R I -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1711-4.〈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/1675488" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Fragile X Syndrome/*genetics ; Humans ; Molecular Sequence Data ; Pedigree ; Polymerase Chain Reaction ; Polymorphism, Restriction Fragment Length ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping ; X Chromosome/ultrastructure
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  • 32
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    HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-30
    Description: In simple eukaryotes, protein kinases regulate mitotic and meiotic cell cycles, the response to polypeptide pheromones, and the initiation of nuclear DNA synthesis. The protein HRR25 from the budding yeast Saccharomyces cerevisiae was defined by the mutation hrr25-1. This mutation resulted in sensitivity to continuous expression of the HO double-strand endonuclease, to methyl methanesulfonate, and to x-irradiation. Homozygotes of hrr25-1 were unable to sporulate and disruption and deletion of HRR25 interfered with mitotic and meiotic cell division. Sequence analysis revealed two distinctive regions in the protein. The NH2-terminus of HRR25 contains the hallmark features of protein kinases, whereas the COOH-terminus is rich in proline and glutamine. Mutations in HRR25 at conserved residues found in all protein kinases inactivated the gene, and these mutants exhibited the hrr25 null phenotypes. Taken together, the hrr25 mutant phenotypes and the features of the gene product indicate that HRR25 is a distinctive member of the protein kinase superfamily.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoekstra, M F -- Liskay, R M -- Ou, A C -- DeMaggio, A J -- Burbee, D G -- Heffron, F -- New York, N.Y. -- Science. 1991 Aug 30;253(5023):1031-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Casein Kinase I ; *DNA Damage ; *DNA Repair ; Fungal Proteins/*genetics/metabolism ; Gene Library ; Genes, Fungal ; Meiosis ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Phenotype ; *Protein Kinases ; Restriction Mapping ; Saccharomyces cerevisiae/enzymology/*genetics/physiology ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid
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  • 33
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    Demonstration that CFTR is a chloride channel by alteration of its anion selectivity (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-12
    Description: Expression of the cystic fibrosis transmembrane conductance regulator (CFTR) generates adenosine 3',5'-monophosphate (cAMP)-regulated chloride channels, indicating that CFTR is either a chloride channel or a chloride channel regulator. To distinguish between these possibilities, basic amino acids in the putative transmembrane domains were mutated. The sequence of anion selectivity of cAMP-regulated channels in cells containing either endogenous or recombinant CFTR was bromide greater than chloride greater than iodide greater than fluoride. Mutation of the lysines at positions 95 or 335 to acidic amino acids converted the selectivity sequence to iodide greater than bromide greater than chloride greater than fluoride. These data indicate that CFTR is a cAMP-regulated chloride channel and that lysines 95 and 335 determine anion selectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, M P -- Gregory, R J -- Thompson, S -- Souza, D W -- Paul, S -- Mulligan, R C -- Smith, A E -- Welsh, M J -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):202-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Internal Medicine, 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/1712984" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chloride Channels ; Chlorides/*physiology ; Cyclic AMP/physiology ; Cystic Fibrosis/physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA Mutational Analysis ; Electric Conductivity ; HeLa Cells ; Humans ; In Vitro Techniques ; Ion Channels/genetics/*physiology ; Membrane Glycoproteins/genetics/physiology ; Membrane Potentials ; Membrane Proteins/genetics/*physiology ; Molecular Sequence Data ; Transfection
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    Requirement of nuclear prolactin for interleukin-2--stimulated proliferation of T lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-05
    Description: Prolactin (PRL) is necessary for the proliferation of cloned T lymphocytes in response to interleukin-2 (IL-2). Translocation of PRL into the nucleus occurs during IL-2--stimulated mitogenesis. Therefore, the function of intranuclear PRL in T cell proliferation was tested. Eukaryotic expression vectors were prepared to express wild-type PRL [PRL(WT)], PRL that lacks the signal sequence for translocation into the endoplasmic reticulum [PRL(ER-)], and chimeric PRL in which the signal peptide was replaced with the sequence that directs the nuclear translocation of the SV40 large T antigen [PRL(NT+)]. Expression of these constructs in a T cell line (Nb2) responsive to PRL and IL-2 resulted in localization of PRL in the extracellular milieu, cytoplasm, or nucleus, respectively. Stimulation with IL-2 alone resulted in a five- to tenfold increase in the incorporation of [3H]thymidine by cells expressing PRL(NT+) or PRL(WT) as compared to PRL(ER-) or the parental Nb2 cells. Only the PRL(NT+) clone proliferated continuously with IL-2 stimulation in the presence of antiserum to PRL. These results demonstrate that nuclear PRL is necessary for IL-2--stimulated proliferation and suggest that a peptide hormone can function in the nucleus without binding to its cell surface receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clevenger, C V -- Altmann, S W -- Prystowsky, M B -- GM-13901/GM/NIGMS NIH HHS/ -- GM-36962/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):77-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063207" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport, Active ; Cell Cycle/drug effects ; Cell Nucleus/metabolism ; Drug Synergism ; Genetic Vectors ; In Vitro Techniques ; Interleukin-2/pharmacology ; Lymphocyte Activation/*drug effects ; Molecular Sequence Data ; Prolactin/pharmacokinetics/*pharmacology ; Rats ; Transfection
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  • 35
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    Global suppression of protein folding defects and inclusion body formation (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-05
    Description: Amino acid substitutions at a site in the center of the bacteriophage protein P22 tailspike polypeptide chain suppress temperature-sensitive folding mutations at many sites throughout the chain. Characterization of the intracellular folding and chain assembly process reveals that the suppressors act in the folding pathway, inhibiting the aggregation of an early folding intermediate into the kinetically trapped inclusion body state. The suppressors alone increase the folding efficiency of the otherwise wild-type polypeptide chain without altering the stability or activity of the native state. These amino acid substitutions identify an unexpected aspect of the protein folding grammar--sequences within the chain that carry information inhibiting unproductive off-pathway conformations. Such mutations may serve to increase the recovery of protein products of cloned genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitraki, A -- Fane, B -- Haase-Pettingell, C -- Sturtevant, J -- King, J -- GMS17,980/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):54-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648264" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Coliphages ; DNA Mutational Analysis ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Inclusion Bodies/*chemistry ; Molecular Sequence Data ; Mutation ; *Protein Conformation ; Viral Proteins/*chemistry ; Viral Tail Proteins
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    Control of alternative splicing by the differential binding of U1 small nuclear ribonucleoprotein particle (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-01
    Description: Cellular factors controlling alternative splicing of precursor messenger RNA are largely unknown, even though this process plays a central role in specifying the diversity of proteins in the eukaryotic cell. For the identification of such factors, a segment of the rat preprotachykinin gene was used in which differential expression of neuropeptides gamma and K is dependent on alternative splicing of the fourth exon (E4). Sequence variants of the three-exon segment, (E3-E4-E5) were created, resulting in a sensitive assay for factors mediating the splicing switch between E4-skipping and E4-inclusion. A dinucleotide mutation in the 5' splice site of E4 that increase base-pairing of this site to U1 small nuclear RNA resulted in uniform selection of E4, whereas a control mutation that destroyed base-pairing resulted in uniform E4-skipping. Affinity selection of spliceosomes formed on these functionally distinct substrates revealed that the extreme difference in splicing was mediated by differential binding of the U1 small nuclear ribonucleoprotein particle (snRNP) to the 5' splice site of E4. These data show that, apart from its established role in selecting 5' splice sites, U1 snRNP plays a fundamental role in 3' exon selection and provides insight into possible mechanisms of alternative splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuo, H C -- Nasim, F H -- Grabowski, P J -- GM-39695/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 1;251(4997):1045-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Biochemistry, Brown University, Providence, RI 02912.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1825520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Mutational Analysis ; Exons ; Hydrogen Bonding ; Macromolecular Substances ; Molecular Sequence Data ; Protein Precursors/*genetics ; *RNA Splicing ; RNA, Messenger/*metabolism ; RNA, Small Nuclear/*physiology ; Rats ; Ribonucleoproteins/chemistry/*physiology ; Ribonucleoproteins, Small Nuclear ; Structure-Activity Relationship ; Tachykinins/*genetics
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    Pulmonary surfactant protein B (SP-B): structure-function relationships (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-10-25
    Description: SP-B is a protein in pulmonary surfactant that is, in greatest part, responsible for resistance to surface tension and prevention of collapse of pulmonary alveoli. Peptides of 21 residues, synthesized following the sequence of SP-B or resembling the hydrophobic and hydrophilic domains of SP-B (such as RLLLLRLLLLRLLLLRLLLLR, R, Arg, and L, Leu), enhanced the abilities of phospholipids to reduce surface tension both in vitro and in vivo. Intermittent positively charged residues were essential for this activity. The SP-B-like peptides were found by tryptophan fluorescence to partition within the phospholipid layer in contact with both polar head groups and acyl side chains. These data, together with findings that the SP-B-related peptides increase inter- and intramolecular order of the phospholipid layer, suggest that SP-B resists surface tension by increasing lateral stability of the phospholipid layer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochrane, C G -- Revak, S D -- GM-37696/GM/NIGMS NIH HHS/ -- HL-23584/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):566-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948032" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Kinetics ; Molecular Sequence Data ; Peptides/*chemical synthesis/chemistry ; Phospholipids/metabolism ; Proteolipids/chemistry/*metabolism ; Pulmonary Surfactants/chemistry/*metabolism ; Structure-Activity Relationship ; Surface Tension
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  • 38
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    Translational potentiation of messenger RNA with secondary structure in Xenopus (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-15
    Description: Differential translation of messenger RNA (mRNA) with stable secondary structure in the 5' untranslated leader may contribute to the dramatic changes in protein synthetic patterns that occur during oogenesis and early development. Plasmids that contained the bacterial gene chloramphenicol acetyltransferase and which encoded mRNA with (hpCAT) or without (CAT) a stable hairpin secondary structure in the 5' noncoding region were transcribed in vitro, and the resulting mRNAs were injected into Xenopus oocytes, eggs, and early embryos. During early oogenesis, hpCAT mRNA was translated at less than 3 percent of the efficiency of CAT mRNA. The relative translational potential of hpCAT reached 100 percent in the newly fertilized egg and returned to approximately 3 percent after the midblastula transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, L N -- Ye, R Q -- Browder, L W -- Johnston, R N -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):807-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Calgary, Alberta, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990443" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chloramphenicol O-Acetyltransferase/genetics ; Egg Proteins/biosynthesis/genetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oogenesis/genetics ; Plasmids ; *Protein Biosynthesis ; RNA, Messenger/*genetics ; Xenopus laevis/embryology/*genetics
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    Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-26
    Description: Malignant hyperthermia (MH) causes neurological, liver, and kidney damage and death in humans and major economic losses in the swine industry. A single point mutation in the porcine gene for the skeletal muscle ryanodine receptor (ryr1) was found to be correlated with MH in five major breeds of lean, heavily muscled swine. Haplotyping suggests that the mutation in all five breeds has a common origin. Assuming that this is the causal mutation for MH, the development of a noninvasive diagnostic test will provide the basis for elimination of the MH gene or its controlled inclusion in swine breeding programs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujii, J -- Otsu, K -- Zorzato, F -- de Leon, S -- Khanna, V K -- Weiler, J E -- O'Brien, P J -- MacLennan, D H -- New York, N.Y. -- Science. 1991 Jul 26;253(5018):448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1862346" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Codon/genetics ; Haplotypes ; Malignant Hyperthermia/genetics/*veterinary ; Molecular Sequence Data ; *Mutation ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Receptors, Cholinergic/*genetics ; Restriction Mapping ; Ryanodine/metabolism ; Ryanodine Receptor Calcium Release Channel ; Species Specificity ; Swine ; Swine Diseases/*genetics
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    Cloning of a factor required for activity of the Ah (dioxin) receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-17
    Description: The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E C -- Reyes, H -- Chu, F F -- Sander, F -- Conley, L H -- Brooks, B A -- Hankinson, O -- CA 16048/CA/NCI NIH HHS/ -- CA 28868/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):954-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1852076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytosol/metabolism ; *DNA-Binding Proteins ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Proteins/*genetics/metabolism ; RNA, Messenger/genetics ; Receptors, Aryl Hydrocarbon ; Receptors, Drug/genetics/*metabolism ; Sequence Homology, Nucleic Acid ; Tetrachlorodibenzodioxin/*metabolism ; *Transcription Factors ; Transfection
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    Specific DNA binding by c-Myb: evidence for a double helix-turn-helix-related motif (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-06
    Description: The c-Myb protein is a sequence-specific DNA binding protein that activates transcription in hematopoietic cells. Three imperfect repeats (R1, R2, and R3) that contain regularly spaced tryptophan residues form the DNA binding domain of c-Myb. A fragment of c-Myb that contained the R2 and R3 regions bound specifically to a DNA sequence recognized by c-Myb plus ten additional base pairs at the 3' end of the element. The R2R3 fragment was predicted to contain two consecutive helix-turn-helix (HTH) motifs with unconventional turns. Mutagenesis of amino acids in R2R3 at positions that correspond to DNA-contacting amino acids in other HTH-containing proteins abolished specific DNA binding without affecting nonspecific DNA interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabrielsen, O S -- Sentenac, A -- Fromageot, P -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Ingenierie des Proteines, Centre d'Etudes de Saclay, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887237" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Oncogenes ; Polymerase Chain Reaction ; Protein Conformation ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-myb ; Recombinant Proteins/metabolism ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Transcription Factors/*metabolism
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    A 32-kD GTP-binding protein associated with the CD4-p56lck and CD8-p56lck T cell receptor complexes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: The guanosine triphosphate (GTP)-binding proteins include signal-transducing heterotrimeric G proteins (for example, Gs, Gi), smaller GTP-binding proteins that function in protein sorting, and the oncogenic protein p21ras. The T cell receptor complexes CD4-p56lck and CD8-p56lck were found to include a 32- to 33-kilodalton phosphoprotein (p32) that was recognized by an antiserum to a consensus GTP-binding region in G proteins. Immunoprecipitated CD4 and CD8 complexes bound GTP and hydrolyzed it to guanosine diphosphate (GDP). The p32 protein was covalently linked to [alpha-32P]GTP by ultraviolet photoaffinity labeling. These results demonstrate an interaction between T cell receptor complexes and an intracellular GTP-binding protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Telfer, J C -- Rudd, C E -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):439-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1925604" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD4/*metabolism ; Antigens, CD8/*metabolism ; Cell Line ; GTP-Binding Proteins/*metabolism ; Humans ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Precipitin Tests ; Protein Binding ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell/*metabolism
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    GRAIL seeks out genes buried in DNA sequence (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):805.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948063" target="_blank"〉PubMed〈/a〉
    Keywords: *Artificial Intelligence ; Base Sequence ; DNA/*genetics ; *Genes ; *Genome, Human ; Humans ; Molecular Sequence Data ; Software
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    Triplex DNA finally comes of age (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1991 Jun 7;252(5011):1374-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047850" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*chemistry ; DNA Replication ; Genes, myc ; Models, Molecular ; Molecular Sequence Data ; Transcription, Genetic/drug effects
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  • 45
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    Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-01
    Description: Apolipoprotein AI (apoAI) is a lipid-binding protein that participates in the transport of cholesterol and other lipids in the plasma. A complementary DNA clone for a protein that bound to regulatory elements of the apoAI gene was isolated. This protein, designated apoAI regulatory protein-1 (ARP-1), is a novel member of the steroid hormone receptor superfamily. ARP-1 bound to DNA as a dimer, and its dimerization domain was localized to the COOH-terminal region. ARP-1 also bound to a thyroid hormone-responsive element and to regulatory regions of the apoB, apoCIII, insulin, and ovalbumin genes. In cotransfection experiments, ARP-1 downregulated the apoAI gene. The involvement of ARP-1 in the regulation of apoAI gene expression suggests that it may participate in lipid metabolism and cholesterol homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ladias, J A -- Karathanasis, S K -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):561-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1899293" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apolipoprotein A-I ; Apolipoproteins A/*genetics ; Base Sequence ; COUP Transcription Factor II ; COUP Transcription Factors ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Gene Expression Regulation ; Humans ; Lipoproteins, HDL/*genetics ; Molecular Sequence Data ; Oligonucleotide Probes ; Receptors, Steroid/*metabolism ; Regulatory Sequences, Nucleic Acid ; *Transcription Factors
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    Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-29
    Description: Human immunodeficiency virus type 1 (HIV-1) gene expression is activated by Tat, a virally encoded protein. Tat trans-activation requires viral (trans-activation--responsive; TAR) RNA sequences located in the R region of the long terminal repeat (LTR). Existing evidence suggests that Tat probably cooperates with cellular factors that bind to TAR RNA in the overall trans-activation process. A HeLa complementary DNA was isolated and characterized that encodes a TAR RNA-binding protein (TRBP). TRBP activated the HIV-1 LTR and was synergistic with Tat function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatignol, A -- Buckler-White, A -- Berkhout, B -- Jeang, K T -- New York, N.Y. -- Science. 1991 Mar 29;251(5001):1597-600.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious 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/2011739" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Carrier Proteins/*genetics ; Endoribonucleases/genetics ; Escherichia coli/enzymology ; *Escherichia coli Proteins ; Gene Products, tat/metabolism ; *HIV Long Terminal Repeat ; HIV-1/*genetics ; Humans ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmids ; RNA, Viral/genetics ; *RNA-Binding Proteins ; Ribonuclease III ; Sequence Homology, Nucleic Acid ; tat Gene Products, Human Immunodeficiency Virus
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    Cystic fibrosis transmembrane conductance regulator: nucleotide binding to a synthetic peptide (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-01
    Description: Multiple mutations in the gene responsible for cystic fibrosis are located within a region predicted to encode a nucleotide-binding fold in the amino terminal half of the cystic fibrosis transmembrane conductance regulator protein. A 67-amino acid peptide (P-67) that corresponds to the central region of this putative nucleotide binding site was chemically synthesized and purified. This peptide bound adenine nucleotides. The apparent dissociation constants (Kd's) for the trinitrophenyl (TNP) adenine nucleotides, TNP-adenosine triphosphate, TNP-adenosine diphosphate, and TNP-adenosine monophosphate, were 300 nanomolar, 200 nanomolar, and greater than 1 micromolar, respectively. The Kd for adenosine triphosphate was 300 micromolar. Circular dichroism spectroscopy was used to show that P-67 assumes a predominantly beta sheet structure in solution, a finding that is consistent with secondary structure predictions. On the basis of this information, the phenylalanine at position 508, which is deleted in approximately 70 percent of individuals with cystic fibrosis, was localized to a beta strand within the nucleotide binding peptide. Deletion of this residue is predicted to induce a significant structural change in the beta strand and altered nucleotide binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, P J -- Shenbagamurthi, P -- Ysern, X -- Pedersen, P L -- CA 10951/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):555-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1703660" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/*metabolism ; Amino Acid Sequence ; Binding Sites ; Chromatography, High Pressure Liquid ; Cystic Fibrosis/*genetics/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator ; Humans ; Membrane Proteins/*genetics/isolation & purification/metabolism ; Molecular Sequence Data
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    Identification of Ets- and notch-related subunits in GA binding protein (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-16
    Description: Recombinant cDNA clones that encode two distinct subunits of the transcription factor GA binding protein (GABP) have been isolated. The predicted amino acid sequence of one subunit, GABP alpha, exhibits similarity to the sequence of the product of the ets-1 protooncogene in a region known to encompass the Ets DNA binding domain. The sequence of the second subunit, GABP beta, contains four 33-amino acid repeats located close to the NH2-terminus of the subunit. The sequences of these repeats are similar to repeats in several transmembrane proteins, including Notch from Drosophila melanogaster and Glp-1 and Lin-12 from Caenorhabditis elegans. Avid, sequence-specific binding to DNA required the presence of both polypeptides, revealing a conceptual convergence of nuclear transforming proteins and membrane-anchored proteins implicated in developmentally regulated signal transduction processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaMarco, K -- Thompson, C C -- Byers, B P -- Walton, E M -- McKnight, S L -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):789-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Carnegie Institution of Washington, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876836" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cloning, Molecular ; DNA-Binding Proteins/*chemistry/genetics ; GA-Binding Protein Transcription Factor ; Gene Expression ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics ; Peptides/chemistry ; Proto-Oncogene Protein c-ets-1 ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-ets ; RNA, Messenger/genetics ; Rats ; Recombinant Proteins ; Transcription Factors/*chemistry/genetics
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    Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-16
    Description: Analysis of the heteromeric DNA binding protein GABP has revealed the interaction of two distinct peptide sequence motifs normally associated with proteins located in different cellular compartments. The alpha subunit of GABP contains an 85-amino acid segment related to the Ets family of DNA binding proteins. The ETS domain of GABP alpha facilitates weak binding to DNA and, together with an adjacent segment of 37 amino acids, mediates stable interaction with GABP beta. The beta subunit of GABP contains four imperfect repeats of a sequence present in several transmembrane proteins including the product of the Notch gene of Drosophila melanogaster. These amino-terminal repeats of GABP beta mediate stable interaction with GABP alpha and, when complexed with GABP alpha, directly contact DNA. These observations provide evidence for a distinct biochemical role for the 33-amino acid repeats, and suggest that they may serve as a module for the generation of specific dimerization interfaces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C C -- Brown, T A -- McKnight, S L -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):762-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Carnegie Institution of Washington, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cross-Linking Reagents ; DNA/metabolism ; DNA-Binding Proteins/*chemistry/metabolism ; GA-Binding Protein Transcription Factor ; Macromolecular Substances ; Molecular Sequence Data ; Molecular Weight ; Multigene Family ; Nuclear Proteins/*chemistry/metabolism ; Oligonucleotides/chemistry ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-ets ; Rats ; Recombinant Proteins ; Structure-Activity Relationship ; Transcription Factors/*chemistry/metabolism
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    A component of calcium-activated potassium channels encoded by the Drosophila slo locus (1991)
    American Association for the Advancement of Science (AAAS)
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    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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    Cell-free, de novo synthesis of poliovirus (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-13
    Description: Cell-free translation of poliovirus RNA in an extract of uninfected human (HeLa) cells yielded viral proteins through proteolysis of the polyprotein. In the extract, newly synthesized proteins catalyzed poliovirus-specific RNA synthesis, and formed infectious poliovirus de novo. Newly formed virions were neutralized by type-specific antiserum, and infection of human cells with them was prevented by poliovirus receptor-specific antibodies. Poliovirus synthesis was increased nearly 70-fold when nucleoside triphosphates were added, but it was abolished in the presence of inhibitors of translation or viral genome replication. The ability to conduct cell-free synthesis of poliovirus will aid in the study of picornavirus proliferation and in the search for the control of picornaviral disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molla, A -- Paul, A V -- Wimmer, E -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1647-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, School of Medicine, State University of New York, Stony Brook 11794.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661029" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell-Free System ; HeLa Cells ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides/chemistry ; Poliovirus/*growth & development ; Polymerase Chain Reaction ; RNA, Viral/analysis/biosynthesis ; Time Factors ; Viral Proteins/biosynthesis/chemistry ; *Virus Replication
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  • 52
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    New role found for a common protein "motif" (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, M -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):742.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1831563" target="_blank"〉PubMed〈/a〉
    Keywords: Ankyrins ; Base Sequence ; Binding Sites ; Blood Proteins/*chemistry ; Membrane Proteins/*chemistry ; Molecular Sequence Data ; *Protein Binding ; Structure-Activity Relationship ; Transcription Factors/chemistry
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    The N-end rule in bacteria (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-29
    Description: The N-end rule relates the in vivo half-life of a protein to the identity of its amino-terminal residue. Distinct versions of the N-end rule operate in all eukaryotes examined. It is shown that the bacterium Escherichia coli also has the N-end rule pathway. Amino-terminal arginine, lysine, leucine, phenylalanine, tyrosine, and tryptophan confer 2-minute half-lives on a test protein; the other amino-terminal residues confer greater than 10-hour half-lives on the same protein. Amino-terminal arginine and lysine are secondary destabilizing residues in E. coli because their activity depends on their conjugation to the primary destabilizing residues leucine or phenylalanine by leucine, phenylalanine-transfer RNA-protein transferase. The adenosine triphosphate-dependent protease Clp (Ti) is required for the degradation of N-end rule substrates in E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tobias, J W -- Shrader, T E -- Rocap, G -- Varshavsky, A -- DK39520/DK/NIDDK NIH HHS/ -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1374-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962196" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteria/*metabolism ; Bacterial Proteins/*metabolism ; Escherichia coli/enzymology/metabolism ; Half-Life ; Kinetics ; Molecular Sequence Data ; Rabbits ; Reticulocytes/metabolism ; Saccharomyces cerevisiae/enzymology/metabolism ; Structure-Activity Relationship ; beta-Galactosidase/*metabolism
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    Oligoclonal expansion and CD1 recognition by human intestinal intraepithelial lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-20
    Description: A human intestinal intraepithelial lymphocyte (IEL) T cell line was established from jejunum to characterize the structure and function of the alpha beta T cell antigen receptors (TCRs) expressed by this population. Single-sided polymerase chain reaction (PCR) amplification cloning and quantitative PCR amplification of the TCR chains from the cell line and from fresh IELs demonstrated that IELs were oligoclonal. The IEL T cell line exhibited CD1-specific cytotoxicity and a dominant IEL T cell clone was CD1c-specific. Thus, human jejunal intraepithelial lymphocytes are oligoclonal and recognize members of the CD1 gene family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balk, S P -- Ebert, E C -- Blumenthal, R L -- McDermott, F V -- Wucherpfennig, K W -- Landau, S B -- Blumberg, R S -- 5 KO8 DK01886/DK/NIDDK NIH HHS/ -- CA-01310/CA/NCI NIH HHS/ -- DK42166/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1411-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hematology-Oncology Division, Beth Israel Hospital, Harvard Medical School, Boston, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1716785" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD/*genetics/immunology ; Antigens, CD1 ; Base Sequence ; Cell Line ; Clone Cells ; Epithelium/physiology ; Humans ; Jejunum/immunology ; Molecular Sequence Data ; Oligonucleotide Probes ; Polymerase Chain Reaction/methods ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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    Conserved sequence and structural elements in the HIV-1 principal neutralizing determinant: further clarifications (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaRosa, G J -- Weinhold, K -- Profy, A T -- Langlois, A J -- Dreesman, G R -- Boswell, R N -- Shadduck, P -- Bolognesi, D P -- Matthews, T J -- Emini, E A -- New York, N.Y. -- Science. 1991 Sep 6;253(5024):1146.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Repligen Corporation, Cambridge, MA 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1887238" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Databases, Factual ; Genes, Viral ; Genetic Variation ; HIV-1/*genetics ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction/methods
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    Conserved sequence and structural elements in the HIV-1 principal neutralizing determinant: corrections and clarifications (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉LaRosa, G J -- Davide, J P -- Weinhold, K -- Waterbury, J A -- Profy, A T -- Lewis, J A -- Langlois, A J -- Dreesman, G R -- Boswell, R N -- Shadduck, P -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):811.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; HIV-1/*genetics ; Molecular Sequence Data
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    FTZ-F1, a steroid hormone receptor-like protein implicated in the activation of fushi tarazu (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: The Drosophila homeobox segmentation gene fushi tarazu (ftz) is expressed in a seven-stripe pattern during early embryogenesis. This characteristic pattern is largely specified by the zebra element located immediately upstream of the ftz transcriptional start site. The FTZ-F1 protein, one of multiple DNA binding factors that interacts with the zebra element, is implicated in the activation of ftz transcription, especially in stripes 1, 2, 3, and 6. An FTZ-F1 complementary DNA has been cloned by recognition site screening of a Drosophila expression library. The identity of the FTZ-F1 complementary DNA clone was confirmed by immunological cross-reaction with antibodies to FTZ-F1 and by sequence analysis of peptides from purified FTZ-F1 protein. The predicted amino acid sequence of FTZ-F1 revealed that the protein is a member of the nuclear hormone receptor superfamily. This finding raises the possibility that a hormonal ligand affects the expression of a homeobox segmentation gene early in embryonic development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lavorgna, G -- Ueda, H -- Clos, J -- Wu, C -- New York, N.Y. -- Science. 1991 May 10;252(5007):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Blotting, Southern ; Blotting, Western ; Chromosome Mapping ; Cloning, Molecular ; Drosophila Proteins ; Drosophila melanogaster ; Fushi Tarazu Transcription Factors ; Gene Expression Regulation ; Genes, Homeobox ; *Homeodomain Proteins ; Insect Hormones/*chemistry ; Molecular Sequence Data ; Open Reading Frames ; RNA/analysis ; Receptors, Steroid/genetics ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Zinc Fingers
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    The three-dimensional structure of canine parvovirus and its functional implications (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-22
    Description: The three-dimensional atomic structure of a single-stranded DNA virus has been determined. Infectious virions of canine parvovirus contain 60 protein subunits that are predominantly VP-2. The central structural motif of VP-2 has the same topology (an eight-stranded antiparallel beta barrel) as has been found in many other icosahedral viruses but represents only about one-third of the capsid protein. There is a 22 angstrom (A) long protrusion on the threefold axes, a 15 A deep canyon circulating about each of the five cylindrical structures at the fivefold axes, and a 15 A deep depression at the twofold axes. By analogy with rhinoviruses, the canyon may be the site of receptor attachment. Residues related to the antigenic properties of the virus are found on the threefold protrusions. Some of the amino termini of VP-2 run to the exterior in full but not empty virions, which is consistent with the observation that some VP-2 polypeptides in full particles can be cleaved by trypsin. Eleven nucleotides are seen in each of 60 symmetry-related pockets on the interior surface of the capsid and together account for 13 percent of the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsao, J -- Chapman, M S -- Agbandje, M -- Keller, W -- Smith, K -- Wu, H -- Luo, M -- Smith, T J -- Rossmann, M G -- Compans, R W -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1456-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006420" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/chemistry ; Capsid/ultrastructure ; Crystallography ; DNA, Viral/ultrastructure ; Hemagglutinins, Viral/chemistry ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Parvoviridae/*ultrastructure ; Virion/ultrastructure ; Virus Replication ; X-Ray Diffraction
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    Critical structural elements of the VP16 transcriptional activation domain (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-01-04
    Description: Virion protein 16 (VP16) of herpes simplex virus type 1 contains an acidic transcriptional activation domain. Missense mutations within this domain have provided insights into the structural elements critical for its function. Net negative charge contributed to, but was not sufficient for, transcriptional activation by VP16. A putative amphipathic alpha helix did not appear to be an important structural component of the activation domain. A phenylalanine residue at position 442 was exquisitely sensitive to mutation. Transcriptional activators of several classes contain hydrophobic amino acids arranged in patterns resembling that of VP16. Therefore, the mechanism of transcriptional activation by VP16 and other proteins may involve both ionic and specific hydrophobic interactions with target molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cress, W D -- Triezenberg, S J -- AI 27323/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):87-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Michigan State University, East Lansing 48824-1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846049" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Immediate-Early Proteins ; Molecular Sequence Data ; Mutation ; Protein Conformation ; *Simplexvirus ; Structure-Activity Relationship ; Transcription Factors/*chemistry/genetics/pharmacology ; Transcription, Genetic/*drug effects ; Transfection ; Viral Proteins/*genetics ; Virion
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    Sequence-specific antirepression of histone H1-mediated inhibition of basal RNA polymerase II transcription (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-08
    Description: To understand the principles of control and selectivity in gene expression, the biochemical mechanisms by which promoter- and enhancer-binding factors regulate transcription by RNA polymerase II were analyzed. A general observed repressor of transcription was purified and identified as histone H1. Since many aspects of H1 binding to naked DNA resemble its interaction with chromatin, purified H1 bound to naked DNA was used as a model for the repressed state of the DNA template. Three sequence-specific transcription factors, Sp1, GAL4-VP16, and GAGA factor, were shown to counteract H1-mediated repression (antirepression). In addition, Sp1 and GAL4-VP16, but not the GAGA factor, activated transcription in the absence of H1. Therefore, true activation and antirepression appear to be distinct activities of sequence-specific factors. Furthermore, transcription antirepression by GAL4-VP16 was sustained for several rounds of transcription. These findings, together with previous studies on H1, suggest that H1 participates in repression of the genome in the ground state and that sequence-specific transcription factors induce selected genes by a combination of true activation and release of basal repression that is mediated at least in part by H1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Croston, G E -- Kerrigan, L A -- Lira, L M -- Marshak, D R -- Kadonaga, J T -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):643-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1899487" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; Cell-Free System ; DNA-Binding Proteins/physiology ; Drosophila melanogaster/genetics ; *Gene Expression Regulation ; HeLa Cells ; Histones/genetics/*physiology ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Nucleosomes/physiology ; RNA Polymerase II/*physiology ; Regulatory Sequences, Nucleic Acid ; Repressor Proteins/physiology ; Templates, Genetic ; Transcription Factors/*physiology ; *Transcription, Genetic
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    Tissue-specific splicing in vivo of the beta-tropomyosin gene: dependence on an RNA secondary structure (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-06-28
    Description: The beta-tropomyosin gene in chicken contains two mutually exclusive exons (exons 6A and 6B) which are used by the splicing apparatus in myogenic cells, respectively, before (myoblast stage) and after (myotube stage) differentiation. The myoblast splicing pattern is shown to depend on multiple sequence elements that are located in the upstream intron and in the exon 6B and that exert a negative control over exon 6B splicing. This regulation of splicing is due, at least in part, to a secondary structure of the primary transcript, which limits in vivo the accessibility of exon 6B in myoblasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Libri, D -- Piseri, A -- Fiszman, M Y -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1842-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063196" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Exons ; Introns ; Models, Molecular ; Molecular Sequence Data ; Muscles/physiology ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; RNA Precursors/*genetics ; *RNA Splicing ; RNA, Messenger/*genetics ; Transcription, Genetic ; Tropomyosin/*genetics
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    Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-03-22
    Description: A DNA probe that spanned a domain conserved among the proto-oncogene c-rel, the Drosophila morphogen dorsal, and the p50 DNA binding subunit of NF-kappa B was generated from Jurkat T cell complementary DNA with the polymerase chain reaction (PCR) and degenerate oligonucleotides. This probe was used to identify a rel-related complementary DNA that hybridized to a 2.6-kilobase messenger RNA present in human T and B lymphocytes. In vitro transcription and translation of the complementary DNA resulted in the synthesis of a protein with an apparent molecular size of 65 kilodaltons (kD). The translated protein showed weak DNA binding with a specificity for the kappa B binding motif. This protein-DNA complex comigrated with the complex obtained with the purified human p65 NF-kappa B subunit and binding was inhibited by I kappa B-alpha and -beta proteins. In addition, the 65-kD protein associated with the p50 subunit of NF-kappa B and the kappa B probe to form a complex with the same electrophoretic mobility as the NF-kappa B-DNA complex. Therefore the rel-related 65-kD protein may represent the p65 subunit of the active NF-kappa B transcription factor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruben, S M -- Dillon, P J -- Schreck, R -- Henkel, T -- Chen, C H -- Maher, M -- Baeuerle, P A -- Rosen, C A -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1490-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110-1199.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006423" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; NF-kappa B/*genetics ; Polymerase Chain Reaction ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-rel ; T-Lymphocytes
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    Expression cloning of an adenylate cyclase-coupled calcitonin receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-25
    Description: A calcitonin receptor complementary DNA (cDNA) was cloned by expression of a cDNA library from a porcine kidney epithelial cell line in COS cells. The 482-amino acid receptor has high affinity for salmon calcitonin (dissociation constant Kd approximately 6 nM) and is functionally coupled to increases in intracellular cyclic adenosine monophosphate (cAMP). The receptor shows no sequence similarity to other reported G protein-coupled receptors but is homologous to the parathyroid hormone-parathyroid hormone-related peptide (PTH-PTHrP) receptor, indicating that the receptors for these hormones, which regulate calcium homeostasis, represent a new family of G protein-coupled receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, H Y -- Harris, T L -- Flannery, M S -- Aruffo, A -- Kaji, E H -- Gorn, A -- Kolakowski, L F Jr -- Lodish, H F -- Goldring, S R -- AM 03564/AM/NIADDK NIH HHS/ -- HL-41484/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1022-4.〈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/1658940" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/physiology ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Calcitonin/*metabolism ; Cloning, Molecular ; Cyclic AMP/physiology ; DNA/genetics ; Gene Expression ; Kidney/physiology ; Molecular Sequence Data ; RNA, Messenger/genetics ; Receptors, Calcitonin ; Receptors, Cell Surface/*genetics ; Swine
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    Functional contribution of neuronal AChR subunits revealed by antisense oligonucleotides (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: Although multiple related genes encoding nicotinic acetylcholine receptor (AChR) subunits have been identified, how each of these subunits contributes to AChRs in neurons is not known. Sympathetic neurons express four classes of AChR channels and six AChR subunit genes (alpha 3, alpha 4, alpha 5, alpha 7, beta 2, and beta 4). The contribution of individual subunits to AChR channel subtypes in these neurons was examined by selective deletion with antisense oligonucleotides. An alpha 3 antisense oligonucleotide decreased the number and altered the properties of the normally expressed ACh-activated channels. The remaining AChR channels have distinct biophysical and pharmacological properties that indicate an important functional contribution of the alpha 7 subunit.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2366811/" 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/PMC2366811/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Listerud, M -- Brussaard, A B -- Devay, P -- Colman, D R -- Role, L W -- NS 29071/NS/NINDS NIH HHS/ -- NS27680/NS/NINDS NIH HHS/ -- R01 NS029071/NS/NINDS NIH HHS/ -- R01 NS029071-09/NS/NINDS NIH HHS/ -- R01 NS029071-10/NS/NINDS NIH HHS/ -- R01 NS029071-11/NS/NINDS NIH HHS/ -- R01 NS029071-12/NS/NINDS NIH HHS/ -- R01 NS029071-13/NS/NINDS NIH HHS/ -- R01 NS029071-13S1/NS/NINDS NIH HHS/ -- R01 NS029071-14/NS/NINDS NIH HHS/ -- R01 NS029071-15/NS/NINDS NIH HHS/ -- R01 NS029071-16/NS/NINDS NIH HHS/ -- R01 NS029071-17/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Columbia College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720573" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bungarotoxins/pharmacology ; Chick Embryo ; Gene Expression ; Ion Channel Gating ; Ion Channels/*physiology ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Receptors, Nicotinic/*physiology/ultrastructure ; Structure-Activity Relationship ; Sympathetic Nervous System/*physiology
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    Cloning of complementary DNA encoding a functional human interleukin-8 receptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-13
    Description: Interleukin-8 (IL-8) is an inflammatory cytokine that activates neutrophil chemotaxis, degranulation, and the respiratory burst. Neutrophils express receptors for IL-8 that are coupled to guanine nucleotide-binding proteins (G proteins); binding of IL-8 to its receptor induces the mobilization of intracellular calcium stores. A cDNA clone from HL-60 neutrophils, designated p2, has now been isolated that encodes a human IL-8 receptor. When p2 is expressed in oocytes from Xenopus laevis, the oocytes bind 125I-labeled IL-8 specifically and respond to IL-8 by mobilizing calcium stores with an EC50 of 20 nM. This IL-8 receptor has 77% amino acid identity with a second human neutrophil receptor isotype that binds IL-8 with higher affinity. It also exhibits 69% amino acid identity with a protein reported to be an N-formyl peptide receptor from rabbit neutrophils, but less than 30% identity with all other known G protein-coupled receptors, including the human N-formyl peptide receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murphy, P M -- Tiffany, H L -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1280-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Host Defenses, National Institute of Allergy and Infectious 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/1891716" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Cloning, Molecular/methods ; DNA/genetics ; Gene Library ; Humans ; Interleukin-8/*metabolism/pharmacology ; Kinetics ; Molecular Sequence Data ; Neutrophils/immunology ; Oocytes/drug effects/physiology ; Protein Biosynthesis ; Rabbits ; Receptors, Immunologic/drug effects/*genetics/physiology ; Receptors, Interleukin-8A ; Recombinant Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Transcription, Genetic ; Xenopus
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    A G protein-linked receptor for parathyroid hormone and parathyroid hormone-related peptide (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-25
    Description: The complementary DNA encoding a 585-amino acid parathyroid hormone-parathyroid hormone-related peptide (PTH-PTHrP) receptor with seven potential membrane-spanning domains was cloned by COS-7 expression using an opossum kidney cell complementary DNA (cDNA) library. The expressed receptor binds PTH and PTHrP with equal affinity, and both ligands equivalently stimulate adenylate cyclase. Striking homology with the calcitonin receptor and lack of homology with other G protein-linked receptors indicate that receptors for these calcium-regulating hormones are related and represent a new family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Juppner, H -- Abou-Samra, A B -- Freeman, M -- Kong, X F -- Schipani, E -- Richards, J -- Kolakowski, L F Jr -- Hock, J -- Potts, J T Jr -- Kronenberg, H M -- DK 11794/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 15;254(5034):1024-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrine Unit, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1658941" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Membrane Glycoproteins/chemistry/genetics/metabolism ; Molecular Sequence Data ; Opossums ; Parathyroid Hormone/metabolism ; Parathyroid Hormone-Related Protein ; Proteins/metabolism ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; Receptors, Parathyroid Hormone ; Sequence Alignment ; Solubility
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    Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: Human apolipoprotein E, a blood plasma protein, mediates the transport and uptake of cholesterol and lipid by way of its high affinity interaction with different cellular receptors, including the low-density lipoprotein (LDL) receptor. The three-dimensional structure of the LDL receptor-binding domain of apoE has been determined at 2.5 angstrom resolution by x-ray crystallography. The protein forms an unusually elongated (65 angstroms) four-helix bundle, with the helices apparently stabilized by a tightly packed hydrophobic core that includes leucine zipper-type interactions and by numerous salt bridges on the mostly charged surface. Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix. This structure provides the basis for understanding the behavior of naturally occurring mutants that can lead to atherosclerosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, C -- Wardell, M R -- Weisgraber, K H -- Mahley, R W -- Agard, D A -- HL-41633/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1817-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063194" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoproteins E/*chemistry/genetics/metabolism ; Binding Sites ; Computer Graphics ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Receptors, LDL/*metabolism ; X-Ray Diffraction
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    Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaanan, B -- Lis, H -- Sharon, N -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):862-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular 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/1948067" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Conformation ; Carbohydrate Sequence ; Computer Simulation ; Erythrina ; Glycosylation ; Hydrogen Bonding ; Lectins/*chemistry ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Oligosaccharides ; Plant Lectins ; Plants, Medicinal ; Protein Conformation ; X-Ray Diffraction
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    Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-08
    Description: The myc protooncogene family has been implicated in cell proliferation, differentiation, and neoplasia, but its mechanism of function at the molecular level is unknown. The carboxyl terminus of Myc family proteins contains a basic region helix-loop-helix leucine zipper motif (bHLH-Zip), which has DNA-binding activity and has been predicted to mediate protein-protein interactions. The bHLH-Zip region of c-Myc was used to screen a complementary DNA (cDNA) expression library, and a bHLH-Zip protein, termed Max, was identified. Max specifically associated with c-Myc, N-Myc, and L-Myc proteins, but not with a number of other bHLH, bZip, or bHLH-Zip proteins. The interaction between Max and c-Myc was dependent on the integrity of the c-Myc HLH-Zip domain, but not on the basic region or other sequences outside the domain. Furthermore, the Myc-Max complex bound to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibited appreciable binding. The DNA-binding activity of the complex was dependent on both the dimerization domain and the basic region of c-Myc. These results suggest that Myc family proteins undergo a restricted set of interactions in the cell and may belong to the more general class of eukaryotic DNA-binding transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blackwood, E M -- Eisenman, R N -- P01 CA28151/CA/NCI NIH HHS/ -- R01 CA20525/CA/NCI NIH HHS/ -- T32 CA09437/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1211-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Cloning, Molecular ; DNA-Binding Proteins/*genetics/metabolism ; Escherichia coli/genetics ; Gene Library ; *Genes, myc ; Glutathione Transferase/genetics/metabolism ; Humans ; Molecular Sequence Data ; Oligonucleotide Probes ; Protein Biosynthesis ; Proto-Oncogene Proteins c-myc/*genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; *Transcription Factors ; Transcription, Genetic
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    Primary structure and functional expression of the 5HT3 receptor, a serotonin-gated ion channel (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-18
    Description: The neurotransmitter serotonin (5HT) activates a variety of second messenger signaling systems and through them indirectly regulates the function of ion channels. Serotonin also activates ion channels directly, suggesting that it may also mediate rapid, excitatory responses. A complementary DNA clone containing the coding sequence of one of these rapidly responding channels, a 5HT3 subtype of the serotonin receptor, has been isolated by screening a neuroblastoma expression library for functional expression of serotonin-gated currents in Xenopus oocytes. The predicted protein product has many of the features shared by other members of the ligand-gated ion channel family. The pharmacological and electrophysiological characteristics of the cloned receptor are largely consistent with the properties of native 5HT3 receptors. Messenger RNA encoding this receptor is found in the brain, spinal cord, and heart. This receptor defines a new class of excitatory ligand-gated channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maricq, A V -- Peterson, A S -- Brake, A J -- Myers, R M -- Julius, D -- GM44298/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 18;254(5030):432-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143-0450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718042" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cell Line ; Ion Channels/*chemistry/drug effects/physiology ; Mice ; Molecular Sequence Data ; Oocytes/metabolism ; Poly A ; RNA, Messenger ; Radioligand Assay ; Receptors, Serotonin/*chemistry/drug effects/physiology ; Xenopus
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    Variable effects of phosphorylation of Pit-1 dictated by the DNA response elements (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: Pit-1, a tissue-specific POU domain transcription factor, is required for the activation of the prolactin, growth hormone, and Pit-1 promoters that confer regulation by epidermal growth factor, adenosine 3',5'-monophosphate (cAMP), and phorbol esters. Pit-1 is phosphorylated in pituitary cells at two distinct sites in response to phorbol esters and cAMP. Phosphorylation of Pit-1 modifies its conformation on DNA recognition elements and results in increased binding at certain sites and decreased binding at other sites, dependent on DNA sequences adjacent to the core Pit-1 binding motif. One residue (Thr220), located in the POU homeodomain within a sequence conserved throughout the POU-domain family, confers these responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kapiloff, M S -- Farkash, Y -- Wegner, M -- Rosenfeld, M G -- DK 18477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):786-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Regulatory Biology Program, School of Medicine, University of California, San Diego, La Jolla 92093-0648.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1652153" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cell Line ; Cyclic AMP/pharmacology ; DNA/metabolism ; DNA-Binding Proteins/chemistry/*physiology ; In Vitro Techniques ; Molecular Sequence Data ; Peptide Mapping ; Phosphorylation ; Phosphothreonine/metabolism ; Pituitary Gland/*physiology ; Protein Kinases/metabolism ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/*physiology ; Trypsin
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    Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-12-06
    Description: Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel beta sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bontems, F -- Roumestand, C -- Gilquin, B -- Menez, A -- Toma, F -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1521-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement d'Ingenierie et d'Etudes des Proteines, Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blood Proteins/*ultrastructure ; Charybdotoxin ; Defensins ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Neurotoxins/*chemistry ; Potassium Channels/drug effects ; Protein Conformation ; Scorpion Venoms/*chemistry ; Scorpions ; Sequence Alignment
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    Sigma factor relatives in eukaryotes (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-08-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaehning, J A -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):859.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876846" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/genetics ; *Eukaryotic Cells ; Humans ; Molecular Sequence Data ; RNA Polymerase II/metabolism ; Sequence Homology, Nucleic Acid ; Sigma Factor/genetics/*metabolism ; Transcription Factors/genetics/*metabolism
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    Long-range structure in ribonuclease P RNA (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-08
    Description: Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA. This feature strongly constrains the three-dimensional structure of RNase P RNA near the active site. Some RNase P RNAs lack this structure but contain a unique, possibly compensating, structural domain. This suggests that different RNA structures located at different positions in the sequence may have equivalent architectural functions in RNase P RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haas, E S -- Morse, D P -- Brown, J W -- Schmidt, F J -- Pace, N R -- GM34527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1719634" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/enzymology/genetics ; Base Composition ; Base Sequence ; Biological Evolution ; Endoribonucleases/*genetics ; Escherichia coli/enzymology/genetics ; *Escherichia coli Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Conformation ; RNA, Bacterial/*genetics ; RNA, Catalytic/*genetics ; Ribonuclease P
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    Mutations affecting internal TEA blockade identify the probable pore-forming region of a K+ channel (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-22
    Description: The active site of voltage-activated potassium channels is a transmembrane aqueous pore that permits ions to permeate the cell membrane in a rapid yet highly selective manner. A useful probe for the pore of potassium-selective channels is the organic ion tetraethylammonium (TEA), which binds with millimolar affinity to the intracellular opening of the pore and blocks potassium current. In the potassium channel encoded by the Drosophila Shaker gene, an amino acid residue that specifically affects the affinity for intracellular TEA has now been identified by site-directed mutagenesis. This residue is in the middle of a conserved stretch of 18 amino acids that separates two locations that are both near the external opening of the pore. These findings suggest that this conserved region is intimately involved in the formation of the ion conduction pore of voltage-activated potassium channels. Further, a stretch of only eight amino acid residues must traverse 80 percent of the transmembrane electric potential difference.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yellen, G -- Jurman, M E -- Abramson, T -- MacKinnon, R -- GM4399/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 22;251(4996):939-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2000494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Drosophila/genetics ; Genes ; Membrane Potentials ; Models, Structural ; Molecular Sequence Data ; *Mutagenesis, Site-Directed ; Potassium Channels/drug effects/genetics/*physiology ; Protein Conformation ; Tetraethylammonium ; Tetraethylammonium Compounds/*pharmacology
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    Deleted HTLV-I provirus in blood and cutaneous lesions of patients with mycosis fungoides (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-07-19
    Description: Mycosis fungoides, a rare form of cutaneous T cell leukemia/lymphoma, is suspected of having a viral etiology on the basis of certain similarities to adult T cell leukemia, which is associated with human T cell leukemia/lymphoma virus type I (HTLV-I) infection. Cell lines were established from peripheral blood mononuclear cells (PBMC) of an HTLV-I-seronegative patient with mycosis fungoides. DNA hybridization analysis revealed the presence of HTLV-I-related sequences with unusual restriction endonuclease sites. Sequence analysis of subcloned fragments demonstrated the presence of a monoclonally integrated provirus with a 5.5-kilobase deletion involving large regions of gag and env and all of pol. Additional evidence for the presence of deleted proviruses was found by polymerase chain reaction (PCR) amplification of DNA from cutaneous lesions of five other HTLV-I-seronegative patients. The findings suggest that HTLV-I infection may be involved in the etiology of at least certain cases of mycosis fungoides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, W W -- Liu, C R -- Schneewind, O -- Takahashi, H -- Kaplan, M H -- Roupe, G -- Vahlne, A -- CA51012-01A1/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Disease, North Shore University Hospital-Cornell University Medical College, Manhasset, NY 11030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857968" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosome Deletion ; DNA, Neoplasm/genetics/isolation & purification ; DNA, Viral/genetics/isolation & purification ; *Genes, Viral ; Human T-lymphotropic virus 1/genetics/*isolation & purification ; Humans ; Lymphocytes/*microbiology ; Molecular Sequence Data ; Mycosis Fungoides/blood/*microbiology ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Proviruses/genetics/*isolation & purification ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Skin/*microbiology ; Skin Neoplasms/blood/*microbiology
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    Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-05-10
    Description: The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pavletich, N P -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 10;252(5007):809-17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2028256" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallography ; DNA/*metabolism ; DNA-Binding Proteins/*chemistry/isolation & purification/physiology ; Early Growth Response Protein 1 ; *Immediate-Early Proteins ; Mice ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Transcription Factors/*chemistry/isolation & purification/physiology ; Zinc Fingers/*physiology
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    Structurally homologous ligand binding of integrin Mac-1 and viral glycoprotein C receptors (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-11-22
    Description: Three spatially distant surface loops were found to mediate the interaction of the coagulation protein factor X with the leukocyte integrin Mac-1. This interacting region, which by computational modeling defines a three-dimensional macromotif in the catalytic domain, was also recognized by glycoprotein C (gC), a factor X receptor expressed on herpes simplex virus (HSV)-infected endothelial cells. Peptidyl mimicry of each loop inhibited factor X binding to Mac-1 and gC, blocked monocyte generation of thrombin, and prevented monocyte adhesion to HSV-infected endothelium. These data link the ligand recognition of Mac-1 to established mechanisms of receptor-mediated vascular injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altieri, D C -- Etingin, O R -- Fair, D S -- Brunck, T K -- Geltosky, J E -- Hajjar, D P -- Edgington, T S -- HL 46408/HL/NHLBI NIH HHS/ -- P01 HL 16411/HL/NHLBI NIH HHS/ -- R01 HL 43773/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957171" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding, Competitive ; Cell Line ; Factor X/*metabolism/ultrastructure ; Humans ; In Vitro Techniques ; Ligands ; Macrophage-1 Antigen/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry/metabolism ; Protein Conformation ; Viral Envelope Proteins/*metabolism
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    Kinetic characterization of ribonuclease-resistant 2'-modified hammerhead ribozymes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-19
    Description: The incorporation of 2'-fluoro- and 2'-aminonucleotides into a hammerhead ribozyme was accomplished by automated chemical synthesis. The presence of 2'-fluorouridines, 2'-fluorocytidines, or 2'-aminouridines did not appreciably decrease catalytic efficiency. Incorporation of 2'-aminocytidines decreased ribozyme activity approximately by a factor of 20. The replacement of all adenosines with 2'-fluoroadenosines abolished catalysis in the presence of MgCl2 within the limits of detection, but some activity was retained in the presence of MnCl2. This effect on catalysis was localized to a specific group of adenines within the conserved single-stranded region of the ribozyme. The decrease in catalytic efficiency was caused by a decrease in the rate constant; the Michaelis constant was unaltered. The 2'-fluoro and 2'-amino modifications conferred resistance toward ribonuclease degradation. Ribozymes containing 2'-fluoro- or 2'-aminonucleotides at all uridine and cytidine positions were stabilized against degradation in rabbit serum by a factor of at least 10(3) compared to unmodified ribozyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pieken, W A -- Olsen, D B -- Benseler, F -- Aurup, H -- Eckstein, F -- New York, N.Y. -- Science. 1991 Jul 19;253(5017):314-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Experimentelle Medizin, Abteilung Chemie, Gottingen, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857967" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chlorides ; Kinetics ; Magnesium Chloride/pharmacology ; Manganese/pharmacology ; *Manganese Compounds ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Catalytic/chemical synthesis/*metabolism ; Ribonucleases/*metabolism ; Ribonucleotides ; Substrate Specificity
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  • 80
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    Identification of a gene located at chromosome 5q21 that is mutated in colorectal cancers (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-15
    Description: Recent studies have suggested the existence of a tumor suppressor gene located at chromosome region 5q21. DNA probes from this region were used to study a panel of sporadic colorectal carcinomas. One of these probes, cosmid 5.71, detected a somatically rearranged restriction fragment in the DNA from a single tumor. Further analysis of the 5.71 cosmid revealed two regions that were highly conserved in rodent DNA. These sequences were used to identify a gene, MCC (mutated in colorectal cancer), which encodes an 829-amino acid protein with a short region of similarity to the G protein-coupled m3 muscarinic acetylcholine receptor. The rearrangement in the tumor disrupted the coding region of the MCC gene. Moreover, two colorectal tumors were found with somatically acquired point mutations in MCC that resulted in amino acid substitutions. MCC is thus a candidate for the putative colorectal tumor suppressor gene located at 5q21. Further studies will be required to determine whether the gene is mutated in other sporadic tumors or in the germ line of patients with an inherited predisposition to colonic tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kinzler, K W -- Nilbert, M C -- Vogelstein, B -- Bryan, T M -- Levy, D B -- Smith, K J -- Preisinger, A C -- Hamilton, S R -- Hedge, P -- Markham, A -- 6M 07184/PHS HHS/ -- CA 06973/CA/NCI NIH HHS/ -- CA 09243/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1366-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Genetics Laboratory, Johns Hopkins Oncology Center, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1848370" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; *Chromosomes, Human, Pair 5 ; Colorectal Neoplasms/*genetics ; Exons ; GTP-Binding Proteins/metabolism ; Gene Expression ; *Genes, Tumor Suppressor ; Humans ; Molecular Sequence Data ; Mutation ; Oligonucleotides/chemistry ; Polymerase Chain Reaction ; Proteins/*genetics/metabolism ; Rats ; Sequence Homology, Nucleic Acid ; *Tumor Suppressor Proteins
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  • 81
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    Regulation of a segmentation stripe by overlapping activators and repressors in the Drosophila embryo (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: Gene expression stripes in Drosophila melanogaster embryos provide a model for how eukaryotic promoters are turned on and off in response to combinations of transcriptional regulators. Genetic studies suggested that even-skipped (eve) stripe 2 is controlled by three gap genes, hunchback (hb), Kruppel (Kr), and giant (gt), and by the maternal morphogen bicoid (bcd). A direct link is established between binding sites for these regulatory proteins in the stripe 2 promoter element and the expression of the stripe during early embryogenesis. The bcd and hb protein binding sites mediate activation, whereas neighboring gt and Kr protein sites repress expression and establish the stripe borders. The stripe 2 element has the properties of a genetic on-off switch.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stanojevic, D -- Small, S -- Levine, M -- GM 34431/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1385-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Fairchild Center, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1683715" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Deletion ; Drosophila melanogaster/embryology/*genetics ; Embryo, Nonmammalian/physiology ; Gene Expression Regulation ; *Genes ; Genes, Homeobox ; Molecular Sequence Data ; Morphogenesis ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Promoter Regions, Genetic
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  • 82
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    Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: A major action of the microbicidal system of human neutrophils is the formation of superoxide anion (O2-) by a multicomponent oxidase that transfers electrons from the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) to molecular oxygen. The mechanism of assembly and activation of the oxidase from its cytosolic and membrane-bound components is unknown, but may require the activity of a guanosine 5'-triphosphate (GTP)-binding component. A cytosolic GTP-binding protein (Gox) that regulates the NADPH oxidase of neutrophils was identified. Gox was purified and shown to augment the rate of O2- production in a cell-free oxidase activation system. Sequence analysis of peptide fragments from Gox identified it as Rac 2, a member of the Ras superfamily of GTP-binding proteins. Antibody to a peptide derived from the COOH-terminus of Rac 2 inhibited O2- generation in a concentration-dependent manner. These results suggest that Rac 2 is a regulatory component of the human neutrophil NADPH oxidase, and provide new insights into the mechanism by which this oxygen radical-generating system is regulated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knaus, U G -- Heyworth, P G -- Evans, T -- Curnutte, J T -- Bokoch, G M -- AI24838/AI/NIAID NIH HHS/ -- GM39434/GM/NIGMS NIH HHS/ -- HL48008/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1512-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1660188" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Free Radicals ; GTP-Binding Proteins/*physiology ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; NADH, NADPH Oxidoreductases/*metabolism ; NADPH Oxidase ; Neutrophils/*physiology ; *Respiratory Burst ; Superoxides/metabolism ; rac GTP-Binding Proteins
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  • 83
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    Suppression of the immune response by a soluble complement receptor of B lymphocytes (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: The CD19-CR2 complex of B lymphocytes contains proteins that participate in two host-defense systems, the immune and complement systems. The ligand for the subunit of the immune system, CD19, is not known, but the complement receptor subunit, CR2 (CD21), binds activation fragments of the C3 component of the complement system and may mediate immunopotentiating effects of complement. A recombinant, soluble CR2 was prepared by fusing the C3-binding region of the receptor to immunoglobulin G1 (IgG1). The (CR2)2-IgG1 chimera competed with cellular CR2 for C3 binding and suppressed the antibody response to a T cell-dependent antigen when administered to mice at the time of immunization. This inhibitory effect of (CR2)2-IgG1 demonstrates the B cell-activating function of the CD19-CR2 complex and suggests a new method for humoral immunosuppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hebell, T -- Ahearn, J M -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- GM-43803/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1718035" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antibody Formation ; Antigens, CD/*physiology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/chemistry/*physiology ; B-Lymphocytes/*physiology ; Base Sequence ; Binding, Competitive ; Cloning, Molecular ; Immunosuppression ; In Vitro Techniques ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Molecular Sequence Data ; Receptors, Complement/chemistry/*physiology ; Receptors, Complement 3d ; Recombinant Fusion Proteins ; Signal Transduction ; Solubility
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  • 84
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    Characterization of a cofactor that regulates dimerization of a mammalian homeodomain protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-20
    Description: Dimerization among transcription factors has become a recurrent theme in the regulation of eukaryotic gene expression. Hepatocyte nuclear factor-1 alpha (HNF-1 alpha) is a homeodomain-containing protein that functions as a dimer. A dimerization cofactor of HNF-1 alpha (DCoH) was identified that displayed a restricted tissue distribution and did not bind to DNA, but, rather, selectively stabilized HNF-1 alpha dimers. The formation of a stable tetrameric DCoH-HNF-1 alpha complex, which required the dimerization domain of HNF-1 alpha, did not change the DNA binding characteristics of HNF-1 alpha, but enhanced its transcriptional activity. However, DCoH did not confer transcriptional activation to the GAL4 DNA binding domain. These results indicate that DCoH regulates formation of transcriptionally active tetrameric complexes and may contribute to the developmental specificity of the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, D B -- Khavari, P A -- Conley, P B -- Graves, M K -- Hansen, L P -- Admon, A -- Crabtree, G R -- CA 09302/CA/NCI NIH HHS/ -- HD 07201/HD/NICHD NIH HHS/ -- HL 33942/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1762-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763325" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Nucleus/physiology ; Chromosome Deletion ; DNA-Binding Proteins/*metabolism ; Gene Library ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Humans ; *Hydro-Lyases ; Liver/physiology ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; *Nuclear Proteins ; Protein Biosynthesis ; RNA, Messenger/genetics ; Rabbits ; Rats ; Reticulocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 85
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    Identity elements for specific aminoacylation of yeast tRNA(Asp) by cognate aspartyl-tRNA synthetase (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-21
    Description: The nucleotides crucial for the specific aminoacylation of yeast tRNA(Asp) by its cognate synthetase have been identified. Steady-state aminoacylation kinetics of unmodified tRNA transcripts indicate that G34, U35, C36, and G73 are important determinants of tRNA(Asp) identity. Mutations at these positions result in a large decrease (19- to 530-fold) of the kinetic specificity constant (ratio of the catalytic rate constant kcat and the Michaelis constant Km) for aspartylation relative to wild-type tRNA(Asp). Mutation to G10-C25 within the D-stem reduced kcat/Km eightfold. This fifth mutation probably indirectly affects the presentation of the highly conserved G10 nucleotide to the synthetase. A yeast tRNA(Phe) was converted into an efficient substrate for aspartyl-tRNA synthetase through introduction of the five identity elements. The identity nucleotides are located in regions of tight interaction between tRNA and synthetase as shown in the crystal structure of the complex and suggest sites of base-specific contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Putz, J -- Puglisi, J D -- Florentz, C -- Giege, R -- New York, N.Y. -- Science. 1991 Jun 21;252(5013):1696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biochimie, Institut de Biologie Moleculaire et Cellulaire du CNRS, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2047878" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartate-tRNA Ligase/*metabolism ; Base Sequence ; Computer Graphics ; DNA Mutational Analysis ; Fungal Proteins/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; RNA, Fungal/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; RNA, Transfer, Asp/*metabolism ; Saccharomyces cerevisiae/*enzymology ; Structure-Activity Relationship ; Substrate Specificity ; *Transfer RNA Aminoacylation
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  • 86
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    Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-23
    Description: FK506 and rapamycin are related immunosuppressive compounds that block helper T cell activation by interfering with signal transduction. In vitro, both drugs bind and inhibit the FK506-binding protein (FKBP) proline rotamase. Saccharomyces cerevisiae cells treated with rapamycin irreversibly arrested in the G1 phase of the cell cycle. An FKBP-rapamycin complex is concluded to be the toxic agent because (i) strains that lack FKBP proline rotamase, encoded by FPR1, were viable and fully resistant to rapamycin and (ii) FK506 antagonized rapamycin toxicity in vivo. Mutations that conferred rapamycin resistance altered conserved residues in FKBP that are critical for drug binding. Two genes other than FPR1, named TOR1 and TOR2, that participate in rapamycin toxicity were identified. Nonallelic noncomplementation between FPR1, TOR1, and TOR2 alleles suggests that the products of these genes may interact as subunits of a protein complex. Such a complex may mediate nuclear entry of signals required for progression through the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heitman, J -- Movva, N R -- Hall, M N -- New York, N.Y. -- Science. 1991 Aug 23;253(5022):905-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1715094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anti-Bacterial Agents/metabolism/pharmacology ; Base Sequence ; Binding Sites ; Carrier Proteins/antagonists & inhibitors/chemistry/genetics/metabolism ; Cell Cycle/*drug effects ; Cyclosporins/pharmacology ; Drug Resistance, Microbial/genetics ; G1 Phase/drug effects ; Humans ; Immunosuppressive Agents/pharmacology ; Molecular Sequence Data ; Molecular Structure ; Mutation ; Polyenes/metabolism/*pharmacology ; Saccharomyces cerevisiae/*cytology/drug effects ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Sirolimus ; Tacrolimus ; Tacrolimus Binding Proteins
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  • 87
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    Site-specific cleavage of human chromosome 4 mediated by triple-helix formation (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: Direct physical isolation of specific DNA segments from the human genome is a necessary goal in human genetics. For testing whether triple-helix mediated enzymatic cleavage can liberate a specific segment of a human chromosome, the tip of human chromosome 4, which contains the entire candidate region for the Huntington's disease gene, was chosen as a target. A 16-base pyrimidine oligodeoxyribonucleotide was able to locate a 16-base pair purine target site within more than 10 gigabase pairs of genomic DNA and mediate the exact enzymatic cleavage at that site in more than 80 percent yield. The recognition motif is sufficiently generalizable that most cosmids should contain a sequence targetable by triple-helix formation. This method may facilitate the orchestrated dissection of human chromosomes from normal and affected individuals into megabase sized fragments and facilitate the isolation of candidate gene loci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strobel, S A -- Doucette-Stamm, L A -- Riba, L -- Housman, D E -- Dervan, P B -- HG00098/HG/NHGRI NIH HHS/ -- HG00329/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1639-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arnold and Mabel Beckman Laboratories of Chemical Synthesis, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1836279" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping/methods ; Chromosomes, Human, Pair 4/*ultrastructure ; DNA Damage ; Humans ; Huntington Disease/genetics ; Hydrogen Bonding ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry ; Restriction Mapping
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  • 88
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    Isolation of sequences that span the fragile X and identification of a fragile X-related CpG island (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 89
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    Light-directed, spatially addressable parallel chemical synthesis (1991)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1991-02-15
    Description: Solid-phase chemistry, photolabile protecting groups, and photolithography have been combined to achieve light-directed, spatially addressable parallel chemical synthesis to yield a highly diverse set of chemical products. Binary masking, one of many possible combinatorial synthesis strategies, yields 2n compounds in n chemical steps. An array of 1024 peptides was synthesized in ten steps, and its interaction with a monoclonal antibody was assayed by epifluorescence microscopy. High-density arrays formed by light-directed synthesis are potentially rich sources of chemical diversity for discovering new ligands that bind to biological receptors and for elucidating principles governing molecular interactions. The generality of this approach is illustrated by the light-directed synthesis of a dinucleotide. Spatially directed synthesis of complex compounds could also be used for microfabrication of devices.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fodor, S P -- Read, J L -- Pirrung, M C -- Stryer, L -- Lu, A T -- Solas, D -- New York, N.Y. -- Science. 1991 Feb 15;251(4995):767-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymax Research Institute, Palo Alto, CA 94304.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990438" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Fluorescent Antibody Technique ; Mathematics ; Molecular Sequence Data ; Oligonucleotides/chemical synthesis ; Oligopeptides/*chemical synthesis ; Photochemistry/*methods
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  • 90
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    Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-02
    Description: To determine the role of the BCR-ABL gene in the proliferation of blast cells of patients with chronic myelogenous leukemia, leukemia blast cells were exposed to synthetic 18-mer oligodeoxynucleotides complementary to two identified BCR-ABL junctions. Leukemia colony formation was suppressed, whereas granulocyte-macrophage colony formation from normal marrow progenitors was unaffected. When equal proportions of normal marrow progenitors and blast cells were mixed, exposed to the oligodeoxynucleotides, and assayed for residual colony formation, the majority of residual cells were normal. These findings demonstrate the requirement for a functional BCR-ABL gene in maintaining the leukemic phenotype and the feasibility of gene-targeted selective killing of neoplastic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szczylik, C -- Skorski, T -- Nicolaides, N C -- Manzella, L -- Malaguarnera, L -- Venturelli, D -- Gewirtz, A M -- Calabretta, B -- CA09644/CA/NCI NIH HHS/ -- CA36896/CA/NCI NIH HHS/ -- CA46782/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):562-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Temple University Medical School, Philadelphia, PA 19140.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857987" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blast Crisis/genetics/pathology ; Cell Division/drug effects ; Exons ; Fusion Proteins, bcr-abl/*genetics ; Gene Expression/drug effects ; Humans ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/genetics/*pathology ; Molecular Sequence Data ; Monocytes/cytology/drug effects ; Oligonucleotides, Antisense/*pharmacology ; *Oncogenes ; RNA, Messenger/analysis/genetics ; Tumor Cells, Cultured/cytology/drug effects ; Tumor Stem Cell Assay ; beta 2-Microglobulin/genetics
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  • 91
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    1990: annus mirabilis of potassium channels (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-24
    Description: Voltage-gated potassium channels make up a large molecular family of integral membrane proteins that are fundamentally involved in the generation of bioelectric signals such as nerve impulses. These proteins span the cell membrane, forming potassium-selective pores that are rapidly switched open or closed by changes in membrane voltage. After the cloning of the first potassium channel over 3 years ago, recombinant DNA manipulation of potassium channel genes is now leading to a molecular understanding of potassium channel behavior. During the past year, functional domains responsible for channel gating and potassium selectivity have been identified, and detailed structural pictures underlying these functions are beginning to emerge.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, C -- New York, N.Y. -- Science. 1991 May 24;252(5009):1092-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031183" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Amino Acid Sequence ; Animals ; Ion Channel Gating ; Models, Structural ; Molecular Sequence Data ; Potassium Channels/genetics/*physiology ; Protein Conformation
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  • 92
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    Regulation of interleukin-2 gene enhancer activity by the T cell accessory molecule CD28 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-18
    Description: The mechanism by which cell surface molecules regulate T cell production of lymphokines is poorly understood. Production of interleukin-2 (IL-2) can be regulated by signal transduction pathways distinct from those induced by the T cell antigen receptor. Stimulation of CD28, a molecule expressed on most human T cells, induced the formation of a protein complex that bound to a site on the IL-2 gene distinct from previously described binding sites and increased IL-2 enhancer activity fivefold. The CD28-responsive complex bound to the IL-2 gene between -164 and -154 base pairs from the transcription start site. The sequence of this element is similar to regions conserved in the 5' flanking regions of several other lymphokine genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fraser, J D -- Irving, B A -- Crabtree, G R -- Weiss, A -- GM39553/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 18;251(4991):313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1846244" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD28 ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; Cell Line ; DNA Mutational Analysis ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; In Vitro Techniques ; Interleukin-2/*genetics ; Molecular Sequence Data ; Oligonucleotides/chemistry ; *Regulatory Sequences, Nucleic Acid ; Signal Transduction ; T-Lymphocytes/*physiology ; Transcription, Genetic
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  • 93
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    The DNA binding arm of lambda repressor: critical contacts from a flexible region (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-11
    Description: Segments of protein that do not adopt a well-ordered conformation in the absence of DNA can still contribute to site-specific recognition of DNA. The first six residues (NH2-Ser1-Thr2-Lys3-Lys4-Lys5-Pro6-) of phage lambda repressor are flexible but are important for site-specific binding. Low-temperature x-ray crystallography and codondirected saturation mutagenesis were used to study the role of this segment. All of the functional sequences have the form [X]1-[X]2-[Lys or Arg]3-[Lys]4-[Lys or Arg]5-[X]6. A high-resolution (1.8 angstrom) crystal structure shows that Lys3 and Lys4 each make multiple hydrogen bonds with guanines and that Lys5 interacts with the phosphate backbone. The symmetry of the complex breaks down near the center of the site, and these results suggest a revision in the traditional alignment of the six lambda operator sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, N D -- Beamer, L J -- Goldberg, H R -- Berkower, C -- Pabo, C O -- GM31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 11;254(5029):267-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1833818" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage lambda/genetics ; DNA, Viral/*chemistry ; *DNA-Binding Proteins ; Genetic Variation ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Repressor Proteins/*chemistry ; Viral Proteins ; Viral Regulatory and Accessory Proteins/*chemistry ; X-Ray Diffraction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 94
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    Energy transfer between two peptides bound to one MHC class II molecule (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: The 17-amino acid peptide from chicken ovalbumin, Ova(323-339), was labeled at the amino terminus with fluorescein [FOva(323-339)] and near the carboxyl terminus with Texas Red [AcOva(323-338)KTR]. Fluorescence spectroscopy was carried out on resolved electrophoretic bands on nonreducing polyacrylamide gels derived from incubation mixtures containing major histocompatibility complex (MHC) class II molecules IAd and the FOva(323-339)- and AcOva(323-338)KTR-labeled peptides. Energy transfer between fluorescein and Texas Red was observed in the "floppy" alpha beta heterodimer band, but not in the "compact" alpha beta heterodimer band. Energy transfer was detected between the truncated peptides FOva(323-328)CONH2 and AcOva(331-338)KTR in both the compact alpha beta and floppy alpha beta gel bands. The energy-transfer data suggest that the two binding sites of floppy alpha beta arise from splitting apart a putative large, single binding site region in compact alpha beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tampe, R -- Clark, B R -- McConnell, H M -- 2R37 AI 13587-16/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):87-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1656526" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Energy Transfer ; Histocompatibility Antigens Class II/chemistry/*metabolism ; In Vitro Techniques ; Mice ; Molecular Sequence Data ; Ovalbumin/chemistry ; Peptides/chemistry/*metabolism ; Spectrometry, Fluorescence ; Structure-Activity Relationship
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  • 95
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    Type-specific regulation of adenylyl cyclase by G protein beta gamma subunits (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-06
    Description: Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)-bound alpha subunits and a complex of beta and gamma subunits after interaction with receptors. The GTP-alpha subunit complex activates appropriate effectors, such as adenylyl cyclase, retinal phosphodiesterase, phospholipase C, and ion channels. G protein beta gamma subunits have been found to have regulatory effects on certain types of adenylyl cyclase. In the presence of Gs alpha, the alpha subunit of the G protein that activates adenylyl cyclase, one form of adenylyl cyclase was inhibited by beta gamma, some forms were activated by beta gamma, and some forms were not affected by beta gamma. These interactions suggest mechanisms for communication between distinct signal-transducing pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, W J -- Gilman, A G -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 6;254(5037):1500-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962211" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/classification/genetics/*metabolism ; Animals ; Base Sequence ; Cattle ; Cloning, Molecular ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; Guanosine Triphosphate/physiology ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Rabbits ; Recombinant Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    RNA secondary structure repression of a muscle-specific exon in HeLa cell nuclear extracts (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: The chicken beta-tropomyosin pre-messenger RNA (pre-mRNA) is spliced in a tissue-specific manner to yield messenger RNA's (mRNA's) coding for different isoforms of this protein. Exons 6A and 6B are spliced in a mutually exclusive manner; exon 6B was included in skeletal muscle, whereas exon 6A was preferred in all other tissues. The distal portion of the intron upstream of exon 6B was shown to form stable double-stranded regions with part of the intron downstream of exon 6B and with sequences in exon 6B. This structure repressed splicing of exon 6B to exon 7 in a HeLa cell extract. Derepression of splicing occurred on disruption of this structure and repression followed when the structure was re-formed, even if the structure was formed between two different RNA molecules. Repression leads to inhibition of formation of spliceosomes. Disrupting either of the two double-stranded regions could lead to derepression, whereas re-forming the helices by suppressor mutations reestablished repression. These results support a simple model of tissue-specific splicing in this region of the pre-mRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clouet d'Orval, B -- d'Aubenton Carafa, Y -- Sirand-Pugnet, P -- Gallego, M -- Brody, E -- Marie, J -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1823-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Genetique Moleculaire, C.N.R.S., Universite de Paris VI, Gif-sur-Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2063195" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/*physiology ; Chickens ; *Exons ; HeLa Cells/physiology ; Humans ; Introns ; Molecular Sequence Data ; Muscles/*physiology ; Nucleic Acid Conformation ; RNA Precursors/chemistry/*genetics ; RNA Splicing ; Tropomyosin/*genetics
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  • 97
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    Prevention of apoptosis by a baculovirus gene during infection of insect cells (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: Programmed cell death is an active process of self destruction that is important in both the development and maintenance of multicellular animals. The molecular mechanisms controlling activation or suppression of programmed cell death are largely unknown. Apoptosis, a morphologically and biochemically defined type of programmed cell death commonly seen in vertebrates, was found to be initiated during baculovirus replication in insect cells. A specific viral gene product, p35, was identified as being responsible for blocking the apoptotic response. Identification of the function of this gene will allow further definition of the molecular pathways involved in the regulation of programmed cell death and may identify the role of apoptosis in invertebrate viral defense systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clem, R J -- Fechheimer, M -- Miller, L K -- AI23719/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1388-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Georgia, Athens 30602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1962198" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Baculoviridae/*genetics ; Base Sequence ; *Cell Death ; Cell Line ; *Genes, Viral ; Insects ; Molecular Sequence Data ; Mutagenesis, Insertional ; Open Reading Frames ; Phenotype ; Restriction Mapping
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Cloning of a serotonin transporter affected by antidepressants (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: A complementary DNA clone for a serotonin (5HT) transporter has been isolated from rat basophilic leukemia cells. The complementary DNA sequence predicts a 653-amino acid protein with 12 to 13 putative transmembrane domains. The 5HT transporter has significant homology to the gamma-aminobutyric acid, dopamine, and norepinephrine transporters. Uptake by CV-1 cells expressing the transporter complementary DNA resembles 5HT uptake by platelets and brain synaptosomes; it is sensitive to antidepressants, amphetamine derivatives, and cocaine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, B J -- Mezey, E -- Brownstein, M J -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):579-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Institute of Mental Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents/*pharmacology ; Base Sequence ; Carrier Proteins/drug effects/*genetics/metabolism ; Cell Line ; Cloning, Molecular ; Kinetics ; Leukemia, Basophilic, Acute ; Molecular Sequence Data ; Oligonucleotide Probes ; Rats ; Serotonin/*metabolism ; Transfection
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  • 99
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    A dominant negative form of transcription activator mTFE3 created by differential splicing (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-04
    Description: Transcription factor E3 (mTFE3) is a murine transcription activator that binds to the intronic enhancer of the immunoglobulin heavy chain gene. A naturally occurring splice product of mTFE3 messenger RNA (mRNA) lacked 105 nucleotides that encode an activation domain; both absolute and relative amounts of long and truncated mRNAs varied in different tissues. Cells were cotransfected with complementary DNAs that encoded the two mRNA forms in amounts that corresponded to the amounts of each mRNA found in different cells. Small changes in substoichiometric amounts of the truncated form of mRNA effected trans-dominant negative modulation of mTFE3 activity. These findings identify a function for differential splicing in the regulation of transcription factor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roman, C -- Cohn, L -- Calame, K -- R01CA38571/CA/NCI NIH HHS/ -- R01GM28361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 4;254(5028):94-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1840705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; DNA-Binding Proteins/*genetics ; *Gene Expression Regulation ; Mice ; Molecular Sequence Data ; RNA Splicing ; RNA, Messenger/genetics ; Regulatory Sequences, Nucleic Acid ; Structure-Activity Relationship ; Transcription Factors/*genetics ; *Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Specificity for aminoacylation of an RNA helix: an unpaired, exocyclic amino group in the minor groove (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-08-16
    Description: An acceptor stem G3.U70 base pair is a major determinant of the identity of an alanine transfer RNA. Hairpin helices and RNA duplexes consisting of complementary single strands are aminoacylated with alanine if they contain G3.U70. Chemical synthesis of RNA duplexes enabled the introduction of base analogs that tested the role of specific functional groups in the major and minor grooves of the RNA helix. The results of these experiments indicate that an unpaired guanine 2-amino group at a specific position in the minor groove of an RNA helix marks a molecule for aminoacylation with alanine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Musier-Forsyth, K -- Usman, N -- Scaringe, S -- Doudna, J -- Green, R -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- GM37641/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Aug 16;253(5021):784-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1876835" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alanine-tRNA Ligase/*metabolism ; Base Sequence ; In Vitro Techniques ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Oligonucleotides/chemistry ; RNA, Transfer, Ala/chemistry/*metabolism ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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