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  • Base Sequence  (74)
  • American Association for the Advancement of Science (AAAS)  (74)
  • American Institute of Physics (AIP)
  • 1995-1999
  • 1985-1989  (74)
  • 1987  (74)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (74)
  • American Institute of Physics (AIP)
Years
  • 1995-1999
  • 1985-1989  (74)
Year
  • 1
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    Sequence analysis on microcomputers (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-02
    Description: Overall, each of the program packages performed their tasks satisfactorily. For analyses where there was a well-defined answer, such as a search for a restriction site, there were few significant differences between the program sets. However, for tasks in which a degree of flexibility is desirable, such as homology or similarity determinations and database searches, DNASTAR consistently afforded the user more options in conducting the required analysis than did the other two packages. However, for laboratories where sequence analysis is not a major effort and the expense of a full sequence analysis workstation cannot be justified, MicroGenie and IBI-Pustell offer a satisfactory alternative. MicroGenie is a polished program system. Many may find that its user interface is more "user friendly" than the standard menu-driven interfaces. Its system of filing sequences under individual passwords facilitates use by more than one person. MicroGenie uses a hardware device for software protection that occupies a card slot in the computer on which it is used. Although I am sympathetic to the problem of software piracy, I feel that a less drastic solution is in order for a program likely to be sharing limited computer space with other software packages. The IBI-Pustell package performs the required analysis functions as accurately and quickly as MicroGenie but it lacks the clearness and ease of use. The menu system seems disjointed, and new or infrequent users often find themselves at apparent "dead-end menus" where the only clear alternative is to restart the entire program package. It is suggested from published accounts that the user interface is going to be upgraded and perhaps when that version is available, use of the system will be improved. The documentation accompanying each package was relatively clear as to how to run the programs, but all three packages assumed that the user was familiar with the computational techniques employed. MicroGenie and IBI-Pustell further complicated their documentation by mixing instructions for the version based on floppy disk operation with that for the hard disk version.(ABSTRACT TRUNCATED AT 400 WORDS)〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cannon, G C -- New York, N.Y. -- Science. 1987 Oct 2;238(4823):97-103.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659902" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Sequence Homology, Nucleic Acid ; *Software
    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 mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-06
    Description: Ribonuclease mitochondrial RNA processing, a site-specific endoribonuclease involved in primer RNA metabolism in mammalian mitochondria, requires an RNA component for its activity. On the basis of copurification and selective inactivation with complementary oligonucleotides, a 135-nucleotide RNA species, not encoded in the mitochondrial genome, is identified as the RNA moiety of the endoribonuclease. This finding implies transport of a nucleus-encoded RNA, essential for organelle DNA replication, to the mitochondrial matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, D D -- Clayton, D A -- GM-33088-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1178-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434997" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/*physiology ; Chemical Phenomena ; Chemistry ; Drug Resistance ; Endonucleases/isolation & purification/metabolism ; Enzyme Activation/drug effects ; *Genetic Code ; Humans ; Mammals/*genetics/metabolism ; Micrococcal Nuclease/pharmacology ; Mitochondria/*metabolism ; Oligonucleotides/pharmacology ; Organoids/physiology ; RNA/*biosynthesis/genetics/isolation & purification/physiology ; Ribonucleases/metabolism ; Subcellular Fractions/metabolism
    Print ISSN: 0036-8075
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  • 3
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    Generation of a hybrid sequence-specific single-stranded deoxyribonuclease (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-04
    Description: The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D R -- Schultz, P G -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1401-3.〈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/3685986" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Single-Stranded/metabolism ; Hydrolysis ; Micrococcal Nuclease/*genetics/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Staphylococcus aureus/enzymology/genetics ; Substrate Specificity
    Print ISSN: 0036-8075
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  • 4
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    Homeo boxes in the study of development (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-06-05
    Description: The body plan of Drosophila is determined to a large extent by homeotic genes, which specify the identity and spatial arrangement of the body segments. Homeotic genes share a characteristic DNA segment, the homeo box, which encodes a defined domain of the homeotic proteins. The homeo domain seems to mediate the binding to specific DNA sequences, whereby the homeotic proteins exert a gene regulatory function. By isolating the normal Antennapedia gene, fusing its protein-coding sequences to an inducible promoter, and reintroducing this fusion gene into the germline of flies, it has been possible to transform head structures into thoracic structures and to alter the body plan in a predicted way. Sequence homologies suggest that similar genetic mechanisms may control development in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gehring, W J -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1245-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2884726" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blastoderm/ultrastructure ; Drosophila/embryology/*genetics ; Embryonic and Fetal Development ; *Genes, Homeobox ; Mutation ; Ovum/ultrastructure
    Print ISSN: 0036-8075
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  • 5
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    Nucleic acid database management (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉George, D G -- Hunt, L T -- Barker, W C -- New York, N.Y. -- Science. 1987 Mar 27;235(4796):1562.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823903" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Database Management Systems ; *Information Systems ; *Nucleic Acids ; Software
    Print ISSN: 0036-8075
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  • 6
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    Alpha 2-antiplasmin Enschede: alanine insertion and abolition of plasmin inhibitory activity (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-09
    Description: An abnormal alpha 2-antiplasmin that is associated with a serious bleeding tendency has been found in a Dutch family and is referred to as alpha 2-antiplasmin Enschede. This abnormal alpha 2-antiplasmin is converted from an inhibitor of plasmin to a substrate. The molecular defect of alpha 2-antiplasmin Enschede, as revealed by sequencing of cloned genomic DNA fragments, consists of an alanine insertion near the active site region of the molecule. Substitution of this fragment into complementary DNA for a wild-type alpha 2-antiplasmin yields a translation product with physical and functional properties typical of the abnormal alpha 2-antiplasmin Enschede. The naturally occurring mutant may serve as a model for investigating the structures that determine the properties of an inhibitor versus those of a substrate in serine protease inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lijnen, H R -- Nelles, L -- Kluft, C -- Nieuwenhuis, H K -- Rijken, D C -- Collen, D -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):209-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Thrombosis and Vascular Research, University of Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2958938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/metabolism ; Fibrinolysin/*antagonists & inhibitors ; *Genes ; Humans ; Molecular Sequence Data ; *Mutation ; Protein Biosynthesis ; alpha-2-Antiplasmin/*genetics/metabolism
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  • 7
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    Functional analysis of a complementary DNA for the 50-kilodalton subunit of calmodulin kinase II (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-17
    Description: The calcium-calmodulin-dependent protein kinase II is a major component of brain synaptic junctions and has been proposed to play a variety of important roles in brain function. A complementary DNA representing a portion of the smaller 50-kilodalton subunit of the rat brain enzyme has been cloned and sequenced. The calmodulin-binding region has been identified and a synthetic analog prepared that binds calmodulin with high affinity in the presence of calcium. Like the 50-kilodalton kinase polypeptide, the concentration of the messenger RNA varies both neuroanatomically and during postnatal development of the brain. The broad tissue and species cross-reactivity of the complementary DNA suggests that the 50-kilodalton subunit found in rat brain is evolutionarily conserved and is the product of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanley, R M -- Means, A R -- Ono, T -- Kemp, B E -- Burgin, K E -- Waxham, N -- Kelly, P T -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):293-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037704" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Amino Acid Sequence ; Animals ; Base Sequence ; Biological Assay ; Brain/enzymology/growth & development ; Calcium-Calmodulin-Dependent Protein Kinases ; Cloning, Molecular ; DNA/genetics ; Protein Kinases/*genetics ; RNA, Messenger/genetics ; Rats ; Species Specificity
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  • 8
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    A novel putative tyrosine kinase receptor encoded by the eph gene (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-18
    Description: Growth factors and their receptors are involved in the regulation of cell proliferation and also play a key role in oncogenesis. In this study, a novel putative kinase receptor gene, termed eph, has been identified and characterized by molecular cloning. Its primary structure is similar to that of tyrosine kinase receptors thus far cloned and includes a cysteine-rich region in the extracellular domain. However, other features of the sequence distinguish the eph gene product from known receptors with tyrosine kinase activity. Thus the eph protein may define a new class of these molecules. The eph gene is overexpressed in several human carcinomas, suggesting that this gene may be involved in the neoplastic process of some tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirai, H -- Maru, Y -- Hagiwara, K -- Nishida, J -- Takaku, F -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1717-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825356" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Restriction Enzymes ; *Genes ; Humans ; Molecular Sequence Data ; Neoplasms/metabolism ; Oncogenes ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/*genetics ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 9
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    Conservation of the Duchenne muscular dystrophy gene in mice and humans (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-16
    Description: A portion of the Duchenne muscular dystrophy (DMD) gene transcript from human fetal skeletal muscle and mouse adult heart was sequenced, representing approximately 25 percent of the total, 14-kb DMD transcript. The nucleic acid and predicted amino acid sequences from the two species are nearly 90 percent homologous. The amino acid sequence that is predicted from this portion of the DMD gene indicates that the protein product might serve a structural role in muscle, but the abundance and tissue distribution of the messenger RNA suggests that the DMD protein is not nebulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E P -- Monaco, A P -- Feener, C C -- Kunkel, L M -- 2T 32 GM07753-07/GM/NIGMS NIH HHS/ -- HD18658/HD/NICHD NIH HHS/ -- R01 NS23740/NS/NINDS NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):347-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Genetics, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/*genetics ; DNA, Recombinant ; Exons ; Humans ; Male ; Mice ; Molecular Sequence Data ; Muscle Proteins/genetics ; Muscles/analysis/embryology ; Muscular Dystrophies/*genetics ; Muscular Dystrophy, Animal/*genetics ; Myocardium/analysis ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; X Chromosome
    Print ISSN: 0036-8075
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  • 10
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    Human cancer gene sequenced (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1323.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823884" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; Eye Neoplasms/*genetics ; *Genes ; Humans ; Retinoblastoma/*genetics
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  • 11
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    My close cousin the chimpanzee (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):273-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3116670" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; DNA/genetics ; Dental Enamel/anatomy & histology ; Gait ; Haplorhini/anatomy & histology/*genetics ; Humans ; Metacarpophalangeal Joint/anatomy & histology ; Molar ; Nucleic Acid Hybridization ; Pan troglodytes/anatomy & histology/*genetics ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
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  • 12
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    Politics of the genome (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1453.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823893" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosome Mapping ; *Genetics, Medical ; Humans ; Politics ; United States
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  • 13
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    Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-24
    Description: Neuronal cells express a pp60c-src variant that displays an altered electrophoretic mobility and a different V8 peptide pattern relative to pp60c-src expressed in tissues of non-neuronal origin. To determine whether the neuronal form of pp60c-src is encoded by a brain-specific messenger RNA, a mouse brain complementary DNA (cDNA) library was screened with a chicken c-src probe and a 3.8-kilobase c-src cDNA clone was isolated. This clone encodes a 60-kilodalton protein that differs from chicken or human pp60c-src primarily in having six extra amino acids (Arg-Lys-Val-Asp-Val-Arg) within the NH2-terminal 16 kilodaltons of the molecule. S1 nuclease protection analysis confirmed that brain c-src RNA contains an 18-nucleotide insertion at the position of the extra six amino acids. This insertion occurs at a position that corresponds to a splice junction in the chicken and human c-src genes. The isolated c-src cDNA clone encodes a protein that displays an identical V8 peptide pattern to that observed in pp60c-src isolated from tissues of neuronal origin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez, R -- Mathey-Prevot, B -- Bernards, A -- Baltimore, D -- P0I CA38497/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):411-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2440106" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/enzymology ; Chickens ; Cloning, Molecular ; DNA/metabolism ; DNA Restriction Enzymes ; DNA Transposable Elements ; Humans ; Isoenzymes/*genetics ; Mice ; Neurons/*enzymology ; Protein Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins pp60(c-src) ; Sequence Homology, Nucleic Acid ; Species Specificity
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  • 14
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    Sequence-specific cleavage of double helical DNA by triple helix formation (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-30
    Description: Homopyrimidine oligodeoxyribonucleotides with EDTA-Fe attached at a single position bind the corresponding homopyrimidine-homopurine tracts within large double-stranded DNA by triple helix formation and cleave at that site. Oligonucleotides with EDTA.Fe at the 5' end cause a sequence specific double strand break. The location and asymmetry of the cleavage pattern reveal that the homopyrimidine-EDTA probes bind in the major groove parallel to the homopurine strand of Watson-Crick double helical DNA. The sequence-specific recognition of double helical DNA by homopyrimidine probes is sensitive to single base mismatches. Homopyrimidine probes equipped with DNA cleaving moieties could be useful tools for mapping chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moser, H E -- Dervan, P B -- GM 35724/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):645-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3118463" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Dna ; Edetic Acid ; Ferrous Compounds ; Humans ; Hydrolysis ; Middle Aged ; Nucleic Acid Conformation ; *Oligodeoxyribonucleotides ; Plasmids ; Solvents
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  • 15
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    Metalloregulatory DNA-binding protein encoded by the merR gene: isolation and characterization (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-01-09
    Description: The MerR protein mediates the induction of the mercury resistance phenotype in bacteria; it has been isolated in order to study the effects of metal-ion induced changes in the metabolism of prokaryotic cells at the molecular level. After DNA sequences responsible for negative autoregulation were removed, the 16-kilodalton protein was overproduced and purified to more than 90 percent homogeneity by a salt extraction procedure that yields about 5 milligrams of protein per gram of cells. Complementation data, amino terminal analysis, gel filtration, and deoxyribonuclease I protection studies demonstrate that the purified merR gene product is a dimer under nondenaturing conditions and that it binds specifically to DNA, in the presence and absence of mercury, at a palindromic site which is directly between the -10 and -35 regions of the structural genes and adjacent to its own promoter. These initial results indicate that MerR is a DNA-binding metalloregulatory protein that plays a central role in this heavy metal responsive system and they delineate an operator site in the mer operon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Halloran, T -- Walsh, C -- AI07256/AI/NIAID NIH HHS/ -- GM20011/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 9;235(4785):211-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3798107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/genetics/*isolation & purification ; Base Sequence ; Chromatography, Gel ; DNA/metabolism ; DNA-Binding Proteins/genetics/*isolation & purification ; Macromolecular Substances ; *Mercury ; Operator Regions, Genetic ; R Factors/*genetics ; Transcription, Genetic
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  • 16
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    Expression and properties of two types of protein kinase C: alternative splicing from a single gene (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-29
    Description: Two complementary DNA's, encoding the complete sequences of 671 and 673 amino acids for subspecies of rat brain protein kinase C, were expressed in COS 7 cells. The complementary DNA sequence analysis predicted that the two enzymes are derived from different ways of splicing and differ from each other only in the short ranges of their carboxyl-terminal regions. Both enzymes showed typical characteristics of protein kinase C that responded to Ca2+, phospholipid, and diacylglycerol. The enzymes showed practically identical physical and kinetic properties and were indistinguishable from one of the several subspecies of protein kinase C that occurs in rat brain but not in untransfected COS 7 cells. Partial analysis of the genomic structure confirmed that these two subspecies of protein kinase C resulted indeed from alternative splicing of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ono, Y -- Kikkawa, U -- Ogita, K -- Fujii, T -- Kurokawa, T -- Asaoka, Y -- Sekiguchi, K -- Ase, K -- Igarashi, K -- Nishizuka, Y -- New York, N.Y. -- Science. 1987 May 29;236(4805):1116-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brain/enzymology ; Chromatography, High Pressure Liquid ; DNA/genetics ; Nucleic Acid Hybridization ; Protein Kinase C/*genetics/metabolism ; RNA Splicing ; Rabbits ; Rats
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  • 17
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    Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-08-14
    Description: On the basis of electrophysiological analysis of Shaker mutants, the Shaker locus of Drosophila melanogaster has been proposed to encode a structural component of a voltage-dependent potassium channel, the A channel. Unlike sodium channels, acetylcholine receptors, and calcium channels, K+ channels have not been purified biochemically. To facilitate biochemical studies of a K+ channel, genomic DNA from the Shaker locus has been cloned. Rearrangements in five Shaker mutants have been mapped to a 60-kilobase segment of the genome. Four complementary DNA clones have been analyzed. These clones indicate that the Shaker gene contains multiple exons distributed over at least 65 kilobases of genomic DNA in the region where the mutations mapped. Furthermore, the gene may produce several classes of alternatively spliced transcripts. Two of the complementary DNA clones have been sequenced and their sequences support the hypothesis that Shaker encodes a component of a K+ channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papazian, D M -- Schwarz, T L -- Tempel, B L -- Jan, Y N -- Jan, L Y -- NS15963/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):749-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2441470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; Drosophila melanogaster/*genetics ; Exons ; *Ion Channels ; Membrane Proteins/*genetics ; Mutation ; Nucleic Acid Hybridization ; Potassium/*metabolism ; RNA Splicing ; Transcription, Genetic ; Translocation, Genetic
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  • 18
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    The mitochondrial genotype can influence nuclear gene expression in yeast (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-01-30
    Description: Isochromosomal, respiratory-deficient yeast strains, such as a mit-, a hypersuppressive petite, and a petite lacking mitochondrial DNA, are phenotypically identical in spite of differences in their mitochondrial genomes. Subtractive hybridizations of complementary DNA's to polyadenylated RNA isolated from derepressed cultures of these strains reveal the presence of nuclear-encoded transcripts whose abundance varies not only between them and their respiratory-competent parent, but among the respiratory-deficient strains themselves. Transcripts of some nuclear-encoded mitochondrial proteins, like cytochrome c and the alpha and beta subunits of the mitochondrial adenosine triphosphatase, whose abundance is affected by glucose or heme, do not vary. In the absence of major metabolic variables, yeast cells seem to respond to the quality and quantity of mitochondrial DNA and modulate the levels of nuclear-encoded RNA's, perhaps as a means of intergenomic regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parikh, V S -- Morgan, M M -- Scott, R -- Clements, L S -- Butow, R A -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):576-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027892" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Nucleus/physiology ; Cytochrome c Group/genetics ; DNA, Fungal/genetics ; DNA, Mitochondrial/genetics ; Electron Transport Complex IV/genetics ; Gene Expression Regulation ; Genes, Fungal ; Genotype ; Mitochondria/*physiology ; Mutation ; RNA, Fungal/genetics ; RNA, Messenger/genetics ; RNA, Ribosomal/genetics ; Saccharomyces cerevisiae/*genetics
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  • 19
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    Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-06-05
    Description: Cell cycle-dependent histone genes are transcribed at a basal level throughout the cell cycle, with a three- to fivefold increase during early S phase. Protein-DNA interactions in the 5' promoter region of a cell cycle-regulated human H4 histone gene have been analyzed at single-nucleotide resolution in vivo. This region contains two sites, with four potential protein-binding domains, at which the DNA is protected from reaction with dimethyl sulfate in cells and from digestion with deoxyribonuclease I in nuclei. These protein-DNA interactions persist during all phases of the cell cycle and dissociate with 0.16 to 0.2M sodium chloride.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pauli, U -- Chrysogelos, S -- Stein, G -- Stein, J -- Nick, H -- GM32010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1308-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3035717" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Cycle ; Cell Line ; Dna ; DNA Restriction Enzymes ; Deoxyribonuclease I ; Gene Expression Regulation ; Histones/*genetics ; Humans ; Nucleic Acid Hybridization ; *Promoter Regions, Genetic ; Protein Binding ; Sulfuric Acid Esters
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  • 20
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    Molecular diversity of the human T-gamma constant region genes (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-08-28
    Description: The human T cell antigen-receptor gamma chain, which is expressed on the surface of a subpopulation of CD3+ T lymphocytes, exhibits size polymorphism and varies in its ability to form disulfide bonds with a second polypeptide. Analysis of both genomic and complementary DNA clones encoding the human gamma polypeptide shows differences in lengths of the coding portions of the two constant region genes, C gamma 1 and C gamma 2. A single second-exon segment is always present in the C gamma 1 gene. C gamma 2 alleles containing either duplicated or triplicated second-exon segments are present in the normal human population and are expressed as messenger RNAs. Furthermore, a cysteine residue, encoded by the second exon of C gamma 1 and probably involved in interchain disulfide bridging, is absent in all C gamma 2 second-exon segments. These differences between C gamma 1 and the two alleles of C gamma 2 may explain the variability in molecular weight and disulfide bonding of gamma molecules expressed in different cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelicci, P G -- Subar, M -- Weiss, A -- Dalla-Favera, R -- Littman, D R -- CA 09454/CA/NCI NIH HHS/ -- CA 37165/CA/NCI NIH HHS/ -- CA 37295/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 28;237(4818):1051-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3112943" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; Genes, MHC Class II ; Humans ; Immunoglobulin Constant Regions/*genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin gamma-Chains/*genetics ; Immunoglobulins/*genetics ; Polymorphism, Genetic ; Receptors, Antigen, T-Cell/*genetics
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  • 21
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    Primary structure and biochemical properties of an M2 muscarinic receptor (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-05-01
    Description: A partial amino acid sequence obtained for porcine atrial muscarinic acetylcholine receptor was used to isolate complementary DNA clones containing the complete receptor coding region. The deduced 466-amino acid polypeptide exhibits extensive structural and sequence homology with other receptors coupled to guanine nucleotide binding (G) proteins (for example, the beta-adrenergic receptor and rhodopsins); this similarity predicts a structure of seven membrane-spanning regions distinguished by the disposition of a large cytoplasmic domain. Stable transfection of the Chinese hamster ovary cell line with the atrial receptor complementary DNA leads to the binding of muscarinic antagonists in these cells with affinities characteristic of the M2 receptor subtype. The atrial muscarinic receptor is encoded by a unique gene consisting of a single coding exon and multiple, alternatively spliced 5' noncoding regions. The atrial receptor is distinct from the cerebral muscarinic receptor gene product, sharing only 38% overall amino acid homology and possessing a completely nonhomologous large cytoplasmic domain, suggesting a role for the latter region in differential effector coupling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peralta, E G -- Winslow, J W -- Peterson, G L -- Smith, D H -- Ashkenazi, A -- Ramachandran, J -- Schimerlik, M I -- Capon, D J -- CA16417/CA/NCI NIH HHS/ -- HL23632/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 May 1;236(4801):600-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107123" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA/genetics ; Exons ; GTP-Binding Proteins/metabolism ; Heart Atria/analysis ; Immunosorbent Techniques ; Membrane Proteins ; Molecular Weight ; Nucleic Acid Hybridization ; Peptide Fragments/metabolism ; Quinuclidinyl Benzilate/metabolism ; Receptors, Muscarinic/*genetics/metabolism ; Sequence Homology, Nucleic Acid ; Swine ; Transfection
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  • 22
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    Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-04-03
    Description: The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein with in vitro immunosuppressive properties, was determined through isolation and characterization of complementary DNA and genomic clones. The amino acid sequence encoded by one of the exons of the uromodulin gene has homology to the low-density-lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided that uromodulin is identical to the previously characterized Tamm-Horsfall glycoprotein, the most abundant protein in normal human urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennica, D -- Kohr, W J -- Kuang, W J -- Glaister, D -- Aggarwal, B B -- Chen, E Y -- Goeddel, D V -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):83-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3453112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Base Sequence ; Chemistry, Physical ; Cloning, Molecular ; Cysteine ; DNA/genetics ; Gene Expression Regulation ; Genes ; Glycoproteins/*genetics ; Humans ; Mucoproteins/*analysis/*genetics ; Peptide Fragments/analysis ; Physicochemical Phenomena ; RNA, Messenger/genetics ; Uromodulin
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    Helix geometry, hydration, and G.A mismatch in a B-DNA decamer (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-10-23
    Description: The DNA double helix is not a regular, featureless barberpole molecule. Different base sequences have their own special signature, in the way that they influence groove width, helical twist, bending, and mechanical rigidity or resistance to bending. These special features probably help other molecules such as repressors to read and recognize one base sequence in preference to another. Single crystal x-ray structure analysis is beginning to show us the various structures possible in the B-DNA family. The DNA decamer C-C-A-A-G-A-T-T-G-G appears to be a better model for mixed-sequence B-DNA than was the earlier C-G-C-G-A-A-T-T-C-G-C-G, which is more akin to regions of poly(dA).poly(dT). The G.A mismatch base pairs at the center of the decamer are in the anti-anti conformation about their bonds from base to sugar, in agreement with nuclear magnetic resonance evidence on this and other sequences, and in contrast to the anti-syn geometry reported for G.A pairs in C-G-C-G-A-A-T-T-A-G-C-G. The ordered spine of hydration seen earlier in the narrow-grooved dodecamer has its counterpart, in this wide-grooved decamer, in two strings of water molecules lining the walls of the minor groove, bridging from purine N3 or pyrimidine O2, to the following sugar O4'. The same strings of hydration are present in the phosphorothioate analog of G-C-G-C-G-C. Unlike the spine, which is broken up by the intrusion of amine groups at guanines, these water strings are found in general, mixed-sequence DNA because they can pass by unimpeded to either side of a guanine N2 amine. The spine and strings are perceived as two extremes of a general pattern of hydration of the minor groove, which probably is the dominant factor in making B-DNA the preferred form at high hydration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prive, G G -- Heinemann, U -- Chandrasegaran, S -- Kan, L S -- Kopka, M L -- Dickerson, R E -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):498-504.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3310237" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Crystallization ; *Dna ; *Nucleic Acid Conformation ; *Oligodeoxyribonucleotides ; Phosphates ; Water
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  • 24
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    erg, a human ets-related gene on chromosome 21: alternative splicing, polyadenylation, and translation (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-08-07
    Description: The avian acute leukemia virus E26 induces a mixed erythroid-myeloid leukemia in chickens and carries two distinct oncogenes, v-myb and v-ets. Recently, a novel gene named erg, closely related to the v-ets oncogene, was identified in human COLO 320 cells and the nucleotide sequence of its approximately 5.0-kilobase transcript, erg 1 was determined. In the present study, the nucleotide sequence of the alternatively spliced transcript, erg 2, was found to differ from erg 1 by a splicing event that causes a coding frameshift near the amino terminus, resulting in an additional 99-amino acid insertion at the amino-terminus. Expression of complementary DNAs for the two transcripts in vitro resulted in synthesis of polypeptides of approximately 41 and 52 kilodaltons, suggesting the use of alternative translation initiation codons in the case of erg proteins. The erg gene was localized by somatic cell genetic analysis to human chromosome 21. It is proposed that alternative sites of splicing and polyadenylation, together with alternative sites of translation initiation, allow the synthesis of two related polypeptides from a single erg gene transcriptional unit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rao, V N -- Papas, T S -- Reddy, E S -- New York, N.Y. -- Science. 1987 Aug 7;237(4815):635-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299708" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; Humans ; Oncogenes ; Plasmids ; Poly A/metabolism ; *Protein Biosynthesis ; Proto-Oncogene Proteins/biosynthesis ; *Proto-Oncogenes ; *RNA Splicing ; RNA, Messenger ; Sequence Homology, Nucleic Acid
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    Polypeptide sequences essential for RNA recognition by an enzyme (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-03-27
    Description: Many RNAs are complex, globular molecules formed from elements of secondary and tertiary structure analogous to those found in proteins. Little is known about recognition of RNAs by proteins. In the case of transfer RNAs (tRNAs), considerable evidence suggests that elements dispersed in both the one- and three-dimensional structure are important for recognition by aminoacyl tRNA synthetases. Fragments of alanine tRNA synthetase were created by in vitro manipulations of the cloned alaS gene and examined for their interaction with alanine-specific tRNA. Sequences essential for recognition were located near the middle of the polypeptide, juxtaposed to the carboxyl-terminal side of the domain for aminoacyl adenylate synthesis. The most essential part of the tRNA interaction strength and specificity was dependent on a sequence of fewer than 100 amino acids. Within this sequence, and in the context of the proper conformation, a segment of no more than 17 amino acids was responsible for 25% or more of the total synthetase-tRNA free energy of association. The results raise the possibility that an important part of specific RNA recognition by an aminoacyl tRNA synthetase involves a polypeptide segment that is short relative to the total size of the protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regan, L -- Bowie, J -- Schimmel, P -- GM23562/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 27;235(4796):1651-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2435005" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Alanine-tRNA Ligase/metabolism ; Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/*metabolism ; Base Sequence ; Cloning, Molecular ; Escherichia coli/enzymology ; RNA/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Structure-Activity Relationship ; Substrate Specificity ; Thermodynamics
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  • 26
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    D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-10-09
    Description: A D-alanine-containing peptide termed dermorphin, with potent opiate-like activity, has been isolated from skin of the frog Phyllomedusa sauvagei. Complementary DNA (cDNA) libraries were constructed from frog skin messenger RNA and screened with a mixture of oligonucleotides that contained the codons complementary to five amino acids of dermorphin. Clones were detected with inserts coding for different dermorphin precursors. The predicted amino acid sequences of these precursors contained homologous repeats of 35 amino acids that included one copy of the heptapeptide dermorphin. In these cloned cDNAs, the alanine codon GCG occurred at the position where D-alanine is present in the end product. This suggests the existence of a novel post-translational reaction for the conversion of an L-amino acid to its D-isomer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richter, K -- Egger, R -- Kreil, G -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, Austrian Academy of Sciences, Salzburg.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659910" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/*metabolism ; Amino Acid Sequence ; Animals ; Anura ; Base Sequence ; Cloning, Molecular ; DNA/analysis ; Molecular Sequence Data ; Oligopeptides/*genetics ; Opioid Peptides ; RNA, Messenger/genetics ; Skin/*metabolism ; Stereoisomerism
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  • 27
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    Human genome: questions of cost (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-09-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1411-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629248" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Costs and Cost Analysis ; *Dna ; Humans ; Nucleotide Mapping
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  • 28
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    Identification of a novel thyroid hormone receptor expressed in the mammalian central nervous system (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-09-25
    Description: A complementary DNA clone derived from rat brain messenger RNA has been isolated on the basis of homology to the human thyroid hormone receptor gene. Expression of this complementary DNA produces a high-affinity binding protein for thyroid hormones. Sequence analysis and the mapping of this gene to a distinct human genetic locus indicate the existence of multiple human thyroid hormone receptors. Messenger RNA from this gene is expressed in a tissue-specific fashion with highest levels in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C C -- Weinberger, C -- Lebo, R -- Evans, R M -- GM-266444-09/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1610-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; DNA/genetics ; DNA-Binding Proteins/*genetics ; Gene Expression Regulation ; Genes ; Humans ; RNA, Messenger/genetics ; Rats ; Receptors, Thyroid Hormone/*genetics/metabolism ; Tissue Distribution ; Triiodothyronine/metabolism
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  • 29
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    A sequence in M13 phage detects hypervariable minisatellites in human and animal DNA (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-02-06
    Description: The term "DNA fingerprint" has been used to describe the extensive restriction fragment length polymorphism associated with hypervariable minisatellites present in the human genome. Until now, it was necessary to hybridize Southern blots to specific probes cloned from human genomic DNA in order to obtain individual-specific restriction patterns. The present study describes the surprising finding that the insert-free, wild-type M13 bacteriophage detects hypervariable minisatellites in human and in animal DNA, provided no competitor DNA is used during hybridization. The effective sequence in M13 was traced to two clusters of 15-base pair repeats within the protein III gene of the bacteriophage. This unexpected use of M13 renders the DNA fingerprinting technology more readily available to molecular biology laboratories.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vassart, G -- Georges, M -- Monsieur, R -- Brocas, H -- Lequarre, A S -- Christophe, D -- New York, N.Y. -- Science. 1987 Feb 6;235(4789):683-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2880398" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Coliphages/*genetics ; *DNA, Satellite ; DNA, Viral/genetics ; Humans ; *Polymorphism, Genetic ; *Polymorphism, Restriction Fragment Length ; *Repetitive Sequences, Nucleic Acid
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  • 30
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    The molecular basis of the sparse fur mouse mutation (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-24
    Description: The ornithine transcarbamylase-deficient sparse fur mouse is an excellent model to study the most common human urea cycle disorder. The mutation has been well characterized by both biochemical and enzymological methods, but its exact nature has not been revealed. A single base substitution in the complementary DNA for ornithine transcarbamylase from the sparse fur mouse has been identified by means of a combination of two recently described techniques for rapid mutational analysis. This strategy is simpler than conventional complementary DNA library construction, screening, and sequencing, which has often been used to find a new mutation. The ornithine transcarbamylase gene in the sparse fur mouse contains a C to A transversion that alters a histidine residue to an asparagine residue at amino acid 117.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veres, G -- Gibbs, R A -- Scherer, S E -- Caskey, C T -- HD21452/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):415-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603027" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/analysis ; Disease Models, Animal ; *Genes ; Mice ; Mice, Mutant Strains ; *Mutation ; Ornithine Decarboxylase/deficiency/*genetics ; RNA, Messenger/genetics
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  • 31
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    Human CSF-1: molecular cloning and expression of 4-kb cDNA encoding the human urinary protein (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-20
    Description: A 4-kilobase complementary DNA (cDNA) encoding human macrophage-specific colony-stimulating factor (CSF-1) was isolated. When introduced into mammalian cells, this cDNA directs the expression of CSF-1 that is structurally and functionally indistinguishable from the natural human urinary CSF-1. Direct structural analysis of both the recombinant CSF-1 and the purified human urinary protein revealed that these species contain a sequence of at least 40 amino acids at their carboxyl termini which are not found in the coding region of a 1.6-kilobase CSF-1 cDNA that was previously described. These results demonstrate that the human CSF-1 gene can be expressed to yield at least two different messenger RNA species that encode distinct but related forms of CSF-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G G -- Temple, P A -- Leary, A C -- Witek-Giannotti, J S -- Yang, Y C -- Ciarletta, A B -- Chung, M -- Murtha, P -- Kriz, R -- Kaufman, R J -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1504-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3493529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Colony-Stimulating Factors/*genetics/urine ; DNA/genetics ; Gene Expression Regulation ; Humans ; Macrophages/physiology ; Molecular Weight ; Peptide Fragments ; Protein Processing, Post-Translational ; RNA, Messenger/genetics
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  • 32
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    Molecular cloning and expression of a human B-cell growth factor gene in Escherichia coli (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-20
    Description: A human B-cell growth factor (BCGF) (12 kilodaltons) supports the clonal proliferation of B lymphocytes. A clone was isolated that contained the proper structural sequence to encode biologically active, 12-kilodalton BCGF in Escherichia coli and to hybridize to a specific messenger RNA, identified by in vitro translation in Xenopus laevis oocytes. A relatively hydrophobic region of 18 amino acids was found at the amino terminal of the 124-amino acid-long polypeptide. The carboxyl terminal is composed of at least 32 amino acids that are derived from nucleotide sequences bearing significant homology to the Alu repeat family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Mehta, S -- Morgan, J -- Maizel, A -- 16672/PHS HHS/ -- CA38499/CA/NCI NIH HHS/ -- CA39798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1489-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3547651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; B-Lymphocytes/*physiology ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Escherichia coli ; Gene Expression Regulation ; Growth Substances/*genetics ; Interleukin-4 ; Lymphokines/*genetics ; Repetitive Sequences, Nucleic Acid ; Sequence Homology, Nucleic Acid
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    Splicing of messenger RNA precursors (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-02-13
    Description: A general mechanism for the splicing of nuclear messenger RNA precursors in eukaryotic cells has been widely accepted. This mechanism, which generates lariat RNAs possessing a branch site, seems related to the RNA-catalyzed reactions of self-splicing introns. The splicing of nuclear messenger RNA precursors involves the formation of a multicomponent complex, the spliceosome. This splicing body contains at least three different small nuclear ribonucleoprotein particles (snRNPs), U2, U5, and U4 + U6. A complex containing precursor RNA and the U2 snRNP particle is a likely intermediate in the formation of the spliceosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharp, P A -- CA14051/CA/NCI NIH HHS/ -- GM34277/GM/NIGMS NIH HHS/ -- P01-CA42063/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):766-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3544217" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Introns ; Mutation ; Nucleic Acid Precursors/*genetics ; Protein Biosynthesis ; RNA Precursors ; *RNA Splicing ; RNA, Catalytic ; RNA, Messenger/*genetics ; RNA, Ribosomal/genetics ; RNA, Small Nuclear/genetics ; Saccharomyces cerevisiae/genetics ; Tetrahymena/genetics
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    Saccharomyces cerevisiae has a U1-like small nuclear RNA with unexpected properties (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-09-18
    Description: Previous experiments indicated that only a small subset of the approximately equal to 24 small nuclear RNAs (snRNAs) in Saccharomyces cerevisiae have binding sites for the Sm antigen, a hallmark of metazoan small nuclear ribonucleoproteins (snRNPs) involved in pre-messenger RNA splicing. Antibodies from human serum to Sm proteins were used to show that four snRNAs (snR7, snR14, snR19, and snR20) can be immunoprecipitated from yeast extracts. Three of these four, snR7, snR14, and snR20, have been shown to be analogs of mammalian U5, U4, and U2, respectively. Several regions of significant homology to U1 (164 nucleotides) have now been found in cloned and sequenced snR19 (568 nucleotides). These include ten out of ten matches to the 5' end of U1, the site known to interact with the 5' splice site of mammalian introns. Surprisingly, the precise conservation of this sequence precludes perfect complementarity between snR19 and the invariant yeast 5' junction (GTATGT), which differs from the mammalian consensus at the fourth position (GTPuAGT).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siliciano, P G -- Jones, M H -- Guthrie, C -- GM21119/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1484-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3306922" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; Autoantigens/metabolism ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Humans ; Nucleic Acid Conformation ; RNA, Fungal/analysis ; RNA, Small Nuclear/*analysis ; *Ribonucleoproteins, Small Nuclear ; Saccharomyces cerevisiae/*genetics ; snRNP Core Proteins
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    Two mammalian genes transcribed from opposite strands of the same DNA locus (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-20
    Description: This report describes the characterization of a genomic locus in the rat that encodes overlapping genes occupying both strands of the same piece of DNA. One gene (strand) encodes gonadotropin-releasing hormone (GnRH). A second gene, SH, is transcribed from the other DNA strand to produce RNA of undefined function. The RNAs transcribed from each DNA strand are spliced and polyadenylated, and share significant exon domains. GnRH is expressed in the central nervous system while SH transcripts are present in the heart. Thus, the genome of a mammalian organism encodes two distinct genes by using both strands of the same DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adelman, J P -- Bond, C T -- Douglass, J -- Herbert, E -- AM-16879/AM/NIADDK NIH HHS/ -- AM-30155/AM/NIADDK NIH HHS/ -- DA-02736/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1514-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3547652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/*genetics ; Exons ; *Genes ; Gonadotropin-Releasing Hormone/*genetics ; Heart/physiology ; Hypothalamus/physiology ; Introns ; RNA Splicing ; RNA, Messenger/*genetics ; Rats ; Templates, Genetic ; Transcription, Genetic
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  • 36
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    Two pairs of recombination signals are sufficient to cause immunoglobulin V-(D)-J joining (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-11-20
    Description: The minimum sequence requirements for antigen receptor V-(D)-J joining were studied by constructing recombination-substrates containing synthetic recombination signals and introducing them into a recombination-competent pre-B cell line. Two sets of heptamer (CACTGTG) and nonamer (GGTTTTTGT) sequences were shown to be sufficient to cause the V-(D)-J joining, if the 12- and 23-base pair spacer rule is satisfied. A point mutation in the heptamer sequence, or a change in the combination of the two spacer lengths, drastically reduced the recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akira, S -- Okazaki, K -- Sakano, H -- AI-18790/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1134-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120312" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Inversion ; *Genes, Immunoglobulin ; Genetic Vectors ; Humans ; Immunoglobulin Variable Region/*genetics ; Immunoglobulin kappa-Chains/genetics ; Mice ; Receptors, Antigen, T-Cell/genetics ; *Recombination, Genetic ; Retroviridae/genetics ; Sequence Homology, Nucleic Acid ; Structure-Activity Relationship
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    Molecular analysis of a constitutional X-autosome translocation in a female with muscular dystrophy (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-09-25
    Description: The gene responsible for Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) maps to the X chromosome short arm, band Xp21. In a few females with DMD or BMD, the Xp21 region is disrupted by an X-autosome translocation. Accumulating evidence suggests that the exchange has physically disrupted the DMD/BMD locus to cause the disease. One affected female with a t(X;21)(p21;p12) translocation was studied in detail. The exchange points from both translocation chromosomes were cloned, restriction-mapped, and sequenced. The translocation is reciprocal, but not conservative. A small amount of DNA is missing from the translocated chromosomes; 71 to 72 base pairs from the X chromosome and 16 to 23 base pairs from the 28S ribosomal gene on chromosome 21.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bodrug, S E -- Ray, P N -- Gonzalez, I L -- Schmickel, R D -- Sylvester, J E -- Worton, R G -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1620-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629260" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; DNA, Ribosomal/genetics ; Female ; Humans ; Muscular Dystrophies/*genetics ; Pedigree ; RNA, Ribosomal/genetics ; *Translocation, Genetic ; *X Chromosome
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    Identification of a family of muscarinic acetylcholine receptor genes (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-31
    Description: Complementary DNAs for three different muscarinic acetylcholine receptors were isolated from a rat cerebral cortex library, and the cloned receptors were expressed in mammalian cells. Analysis of human and rat genomic clones indicates that there are at least four functional muscarinic receptor genes and that these genes lack introns in the coding sequence. This gene family provides a new basis for evaluating the diversity of muscarinic mechanisms in the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, T I -- Buckley, N J -- Young, A C -- Brann, M R -- New York, N.Y. -- Science. 1987 Jul 31;237(4814):527-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/metabolism ; Cloning, Molecular ; Codon ; Dna ; DNA Restriction Enzymes ; *Genes ; Genetic Code ; Humans ; Models, Molecular ; Nucleic Acid Hybridization ; Rats ; Receptors, Muscarinic/classification/*genetics ; Swine ; Transfection
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    Disease diagnosis by recombinant DNA methods (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-06-05
    Description: Recombinant DNA procedures have now been applied to the problem of the identification of molecular defects in man that account for heritable diseases, somatic mutations associated with neoplasia, and acquired infectious disease. Thus recombinant DNA technology has rapidly expanded our ability to diagnose disease. Substantial advances in the simplification of procedures for diagnostic purposes have been made, and the informed physician has gained in diagnostic accuracy as a consequence of these developments. The wide application of recombinant DNA diagnostics will depend on simplicity, speed of results, and cost containment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caskey, C T -- DK31428/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1223-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3296189" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; *DNA, Recombinant ; Forensic Medicine/methods ; Genetic Diseases, Inborn/*diagnosis ; Genetic Linkage ; *Genetic Techniques ; Humans ; Infection/*diagnosis ; Mutation ; Neoplasms/*genetics
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    Apolipoprotein B-48 is the product of a messenger RNA with an organ-specific in-frame stop codon (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-16
    Description: The primary structure of human apolipoprotein (apo) B-48 has been deduced and shown by a combination of DNA excess hybridization, sequencing of tryptic peptides, cloned complementary DNAs, and intestinal messenger RNAs (mRNAs) to be the product of an intestinal mRNA with an in-frame UAA stop codon resulting from a C to U change in the codon CAA encoding Gln2153 in apoB-100 mRNA. The carboxyl-terminal Ile2152 of apoB-48 purified from chylous ascites fluid has apparently been cleaved from the initial translation product, leaving Met2151 as the new carboxyl-terminus. These data indicate that approximately 85% of the intestinal mRNAs terminate within approximately 0.1 to 1.0 kilobase downstream from the stop codon. The other approximately 15% have lengths similar to hepatic apoB-100 mRNA even though they have the same in-frame stop codon. The organ-specific introduction of a stop codon to a mRNA appears unprecedented and might have implications for cryptic polyadenylation signal recognition and RNA processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, S H -- Habib, G -- Yang, C Y -- Gu, Z W -- Lee, B R -- Weng, S A -- Silberman, S R -- Cai, S J -- Deslypere, J P -- Rosseneu, M -- GM-30998/GM/NIGMS NIH HHS/ -- HL-27341/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659919" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein B-48 ; Apolipoproteins B/*genetics/metabolism ; Base Sequence ; Chylous Ascites/metabolism ; *Codon ; DNA/genetics ; Humans ; Intestine, Small/analysis ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Peptide Fragments ; *RNA, Messenger/analysis/*genetics ; Trypsin/metabolism
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    Reading frame selection and transfer RNA anticodon loop stacking (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-12-11
    Description: Messenger RNA's are translated in successive three-nucleotide steps (a reading frame), therefore decoding must proceed in only one of three possible frames. A molecular model for correct propagation of the frame is presented based on (i) the measured translational properties of transfer RNA's (tRNA's) that contain an extra nucleotide in the anticodon loop and (ii) a straightforward concept about anticodon loop structure. The model explains the high accuracy of reading frame maintenance by normal tRNA's, as well as activities of all characterized frameshift suppressor tRNA's that have altered anticodon loops.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curran, J F -- Yarus, M -- GM30881/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1545-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685992" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/*genetics ; Base Sequence ; Codon ; Mutation ; Nucleic Acid Conformation ; Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Transfer/*genetics
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    Identification of the iron-responsive element for the translational regulation of human ferritin mRNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-11
    Description: Regulated translation of messenger RNA offers an important mechanism for the control of gene expression. The biosynthesis of the intracellular iron storage protein ferritin is translationally regulated by iron. A cis-acting element that is both necessary and sufficient for this translational regulation is present within the 5' nontranslated leader region of the human ferritin H-chain messenger RNA. In this report the iron-responsive element (IRE) was identified by deletional analysis. Moreover, a synthetic oligodeoxynucleotide was shown to be able to transfer iron regulation to a construct that would otherwise not be able to respond to iron. The IRE has been highly conserved and predates the evolutionary segregation between amphibians, birds, and man. The IRE may prove to be useful for the design of translationally regulated expression systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- Caughman, S W -- Rouault, T A -- Barriocanal, J G -- Dancis, A -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1570-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685996" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; Ferritins/*genetics ; *Gene Expression Regulation ; Genes ; Humans ; Iron/*pharmacology ; Molecular Sequence Data ; Plasmids ; Promoter Regions, Genetic/*drug effects ; *Protein Biosynthesis ; RNA, Messenger/*genetics
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    Cloning of complementary DNA for GAP-43, a neuronal growth-related protein (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-05-01
    Description: GAP-43 is one of a small subset of cellular proteins selectively transported by a neuron to its terminals. Its enrichment in growth cones and its increased levels in developing or regenerating neurons suggest that it has an important role in neurite growth. A complementary DNA (cDNA) that encodes rat GAP-43 has been isolated to study its structural characteristics and regulation. The predicted molecular size is 24 kilodaltons, although its migration in SDS-polyacrylamide gels is anomalously retarded. Expression of GAP-43 is limited to the nervous system, where its levels are highest during periods of neurite outgrowth. Nerve growth factor or adenosine 3',5'-monophosphate induction of neurites from PC12 cells is accompanied by increased GAP-43 expression. GAP-43 RNA is easily detectable, although at diminished levels, in the adult rat nervous system. This regulation of GAP-43 is concordant with a role in growth-related processes of the neuron, processes that may continue in the mature animal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karns, L R -- Ng, S C -- Freeman, J A -- Fishman, M C -- New York, N.Y. -- Science. 1987 May 1;236(4801):597-600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2437653" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/physiology ; Bacteriophage lambda/genetics ; Base Sequence ; *Cloning, Molecular ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; GAP-43 Protein ; Ganglia, Spinal/analysis/embryology ; Gene Expression Regulation ; Growth Substances/genetics ; Immunosorbent Techniques ; Membrane Proteins/*genetics ; Nerve Tissue Proteins/*genetics ; Protein Biosynthesis ; RNA/genetics ; RNA, Messenger/genetics ; Rats
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    Structurally divergent human T cell receptor gamma proteins encoded by distinct C gamma genes (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-03
    Description: The human T cell receptor (TCR) gamma polypeptide occurs in structurally distinct forms on certain peripheral blood T lymphocytes. Complementary DNA clones representing the transcripts of functionally rearranged TCR gamma genes in these cells have been analyzed. The expression of a disulfide-linked and a nondisulfide-linked form of TCR gamma correlates with the use of the C gamma 1 and C gamma 2 constant-region gene segments, respectively. Variability in TCR gamma polypeptide size and disulfide linkage is determined by the number of copies and the sequence of a repeated segment of the constant region. Thus C gamma 1 and C gamma 2 are used to generate structurally distinct, yet functional, T3-associated receptor complexes on peripheral blood lymphocytes. Tryptic peptide mapping suggests that the T3-associated TCR gamma and delta peptides in the nondisulfide-linked form are distinct.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krangel, M S -- Band, H -- Hata, S -- McLean, J -- Brenner, M B -- 1-KO1-AM01598/AM/NIADDK NIH HHS/ -- 1-RO1-GM38308/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 3;237(4810):64-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2955517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Exons ; Genes ; Humans ; Peptide Fragments/*genetics ; Receptors, Antigen, T-Cell/*genetics ; Receptors, Antigen, T-Cell, gamma-delta ; Repetitive Sequences, Nucleic Acid ; T-Lymphocytes/*physiology
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    Detection of minimal residual cells carrying the t(14;18) by DNA sequence amplification (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-10
    Description: By means of the polymerase chain reaction (PCR) technique, DNA sequences were amplified that flank the crossover sites of a characteristic chromosomal translocation for follicular lymphomas, t(14;18)(q32;q21). This technique permitted the detection of cells carrying the t(14;18) hybrid DNA sequences at a dilution of 1:100,000. The remission marrow and blood samples of a patient with follicular lymphoma and the t(14;18) failed to show any abnormality by morphological examination and conventional Southern blot analysis. However, the t(14;18) hybrid DNA sequences were detected by the PCR technique. Thus, this technique is a highly sensitive tool to detect minimal residual cells carrying the t(14;18) and has the potential to identify a subpopulation of patients with subclinical disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, M S -- Chang, K S -- Cabanillas, F -- Freireich, E J -- Trujillo, J M -- Stass, S A -- New York, N.Y. -- Science. 1987 Jul 10;237(4811):175-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3110950" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosomes, Human, Pair 14/*ultrastructure ; Chromosomes, Human, Pair 18/*ultrastructure ; DNA, Neoplasm/*analysis ; Gene Amplification ; Genetic Markers ; Humans ; Immunoglobulin J-Chains/genetics ; Lymphadenitis/genetics ; Lymphoma, Follicular/*genetics ; Neoplasm Recurrence, Local/diagnosis ; Oligodeoxyribonucleotides/chemical synthesis/genetics ; *Translocation, Genetic
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  • 46
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    Isolation of an olfactory cDNA: similarity to retinol-binding protein suggests a role in olfaction (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-02-27
    Description: Molecular cloning techniques were used to isolate and characterize a protein possibly involved in the signal transducing system in olfactory tissue of the frog Rana pipiens. A complementary DNA library was constructed with messenger RNA obtained from frog olfactory neuroepithelium. A 700-base pair complementary DNA clone encoding a protein with a molecular weight of 20,300 was identified by differential hybridization analysis with polyadenylated RNA from olfactory epithelium and nonsensory respiratory epithelium. The messenger RNA corresponding to this clone was abundant in the cells of Bowman's glands in olfactory tissue but not in respiratory epithelium nor in several other tissues. The predicted sequence of this protein is homologous to members of a family of proteins that bind and transport small molecules in serum, suggesting that this protein may also bind and transport odorants in the mucus secreted by Bowman's glands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K H -- Wells, R G -- Reed, R R -- 5 PO1 CA16519/CA/NCI NIH HHS/ -- 5 T32 GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 27;235(4792):1053-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3493528" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; Epithelium/analysis ; Molecular Weight ; Mucus/metabolism ; Nucleic Acid Hybridization ; Odors ; Olfactory Mucosa/*analysis/physiology ; RNA, Messenger/genetics/metabolism ; Rana pipiens ; Respiratory System/analysis ; Retinol-Binding Proteins/genetics/*physiology
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  • 47
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    Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-08-14
    Description: Potassium currents are crucial for the repolarization of electrically excitable membranes, a role that makes potassium channels a target for physiological modifications that alter synaptic efficacy. The Shaker locus of Drosophila is thought to encode a K+ channel. The sequence of two complementary DNA clones from the Shaker locus is reported here. The sequence predicts an integral membrane protein of 70,200 daltons containing seven potential membrane-spanning sequences. In addition, the predicted protein is homologous to the vertebrate sodium channel in a region previously proposed to be involved in the voltage-dependent activation of the Na+ channel. These results support the hypothesis that Shaker encodes a structural component of a voltage-dependent K+ channel and suggest a conserved mechanism for voltage activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tempel, B L -- Papazian, D M -- Schwarz, T L -- Jan, Y N -- Jan, L Y -- NS15963/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):770-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2441471" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Codon ; DNA/*genetics ; Drosophila melanogaster/*genetics ; Electrophorus/genetics ; Genes ; *Ion Channels ; Membrane Proteins/*genetics ; Mutation ; Potassium/*metabolism ; Sodium/metabolism
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    Early restriction of the human antibody repertoire (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-11-06
    Description: Diversification of the antibody repertoire in mammals results from a series of apparently random somatically propagated gene rearrangement and mutational events. Nevertheless, it is well known that the adult repertoire of antibody specificities is acquired in a developmentally programmed fashion. As previously shown, rearrangement of the gene segments encoding the heavy-chain variable regions (VH) of mouse antibodies is also developmentally ordered: the number of VH gene segments rearranged in B lymphocytes of fetal mice is small but increased progressively after birth. In this report, human fetal B-lineage cells were also shown to rearrange a highly restricted set of VH gene segments. In a sample of heavy-chain transcripts from a 130-day human fetus the most frequently expressed human VH element proved to be closely related to the VH element most frequently expressed in murine fetal B-lineage cells. These observations are important in understanding the development of immunocompetence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroeder, H W Jr -- Hillson, J L -- Perlmutter, R M -- AI07470/AI/NIAID NIH HHS/ -- GM07454/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):791-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3118465" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology ; Base Sequence ; Fetus ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Variable Region/genetics ; Mice ; Molecular Sequence Data ; Mutation ; Sequence Homology, Nucleic Acid
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    Purification and properties of Drosophila heat shock activator protein (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-27
    Description: Drosophila heat shock activator protein, a rare transacting factor which is induced upon heat shock to bind specifically to the heat shock regulatory sequence in vivo, has been purified from shocked cells to more than 95 percent homogeneity by sequence-specific duplex oligonucleotide affinity chromatography. The purified protein has a relative molecular mass of 110 kilodaltons, binds to the regulatory sequence with great affinity and specificity, and strongly stimulates transcription of the Drosophila hsp70 gene. Studies with this regulatory protein should lead to an understanding of the biochemical pathway underlying the heat shock phenomenon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, C -- Wilson, S -- Walker, B -- Dawid, I -- Paisley, T -- Zimarino, V -- Ueda, H -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1247-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685975" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Drosophila/*genetics ; *Genes ; *Genes, Regulator ; Heat-Shock Proteins/*genetics ; Kinetics ; Molecular Weight
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    Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-07-17
    Description: Low-stringency hybridization with human glucocorticoid receptor (hGR) complementary DNA was used to isolate a new gene encoding a predicted 107-kilodalton polypeptide. Expression studies demonstrate its ability to bind aldosterone with high affinity and to activate gene transcription in response to aldosterone, thus establishing its identity as the human mineralocorticoid receptor (hMR). This molecule also shows high affinity for glucocorticoids and stimulates a glucocorticoid-responsive promoter. Together the hMR and hGR provide unexpected functional diversity in which hormone-binding properties, target gene interactions, and patterns of tissue-specific expression may be used in a combinatorial fashion to achieve complex physiologic control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arriza, J L -- Weinberger, C -- Cerelli, G -- Glaser, T M -- Handelin, B L -- Housman, D E -- Evans, R M -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):268-75.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037703" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosomes, Human, Pair 4 ; Cloning, Molecular ; DNA/genetics ; DNA-Binding Proteins/genetics ; Humans ; Rats ; Receptors, Glucocorticoid/*genetics ; Receptors, Mineralocorticoid ; Receptors, Steroid/*genetics ; Sequence Homology, Nucleic Acid ; Tissue Distribution ; Transcription Factors/*genetics ; Transcription, Genetic
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    Neural cell adhesion molecule: structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-15
    Description: The neural cell adhesion molecule, N-CAM, appears on early embryonic cells and is important in the formation of cell collectives and their boundaries at sites of morphogenesis. Later in development it is found on various differentiated tissues and is a major CAM mediating adhesion among neurons and between neurons and muscle. To provide a molecular basis for understanding N-CAM function, the complete amino acid sequences of the three major polypeptides of N-CAM and most of the noncoding sequences of their messenger RNA's were determined from the analysis of complementary DNA clones and were verified by amino acid sequences of selected CNBr fragments and proteolytic fragments. The extracellular region of each N-CAM polypeptide includes five contiguous segments that are homologous in sequence to each other and to members of the immunoglobulin superfamily, suggesting that interactions among immunoglobulin-like domains form the basis for N-CAM homophilic binding. Although different in their membrane-associated and cytoplasmic domains, the amino acid sequences of the three polypeptides appear to be identical throughout this extracellular region (682 amino acids) where the binding site is located. Variations in N-CAM activity thus do not occur by changes in the amino acid sequence that alter the specificity of binding. Instead, regulation is achieved by cell surface modulation events that alter N-CAM affinity, prevalence, mobility, and distribution on the surface. A major mechanism for modulation is alternative RNA splicing resulting in N-CAM's with different cytoplasmic domains that differentially interact with the cell membrane. Such regulatory mechanisms may link N-CAM binding function with other primary cellular processes during the embryonic development of pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B A -- Hemperly, J J -- Murray, B A -- Prediger, E A -- Brackenbury, R -- Edelman, G M -- AM-04256/AM/NIADDK NIH HHS/ -- HD-09635/HD/NICHD NIH HHS/ -- HD-16550/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 May 15;236(4803):799-806.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576199" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Surface/*genetics/immunology ; Base Sequence ; Cell Adhesion ; Cell Adhesion Molecules ; Cloning, Molecular ; DNA/metabolism ; Immunoglobulins ; Oligosaccharides/analysis ; Peptide Fragments/analysis ; *RNA Splicing ; Sequence Homology, Nucleic Acid
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    Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-02-13
    Description: Leader peptidase spans the Escherichia coli plasma membrane with its amino-terminal domain facing the cytoplasm and its carboxyl terminus facing the periplasm. It is made without a cleavable leader sequence. The three apolar domains near the amino terminus of the peptidase are candidates for internal "signal sequences" and they anchor the protein to the lipid bilayer. Oligonucleotide-directed deletion was used to show that only the second domain has an essential function in membrane assembly. While this second apolar domain is crucial for membrane assembly, its continued function when disrupted by arginine suggests that its apolar character per se is not its only important feature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dalbey, R E -- Wickner, W -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):783-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3544218" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/ultrastructure ; Chromosome Deletion ; Endopeptidases/genetics/*metabolism ; Escherichia coli/*enzymology/genetics ; Genes, Bacterial ; Lipid Bilayers ; Membrane Lipids/physiology ; *Membrane Proteins ; *Serine Endopeptidases
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    Structurally distinct, stage-specific ribosomes occur in Plasmodium (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-13
    Description: Two structurally distinct nuclear genes code for cytoplasmic small subunit ribosomal RNA's in the parasite Plasmodium berghei. Stable transcripts from one of the ribosomal RNA genes are found almost exclusively in those stages of the life cycle that develop in the mosquito. When the parasite infects the mammalian host, transcripts from the second gene become the predominant small subunit ribosomal RNA species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gunderson, J H -- Sogin, M L -- Wollett, G -- Hollingdale, M -- de la Cruz, V F -- Waters, A P -- McCutchan, T F -- GM 32964/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 13;238(4829):933-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672135" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Genes ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmodium/*genetics/growth & development ; RNA, Ribosomal/*genetics ; Ribosomes/*physiology ; Transcription, Genetic
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    Identification of putative human T cell receptor delta complementary DNA clones (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-30
    Description: A novel T cell receptor (TCR) subunit termed TCR delta, associated with TCR gamma and CD3 polypeptides, was recently found on a subpopulation of human T lymphocytes. T cell-specific complementary DNA clones present in a human TCR gamma delta T cell complementary DNA library were obtained and characterized in order to identify candidate clones encoding TCR delta. One cross-hybridizing group of clones detected transcripts that are expressed in lymphocytes bearing TCR gamma delta but not in other T lymphocytes and are encoded by genes that are rearranged in TCR gamma delta lymphocytes but deleted in other T lymphocytes. Their sequences indicate homology to the variable, joining, and constant elements of other TCR and immunoglobulin genes. These characteristics, as well as the immunochemical data presented in a companion paper, are strong evidence that the complementary DNA clones encode TCR delta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hata, S -- Brenner, M B -- Krangel, M S -- 1-K01-AM01598/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):678-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Virology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3499667" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Genes ; Humans ; Membrane Proteins/genetics ; Molecular Sequence Data ; RNA, Messenger/genetics ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*physiology
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    Efficient packaging of readthrough RNA in ALV: implications for oncogene transduction (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-05-15
    Description: Readthrough viral transcripts are present at relatively high levels in cells infected with avian leukosis virus. It has been proposed that they can function as intermediates in the transduction of proto-oncogenes by retroviruses. It is shown here, by the analysis of viruses containing a mutation in the AAUAAA polyadenylation signal, that readthrough RNAs have the requisite properties to function as transduction intermediates: readthrough RNAs were polyadenylated and packaged as efficiently as normal viral RNA, RNAs nearly 11.2 kilobases (3.5 kilobases larger than wild-type avian leukosis virus genomes) were present in virions of the mutant virus, and virus particles containing both readthrough and normal genomes were most likely infectious.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herman, S A -- Coffin, J M -- CA17659/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 May 15;236(4803):845-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3033828" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses/*genetics ; Base Sequence ; DNA Replication ; Fibroblasts ; *Genes, Viral ; *Oncogenes ; RNA, Viral/*genetics ; *Transduction, Genetic ; Turkeys ; Virion/genetics ; Virus Replication
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  • 56
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    Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-09-18
    Description: The protein portion of the immunosuppressive glycoprotein uromodulin is identical to the Tamm-Horsfall urinary glycoprotein and is synthesized in the kidney. Evidence that the glycoproteins are the same is based on amino acid sequence identity, immunologic cross-reactivity, and tissue localization to the thick ascending limb of Henle's loop. Nucleic acid sequencing of clones for uromodulin isolated from a complementary DNA bank from human kidney predicts a protein 639 amino acids in length, including a 24--amino acid leader sequence and a cysteine-rich mature protein with eight potential glycosylation sites. Uromodulin and preparations of Tamm-Horsfall glycoprotein bind to recombinant murine interleukin-1 (rIL-1) and human rIL-1 alpha, rIL-1 beta, and recombinant tumor necrosis factor (rTNF). Uromodulin isolated from urine of pregnant women by lectin adherence is more immunosuppressive than material isolated by the original salt-precipitation protocol of Tamm and Horsfall. Immunohistologic studies demonstrate that rIL-1 and rTNF bind to the same area of the human kidney that binds to antiserum specific for uromodulin. Thus, uromodulin (Tamm-Horsfall glycoprotein) may function as a unique renal regulatory glycoprotein that specifically binds to and regulates the circulating activity of a number of potent cytokines, including IL-1 and TNF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hession, C -- Decker, J M -- Sherblom, A P -- Kumar, S -- Yue, C C -- Mattaliano, R J -- Tizard, R -- Kawashima, E -- Schmeissner, U -- Heletky, S -- New York, N.Y. -- Science. 1987 Sep 18;237(4821):1479-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3498215" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Enzyme-Linked Immunosorbent Assay ; Glycoproteins/metabolism ; Humans ; Interleukin-1/metabolism ; Kidney/*metabolism ; Ligands/metabolism ; Lymphokines/*metabolism ; Molecular Weight ; Mucoproteins/*analysis/genetics ; RNA, Messenger/analysis ; Recombinant Proteins/metabolism ; Tumor Necrosis Factor-alpha ; Uromodulin
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    Clathrin light chains LCA and LCB are similar, polymorphic, and share repeated heptad motifs (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-04-17
    Description: The clathrin light chains fall into two major classes, LCA and LCB. In an intact clathrin triskelion, one light chain, of either class, is bound to the proximal segment of a heavy chain leg. Analysis of rat brain and liver complementary DNA clones for LCA and LCB shows that the two light chain classes are closely related. There appear to be several members of each class having deletions of varying length aligned at the same position. A set of ten heptad elements, characteristic of alpha-helical coiled coils, is a striking feature of the central part of each derived amino acid sequence. These observations suggest a model in which the alpha-helical segment mediates binding to clathrin heavy chains and the amino- and carboxyl-terminal segments mediate interactions with other proteins. They also suggest an explanation for the observed tissue-dependent size variation for members of each class.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kirchhausen, T -- Scarmato, P -- Harrison, S C -- Monroe, J J -- Chow, E P -- Mattaliano, R J -- Ramachandran, K L -- Smart, J E -- Ahn, A H -- Brosius, J -- MH 38819/MH/NIMH NIH HHS/ -- R01 GM 36548-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 17;236(4799):320-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3563513" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/metabolism ; Clathrin/*genetics ; Cloning, Molecular ; DNA/analysis ; Liver/metabolism ; Macromolecular Substances ; *Polymorphism, Genetic ; Rats ; Repetitive Sequences, Nucleic Acid
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    Clustering of genes dispensable for growth in culture in the S component of the HSV-1 genome (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-01
    Description: The herpes simplex virus 1 genome consists of one long and one short stretch of unique sequences flanked by inverted repeat sequences. The nucleotide sequence and RNA map predict 12 open reading frames designated as US1 through US12 within the short stretch of unique sequences. This paper reports the construction of virus mutants from which US2, US3, or US4 had been deleted that are capable of growth in cell culture. One of the three deleted genes, US4, specifies the viral envelope glycoprotein G. Mutants with deletions in US1, US8, US9, US10, US11, and US12 have been previously reported. The nine genes deleted from this region form two clusters, US1 through US4 and US8 through US12, and encode at least two and possibly more structural proteins. The presence of so many genes dispensable for growth in cell culture suggests several hypotheses regarding their function and evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Longnecker, R -- Roizman, B -- CA-08494/CA/NCI NIH HHS/ -- CA-19264/CA/NCI NIH HHS/ -- T32 PHS AI 07182/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1987 May 1;236(4801):573-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3033823" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Restriction Enzymes ; DNA, Recombinant ; DNA, Viral/genetics ; *Genes, Viral ; Glycoproteins/genetics ; Mutation ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Simplexvirus/*genetics/growth & development ; Viral Proteins/genetics
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    Model substrates for an RNA enzyme (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-10-23
    Description: M1 RNA, the catalytic RNA subunit of Escherichia coli ribonuclease P, can cleave novel transfer RNA (tRNA) precursors that lack specific domains of the normal tRNA sequence. The smallest tRNA precursor that was cleaved efficiently retained only the domain of the amino acid acceptor stem and the T stem and loop. The importance of the 3' terminal CCA nucleotide residues in the processing of both novel and normal tRNA precursors implies that the same enzymatic function of M1 RNA is involved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McClain, W H -- Guerrier-Takada, C -- Altman, S -- AI10257/AI/NIAID NIH HHS/ -- GM19422/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):527-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2443980" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; DNA, Recombinant ; Endoribonucleases/*metabolism ; Escherichia coli/*enzymology ; *Escherichia coli Proteins ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Plasmids ; RNA Precursors/*metabolism ; RNA, Bacterial/genetics ; RNA, Transfer, Amino Acyl/genetics ; Ribonuclease P ; Ribonuclease T1/metabolism ; Structure-Activity Relationship ; Substrate Specificity ; Suppression, Genetic
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    A nerve growth factor-induced gene encodes a possible transcriptional regulatory factor (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-11-06
    Description: Nerve growth factor (NGF) is a trophic agent that promotes the outgrowth of nerve fibers from sympathetic and sensory ganglia. The neuronal differentiation stimulated by this hormone was examined in the NGF-responsive cell line PC12. Differential hybridization was used to screen a complementary DNA library constructed from PC12 cells treated with NGF and cycloheximide. One of the complementary DNA clones that was rapidly induced by NGF was found to have a nucleotide sequence that predicts a 54-kilodalton protein with homology to transcriptional regulatory proteins. This clone, NGFI-A, contains three tandemly repeated copies of the 28- to 30-amino acid "zinc finger" domain present in Xenopus laevis TFIIIA and other DNA-binding proteins. It also contains another highly conserved unit of eight amino acids that is repeated at least 11 times. The NGFI-A gene is expressed at relatively high levels in the brain, lung, and superior cervical ganglion of the adult rat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):797-9.〈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/3672127" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Gland Neoplasms ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cycloheximide/pharmacology ; DNA/metabolism ; Genes/*drug effects ; Genes, Regulator/drug effects ; Molecular Sequence Data ; Molecular Weight ; Nerve Growth Factors/*pharmacology ; Pheochromocytoma ; Sequence Homology, Nucleic Acid ; Transcription Factors/*genetics
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    The tat gene of human T-lymphotropic virus type 1 induces mesenchymal tumors in transgenic mice (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-09-11
    Description: Human T-lymphotropic virus type 1 (HTLV-1) is a suspected causative agent of adult T-cell leukemia. One of the viral genes encodes a protein (tat) that not only results in transactivation of viral gene expression but may also regulate the expression of certain cellular genes that are important for cell growth. Transgenic mice that expressed the authentic tat protein under the control of the HTLV-1 long terminal repeat were generated, and cell types that are permissive for the viral promoter and the effects of the tat gene on these cells were studied. Three of eight founder mice with high levels of expression of the transgene in muscle were bred and then analyzed. All developed soft tissue tumors at multiple sites between 13 to 17 weeks of age. This phenotype was transmitted to nine of nine offspring that inherited the tat gene and were available for analysis. The remaining five founders expressed the transgene in the thymus, as well as in muscle. This second group of mice all exhibited extensive thymic depletion and growth retardation; in all of these mice, death occurred between 3 to 6 weeks of age before tumors became macroscopically visible. The tat gene under the control of the HTLV-1 regulatory region showed tissue-specific expression and the tat protein efficiently induced mesenchymal tumors. The data establish tat as an oncogenic protein and HTLV-1 as a transforming virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nerenberg, M -- Hinrichs, S H -- Reynolds, R K -- Khoury, G -- Jay, G -- New York, N.Y. -- Science. 1987 Sep 11;237(4820):1324-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2888190" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Deltaretrovirus/*genetics ; Deltaretrovirus Infections/*genetics ; Female ; *Genes, Viral ; Genetic Engineering ; Genetic Vectors ; Male ; Mesenchymoma/genetics/*microbiology ; Mice ; Pedigree ; Plasmids ; Protein Biosynthesis ; Transcription, Genetic
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    Region-specific expression of two mouse homeo box genes (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-03-13
    Description: Mammalian homeo box genes have been identified on the basis of sequence homology to Drosophila homeotic and segmentation genes. These studies examine the distribution of transcripts from two mouse homeo box genes, Hox-2.1 and Hox-3.1, throughout the latter third of prenatal development. Transcripts from these genes are regionally localized along the rostro-caudal axis of the developing central nervous system, yielding expression patterns very similar to patterns of Drosophila homeotic gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Utset, M F -- Awgulewitsch, A -- Ruddle, F H -- McGinnis, W -- GM09966/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1379-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2881353" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn/genetics ; Base Sequence ; Brain/metabolism ; Cell Differentiation ; Drosophila melanogaster/genetics ; Fetus/metabolism ; *Gene Expression Regulation ; *Genes, Homeobox ; Mice ; Morphogenesis ; Nucleic Acid Hybridization ; Spinal Cord/metabolism ; Transcription, Genetic
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    Human lipoprotein lipase complementary DNA sequence (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-03-27
    Description: Lipoprotein lipase is a key enzyme of lipid metabolism that acts to hydrolyze triglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins. It has been proposed that the enzyme plays a role in the development of obesity and atherosclerosis. The human enzyme has been difficult to purify and its protein sequence was heretofore undetermined. A complementary DNA for human lipoprotein lipase that codes for a mature protein of 448 amino acids has now been cloned and sequenced. Analysis of the sequence indicates that human lipoprotein lipase, hepatic lipase, and pancreatic lipase are members of a gene family. Two distinct species of lipoprotein lipase messenger RNA that arise from alternative sites of 3'-terminal polyadenylation were detected in several different tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wion, K L -- Kirchgessner, T G -- Lusis, A J -- Schotz, M C -- Lawn, R M -- HL28481/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 27;235(4796):1638-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823907" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/*analysis ; Fatty Acids, Nonesterified/metabolism ; Humans ; Lipase/analysis/genetics ; Lipoprotein Lipase/analysis/*genetics ; Liver/enzymology ; Nucleic Acid Hybridization
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    A promoter with an internal regulatory domain is part of the origin of replication in BPV-1 (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-06-26
    Description: Extrachromosomal elements that are stably maintained at a constant copy number through cell doublings are a good model system for the study of the regulation of DNA replication in higher eukaryotes. Previous studies have defined both cis and trans functions required for the regulated plasmid replication of the bovine papilloma virus in stably transformed cells. Here, a sequence known to be a cis-dominant element of the replication origin of the plasmid is shown to contain a promoter for transcription. Both in vitro and in vivo assays have been used to define this promoter and show that a sequence located just 3' to the transcriptional start site is required for activity. This DNA sequence element, which has been defined through deletions, coincides with a binding site for a cellular factor and is also required for a functional origin of replication. Possible models for how a transcription factor may play a role in the regulation of DNA replication are discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stenlund, A -- Bream, G L -- Botchan, M R -- CA 42414/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 26;236(4809):1666-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037693" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Base Sequence ; Bovine papillomavirus 1/*genetics/physiology ; Chloramphenicol O-Acetyltransferase ; Chromosome Deletion ; Cycloheximide/pharmacology ; *DNA Replication ; Genes, Viral ; Papillomaviridae/*genetics ; *Promoter Regions, Genetic ; RNA, Viral/analysis ; Templates, Genetic ; Transcription, Genetic ; *Virus Replication
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    Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1 (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-12-04
    Description: Nuclear oncogene products have the potential to induce alterations in gene regulation leading to the genesis of cancer. The biochemical mechanisms by which nuclear oncoproteins act remain unknown. Recently, an oncogene, v-jun, was found to share homology with the DNA binding domain of a yeast transcription factor, GCN4. Furthermore, GCN4 and the phorbol ester-inducible enhancer binding protein, AP-1, recognize very similar DNA sequences. The human proto-oncogene c-jun has now been isolated, and the deduced amino acid sequence indicates more than 80 percent identity with v-jun. Expression of cloned c-jun in bacteria produced a protein with sequence-specific DNA binding properties identical to AP-1. Antibodies raised against two distinct peptides derived from v-jun reacted specifically with human AP-1. In addition, partial amino acid sequence of purified AP-1 revealed tryptic peptides in common with the c-jun protein. The structural and functional similarities between the c-jun product and the enhancer binding protein suggest that AP-1 may be encoded by c-jun. These findings demonstrate that the proto-oncogene product of c-jun interacts directly with specific target DNA sequences to regulate gene expression, and therefore it may now be possible to identify genes under the control of c-jun that affect cell growth and neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohmann, D -- Bos, T J -- Admon, A -- Nishimura, T -- Vogt, P K -- Tjian, R -- CA25417/CA/NCI NIH HHS/ -- CA42564/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1386-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, University of California, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825349" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies/immunology ; Avian Sarcoma Viruses/genetics ; Base Sequence ; Cross Reactions ; DNA/genetics ; DNA-Binding Proteins/genetics/immunology/*physiology ; Enhancer Elements, Genetic ; Fungal Proteins/genetics ; Gene Expression Regulation ; Genes, Viral ; Humans ; Molecular Sequence Data ; Oncogene Protein p65(gag-jun) ; Oncogenes ; *Protein Kinases ; Proto-Oncogene Proteins/genetics/immunology/*physiology ; Proto-Oncogene Proteins c-jun ; *Proto-Oncogenes ; Recombinant Proteins/genetics ; Retroviridae Proteins/genetics ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid ; Transcription Factors/genetics/immunology/*physiology ; Transcription, Genetic
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    Interaction of a liver-specific nuclear factor with the fibrinogen and alpha 1-antitrypsin promoters (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-30
    Description: The orderly and sequential activation of genes during development is hypothesized to be related to the selective expression of groups of regulatory proteins acting primarily at the level of transcription. A nuclear protein was found in hepatocytes, but not other cell types, that binds to a sequence required for hepatocyte-specific transcription of the gene for the beta chain of fibrinogen. This protein, hepatocyte nuclear factor 1 (HNF1), also interacts with homologous sequences required for optimal promoter function of the genes for the alpha chain of fibrinogen and alpha 1-antitrypsin. The promoter or enhancer regions for several viral and cellular genes not expressed in the liver did not compete for this binding. The restricted expression of HNF1 and its selective interaction with the control regions of several liver-specific genes indicate that it is involved in developmentally regulated gene expression in the liver.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Courtois, G -- Morgan, J G -- Campbell, L A -- Fourel, G -- Crabtree, G R -- CA39612/CA/NCI NIH HHS/ -- HL33942/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):688-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3499668" target="_blank"〉PubMed〈/a〉
    Keywords: Albumins/genetics ; Base Sequence ; Binding, Competitive ; Cell Line ; DNA-Binding Proteins/*genetics ; Deoxyribonuclease I ; Fibrinogen/*genetics ; *Gene Expression Regulation ; Liver/*physiology ; Nuclear Proteins/*physiology ; *Promoter Regions, Genetic ; Regulatory Sequences, Nucleic Acid ; Transcription Factors/*genetics ; alpha 1-Antitrypsin/*genetics
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    Sevenless, a cell-specific homeotic gene of Drosophila, encodes a putative transmembrane receptor with a tyrosine kinase domain (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-04-03
    Description: The determination of cell fates during the assembly of the ommatidia in the compound eye of Drosophila appears to be controlled by cell-cell interactions. In this process, the sevenless gene is essential for the development of a single type of photoreceptor cell. In the absence of proper sevenless function the cells that would normally become the R7 photoreceptors instead become nonneuronal cells. Previous morphological and genetic analysis has indicated that the product of the sevenless gene is involved in reading or interpreting the positional information that specifies this particular developmental pathway. The sevenless gene has now been isolated and characterized. The data indicate that sevenless encodes a transmembrane protein with a tyrosine kinase domain. This structural similarity between sevenless and certain hormone receptors suggests that similar mechanisms are involved in developmental decisions based on cell-cell interaction and physiological or developmental changes induced by diffusible factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hafen, E -- Basler, K -- Edstroem, J E -- Rubin, G M -- GM32795/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):55-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2882603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; DNA Restriction Enzymes ; Drosophila melanogaster/*embryology/genetics ; Eye/cytology/embryology ; Gene Expression Regulation ; Genes ; *Genes, Homeobox ; Growth Substances/physiology ; Membrane Proteins/genetics ; Phenotype ; Protein-Tyrosine Kinases/*genetics/physiology ; Receptors, Cell Surface/*genetics/physiology ; Transcription, Genetic
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    Homeo domain of the yeast repressor alpha 2 is a sequence-specific DNA-binding domain but is not sufficient for repression (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-08-28
    Description: The alpha 2 protein, the product of the MAT alpha 2 gene, is a regulator of cell type in the yeast Saccharomyces cerevisiae. It represses transcription of a group of cell type-specific genes by binding to an operator located upstream of each target gene. Fifteen in-frame deletions within the coding region of the MAT alpha 2 gene were constructed. The deletion alleles were examined for phenotypes conferred in vivo, and the encoded mutant proteins were assayed for ability to bind specifically to the operator in vitro. This analysis has revealed that the sequence-specific DNA-binding domain of alpha 2 is located within a region of 68 amino acids. This region of alpha 2 has significant homology with the homeo domain, a conserved sequence found in the products of several Drosophila homeotic and segmentation genes. In addition, there is a class of mutant alpha 2 proteins that binds tightly and specifically to the operator in vitro, but fails to repress transcription in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, M N -- Johnson, A D -- GM35284/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 28;237(4818):1007-12.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2887035" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Fungal/genetics ; DNA-Binding Proteins/*genetics ; Drosophila melanogaster/genetics ; Genes, Homeobox ; *Genes, Regulator ; Mutation ; Phenotype ; Repressor Proteins/*genetics ; Saccharomyces cerevisiae/*genetics ; Transcription Factors/*genetics
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    Cloning, sequencing, and expression of the gene coding for the human platelet alpha 2-adrenergic receptor (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-10-30
    Description: The gene for the human platelet alpha 2-adrenergic receptor has been cloned with oligonucleotides corresponding to the partial amino acid sequence of the purified receptor. The identity of this gene has been confirmed by the binding of alpha 2-adrenergic ligands to the cloned receptor expressed in Xenopus laevis oocytes. The deduced amino acid sequence is most similar to the recently cloned human beta 2- and beta 1-adrenergic receptors; however, similarities to the muscarinic cholinergic receptors are also evident. Two related genes have been identified by low stringency Southern blot analysis. These genes may represent additional alpha 2-adrenergic receptor subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobilka, B K -- Matsui, H -- Kobilka, T S -- Yang-Feng, T L -- Francke, U -- Caron, M G -- Lefkowitz, R J -- Regan, J W -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):650-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blood Platelets/*physiology ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation ; Genes ; Humans ; Infant, Newborn ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Multigene Family ; Oligodeoxyribonucleotides ; Phosphoproteins/genetics ; Receptors, Adrenergic, alpha/*genetics
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    Human retinoblastoma susceptibility gene: cloning, identification, and sequence (1987)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1987-03-13
    Description: Recent evidence indicates the existence of a genetic locus in chromosome region 13q14 that confers susceptibility to retinoblastoma, a cancer of the eye in children. A gene encoding a messenger RNA (mRNA) of 4.6 kilobases (kb), located in the proximity of esterase D, was identified as the retinoblastoma susceptibility (RB) gene on the basis of chromosomal location, homozygous deletion, and tumor-specific alterations in expression. Transcription of this gene was abnormal in six of six retinoblastomas examined: in two tumors, RB mRNA was not detectable, while four others expressed variable quantities of RB mRNA with decreased molecular size of about 4.0 kb. In contrast, full-length RB mRNA was present in human fetal retina and placenta, and in other tumors such as neuroblastoma and medulloblastoma. DNA from retinoblastoma cells had a homozygous gene deletion in one case and hemizygous deletion in another case, while the remainder were not grossly different from normal human control DNA. The gene contains at least 12 exons distributed in a region of over 100 kb. Sequence analysis of complementary DNA clones yielded a single long open reading frame that could encode a hypothetical protein of 816 amino acids. A computer-assisted search of a protein sequence database revealed no closely related proteins. Features of the predicted amino acid sequence include potential metal-binding domains similar to those found in nucleic acid-binding proteins. These results provide a framework for further study of recessive genetic mechanisms in human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, W H -- Bookstein, R -- Hong, F -- Young, L J -- Shew, J Y -- Lee, E Y -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1394-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823889" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Carboxylesterase ; Carboxylic Ester Hydrolases/genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 13 ; *Cloning, Molecular ; DNA/genetics ; Eye Neoplasms/*genetics ; Female ; Homozygote ; Humans ; Nucleic Acid Hybridization ; Placenta/analysis ; Pregnancy ; RNA, Messenger/genetics ; Retina/analysis/embryology ; Retinoblastoma/*genetics ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 71
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    Phylogenetic relations of humans and African apes from DNA sequences in the psi eta-globin region (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-16
    Description: Sequences from the upstream and downstream flanking DNA regions of the psi eta-globin locus in Pan troglodytes (common chimpanzee), Gorilla gorilla (gorilla), and Pongo pygmaeus (orangutan, the closest living relative to Homo, Pan, and Gorilla) provided further data for evaluating the phylogenetic relations of humans and African apes. These newly sequenced orthologs [an additional 4.9 kilobase pairs (kbp) for each species] were combined with published psi eta-gene sequences and then compared to the same orthologous stretch (a continuous 7.1-kbp region) available for humans. Phylogenetic analysis of these nucleotide sequences by the parsimony method indicated (i) that human and chimpanzee are more closely related to each other than either is to gorilla and (ii) that the slowdown in the rate of sequence evolution evident in higher primates is especially pronounced in humans. These results indicate that features (for example, knuckle-walking) unique to African apes (but not to humans) are primitive and that even local molecular clocks should be applied with caution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyamoto, M M -- Slightom, J L -- Goodman, M -- R01 HL 33940/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):369-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, MI 48201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3116671" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; DNA/*genetics ; DNA, Mitochondrial/genetics ; Gait ; Globins/*genetics ; Gorilla gorilla/*genetics ; Haplorhini/*genetics ; Humans ; Metacarpophalangeal Joint ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Pan troglodytes/*genetics ; *Phylogeny ; Polymorphism, Genetic ; Sequence Homology, Nucleic Acid
    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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  • 72
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    Identification of the human U7 snRNP as one of several factors involved in the 3' end maturation of histone premessenger RNA's (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-18
    Description: In eukaryotic cells, the conversion of gene transcripts into messenger RNA's involves multiple factors, including the highly abundant small nuclear ribonucleoprotein (snRNP) complexes that mediate the splicing reaction. Separable factors are also required for the 3' end processing of histone pre-mRNA's. The two conserved signals flanking the 3' cleavage site are recognized by discrete components present in active HeLa cell extracts: the upstream stem loop associates with a nuclease-insensitive factor, while binding to the downstream element is mediated by a component having the properties of a snRNP. The sequence of the RNA moiety of the low abundance human U7 snRNP suggests how the relatively degenerate downstream element of mammalian pre-mRNA's could be recognized by RNA base-pairing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mowry, K L -- Steitz, J A -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1682-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825355" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Endoribonucleases ; HeLa Cells/metabolism ; Histones/*genetics ; Humans ; Molecular Sequence Data ; RNA Precursors/*genetics ; RNA Processing, Post-Transcriptional ; Ribonuclease H ; Ribonucleoproteins/*genetics ; Ribonucleoproteins, Small Nuclear
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 73
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    The maize transposable element Ds is spliced from RNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-08-21
    Description: In some instances, insertion of maize transposable elements into exons does not result in the total loss of enzymatic activity. In other instances, messenger RNAs of wild-type size are encoded by genes known to contain the maize transposable element Dissociation (Ds) in exons. To understand how Ds is processed from RNA, a study was made of transcripts encoded by two alleles of the maize waxy (wx) gene containing Ds insertions in exon sequences. The analysis was carried out in strains where the Ds element could not excise from the wx gene. Despite insertions of 4.3- and 1.5-Ds elements, the predominant transcripts encoded by these two genes were wild type in size. For both alleles, DNA sequencing of complementary DNAs revealed that the Ds elements had been spliced in a similar manner. Splicing was accomplished by the utilization of multiple 5' donor splice sites in the Ds termini and a 3' acceptor site within the wx gene adjacent to the Ds element. The net effect in both cases was the removal of most of the Ds element from the messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wessler, S R -- Baran, G -- Varagona, M -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):916-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3039661" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; DNA/genetics ; *DNA Transposable Elements ; Exons ; *RNA Splicing ; RNA, Messenger/*genetics ; Transcription, Genetic ; Zea mays/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 74
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    Regulation in vitro of metallothionein gene binding factors (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-03-13
    Description: Mouse nuclear factors that bind to an upstream metal regulatory element of the mouse metallothionein-I gene have been identified by DNA footprinting and oligonucleotide band shift assays. The formation of complexes at this site can be activated 20- to 40-fold by the vitro addition of ionic cadmium. The activation reaction is rapid, reversible by a metal chelator, and may involve multiple proteins. These results suggest that the initial step in cadmium detoxification is an interaction between the metal and nuclear DNA-binding factors leading to an increase in metallothionein gene transcription. The ability to observe metal activation in vitro makes this a powerful system to study the biochemistry of eukaryotic gene regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seguin, C -- Hamer, D H -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1383-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3103216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cadmium/pharmacology ; Cell Nucleus/analysis ; DNA/genetics/metabolism ; DNA-Binding Proteins/metabolism ; Deoxyribonuclease I ; Edetic Acid/pharmacology ; Exodeoxyribonucleases ; *Genes, Regulator ; Metallothionein/*genetics ; Mice ; Oligonucleotides/genetics ; Transcription Factors/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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