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  • Mutation  (25)
  • American Association for the Advancement of Science (AAAS)  (25)
  • American Association of Petroleum Geologists (AAPG)
  • International Union of Crystallography (IUCr)
  • 1985-1989  (25)
  • 1985  (25)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (25)
  • American Association of Petroleum Geologists (AAPG)
  • International Union of Crystallography (IUCr)
  • Springer  (3)
Years
  • 1985-1989  (25)
Year
  • 1
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    Evolution of bunyaviruses by genome reassortment in dually infected mosquitoes (Aedes triseriatus) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: Aedes triseriatus mosquitoes became dually infected after ingesting two mutants of LaCrosse (LAC) virus simultaneously or after ingesting, by interrupted feeding, the two viruses sequentially within a 2-day period. After 2 weeks of incubation, approximately 25 percent of the vectors contained new virus genotypes as the result of RNA segment reassortment. New viruses were transmitted when the mosquitoes fed on mice. Viruses ingested more than 2 days after the initial infecting virus did not cause superinfection of the mosquito vectors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beaty, B J -- Sundin, D R -- Chandler, L J -- Bishop, D H -- AI 15400/AI/NIAID NIH HHS/ -- AI 19688/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):548-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4048949" target="_blank"〉PubMed〈/a〉
    Keywords: Aedes/*microbiology ; Animals ; Blood ; Bunyaviridae/*genetics ; Genotype ; Insect Vectors ; Mutation ; Phenotype ; RNA, Viral/analysis ; Time Factors
    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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    The mosaic genome of warm-blooded vertebrates (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: Most of the nuclear genome of warm-blooded vertebrates is a mosaic of very long (much greater than 200 kilobases) DNA segments, the isochores; these isochores are fairly homogeneous in base composition and belong to a small number of major classes distinguished by differences in guanine-cytosine (GC) content. The families of DNA molecules derived from such classes can be separated and used to study the genome distribution of any sequence which can be probed. This approach has revealed (i) that the distribution of genes, integrated viral sequences, and interspersed repeats is highly nonuniform in the genome, and (ii) that the base composition and ratio of CpG to GpC in both coding and noncoding sequences, as well as codon usage, mainly depend on the GC content of the isochores harboring the sequences. The compositional compartmentalization of the genome of warm-blooded vertebrates is discussed with respect to its evolutionary origin, its causes, and its effects on chromosome structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernardi, G -- Olofsson, B -- Filipski, J -- Zerial, M -- Salinas, J -- Cuny, G -- Meunier-Rotival, M -- Rodier, F -- New York, N.Y. -- Science. 1985 May 24;228(4702):953-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001930" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Biological Evolution ; Centrifugation, Density Gradient ; Chickens/*genetics ; Chromosome Banding ; Codon ; Cytosine/analysis ; DNA/analysis/*genetics ; DNA Replication ; DNA, Viral/genetics ; Gene Amplification ; *Genes ; Genes, Viral ; Guanine/analysis ; Humans ; Mammals/*genetics ; Mice/genetics ; Mutation ; Rabbits/genetics ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Xenopus/*genetics
    Print ISSN: 0036-8075
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  • 3
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    The "spliceosome": yeast pre-messenger RNA associates with a 40S complex in a splicing-dependent reaction (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: The in vitro splicing reactions of pre-messenger RNA (pre-mRNA) in a yeast extract were analyzed by glycerol gradient centrifugation. Labeled pre-mRNA appears in a 40S peak only if the pre-mRNA undergoes the first of the two partial splicing reactions. RNA analysis after extraction of glycerol gradient fractions shows that lariat-form intermediates, molecules that occur only in mRNA splicing, are found almost exclusively in this 40S complex. Another reaction intermediate, cut 5' exon RNA, can also be found concentrated in this complex. The complex is stable even in 400 mM KCl, although at this salt concentration, it sediments at 35S and is clearly distinguishable from 40S ribosomal subunits. This complex, termed a "spliceosome," is thought to contain components necessary for mRNA splicing; its existence can explain how separated exons on pre-mRNA are brought into contact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brody, E -- Abelson, J -- New York, N.Y. -- Science. 1985 May 24;228(4702):963-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3890181" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Base Sequence ; Centrifugation, Density Gradient ; Mutation ; Nucleic Acid Conformation ; Nucleic Acid Precursors/*genetics/metabolism ; RNA Precursors ; *RNA Splicing ; RNA, Fungal/*genetics/metabolism ; RNA, Messenger/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism
    Print ISSN: 0036-8075
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  • 4
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    The unusual varl gene of yeast mitochondrial DNA (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-28
    Description: The var1 gene specifies the only mitochondrial ribosomal protein known to be encoded by yeast mitochondrial DNA. The gene is unusual in that its base composition is nearly 90 percent adenine plus thymine. It and its expression product show a strain-dependent variation in size of up to 7 percent; this variation does not detectably interfere with function. Furthermore, var1 is an expandable gene that participates in a novel recombinational event resembling gene conversion whereby shorter alleles are preferentially converted to longer ones. The remarkable features of var1 indicate that it may have evolved by a mechanism analogous to exon shuffling, although no introns are actually present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Butow, R A -- Perlman, P S -- Grossman, L I -- GM-22525/GM/NIGMS NIH HHS/ -- GM-26546/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 28;228(4707):1496-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990030" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Biological Evolution ; DNA Restriction Enzymes/metabolism ; DNA, Mitochondrial/*analysis ; *Genes, Fungal ; Mutation ; Neurospora/*genetics ; Polymorphism, Genetic
    Print ISSN: 0036-8075
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  • 5
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    Activated proto-onc genes: sufficient or necessary for cancer? (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: Proto-onc genes are normal cellular genes that are related to the transforming (onc) genes of retroviruses. Because of this relationship these genes are now widely believed to be potential cancer genes. In some tumors, proto-onc genes are mutated or expressed more than in normal cells. Under these conditions, proto-onc genes are hypothesized to be active cancer genes in one of two possible ways: The one gene-one cancer hypothesis suggests that one activated proto-onc gene is sufficient to cause cancer. The multigene-one cancer hypothesis suggests that an activated proto-onc gene is a necessary but not a sufficient cause of cancer. However, mutated or transcriptionally activated proto-onc genes are not consistently associated with the tumors in which they are occasionally found and do not transform primary cells. Further, no set of an activated proto-onc gene and a complementary cancer gene with transforming function has yet been isolated from a tumor. Thus, there is still no proof that activated proto-onc genes are sufficient or even necessary to cause cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duesberg, P H -- CA 11426/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 10;228(4700):669-77.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3992240" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Transformation, Neoplastic/metabolism ; Chickens ; DNA, Neoplasm/genetics ; Genes, Viral ; Humans ; Kirsten murine sarcoma virus/genetics ; Lymphoma/genetics ; Melanoma/genetics ; Mice ; Mutation ; Neoplasms/etiology/*genetics ; *Oncogenes ; Plasmacytoma/genetics ; Rats ; Retroviridae/genetics ; Sarcoma, Experimental/genetics ; Transduction, Genetic ; Translocation, Genetic ; Tumor Virus Infections/genetics
    Print ISSN: 0036-8075
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  • 6
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    Bidirectional SV40 transcription mediated by tandem Sp1 binding interactions (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-01
    Description: The 21-base pair repeat elements of the SV40 promoter contain six tandem copies of the GGGCGG hexanucleotide (GC-box), each of which can bind, with varying affinity, to the cellular transcription factor, Sp1. In vitro SV40 early RNA synthesis is mediated by interaction of Sp1 with GC-boxes I, II, and III, whereas transcription in the late direction is mediated by binding to GC-boxes III, V, and VI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gidoni, D -- Kadonaga, J T -- Barrera-Saldana, H -- Takahashi, K -- Chambon, P -- Tjian, R -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):511-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996137" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Polyacrylamide Gel ; Gene Expression Regulation ; Mutation ; Pregnancy Proteins/*metabolism ; RNA, Messenger/analysis ; RNA, Viral/biosynthesis ; Simian virus 40/*genetics ; Sp1 Transcription Factor ; Templates, Genetic ; Transcription Factors/*metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
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  • 7
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    Rescue of the Drosophila phototransduction mutation trp by germline transformation (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-29
    Description: Phototransduction is the process by which light-stimulated photoreceptor cells of the visual system send electrical signals to the nervous system. Many of the steps that follow the initial event in phototransduction, absorption of light by rhodopsin, are ill-defined. The fruitfly, Drosophila melanogaster, provides a means to dissect phototransduction genetically. Mutations such as transient receptor potential (trp) affect intermediate steps in phototransduction. In order to facilitate molecular studies of phototransduction, the trp gene was isolated and its identity was confirmed by complementing the mutant trpCM allele of the trp gene by P-element mediated germline transformation of a 7.1-kilobase DNA fragment. Expression of the trp gene begins late in pupal development and appears to be limited to the eyes and ocelli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montell, C -- Jones, K -- Hafen, E -- Rubin, G -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1040-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3933112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/genetics ; Drosophila melanogaster/*genetics/physiology ; Gene Expression Regulation ; Genes ; Mutation ; Ocular Physiological Phenomena ; RNA, Messenger/genetics ; *Vision, Ocular
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  • 8
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    Measles virus matrix protein synthesized in a subacute sclerosing panencephalitis cell line (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Measles virus generally produces acute illness. Rarely, however, persistent infection of brain cells occurs, resulting in a chronic and fatal neurological disease, subacute sclerosing panencephalitis (SSPE). Evidence indicates that expression of the measles virus matrix protein is selectively restricted in this persistent infection, but the mechanism underlying this restriction has not been identified. Defective translation of matrix messenger RNA has been described in one SSPE cell line. This report presents evidence that in a different SSPE tissue culture cell line IP-3-Ca, the matrix protein is synthesized but fails to accumulate. A general scheme is proposed to reconcile the different levels at which restriction of matrix protein has been observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheppard, R D -- Raine, C S -- Bornstein, M B -- Udem, S A -- CA13330-12/CA/NCI NIH HHS/ -- NS 08952/NS/NINDS NIH HHS/ -- NS 11920/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1219-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001938" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Gene Expression Regulation ; Humans ; Hydrolysis ; Measles virus/genetics/growth & development/*metabolism ; Molecular Weight ; Mutation ; Protein Processing, Post-Translational ; Subacute Sclerosing Panencephalitis/*microbiology ; Viral Matrix Proteins ; Viral Proteins/*biosynthesis/genetics ; Virus Replication
    Print ISSN: 0036-8075
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  • 9
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    Heterologous protein secretion from yeast (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, R A -- Duncan, M J -- Moir, D T -- New York, N.Y. -- Science. 1985 Sep 20;229(4719):1219-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3939723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Chymosin/*secretion ; Cloning, Molecular ; Cytoplasm/enzymology ; Enzyme Activation ; Enzyme Precursors/*secretion ; Fungal Proteins/secretion ; Glycosylation ; Mutation ; Plasmids ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/secretion ; Saccharomyces cerevisiae/enzymology/*genetics ; Solubility
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  • 10
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    Function and autoregulation of yeast copperthionein (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: The CUP1 gene of yeast encodes a small, metallothionein-like protein that binds to and is inducible by copper. A gene replacement experiment shows that this protein protects cells against copper poisoning but is dispensable for normal cellular growth and development throughout the yeast life cycle. The transcription of CUP1 is negatively autoregulated. This feedback mechanism, which is mediated through upstream control sequences, may play an important role in heavy metal homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamer, D H -- Thiele, D J -- Lemontt, J E -- New York, N.Y. -- Science. 1985 May 10;228(4700):685-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3887570" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins ; Copper/metabolism ; Copper Sulfate ; Enzyme Induction ; Genes, Fungal ; Metallothionein/biosynthesis/genetics/*physiology ; Mutation ; Operon ; Plasmids ; RNA, Messenger/biosynthesis ; Saccharomyces cerevisiae/*enzymology/genetics
    Print ISSN: 0036-8075
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  • 11
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    Three-dimensional structure of poliovirus at 2.9 A resolution (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-27
    Description: The three-dimensional structure of poliovirus has been determined at 2.9 A resolution by x-ray crystallographic methods. Each of the three major capsid proteins (VP1, VP2, and VP3) contains a "core" consisting of an eight-stranded antiparallel beta barrel with two flanking helices. The arrangement of beta strands and helices is structurally similar and topologically identical to the folding pattern of the capsid proteins of several icosahedral plant viruses. In each of the major capsid proteins, the "connecting loops" and NH2- and COOH-terminal extensions are structurally dissimilar. The packing of the subunit "cores" to form the virion shell is reminiscent of the packing in the T = 3 plant viruses, but is significantly different in detail. Differences in the orientations of the subunits cause dissimilar contacts at protein-protein interfaces, and are also responsible for two major surface features of the poliovirion: prominent peaks at the fivefold and threefold axes of the particle. The positions and interactions of the NH2- and COOH-terminal strands of the capsid proteins have important implications for virion assembly. Several of the "connecting loops" and COOH-terminal strands form prominent radial projections which are the antigenic sites of the virion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hogle, J M -- Chow, M -- Filman, D J -- AI-20566/AI/NIAID NIH HHS/ -- AI-22346/AI/NIAID NIH HHS/ -- NS-07078/NS/NINDS NIH HHS/ -- R01 AI020566/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Sep 27;229(4720):1358-65.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2994218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/immunology ; Capsid/physiology ; Chemical Phenomena ; Chemistry ; HeLa Cells/microbiology ; Mutation ; Poliovirus/physiology/*ultrastructure ; Protein Conformation ; Virus Replication ; X-Ray Diffraction
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  • 12
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    Thermosensitivity of a DNA recognition site: activity of a truncated nutL antiterminator of coliphage lambda (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-05
    Description: Antitermination is an important transcriptional control. In bacteriophage lambda, the presence of the nut antiterminators between the promoters and terminators results in relatively unhindered transcription when the lambda N gene product and necessary host factors are supplied. This antitermination system has been rendered thermosensitivity by modification of the nut site. A fragment of lambda DNA [74 base pairs (bp) in length]that contained the 17-bp nutL core sequence, but lacked the 8-bp boxA sequence, was cloned in a pp-N-tL1-galK plasmid between the pp promoter and gene N. This fragment mediated antitermination of transcription at 30 degrees C, as measured by assaying galK gene expression in Escherichia coli. At 42 degrees C, however, antitermination at the lambda tL1 terminator was abolished. Antitermination at 42 degrees C was restored by replacing the 74-bp nutL fragment with longer sequences containing both nutL and boxA or by cloning a synthetic boxA sequence ahead of the 74-bp nutL fragment. Thus, efficient antitermination required both boxA and the 17-bp nutL core, with the latter becoming conditionally defective when the boxA sequence was deleted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peltz, S W -- Brown, A L -- Hasan, N -- Podhajska, A J -- Szybalski, W -- 5-P30-CA-07175/CA/NCI NIH HHS/ -- 5-PO1-CA-23076/CA/NCI NIH HHS/ -- CA-09135/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Apr 5;228(4695):91-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3156406" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/*genetics ; DNA, Viral/*genetics/physiology ; Escherichia coli/genetics ; Hot Temperature ; Mutation ; Plasmids ; Promoter Regions, Genetic ; Terminator Regions, Genetic
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  • 13
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    A model for the tertiary structure of p21, the product of the ras oncogene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: A model was developed for the structure of p21, the protein with a molecular weight of 21,000 that is produced by the ras genes. This model predicts that p21 consists of a central core of beta-sheet structure, connected by loops and alpha helices. Four of these loops comprise the guanine nucleotide binding site. The phosphoryl binding region is made up of amino acid sequences from 10 to 16 and from 57 to 63 of p21. The latter sequence may contain a site for magnesium binding. Amino acids defining guanine specificity are Asn-116 and Asp-119, and sequences around amino acid 145 may contribute to guanine binding. The model makes it possible to visualize how oncogenic mutations of p21 affect interaction with guanine nucleotides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCormick, F -- Clark, B F -- la Cour, T F -- Kjeldgaard, M -- Norskov-Lauritsen, L -- Nyborg, J -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):78-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3898366" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/analysis ; Animals ; *Aspartate Carbamoyltransferase ; Base Sequence ; Binding Sites ; *Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) ; Cattle ; *Dihydroorotase ; Escherichia coli ; Guanine Nucleotides/metabolism ; Humans ; Macromolecular Substances ; Magnesium/metabolism ; Membrane Proteins/analysis ; Models, Chemical ; *Multienzyme Complexes ; Mutation ; *Oncogenes ; Peptide Elongation Factor Tu ; Peptide Elongation Factors/analysis ; Protein Conformation ; Proteins/*analysis ; RNA, Transfer, Amino Acyl/metabolism ; Saccharomyces cerevisiae ; Transducin
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  • 14
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    Redesigning trypsin: alteration of substrate specificity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: A general method for modifying eukaryotic genes by site-specific mutagenesis and subsequent expression in mammalian cells was developed to study the relation between structure and function of the proteolytic enzyme trypsin. Glycine residues at positions 216 and 226 in the binding cavity of trypsin were replaced by alanine residues, resulting in three trypsin mutants. Computer graphic analysis suggested that these substitutions would differentially affect arginine and lysine substrate binding of the enzyme. Although the mutant enzymes were reduced in catalytic rate, they showed enhanced substrate specificity relative to the native enzyme. This increased specificity was achieved by the unexpected differential effects on the catalytic activity toward arginine and lysine substrates. Mutants containing alanine at position 226 exhibited an altered conformation that may be converted to a trypsin-like structure upon binding of a substrate analog.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Largman, C -- Fletcher, T -- Roczniak, S -- Barr, P J -- Fletterick, R -- Rutter, W J -- AM26081/AM/NIADDK NIH HHS/ -- GM07216/GM/NIGMS NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):291-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3838593" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Electrophoresis ; Mutation ; Rats ; Substrate Specificity ; Trypsin/biosynthesis/*genetics/metabolism ; Trypsinogen/metabolism
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  • 15
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    Amino acid replacements that compensate for a large polypeptide deletion in an enzyme (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-26
    Description: Deletion of more than 400 amino acids from the carboxyl terminus of an enzyme causes a severe reduction in catalytic activity. Selected point mutations within the residual protein partially reverse the effects of the missing segment. The selection can yield mutants with activities at least ten times as high as those of the starting polypeptides. One well-characterized mutation, a single amino acid replacement in the residual polypeptide, increases the catalytic activity of the polypeptide by a factor of 5. The results suggest substantial potential for design of protein elements to compensate for missing polypeptide sequences. They also may reflect that progenitors of large aminoacyl-tRNA (transfer RNA) synthetases--one of which was used in these studies--were themselves much smaller.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, C -- Jasin, M -- Schimmel, P -- New York, N.Y. -- Science. 1985 Jul 26;229(4711):389-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3892692" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine-tRNA Ligase/genetics ; *Amino Acid Sequence ; DNA, Recombinant ; Enzymes/*genetics/metabolism ; Escherichia coli/enzymology/genetics ; Genetic Engineering ; Genetic Vectors ; Mutation ; Nucleic Acid Heteroduplexes/genetics ; Plasmids
    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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  • 16
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    Mutation in LDL receptor: Alu-Alu recombination deletes exons encoding transmembrane and cytoplasmic domains (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-11
    Description: The molecular size of the plasma LDL (low density lipoprotein) receptor synthesized by cultured fibroblasts from a patient with the internalization-defective form of familial hypercholesterolemia (FH 274) was smaller by 10,000 daltons than the size of the normal LDL receptor. The segment of the gene encoding the truncated portion of the FH 274 receptor was cloned into bacteriophage lambda. Comparison of the nucleotide sequences of the normal and FH 274 genes revealed a 5-kilobase deletion, which eliminated the exons encoding the membrane-spanning region and the carboxyl terminal cytoplasmic domain of the receptor. The deletion appeared to be caused by a novel intrastrand recombination between two repetitive sequences of the Alu family that were oriented in opposite directions. The truncated receptors lack membrane-spanning regions and cytoplasmic domains; they are largely secreted into the culture medium, but a small fraction remains adherent to the cell surface. The surface-adherent receptors bind LDL, but they are unable to cluster in coated pits, thus explaining the internalization-defective phenotype.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449727/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449727/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehrman, M A -- Schneider, W J -- Sudhof, T C -- Brown, M S -- Goldstein, J L -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):140-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3155573" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda ; Base Sequence ; Cell Membrane ; Cloning, Molecular ; Coated Pits, Cell-Membrane/metabolism ; Cytoplasm ; Fibroblasts ; Genes ; Humans ; Hyperlipoproteinemia Type II/*genetics ; Male ; Molecular Weight ; Mutation ; Receptors, LDL/*genetics ; Recombination, Genetic ; *Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Effects of genomic position on the expression of transduced copies of the white gene of Drosophila (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-09
    Description: The white gene of Drosophila is expressed normally when introduced at many different sites in the genome by P-element-mediated DNA transformation, but is expressed abnormally when inserted at two particular genomic positions. It is now demonstrated that the mutant expression in these two cases is caused by the surrounding chromosomal region into which the white gene has been inserted. The white gene could be moved from these two positions, where it confers a mutant phenotype, to other positions in the genome where it confers a wild-type phenotype. However, flies in which white has been moved to one new location have an unusual mosaic phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levis, R -- Hazelrigg, T -- Rubin, G M -- New York, N.Y. -- Science. 1985 Aug 9;229(4713):558-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992080" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; DNA Transposable Elements ; Drosophila/*genetics ; *Gene Expression Regulation ; Mosaicism ; Mutation ; Phenotype ; Pigmentation ; *Transformation, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    Antigenic variation and resistance to neutralization in poliovirus type 1 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-09-13
    Description: Mutations have been identified in variants of poliovirus, type 1 (Mahoney) on the basis of their resistance to neutralization by individual monoclonal antibodies. The phenotypes of these variants were defined in terms of antibody binding; the pattern of epitopes expressed or able to be exploited for neutralization were complex. Single amino acid changes can have distant (in terms of linear sequence) and generalized effects on the antigenic structure of poliovirus and similarly constituted virions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, D C -- Jameson, B A -- Bonin, J -- Kohara, M -- Abe, S -- Itoh, H -- Komatsu, T -- Arita, M -- Kuge, S -- Nomoto, A -- AI-15122/AI/NIAID NIH HHS/ -- CA-28146/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1090-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2412292" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Antibodies, Monoclonal ; Epitopes/*analysis ; Immunity, Innate ; Mutation ; Phenotype ; Poliovirus/genetics/*immunology ; Virion/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    The x gene is essential for HTLV replication (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-05
    Description: The human T-cell leukemia viruses (HTLV) are associated with T-cell malignancies in man and will transform normal human T cells in vitro. The mechanism of malignant transformation by HTLV is unknown but appears to be distinct from that of other classes of retroviruses, which induce malignant transformation through viral or cellular oncogenes. Recently a new gene, termed x, was identified in HTLV. This gene has been hypothesized to be the transforming gene of HTLV because of its conservation within the HTLV class of retroviruses. By in vitro mutagenesis of the HTLV-II x gene, it is now demonstrated that the presence of a functional x gene product is necessary for efficient HTLV transcription. Therefore, these studies provide direct evidence for an important function of the x gene in HTLV replication. The functional analogies between the x gene and transcriptional regulatory genes of some DNA viruses suggest that these viruses share similar mechanisms for cellular transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, I S -- Slamon, D J -- Rosenblatt, J D -- Shah, N P -- Quan, S G -- Wachsman, W -- CA 09297/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):54-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990037" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Deltaretrovirus/*genetics/growth & development ; Genes, Viral ; Humans ; Mutation ; RNA, Viral/*biosynthesis ; Transcription, Genetic ; *Virus Replication
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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    Prooxidant states and tumor promotion (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-01-25
    Description: There is convincing evidence that cellular prooxidant states--that is, increased concentrations of active oxygen and organic peroxides and radicals--can promote initiated cells to neoplastic growth. Prooxidant states can be caused by different classes of agents, including hyperbaric oxygen, radiation, xenobiotic metabolites and Fenton-type reagents, modulators of the cytochrome P-450 electron-transport chain, peroxisome proliferators, inhibitors of the antioxidant defense, and membrane-active agents. Many of these agents are promoters or complete carcinogens. They cause chromosomal damage by indirect action, but the role of this damage in carcinogenesis remains unclear. Prooxidant states can be prevented or suppressed by the enzymes of the cellular antioxidant defense and low molecular weight scavenger molecules, and many antioxidants are antipromoters and anticarcinogens. Finally, prooxidant states may modulate the expression of a family of prooxidant genes, which are related to cell growth and differentiation, by inducing alterations in DNA structure or by epigenetic mechanisms, for example, by polyadenosine diphosphate-ribosylation of chromosomal proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerutti, P A -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):375-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antioxidants/pharmacology ; *Carcinogens/metabolism/pharmacology ; Cations/metabolism ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Membrane/physiology ; *Cell Transformation, Neoplastic ; Chromosome Aberrations ; Chromosomes/drug effects ; Cytochrome P-450 Enzyme System/metabolism ; DNA/metabolism ; Electron Transport ; Gene Expression Regulation ; Humans ; Hydrogen Peroxide/metabolism ; Hydroxides/metabolism ; Hydroxyl Radical ; Lipid Peroxides/metabolism ; Microbodies/metabolism ; Mutation ; Neoplasms/*chemically induced ; Oxidation-Reduction ; Oxygen/*metabolism/physiology ; Poly Adenosine Diphosphate Ribose/metabolism ; Singlet Oxygen ; Sulfhydryl Compounds/physiology ; Superoxides/metabolism ; Ultraviolet Rays
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Cell interactions in myxobacterial growth and development (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-10-04
    Description: During their complex life cycle, myxobacteria manifest a number of cell interactions. These include contact-mediated interactions as well as those mediated by soluble extracellular signals. Some of these interactions are well-defined; in addition, the tools for molecular and genetic analysis of these interactions in Myxococcus xanthus are now available.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dworkin, M -- Kaiser, D -- GM19957/GM/NIGMS NIH HHS/ -- GM23441/GM/NIGMS NIH HHS/ -- GM34317/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Oct 4;230(4721):18-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3929384" target="_blank"〉PubMed〈/a〉
    Keywords: Microscopy, Electron, Scanning ; Movement ; Mutation ; Myxococcales/genetics/*growth & development ; Spores, Bacterial ; Transduction, Genetic
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  • 22
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    Evolution in inbred strains of mice appears rapid (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-07
    Description: Genetic variation at 97 loci in ten commonly used inbred strains of mice is greatly in excess of that expected under current assumptions. Evidence against all of the readily apparent explanations is presented and the possibility of early selection for heterozygosity or of conversion is suggested. The common ancestor of these strains is estimated to have occurred about 150 years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fitch, W M -- Atchley, W R -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1169-75.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001935" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Heterozygote ; Mice ; Mice, Inbred Strains/*genetics ; Mutation ; Species Specificity ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 23
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    Measuring gene expression with light (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-03-15
    Description: Light is produced by recombinant Escherichia coli that contain lux genes cloned from the marine bacterium Vibrio fischeri. The bioluminescence phenotype requires genes for regulatory and biochemical functions, the latter encoded by five lux genes contained in a single operon. These lux genes were disconnected from their native promoter and inserted into the transposon mini-Mu. The resulting transposon, mini-Mulux, could induce mutations by insertional inactivation of a target gene, and the lux DNA was oriented to align target gene transcription with that of the lux genes. Genes in Escherichia coli and Vibrio parahaemolyticus were mutagenized, and mutants containing transposon-generated lux gene fusions produced light as a function of target gene transcription. Light production offers a simple, sensitive, in vivo indicator of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engebrecht, J -- Simon, M -- Silverman, M -- New York, N.Y. -- Science. 1985 Mar 15;227(4692):1345-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2983423" target="_blank"〉PubMed〈/a〉
    Keywords: DNA Transposable Elements ; DNA, Recombinant/*metabolism ; Escherichia coli/genetics ; *Gene Expression Regulation ; Luciferases/genetics ; Luminescence ; Luminescent Proteins/*genetics ; Mutation ; Phenotype ; Protein Biosynthesis ; Vibrio/genetics ; Vibrio parahaemolyticus/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 24
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    Construction and recovery of viable retroviral genomes carrying a bacterial suppressor transfer RNA gene (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-04-19
    Description: The integration of retroviral genomes into cellular DNA can induce mutations by altering the expression of nearby cellular genes and can serve to identify the gene affected. The construction of a retrovirus that stably carries a suppressor transfer RNA gene from Escherichia coli has allowed facile recovery of the viral genome in vectors marked with amber mutations. This virus can be used for rapid isolation of cellular sequences at the site of proviral insertion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lobel, L I -- Patel, M -- King, W -- Nguyen-Huu, M C -- Goff, S P -- 2 P30 CA 23767/CA/NCI NIH HHS/ -- R01 CA 37176/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):329-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2984770" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Transposable Elements ; DNA, Recombinant/metabolism ; DNA, Viral/genetics ; Escherichia coli/genetics ; *Genes, Bacterial ; *Genes, Viral ; Moloney murine leukemia virus/genetics ; Mutation ; Nucleic Acid Hybridization ; RNA, Transfer/*genetics ; Retroviridae/*genetics ; *Suppression, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 25
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    The action of oncogenes in the cytoplasm and nucleus (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: As many as 40 distinct oncogenes of viral and cellular origin have been identified to date. Many of these genes can be grouped into functional classes on the basis of their effects on cellular phenotype. These groupings suggest a small number of mechanisms of action of the oncogene-encoded proteins. Some data suggest that, in the cytoplasm, these proteins may regulate levels of critical second messenger molecules; in the nucleus, these proteins may modulate the activity of the cell's transcriptional machinery. Many of the gene products can also be related to a signaling pathway that determines the cell's response to growth-stimulating factors. Because some of these genes are expressed in nongrowing, differentiated cells, the encoded proteins may in certain tissues mediate functions that are unrelated to cellular growth control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinberg, R A -- CA39826/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):770-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; Cell Nucleus/metabolism ; Cell Transformation, Neoplastic/metabolism ; Chickens ; Cytoplasm/metabolism ; DNA Tumor Viruses/genetics ; Deltaretrovirus/genetics ; Drosophila ; Epidermal Growth Factor/physiology ; Growth Substances/physiology ; Guanosine Triphosphate/metabolism ; Humans ; Mutation ; Neoplasms/genetics ; *Oncogenes ; Platelet-Derived Growth Factor/physiology ; Polyomavirus/genetics ; Proto-Oncogenes ; Rats ; Repetitive Sequences, Nucleic Acid ; Retroviridae/genetics ; Simian virus 40/genetics ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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