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  • Mutation  (53)
  • American Association for the Advancement of Science (AAAS)  (53)
  • Elsevier
  • International Union of Crystallography (IUCr)
  • 1985-1989  (53)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (53)
  • Elsevier
  • International Union of Crystallography (IUCr)
  • Springer  (3)
  • Wiley-Blackwell  (1)
Years
Year
  • 1
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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
    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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    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
    Print ISSN: 0036-8075
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  • 3
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    Mutants of pertussis toxin suitable for vaccine development (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-10-27
    Description: Immunization with chemically detoxified pertussis toxin can prevent severe whooping cough with an efficacy similar to that of the cellular pertussis vaccine, which normally gives unwanted side effects. To avoid the reversion to toxicity and the loss of immunogenicity that may follow chemical treatment of pertussis toxin, inactive toxins were constructed by genetic manipulation. A number of genetically engineered alleles of the pertussis toxin genes, constructed by replacing either one or two key amino acids within the enzymatically active S1 subunit, were introduced into the chromosome of strains of Bordetella pertussis, B. parapertussis, and B. bronchiseptica. These strains produce mutant pertussis toxin molecules that are nontoxic and immunogenic and that protect mice from the intracerebral challenge with virulent Bordetella pertussis. Such molecules are ideal for the development of new and safer vaccines against whooping cough.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizza, M -- Covacci, A -- Bartoloni, A -- Perugini, M -- Nencioni, L -- De Magistris, M T -- Villa, L -- Nucci, D -- Manetti, R -- Bugnoli, M -- New York, N.Y. -- Science. 1989 Oct 27;246(4929):497-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sclavo Research Center, Siena, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2683073" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Genetic Techniques ; Mice ; Mice, Inbred BALB C ; Mutation ; *Pertussis Toxin ; Pertussis Vaccine/*toxicity ; Rabbits ; Vaccines, Synthetic/toxicity ; Virulence Factors, Bordetella/genetics/immunology/*toxicity
    Print ISSN: 0036-8075
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  • 4
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    Identification of the fusion peptide of primate immunodeficiency viruses (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-12
    Description: Membrane fusion induced by the envelope glycoproteins of human and simian immunodeficiency viruses (HIV and SIVmac) is a necessary step for the infection of CD4 cells and for the formation of syncytia after infection. Identification of the region in these molecules that mediates the fusion events is important for understanding and possibly interfering with HIV/SIVmac infection and pathogenesis. Amino acid substitutions were made in the 15 NH2-terminal residues of the SIVmac gp32 transmembrane glycoprotein, and the mutants were expressed in recombinant vaccinia viruses, which were then used to infect CD4-expressing T cell lines. Mutations that increased the overall hydrophobicity of the gp32 NH2-terminus increased the ability of the viral envelope to induce syncytia formation, whereas introduction of polar or charged amino acids in the same region abolished the fusogenic function of the viral envelope. Hydrophobicity in the NH2-terminal region of gp32 may therefore be an important correlate of viral virulence in vivo and could perhaps be exploited to generate a more effective animal model for the study of acquired immunodeficiency syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bosch, M L -- Earl, P L -- Fargnoli, K -- Picciafuoco, S -- Giombini, F -- Wong-Staal, F -- Franchini, G -- New York, N.Y. -- Science. 1989 May 12;244(4905):694-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tumor Cell Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2541505" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cloning, Molecular ; DNA, Viral/genetics ; *Gene Products, env ; HIV/*analysis ; HIV Antigens/metabolism ; HIV Envelope Protein gp120 ; HIV Envelope Protein gp41 ; Humans ; Membrane Glycoproteins ; Molecular Sequence Data ; Mutation ; *Retroviridae Proteins/genetics/metabolism/pharmacology ; *Retroviridae Proteins, Oncogenic ; Retroviruses, Simian/*analysis ; Structure-Activity Relationship ; T-Lymphocytes, Helper-Inducer/microbiology ; Transfection ; Vaccinia virus/genetics ; *Viral Envelope Proteins/genetics/metabolism/pharmacology ; *Viral Fusion Proteins
    Print ISSN: 0036-8075
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  • 5
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    HTLV x gene mutants exhibit novel transcriptional regulatory phenotypes (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-02-06
    Description: The human T-cell leukemia viruses, HTLV-I and HTLV-II, contain a gene, termed x, with transcriptional regulatory function. The properties of the x proteins were analyzed by constructing mutant genes containing site-directed deletions and point mutations. The results demonstrate that the amino terminal 17 amino acids of the x protein constitute part of a functional domain that is critical for the transcriptional activating properties of the protein. Within this region, substitution of a leucine residue for a proline residue results in major changes in the trans-activation phenotype of the protein. The mutant HTLV-II x protein, though incapable of activating the HTLV-II long terminal repeat, will block trans-activation of the HTLV-II long terminal repeat by the wild-type protein. The altered phenotype of this mutant suggests a potential negative regulatory function of the x protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wachsman, W -- Cann, A J -- Williams, J L -- Slamon, D J -- Souza, L -- Shah, N P -- Chen, I S -- CA 30388/CA/NCI NIH HHS/ -- CA 32727/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Feb 6;235(4789):674-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027894" target="_blank"〉PubMed〈/a〉
    Keywords: Deltaretrovirus/*genetics ; Gene Expression Regulation ; *Genes, Viral ; Mutation ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 6
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    ADP-ribosyltransferase activity of pertussis toxin and immunomodulation by Bordetella pertussis (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-29
    Description: Pertussis toxin is produced by the causative agent of whooping cough, Bordetella pertussis, and is an adenosine diphosphate (ADP)-ribosyltransferase capable of covalently modifying and thereby inactivating many eukaryotic G proteins involved in cellular metabolism. The toxin is a principal determinant of virulence in whooping cough and is a primary candidate for an acellular pertussis vaccine, yet it is unclear whether the ADP-ribosyltransferase activity is required for both pathogenic and immunoprotective activities. A B. pertussis strain that produced an assembled pertussis holotoxin with only 1 percent of the ADP-ribosyltransferase activity of the native toxin was constructed and was found to be deficient in pathogenic activities associated with B. pertussis including induction of leukocytosis, potentiation of anaphylaxis, and stimulation of histamine sensitivity. Moreover, this mutant strain failed to function as an adjuvant and was less effective in protecting mice from intracerebral challenge infection. These data suggest that the ADP-ribosyltransferase activity is necessary for both pathogenicity and optimum immunoprotection. These findings bear directly on the design of a nontoxic pertussis vaccine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Black, W J -- Munoz, J J -- Peacock, M G -- Schad, P A -- Cowell, J L -- Burchall, J J -- Lim, M -- Kent, A -- Steinman, L -- Falkow, S -- AI-22462/AI/NIAID NIH HHS/ -- AI-23945/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):656-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2896387" target="_blank"〉PubMed〈/a〉
    Keywords: ADP Ribose Transferases ; Adjuvants, Immunologic ; Anaphylaxis/etiology ; Animals ; Antigens/immunology ; Bordetella pertussis/enzymology/genetics/*immunology ; Codon ; Drug Tolerance ; Histamine/pharmacology ; Immunization ; Leukocytosis/etiology ; Macromolecular Substances ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mutation ; Ovalbumin/immunology ; Pentosyltransferases/*metabolism ; *Pertussis Toxin ; Virulence Factors, Bordetella/genetics/immunology/*metabolism
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  • 7
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    Two mutant alleles of the insulin receptor gene in a patient with extreme insulin resistance (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-06
    Description: Insulin receptor complementary DNA has been cloned from an insulin-resistant patient with leprechaunism whose receptors exhibited multiple abnormalities in insulin binding. The patient is a compound heterozygote, having inherited two different mutant alleles of the insulin receptor gene. One allele contains a missense mutation encoding the substitution of glutamic acid for lysine at position 460 in the alpha subunit of the receptor. The second allele has a nonsense mutation causing premature chain termination after amino acid 671 in the alpha subunit, thereby deleting both the transmembrane and tyrosine kinase domains of the receptor. Interestingly, the father is heterozygous for this nonsense mutation and exhibits a moderate degree of insulin resistance. This raises the possibility that mutations in the insulin receptor gene may account for the insulin resistance in some patients with non-insulin-dependent diabetes mellitus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kadowaki, T -- Bevins, C L -- Cama, A -- Ojamaa, K -- Marcus-Samuels, B -- Kadowaki, H -- Beitz, L -- McKeon, C -- Taylor, S I -- New York, N.Y. -- Science. 1988 May 6;240(4853):787-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry and Molecular Pathophysiology Section, National Institute of Diabetes, Digestive, and Kidney Disease, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2834824" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cell Line ; Cell Membrane/metabolism ; Cell Transformation, Viral ; DNA/genetics ; Diabetes Mellitus, Type 2/*genetics ; Endocrine System Diseases/genetics ; Female ; Gene Amplification ; Growth Disorders/genetics ; Herpesvirus 4, Human ; Heterozygote ; Humans ; Hydrogen-Ion Concentration ; Insulin/blood ; Insulin Resistance/*genetics ; Lymphocytes/metabolism ; Monocytes/metabolism ; Mutation ; Receptor, Insulin/*genetics ; Syndrome ; Transfection
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  • 8
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    Infectious mutants of HTLV-III with changes in the 3' region and markedly reduced cytopathic effects (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-08
    Description: A variant of human T-lymphotropic virus type III (HTLV-III) is described that replicates but does not kill normal human T cells in vitro. This variant, designated X10-1, was derived from the genome of a cytopathic HTLV-III clone (pHXB2D) by excision of a 200-base pair segment in the 3' region of the virus, spanning the env and 3'-orf genes. Comparable variants with 55 to 109 base pairs deleted exclusively in 3'-orf produced, in contrast, virus that was extremely cytopathic. On the basis of these findings it is concluded that the 3'-orf gene is not required for cytopathogenicity or replication of HTLV-III. In addition, the results suggest that virus replication and cytotoxicity are not intrinsically coupled. Furthermore, since clone X10-1 retains the ability to trans-activate genes linked to the viral long terminal repeats, trans-activation per se is not responsible for T-cell killing by HTLV-III. These results also raise the possibility that the carboxyl terminus of the envelope gene of HTLV-III has a direct role in T-cell killing by this virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fisher, A G -- Ratner, L -- Mitsuya, H -- Marselle, L M -- Harper, M E -- Broder, S -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1986 Aug 8;233(4764):655-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014663" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Cloning, Molecular ; Deltaretrovirus/*genetics/pathogenicity ; Humans ; Mutation ; Nucleic Acid Hybridization ; RNA, Viral/genetics ; T-Lymphocytes/microbiology
    Print ISSN: 0036-8075
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  • 9
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    Fidelity of HIV-1 reverse transcriptase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-25
    Description: The human immunodeficiency virus type 1 (HIV-1) shows extensive genetic variation and undergoes rapid evolution. The fidelity of purified HIV-1 reverse transcriptase was measured during DNA polymerization in vitro by means of three different assays. Reverse transcriptase from HIV-1 introduced base-substitution errors in DNA from the bacteriophage phi X174 amber3 at estimated frequencies of 1/2000 to 1/4000. Analyses of misincorporation rates opposite a single template adenine residue showed that HIV-1 reverse transcriptase catalyzed nucleotide mismatches with a specificity of A:C much greater than A:G greater than A:A. The high error rate of HIV-1 reverse transcriptase in vitro translates to approximately five to ten errors per HIV-1 genome per round of replication in vivo. This high error rate suggests that misincorporation by HIV-1 reverse transcriptase is, at least in part, responsible for the hypermutability of the AIDS virus. The specificity of misincorporation may provide a basis for the systematic construction of antiviral nucleosides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, B D -- Poiesz, B J -- Loeb, L A -- CA-07263-03/CA/NCI NIH HHS/ -- N01AI72654/AI/NIAID NIH HHS/ -- R35-CA-39903/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 25;242(4882):1168-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2460924" target="_blank"〉PubMed〈/a〉
    Keywords: Avian Myeloblastosis Virus/enzymology ; Bacteriophage phi X 174/genetics ; DNA/*biosynthesis ; DNA Polymerase II/metabolism ; DNA, Viral/biosynthesis ; Electrophoresis, Polyacrylamide Gel ; HIV/*enzymology/genetics ; Kinetics ; Moloney murine leukemia virus/enzymology ; Mutation ; Nucleotides/metabolism ; RNA-Directed DNA Polymerase/*metabolism
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  • 10
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    Structural rearrangement of the retinoblastoma gene in human breast carcinoma (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: Structural changes of the human retinoblastoma gene have been demonstrated previously in retinoblastoma and some clinically related tumors including osteosarcoma. Structural aberrations of the retinoblastoma locus (RB1) were observed in 25% of breast tumor cell lines studied and 7% of the primary tumors. These changes include homozygous internal deletions and total deletion of RB1; a duplication of an exon was observed in one of the cell lines. In all cases, structural changes either resulted in the absence or truncation of the RB1 transcript. No obvious defect in RB1 was detected by DNA blot analysis in primary tumors or cell lines from Wilms' tumor, cervical carcinoma, or hepatoma. These results further support the concept that the human RB1 gene has pleiotropic effects on specific types of cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉T'Ang, A -- Varley, J M -- Chakraborty, S -- Murphree, A L -- Fung, Y K -- CA44754/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):263-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology/Oncology, Childrens Hospital of Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175651" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*genetics ; Chromosome Aberrations ; Chromosomes, Human, Pair 13 ; DNA/genetics ; DNA Probes ; Exons ; Eye Neoplasms/*genetics ; Female ; *Gene Rearrangement ; Homozygote ; Humans ; Lymphatic Metastasis ; Menopause ; Mutation ; Nucleic Acid Hybridization ; Retinoblastoma/*genetics ; Risk Factors ; Tumor Cells, Cultured
    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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