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  • Articles  (886)
  • Life and Medical Sciences  (793)
  • Base Sequence  (62)
  • Nucleic Acid Hybridization  (44)
  • Organic Chemistry
  • 1985-1989  (886)
  • 1986  (886)
  • Medicine  (886)
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  • Articles  (886)
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  • 1985-1989  (886)
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  • 1
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    Identification of specific transducin alpha subunits in retinal rod and cone photoreceptors (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-10-03
    Description: Transducin is a guanyl nucleotide-binding protein that couples rhodopsin photolysis to hydrolysis of guanosine 3',5'-monophosphate in rod photoreceptor cells of vertebrate retinas. Several complementary DNA clones encoding transducin subunits have recently been characterized. One clone, isolated from a bovine retina complementary DNA library, encodes a previously unidentified polypeptide with an amino acid sequence 78% identical to the sequence of the alpha subunit of bovine rod outer segment transducin. Antibodies to a synthetic peptide with amino acid sequence derived specifically from this novel polypeptide recognize a 41-kilodalton polypeptide in homogenates of bovine retina. Localization of this polypeptide in bovine retina by indirect immunofluorescence demonstrates that it is expressed only in cone outer segments. Antibodies to specific sequences found only in the rod transducin alpha subunit recognize a polypeptide localized only in the rod outer segment. Therefore, bovine rod and cone cells each express structurally related yet significantly different forms of transducin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerea, C L -- Somers, D E -- Hurley, J B -- Klock, I B -- Bunt-Milam, A H -- EYO 1311/EY/NEI NIH HHS/ -- EYO 1730/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1986 Oct 3;234(4772):77-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3529395" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; DNA/genetics ; Fluorescent Antibody Technique ; Membrane Proteins/genetics/*physiology ; Photoreceptor Cells/*metabolism ; Transducin
    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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    Structural heterogeneity and functional domains of murine immunoglobulin G Fc receptors (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-07
    Description: Binding of antibodies to effector cells by way of receptors to their constant regions (Fc receptors) is central to the pathway that leads to clearance of antigens by the immune system. The structure and function of this important class of receptors on immune cells is addressed through the molecular characterization of Fc receptors (FcR) specific for the murine immunoglobulin G isotype. Structural diversity is encoded by two genes that by alternative splicing result in expression of molecules with highly conserved extracellular domains and different transmembrane and intracytoplasmic domains. The proteins encoded by these genes are members of the immunoglobulin supergene family, most homologous to the major histocompatibility complex molecule E beta. Functional reconstitution of ligand binding by transfection of individual FcR genes demonstrates that the requirements for ligand binding are encoded in a single gene. These studies demonstrate the molecular basis for the functional heterogeneity of FcR's, accounting for the possible transduction of different signals in response to a single ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravetch, J V -- Luster, A D -- Weinshank, R -- Kochan, J -- Pavlovec, A -- Portnoy, D A -- Hulmes, J -- Pan, Y C -- Unkeless, J C -- AI 24322/AI/NIAID NIH HHS/ -- GM 36306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 7;234(4777):718-25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2946078" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/genetics ; Gene Expression Regulation ; Histocompatibility Antigens Class II/genetics ; Immunoglobulin G ; Lymphocytes/*physiology ; Macrophages/*physiology ; Membrane Proteins ; Mice ; Protein Conformation ; *Receptors, Fc/genetics ; Receptors, IgG ; Transcription, Genetic ; Transfection
    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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  • 3
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    Human multidrug-resistant cell lines: increased mdr1 expression can precede gene amplification (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-02
    Description: The development of simultaneous resistance to multiple structurally unrelated drugs is a major impediment to cancer chemotherapy. Multidrug resistance in human KB carcinoma cells selected in colchicine, vinblastine, or Adriamycin is associated with amplification of specific DNA sequences (the multidrug resistance locus, mdr1). During colchicine selection resistance is initially accompanied by elevated expression of a 4.5-kilobase mdr1 messenger RNA (mRNA) without amplification of the corresponding genomic sequences. During selection for increased levels of resistance, expression of this mRNA is increased simultaneously with amplification of mdr1 DNA. Increased expression and amplification of mdr1 sequences were also found in multidrug-resistant sublines of human leukemia and ovarian carcinoma cells. These results suggest that increased expression of mdr1 mRNA is a common mechanism for multidrug resistance in human cells. Activation of the mdr1 gene by mutations or epigenetic changes may precede its amplification during the development of resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shen, D W -- Fojo, A -- Chin, J E -- Roninson, I B -- Richert, N -- Pastan, I -- Gottesman, M M -- New York, N.Y. -- Science. 1986 May 2;232(4750):643-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3457471" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Colchicine/pharmacology ; Cricetinae ; Cricetulus ; DNA, Neoplasm/genetics ; Doxorubicin/pharmacology ; *Drug Resistance ; Female ; *Gene Amplification ; Humans ; Leukemia, Lymphoid/drug therapy ; Neoplasms/*drug therapy/genetics ; Nucleic Acid Hybridization ; Ovarian Neoplasms/drug therapy ; RNA, Messenger/genetics ; Vinblastine/pharmacology
    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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  • 4
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    Tandem duplication of D-loop and ribosomal RNA sequences in lizard mitochondrial DNA (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-09-26
    Description: Some Cnemidophorus exsanguis have mitochondrial DNA's (mtDNA's) that are 22.2 kilobases (kb) in size, whereas most have mtDNA's of 17.4 kb. Restriction site mapping, DNA transfer hybridization experiments, and electron microscopy show that the size increment stems from the tandem duplication of a 4.8-kb region that includes regulatory sequences and transfer and ribosomal RNA genes. This observation is notable in that sequences outside of the control region are involved in major length variation. Besides revealing a novel form of mtDNA evolution in animals, these duplications provide a useful system for investigating the molecular and evolutionary biology of animal mtDNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moritz, C -- Brown, W M -- GM30144/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Sep 26;233(4771):1425-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3018925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA Restriction Enzymes ; DNA, Mitochondrial/*genetics ; Lizards ; Microscopy, Electron ; Nucleic Acid Conformation ; Nucleic Acid Hybridization ; RNA, Ribosomal/*genetics ; Repetitive Sequences, 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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  • 5
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    Equine infectious anemia virus gag and pol genes: relatedness to visna and AIDS virus (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-02-07
    Description: Comparison of HTLV-III, the putative AIDS virus, with other related viruses, may help to reveal more about the origin of AIDS in humans. In this study, the nucleotide sequence of the gag and pol genes of an equine infectious anemia virus (EIAV) proviral DNA clone was determined. The sequence was compared with that of HTLV-III and of visna, a pathogenic lentivirus of sheep. The results show that these viruses constitute a family clearly distinct from that of the type C viruses or the BLV-HTLV-I and -II group. Within the family, EIAV, HTLV-III, and visna appear to be equally divergent from a common evolutionary ancestor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, R M -- Casey, J W -- Rice, N R -- N0I-C-23909/PHS HHS/ -- New York, N.Y. -- Science. 1986 Feb 7;231(4738):589-94.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3003905" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Codon ; DNA, Viral/genetics ; Deltaretrovirus/*genetics ; *Genes, Viral ; Horses ; Humans ; Infectious Anemia Virus, Equine/*genetics ; Mice ; Visna-maedi virus/*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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  • 6
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    Identification and characterization of the protein encoded by the human N-myc oncogene (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-05-09
    Description: The human N-myc gene is related to the c-myc proto-oncogene, and has been shown to have transforming potential in vitro. Many studies have reported amplification of N-myc in human neuroblastoma and retinoblastoma cell lines. In primary tumors, amplification of the gene was found to correlate directly with behavior of the tumor. Specific restriction fragments of a partial complementary DNA clone of N-myc from LA-N-5 human neuroblastoma cells were placed into a bacterial expression vector for the purpose of producing antigens representative of the N-myc protein. Rabbits immunized with these antigens produced antisera that recognized a protein of 62-64 kilodaltons in neuroblastoma cells. By several criteria, this protein appears to be part of the same proto-oncogene family as the c-myc protein. Moreover, the antisera to fragments of this protein were capable of histochemically identifying malignant cells in clinical specimens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- Boone, T C -- Seeger, R C -- Keith, D E -- Chazin, V -- Lee, H C -- Souza, L M -- CA 16042/CA/NCI NIH HHS/ -- CA 36827/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 May 9;232(4751):768-72.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3008339" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Carcinoma, Small Cell/metabolism ; Immune Sera/immunology ; Immunoenzyme Techniques ; Leukemia, Myeloid, Acute/metabolism ; Lung Neoplasms/metabolism ; Neoplasm Proteins/genetics/*isolation & purification/physiology ; Neuroblastoma/metabolism ; *Oncogenes ; Proto-Oncogene Proteins/genetics/*isolation & purification/physiology ; Proto-Oncogene Proteins c-myc ; Proto-Oncogenes ; Rabbits/immunology
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  • 7
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    Immortalization of human T lymphocytes after transfection of Epstein-Barr virus DNA (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-29
    Description: Epstein-Barr virus (EBV), a ubiquitous human herpesvirus, has the ability to transform human B lymphocytes. No other cell type has been experimentally transformed by EBV, either by intact virions or naked viral DNA and subgenomic fragments. Two immortalized human T-lymphoblastoid cell lines have now been established by transfecting cord blood lymphocytes with purified B95-8 viral DNA enclosed in fusogenic Sendai virus envelopes (RSVE) and then exposing the cells to EBV from a P3HR-1 cell subclone. One of these lines, which has been fully characterized, is termed HBD-1. This line is positive for EBV DNA and expresses surface OKT11, OKT4, and Tac receptors, but not M-1, mu immunoglobulin chains, EBV receptors, or B-1 surface markers. The cells contain fully rearranged T-cell receptor genes and germline immunoglobulin genes. The karyotype of the cells is normal, they do not require interleukin-2 for growth, and do not contain human T-lymphotropic virus type I. However, the HBD-1 cells contain incomplete EBV genomes and express several EBV-determined antigens, including the early antigen type D, membrane antigens, but not EBV-determined nuclear antigen (EBNA). This association of the EBV genome with permanently growing hematopoietic cells of non B-cell lineage should prove useful in studies on the mechanism of EBV-mediated cell transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevenson, M -- Volsky, B -- Hedenskog, M -- Volsky, D J -- CA33386/CA/NCI NIH HHS/ -- CA37465/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 29;233(4767):980-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3016899" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cell Survival ; DNA, Viral/*genetics ; Deltaretrovirus/genetics ; Herpesvirus 4, Human/*genetics ; Humans ; Nucleic Acid Hybridization ; T-Lymphocytes/*microbiology/physiology ; *Transfection
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Suprachiasmatic nucleus vasopressin messenger RNA: circadian variation in normal and Brattleboro rats (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-18
    Description: In situ hybridization of an oligonucleotide probe complementary to vasopressin messenger RNA (mRNA) in sections from normal or Brattleboro rat hypothalami revealed hybridization densities in each of three vasopressin-rich nuclei: the supraoptic, paraventricular, and suprachiasmatic. When entrained to a daily light-dark cycle, each rat strain displayed diurnal variation in hybridizable mRNA in the suprachiasmatic, but not in the supraoptic or paraventricular nuclei. The higher values for suprachiasmatic mRNA in the morning correlate well with previously elucidated morning increases in vasopressin immunoreactivity in the cerebrospinal fluid. These results support the utility of in situ hybridization techniques for elucidating physiological influences on regional peptidergic function, are consistent with a prominent role for vasopressinergic suprachiasmatic neurons in generating the cerebrospinal fluid vasopressin rhythm, and suggest that regulation of this mRNA rhythm is not dependent on release of intact peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Uhl, G R -- Reppert, S M -- New York, N.Y. -- Science. 1986 Apr 18;232(4748):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3961487" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; *Circadian Rhythm ; Nucleic Acid Hybridization ; Paraventricular Hypothalamic Nucleus/analysis/physiology ; RNA, Messenger/*analysis/isolation & purification ; Rats ; Rats, Brattleboro ; Rats, Inbred Strains ; Suprachiasmatic Nucleus/*analysis/physiology ; Supraoptic Nucleus/analysis/physiology ; Vasopressins/genetics/*physiology
    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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  • 9
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    The 35-nucleotide spliced leader sequence is common to all trypanosome messenger RNA's (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-01
    Description: In Trypanosomatidae the messenger RNA's (mRNA's) that code for the variant surface glycoproteins (VSG's), tubulins, calmodulin, and at least a subset of other proteins contain a common 35-nucleotide leader sequence at their 5' ends. Hybrid-arrested in vitro translation has been used to show that all mRNA's in both African and South American trypanosomes contain this 35-nucleotide sequence. Oligonucleotides complementary to this sequence blocked translation of all trypanosome mRNA's in a rabbit reticulocyte lysate system, but did not inhibit translation of mRNA's from other organisms lacking this sequence. An oligonucleotide complementary to the VSG mRNA downstream from the spliced leader sequence arrested only VSG synthesis. Thus, the 35-nucleotide leader sequence is a general feature of all trypanosome mRNA's. The high specificity of oligonucleotides complementary to the spliced leader for their target sequence suggests that analogues permeable to the cell membrane may be useful in the treatment of trypanosomal infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walder, J A -- Eder, P S -- Engman, D M -- Brentano, S T -- Walder, R Y -- Knutzon, D S -- Dorfman, D M -- Donelson, J E -- AI-18954/AI/NIAID NIH HHS/ -- AM-25295/AM/NIADDK NIH HHS/ -- HL-33555/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):569-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3523758" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Protein Biosynthesis ; Protein Sorting Signals/*genetics ; RNA, Messenger/*genetics ; Trypanosoma/*genetics ; Trypanosoma brucei brucei/genetics ; Trypanosoma cruzi/genetics
    Print ISSN: 0036-8075
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  • 10
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    Expression and characterization of the trans-activator of HTLV-III/LAV virus (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-21
    Description: The human T-lymphotropic retrovirus HTLV-III/LAV encodes a trans-activator that increases viral gene expression. We expressed this trans-activator in animal cells and studied its structural and functional characteristics. The putative trans-activator protein was immunoprecipitated from overproducing stable cell lines and shown to migrate as a 14-kilodalton polypeptide on sodium dodecyl sulfate-polyacrylamide gels. S1 nuclease mapping experiments showed that the trans-activator increases the levels of steady-state messenger RNA transcribed from the viral long terminal repeat promoter. Sequences within the R region of the HTLV-III/LAV long terminal repeat are essential for trans-activation. Quantitations of messenger RNA and protein showed that the protein increase was greater than the messenger RNA increase in CV1 and HeLa cells, indicating that more than one mechanism was responsible for the trans-activation and that cell type-specific factors may determine the final level of trans-activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, C M -- Felber, B K -- Paskalis, H -- Pavlakis, G N -- N01-CO-23909/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 21;234(4779):988-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3490693" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Electrophoresis, Polyacrylamide Gel ; Gene Products, rev ; HIV/*genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA, Messenger/analysis ; Retroviridae Proteins/*metabolism ; Transfection ; Viral Proteins/*biosynthesis ; Virus Activation ; rev Gene Products, Human Immunodeficiency Virus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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