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  • Articles  (897)
  • Life and Medical Sciences  (793)
  • Base Sequence  (62)
  • Cell Line  (46)
  • Organic Chemistry
  • 1985-1989  (897)
  • 1986  (897)
  • Medicine  (897)
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  • Articles  (897)
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  • 1985-1989  (897)
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  • 1
    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
    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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    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
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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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    American Association for the Advancement of Science (AAAS)
    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
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  • 5
    Publication Date: 1986-08-22
    Description: Continuous measurement and imaging of the intracellular free calcium ion concentration ([Ca2+]i) of mitotic and interphase PtK1 cells was accomplished with the new fluorescent Ca2+ indicator fura-2. No statistically significant difference between basal [Ca2+]i of interphase and mitotic cells was detected. However, mitotic cells showed a rapid elevation of [Ca2+]i from basal levels of 130 nM to 500 to 800 nM at the metaphase-anaphase transition. The [Ca2+]i transient was brief, lasting approximately 20 seconds and the elevated [Ca2+]i appeared uniformly distributed over the entire spindle and central region of the cell. The close temporal association of the [Ca2+]i transient with the onset of anaphase suggests that calcium may have a signaling role in this event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poenie, M -- Alderton, J -- Steinhardt, R -- Tsien, R -- EY04372/EY/NEI NIH HHS/ -- GM31004/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 22;233(4766):886-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3755550" target="_blank"〉PubMed〈/a〉
    Keywords: *Anaphase ; Animals ; Benzofurans ; Calcium/*metabolism ; Cell Line ; Fluorescent Dyes ; Fura-2 ; Mitosis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1986-03-28
    Description: The genome of the human T-lymphotropic virus type III (HTLV-III/LAV) has the potential to encode at least three polypeptides in addition to those encoded by the gag, pol, and env genes. In this study, the product of the sor (short open reading frame) region, which overlaps the 3' end of the pol gene, was found to be a protein with a molecular weight of 23,000. An assay was developed for testing the ability of cloned HTLV-III proviruses to produce viruses cytopathic for T4+ lymphocytes. In the cell line used, C8166, neither the HTLV-III sor gene product nor the complete 3'-orf gene product were necessary for the replication or cytopathic effects of the HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodroski, J -- Goh, W C -- Rosen, C -- Tartar, A -- Portetelle, D -- Burny, A -- Haseltine, W -- CA07580/CA/NCI NIH HHS/ -- CA40658/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 28;231(4745):1549-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006244" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cytopathogenic Effect, Viral ; Deltaretrovirus/*genetics/pathogenicity ; *Genes, Viral ; Humans ; Retroviridae Proteins/genetics ; T-Lymphocytes/microbiology ; *Virus Replication
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  • 7
    Publication Date: 1986-04-04
    Description: Experiments were conducted to isolate and characterize the gene and gene product of a human hematopoietic colony-stimulating factor with pluripotent biological activities. This factor has the ability to induce differentiation of a murine myelomonocytic leukemia cell line WEHI-3B(D+) and cells from patients with newly diagnosed acute nonlymphocytic leukemia (ANLL). A complementary DNA copy of the gene encoding a pluripotent human granulocyte colony-stimulating factor (hG-CSF) was cloned and expressed in Escherichia coli. The recombinant form of hG-CSF is capable of supporting neutrophil proliferation in a CFU-GM assay. In addition, recombinant hG-CSF can support early erythroid colonies and mixed colony formation. Competitive binding studies done with 125I-labeled hG-CSF and cell samples from two patients with newly diagnosed human leukemias as well as WEHI-3B(D+) cells showed that one of the human leukemias (ANLL, classified as M4) and the WEHI-3B(D+) cells have receptors for hG-CSF. Furthermore, the murine WEHI-3B(D+) cells and human leukemic cells classified as M2, M3, and M4 were induced by recombinant hG-CSF to undergo terminal differentiation to macrophages and granulocytes. The secreted form of the protein produced by the bladder carcinoma cell line 5637 was found to be O-glycosylated and to have a molecular weight of 19,600.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Souza, L M -- Boone, T C -- Gabrilove, J -- Lai, P H -- Zsebo, K M -- Murdock, D C -- Chazin, V R -- Bruszewski, J -- Lu, H -- Chen, K K -- CA00966/CA/NCI NIH HHS/ -- CA20194/CA/NCI NIH HHS/ -- CA32516/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):61-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2420009" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Cell Line ; Colony-Forming Units Assay ; Colony-Stimulating Factors/genetics/*pharmacology ; DNA/metabolism ; Escherichia coli/genetics ; Genes ; Granulocyte Colony-Stimulating Factor ; Granulocytes/*physiology ; Humans ; Leukemia/*pathology ; Leukemia, Myeloid/pathology ; Mice ; Plasmids ; Recombinant Proteins/*pharmacology
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  • 8
    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
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  • 9
    Publication Date: 1986-10-24
    Description: The protein product of oncogene c-myc is believed to be important in regulation of the cell cycle. However, its direct role in DNA synthesis has not been explored. Experiments presented here show that the addition of affinity-purified antibodies against the human c-myc protein to nuclei isolated from several types of human cells reversibly inhibited DNA synthesis and DNA polymerase activity of these nuclei. This suggests that c-myc encodes a protein that is functionally involved in DNA synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Studzinski, G P -- Brelvi, Z S -- Feldman, S C -- Watt, R A -- New York, N.Y. -- Science. 1986 Oct 24;234(4775):467-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3532322" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cell Nucleus/physiology ; Cell-Free System ; DNA/biosynthesis ; *DNA Replication ; Humans ; Immunologic Techniques ; Nucleic Acid Synthesis Inhibitors ; Proto-Oncogene Proteins/*physiology ; *Proto-Oncogenes
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  • 10
    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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