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  • Articles  (15)
  • Cell Line  (15)
  • American Association for the Advancement of Science (AAAS)  (15)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Oxford University Press
  • Springer
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  • 1995-1999  (15)
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  • 1997  (15)
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  • Articles  (15)
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  • American Association for the Advancement of Science (AAAS)  (15)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Oxford University Press
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  • 1995-1999  (15)
  • 1980-1984
  • 1960-1964
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  • 1
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    Differential effects of cytolytic T cell subsets on intracellular infection (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: In analyzing mechanisms of protection against intracellular infections, a series of human CD1-restricted T cell lines of two distinct phenotypes were derived. Both CD4(-)CD8(-) (double-negative) T cells and CD8(+) T cells efficiently lysed macrophages infected with Mycobacterium tuberculosis. The cytotoxicity of CD4(-)CD8(-) T cells was mediated by Fas-FasL interaction and had no effect on the viability of the mycobacteria. The CD8(+) T cells lysed infected macrophages by a Fas-independent, granule-dependent mechanism that resulted in killing of bacteria. These data indicate that two phenotypically distinct subsets of human cytolytic T lymphocytes use different mechanisms to kill infected cells and contribute in different ways to host defense against intracellular infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stenger, S -- Mazzaccaro, R J -- Uyemura, K -- Cho, S -- Barnes, P F -- Rosat, J P -- Sette, A -- Brenner, M B -- Porcelli, S A -- Bloom, B R -- Modlin, R L -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1684-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California Los Angeles School of Medicine, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180075" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD1/*immunology ; Antigens, CD95/immunology/metabolism ; Cell Line ; Coculture Techniques ; Colony Count, Microbial ; Cytoplasmic Granules/immunology ; *Cytotoxicity, Immunologic ; Fas Ligand Protein ; Granzymes ; Humans ; Lymphocyte Activation ; Macrophages/*immunology/microbiology ; Membrane Glycoproteins/genetics/immunology/metabolism ; Mycobacterium tuberculosis/growth & development/*immunology ; Perforin ; Phenotype ; Pore Forming Cytotoxic Proteins ; Serine Endopeptidases/metabolism ; Strontium/pharmacology ; T-Lymphocyte Subsets/*immunology ; T-Lymphocytes, Cytotoxic/*immunology
    Print ISSN: 0036-8075
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  • 2
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    Peptide agonist of the thrombopoietin receptor as potent as the natural cytokine (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: Two families of small peptides that bind to the human thrombopoietin receptor and compete with the binding of the natural ligand thrombopoietin (TPO) were identified from recombinant peptide libraries. The sequences of these peptides were not found in the primary sequence of TPO. Screening libraries of variants of one of these families under affinity-selective conditions yielded a 14-amino acid peptide (Ile-Glu-Gly-Pro-Thr-Leu-Arg-Gln-Trp-Leu-Ala-Ala-Arg-Ala) with high affinity (dissociation constant approximately 2 nanomolar) that stimulates the proliferation of a TPO-responsive Ba/F3 cell line with a median effective concentration (EC50) of 400 nanomolar. Dimerization of this peptide by a carboxyl-terminal linkage to a lysine branch produced a compound with an EC50 of 100 picomolar, which was equipotent to the 332-amino acid natural cytokine in cell-based assays. The peptide dimer also stimulated the in vitro proliferation and maturation of megakaryocytes from human bone marrow cells and promoted an increase in platelet count when administered to normal mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cwirla, S E -- Balasubramanian, P -- Duffin, D J -- Wagstrom, C R -- Gates, C M -- Singer, S C -- Davis, A M -- Tansik, R L -- Mattheakis, L C -- Boytos, C M -- Schatz, P J -- Baccanari, D P -- Wrighton, N C -- Barrett, R W -- Dower, W J -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Affymax Research Institute, 4001 Miranda Avenue, Palo Alto, CA 94304, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180079" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Blood Platelets/cytology ; Cell Division ; Cell Line ; Cells, Cultured ; Consensus Sequence ; Dimerization ; Erythropoietin/pharmacology ; Hematopoiesis/drug effects ; Humans ; Megakaryocytes/cytology ; Mice ; Molecular Sequence Data ; *Neoplasm Proteins ; Oligopeptides/*metabolism/*pharmacology ; Peptide Library ; Peptides/metabolism/pharmacology ; Platelet Count ; Proto-Oncogene Proteins/*agonists/metabolism ; *Receptors, Cytokine ; Receptors, Thrombopoietin ; Recombinant Proteins/metabolism/pharmacology ; Thrombopoietin/*metabolism/pharmacology ; Transfection
    Print ISSN: 0036-8075
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  • 3
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    Activation of the G protein Gq/11 through tyrosine phosphorylation of the alpha subunit (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: Various receptors coupled to the heterotrimeric guanine nucleotide-binding protein Gq/11 stimulate formation of inositol-1,4,5-trisphosphate (IP3). Activation of these receptors also induces protein tyrosine phosphorylation. Formation of IP3 in response to stimulated receptors that couple to Gq/11 was blocked by protein tyrosine kinase inhibitors. These inhibitors appeared to act before activation of Gq/11. Moreover, stimulation of receptors coupled to Gq/11 induced phosphorylation on a tyrosine residue (Tyr356) of the Galphaq/11 subunit, and this tyrosine phosphorylation event was essential for Gq/11 activation. Tyrosine phosphorylation of Galphaq/11 induced changes in its interaction with receptors. Therefore, tyrosine phosphorylation of Galphaq/11 appears to regulate the activation of Gq/11 protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Umemori, H -- Inoue, T -- Kume, S -- Sekiyama, N -- Nagao, M -- Itoh, H -- Nakanishi, S -- Mikoshiba, K -- Yamamoto, T -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1878-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Calcium/metabolism ; Carbachol/pharmacology ; Cell Line ; Cricetinae ; Enzyme Inhibitors/pharmacology ; GTP-Binding Proteins/*metabolism ; Genistein ; Inositol 1,4,5-Trisphosphate/metabolism ; Isoflavones/pharmacology ; Phosphorylation ; Phosphotyrosine/*metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Receptors, Cholinergic/*metabolism ; Receptors, Metabotropic Glutamate/*metabolism ; Signal Transduction
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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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    Differential ligand activation of estrogen receptors ERalpha and ERbeta at AP1 sites (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: The transactivation properties of the two estrogen receptors, ERalpha and ERbeta, were examined with different ligands in the context of an estrogen response element and an AP1 element. ERalpha and ERbeta were shown to signal in opposite ways when complexed with the natural hormone estradiol from an AP1 site: with ERalpha, 17beta-estradiol activated transcription, whereas with ERbeta, 17beta-estradiol inhibited transcription. Moreover, the antiestrogens tamoxifen, raloxifene, and Imperial Chemical Industries 164384 were potent transcriptional activators with ERbeta at an AP1 site. Thus, the two ERs signal in different ways depending on ligand and response element. This suggests that ERalpha and ERbeta may play different roles in gene regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paech, K -- Webb, P -- Kuiper, G G -- Nilsson, S -- Gustafsson, J -- Kushner, P J -- Scanlan, T S -- GM 50672/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1508-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143-0446, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/metabolism ; Cell Line ; Diethylstilbestrol/metabolism/pharmacology ; *Enhancer Elements, Genetic ; Estradiol/analogs & derivatives/metabolism/pharmacology ; Estrogen Antagonists/*pharmacology ; Estrogen Receptor alpha ; Estrogen Receptor beta ; Estrogens/*pharmacology ; Female ; HeLa Cells ; Humans ; Ligands ; Piperidines/metabolism/pharmacology ; Polyunsaturated Alkamides ; Raloxifene Hydrochloride ; Rats ; Receptors, Estrogen/*metabolism ; Tamoxifen/metabolism/pharmacology ; Transcription Factor AP-1/*genetics ; *Transcriptional Activation/drug effects ; Transfection ; Tumor Cells, Cultured ; Uterus/metabolism
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  • 5
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    Fluorescence-based isolation of bacterial genes expressed within host cells (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-26
    Description: A selection strategy was devised to identify bacterial genes preferentially expressed when a bacterium associates with its host cell. Fourteen Salmonella typhimurium genes, which were under the control of at least four independent regulatory circuits, were identified to be selectively induced in host macrophages. Four genes encode virulence factors, including a component of a type III secretory apparatus. This selection methodology should be generally applicable to the identification of genes from pathogenic organisms that are induced upon association with host cells or tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valdivia, R H -- Falkow, S -- AI26195/AI/NIAID NIH HHS/ -- DK38707/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 26;277(5334):2007-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. valdivia@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9302299" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/genetics ; Cell Line ; Cloning, Molecular ; Female ; Flow Cytometry ; Fluorescence ; *Gene Expression Regulation, Bacterial ; Green Fluorescent Proteins ; HeLa Cells ; Humans ; Luminescent Proteins/genetics ; Macrophages/*microbiology ; Mice ; Mice, Inbred BALB C ; Microscopy, Fluorescence ; Molecular Sequence Data ; Open Reading Frames ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Salmonella Infections, Animal/microbiology ; Salmonella typhimurium/*genetics/isolation & purification/*pathogenicity ; Spleen/microbiology ; Transcription Factors/genetics ; Virulence/genetics
    Print ISSN: 0036-8075
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  • 6
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    Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: A leucine-rich nuclear export signal (NES) allows rapid export of proteins from cell nuclei. Microinjection studies revealed a role for the guanosine triphosphatase (GTPase) Ran in NES-mediated export. Nuclear injection of a Ran mutant (Thr24 --〉 Asn) blocked protein export but not import, whereas depletion of the Ran nucleotide exchange factor RCC1 blocked protein import but not export. However, injection of Ran GTPase-activating protein (RanGAP) into RCC1-depleted cell nuclei inhibited export. Coinjection with Ran mutants insensitive to RanGAP prevented this inhibition. Therefore, NES-mediated protein export appears to require a Ran-GTP complex but does not require Ran-dependent GTP hydrolysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richards, S A -- Carey, K L -- Macara, I G -- EST3207122/ES/NIEHS NIH HHS/ -- GM 50526/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1842-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Vermont, Burlington, VT 05405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Carrier Proteins/metabolism ; *Cell Cycle Proteins ; Cell Line ; Cell Nucleus/*metabolism ; Cricetinae ; Cytoplasm ; DNA-Binding Proteins/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/metabolism ; *GTPase-Activating Proteins ; Glutathione Transferase/metabolism ; Green Fluorescent Proteins ; *Guanine Nucleotide Exchange Factors ; Guanosine Triphosphate/*metabolism ; Luminescent Proteins/metabolism ; Mutation ; Nuclear Envelope/metabolism ; Nuclear Localization Signals ; Nuclear Proteins/genetics/*metabolism ; Receptors, Glucocorticoid/metabolism ; Recombinant Fusion Proteins/metabolism ; Temperature ; ran GTP-Binding Protein
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  • 7
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    Telomerase catalytic subunit homologs from fission yeast and human (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: Catalytic protein subunits of telomerase from the ciliate Euplotes aediculatus and the yeast Saccharomyces cerevisiae contain reverse transcriptase motifs. Here the homologous genes from the fission yeast Schizosaccharomyces pombe and human are identified. Disruption of the S. pombe gene resulted in telomere shortening and senescence, and expression of mRNA from the human gene correlated with telomerase activity in cell lines. Sequence comparisons placed the telomerase proteins in the reverse transcriptase family but revealed hallmarks that distinguish them from retroviral and retrotransposon relatives. Thus, the proposed telomerase catalytic subunits are phylogenetically conserved and represent a deep branch in the evolution of reverse transcriptases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, T M -- Morin, G B -- Chapman, K B -- Weinrich, S L -- Andrews, W H -- Lingner, J -- Harley, C B -- Cech, T R -- GM28039/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):955-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252327" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Catalysis ; Cell Line ; DNA-Binding Proteins ; Evolution, Molecular ; Genes, Fungal ; Humans ; Introns ; Molecular Sequence Data ; Phylogeny ; Proteins/*chemistry/genetics/metabolism ; *Rna ; RNA, Messenger/genetics/metabolism ; RNA-Directed DNA Polymerase/chemistry ; Retroelements ; Schizosaccharomyces/*enzymology/genetics/growth & development ; Schizosaccharomyces pombe Proteins ; Sequence Alignment ; Telomerase/*chemistry/genetics/metabolism ; Telomere/metabolism
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  • 8
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    Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-10
    Description: The caspase-3 (CPP32, apopain, YAMA) family of cysteinyl proteases has been implicated as key mediators of apoptosis in mammalian cells. Gelsolin was identified as a substrate for caspase-3 by screening the translation products of small complementary DNA pools for sensitivity to cleavage by caspase-3. Gelsolin was cleaved in vivo in a caspase-dependent manner in cells stimulated by Fas. Caspase-cleaved gelsolin severed actin filaments in vitro in a Ca2+-independent manner. Expression of the gelsolin cleavage product in multiple cell types caused the cells to round up, detach from the plate, and undergo nuclear fragmentation. Neutrophils isolated from mice lacking gelsolin had delayed onset of both blebbing and DNA fragmentation, following apoptosis induction, compared with wild-type neutrophils. Thus, cleaved gelsolin may be one physiological effector of morphologic change during apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kothakota, S -- Azuma, T -- Reinhard, C -- Klippel, A -- Tang, J -- Chu, K -- McGarry, T J -- Kirschner, M W -- Koths, K -- Kwiatkowski, D J -- Williams, L T -- P01 HL48743/HL/NHLBI NIH HHS/ -- R01 HL54188/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 10;278(5336):294-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chiron Corporation, Emeryville, CA 94608, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9323209" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Antigens, CD95/physiology ; *Apoptosis ; Caspase 3 ; *Caspases ; Cell Line ; *Cell Size ; Cycloheximide/pharmacology ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Cytoskeleton/metabolism ; DNA Fragmentation ; Gelsolin/*metabolism ; Humans ; Mice ; Neutrophils/cytology/metabolism ; Recombinant Proteins/metabolism ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/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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  • 9
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    Activation of heat shock transcription factor 3 by c-Myb in the absence of cellular stress (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: In vertebrates, the presence of multiple heat shock transcription factors (HSFs) indicates that these factors may be regulated by distinct stress signals. HSF3 was specifically activated in unstressed proliferating cells by direct binding to the c-myb proto-oncogene product (c-Myb). These factors formed a complex through their DNA binding domains that stimulated the nuclear entry and formation of the transcriptionally active trimer of HSF3. Because c-Myb participates in cellular proliferation, this regulatory pathway may provide a link between cellular proliferation and the stress response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanei-Ishii, C -- Tanikawa, J -- Nakai, A -- Morimoto, R I -- Ishii, S -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):246-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Tsukuba Life Science Center, RIKEN, Tsukuba, Ibaraki 305, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211854" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Cycle ; Cell Line ; Cell Nucleus/metabolism ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Promoter Regions, Genetic ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-myb ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/*metabolism ; Transcriptional Activation ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Targeting of HIV- and SIV-infected cells by CD4-chemokine receptor pseudotypes (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Retroviral vectors containing CD4 and an appropriate chemokine receptor were evaluated for the ability to transduce cells infected with human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV). These CD4-chemokine receptor pseudotypes were able to target HIV- and SIV-infected cell lines and monocyte-derived macrophages in a manner that corresponded to the specificity of the viral envelope glycoprotein for its CD4-chemokine receptor complex. This approach could offer a way to deliver antiviral genes directly to HIV-infected cells in vivo and could provide an additional treatment strategy in conjunction with existing antiviral therapies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Endres, M J -- Jaffer, S -- Haggarty, B -- Turner, J D -- Doranz, B J -- O'Brien, P J -- Kolson, D L -- Hoxie, J A -- AI33854/AI/NIAID NIH HHS/ -- AI40880/AI/NIAID NIH HHS/ -- HL 07439/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Nov 21;278(5342):1462-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Hematology-Oncology Division, University of Pennsylvania, Philadelphia, PA 19104, USA. endres@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9367958" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*genetics/metabolism ; Cell Line ; Gene Products, env/metabolism ; *Gene Transfer Techniques ; *Genetic Vectors ; HIV-1/*physiology ; Humans ; Macrophages/virology ; Plasmids ; Receptors, CCR5/genetics/metabolism ; Receptors, CXCR4/genetics/metabolism ; Receptors, Chemokine/*genetics/metabolism ; Simian Immunodeficiency Virus/*physiology ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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