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  • Transfection  (44)
  • Binding Sites  (39)
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Institute of Physics
  • 2020-2022
  • 1995-1999  (83)
  • 1980-1984
  • 1940-1944
  • 1996  (41)
  • 1995  (42)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Institute of Physics
  • Springer  (1)
Years
  • 2020-2022
  • 1995-1999  (83)
  • 1980-1984
  • 1940-1944
Year
  • 1
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    Association of anxiety-related traits with a polymorphism in the serotonin transporter gene regulatory region (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: Transporter-facilitated uptake of serotonin (5-hydroxytryptamine or 5-HT) has been implicated in anxiety in humans and animal models and is the site of action of widely used uptake-inhibiting antidepressant and antianxiety drugs. Human 5-HT transporter (5-HTT) gene transcription is modulated by a common polymorphism in its upstream regulatory region. The short variant of the polymorphism reduces the transcriptional efficiency of the 5-HTT gene promoter, resulting in decreased 5-HTT expression and 5-HT uptake in lymphoblasts. Association studies in two independent samples totaling 505 individuals revealed that the 5-HTT polymorphism accounts for 3 to 4 percent of total variation and 7 to 9 percent of inherited variance in anxiety-related personality traits in individuals as well as sibships.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lesch, K P -- Bengel, D -- Heils, A -- Sabol, S Z -- Greenberg, B D -- Petri, S -- Benjamin, J -- Muller, C R -- Hamer, D H -- Murphy, D L -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1527-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of Wurzburg, Fuchsleinstrasse 15, 97080 Wurzburg, Germany. kplesch@rzbox.uni-wuerzburg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929413" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Alleles ; Anxiety Disorders/*genetics ; Carrier Proteins/*genetics ; Cell Line ; Female ; Genetic Markers ; Genotype ; Humans ; Male ; Membrane Glycoproteins/*genetics ; *Membrane Transport Proteins ; Middle Aged ; *Nerve Tissue Proteins ; Neurotic Disorders/*genetics ; Nuclear Family ; Personality Tests ; Phenotype ; *Polymorphism, Genetic ; *Promoter Regions, Genetic ; Serotonin/*metabolism ; Serotonin Plasma Membrane Transport Proteins ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Liposomes revisited (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lasic, D D -- Papahadjopoulos, D -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1275-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MegaBios Corporation, Burlingame, CA 94010.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871422" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Doxorubicin/administration & dosage ; *Drug Carriers ; *Genetic Therapy ; Humans ; Lipid Bilayers/chemistry ; *Liposomes/chemistry/pharmacokinetics ; Neoplasms/drug therapy ; 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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    Immunostimulatory DNA sequences necessary for effective intradermal gene immunization (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: Vaccination with naked DNA elicits cellular and humoral immune responses that have a T helper cell type 1 bias. However, plasmid vectors expressing large amounts of gene product do not necessarily induce immune responses to the encoded antigens. Instead, the immunogenicity of plasmid DNA (pDNA) requires short immunostimulatory DNA sequences (ISS) that contain a CpG dinucleotide in a particular base context. Human monocytes transfected with pDNA or double-stranded oligonucleotides containing the ISS, but not those transfected with ISS-deficient pDNA or oligonucleotides, transcribed large amounts of interferon-alpha, interferon-beta, and interleukin-12. Although ISS are necessary for gene vaccination, they down-regulate gene expression and thus may interfere with gene replacement therapy by inducing proinflammatory cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, Y -- Roman, M -- Tighe, H -- Lee, D -- Corr, M -- Nguyen, M D -- Silverman, G J -- Lotz, M -- Carson, D A -- Raz, E -- AI36214/AI/NIAID NIH HHS/ -- AI37305/AI/NIAID NIH HHS/ -- AR41897/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):352-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine and The Sam and Rose Stein Institute for Research on Aging, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0663, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662521" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ampicillin Resistance/*genetics ; Animals ; *Antibody Formation ; Base Sequence ; CpG Islands ; Cytokines/*biosynthesis ; DNA/chemistry/genetics/*immunology ; Female ; Gene Expression Regulation ; Genetic Vectors ; Humans ; Injections, Intradermal ; Interferons/biosynthesis ; Interleukin-12/biosynthesis ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Monocytes/immunology ; Plasmids/genetics/*immunology ; Th1 Cells/immunology ; Transfection ; *Vaccination ; beta-Galactosidase/*immunology
    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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  • 4
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    Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-16
    Description: A signaling pathway has been elucidated whereby growth factors activate the transcription factor cyclic adenosine monophosphate response element-binding protein (CREB), a critical regulator of immediate early gene transcription. Growth factor-stimulated CREB phosphorylation at serine-133 is mediated by the RAS-mitogen-activated protein kinase (MAPK) pathway. MAPK activates CREB kinase, which in turn phosphorylates and activates CREB. Purification, sequencing, and biochemical characterization of CREB kinase revealed that it is identical to a member of the pp90(RSK) family, RSK2. RSK2 was shown to mediate growth factor induction of CREB serine-133 phosphorylation both in vitro and in vivo. These findings identify a cellular function for RSK2 and define a mechanism whereby growth factor signals mediated by RAS and MAPK are transmitted to the nucleus to activate gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xing, J -- Ginty, D D -- Greenberg, M E -- CA43855/CA/NCI NIH HHS/ -- NS34814-01/NS/NINDS NIH HHS/ -- P30-HD18655/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):959-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Biological and Biomedical Sciences, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688081" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cyclic AMP Response Element-Binding Protein/*metabolism ; Epidermal Growth Factor/pharmacology ; *Gene Expression Regulation ; Growth Substances/*pharmacology ; Humans ; Molecular Sequence Data ; Nerve Growth Factors/pharmacology ; PC12 Cells ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Rats ; Ribosomal Protein S6 Kinases ; *Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; ras Proteins/metabolism
    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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    A permease-oxidase complex involved in high-affinity iron uptake in yeast (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene--were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stearman, R -- Yuan, D S -- Yamaguchi-Iwai, Y -- Klausner, R D -- Dancis, A -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1552-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599111" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Membrane/metabolism ; *Ceruloplasmin ; Copper/metabolism/pharmacology ; Endoplasmic Reticulum/metabolism ; Ferric Compounds/metabolism ; Ferritins/chemistry/metabolism ; Ferrous Compounds/metabolism ; Genes, Fungal ; Golgi Apparatus/metabolism ; Iron/*metabolism ; Membrane Transport Proteins/chemistry/*genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Multienzyme Complexes/*metabolism ; Mutation ; Open Reading Frames ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transformation, 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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  • 6
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    Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Human leukocyte antigen (HLA)-DM is a critical participant in antigen presentation that catalyzes the release of class II-associated invariant chain-derived peptides (CLIP) from newly synthesized class II histocompatibility molecules, freeing the peptide-binding site for acquisition of antigenic peptides. The mechanism for the selective release of CLIP but not other peptides is unknown. DM was found to enhance the rate of peptide dissociation to an extent directly proportional to the intrinsic rate of peptide dissociation from HLA-DR, regardless of peptide sequence. Thus, CLIP is rapidly released in the presence of DM, because its intrinsic rate of dissociation is relatively high. In antigen presentation, DM has the potential to markedly enhance the rate of peptide exchange, favoring the presentation of peptides with slower intrinsic rates of dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, D A -- Evavold, B D -- Jensen, P E -- AI30554/AI/NIAID NIH HHS/ -- AI33614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):618-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849454" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen Presentation ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Binding Sites ; HLA-D Antigens/*metabolism ; HLA-DR Antigens/immunology/*metabolism ; Histocompatibility Antigens Class II/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Recombinant Fusion Proteins/metabolism
    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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  • 7
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    Nonselective and G betagamma-insensitive weaver K+ channels (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-28
    Description: Homozygous weaver mice are profoundly ataxic because of the loss of granule cell neurons during cerebellar development. This granule cell loss appears to be caused by a genetic defect in the pore region (Gly156--〉Ser) of the heterotrimeric guanine nucleotide-binding protein (G protein)-gated inwardly rectifying potassium (K+) channel subunit (GIRK2). A related subunit, GIRK1, associates with GIRK2 to constitute a neuronal G protein-gated inward rectifier K+ channel. The weaver allele of the GIRK2 subunit (wvGIRK2) caused loss of K+ selectivity when expressed either as wvGIRK2 homomultimers or as GIRK1-wvGIRK2 heteromultimers. The mutation also let to loss of sensitivity to G protein betagamma dimers. Expression of wvGIRK2 subunits let to increased cell death, presumably as a result of basal nonselective channel opening.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Navarro, B -- Kennedy, M E -- Velimirovic, B -- Bhat, D -- Peterson, A S -- Clapham, D E -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1950-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mayo Foundation, Rochester, Minnesota 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658170" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antisense Elements (Genetics) ; CHO Cells ; Cell Death ; Cell Line ; Cerebellum/cytology/*metabolism ; Cricetinae ; G Protein-Coupled Inwardly-Rectifying Potassium Channels ; GTP-Binding Proteins/*physiology ; Membrane Potentials ; Mice ; Mice, Neurologic Mutants ; Molecular Sequence Data ; Neurons/cytology/metabolism ; Oocytes/cytology ; Patch-Clamp Techniques ; Point Mutation ; Potassium Channels/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; 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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  • 8
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    A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-23
    Description: A previously unknown redox cofactor has been identified in the active site of lysyl oxidase from the bovine aorta. Edman sequencing, mass spectrometry, ultraviolet-visible spectra, and resonance Raman studies showed that this cofactor is a quinone. Its structure is derived from the crosslinking of the epsilon-amino group of a peptidyl lysine with the modified side chain of a tyrosyl residue, and it has been designated lysine tyrosylquinone. This quinone appears to be the only example of a mammalian cofactor formed from the crosslinking of two amino acid side chains. This discovery expands the range of known quino-cofactor structures and has implications for the mechanism of their biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, S X -- Mure, M -- Medzihradszky, K F -- Burlingame, A L -- Brown, D E -- Dooley, D M -- Smith, A J -- Kagan, H M -- Klinman, J P -- GM27659/GM/NIGMS NIH HHS/ -- GM39296/GM/NIGMS NIH HHS/ -- P41 RR01614/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 23;273(5278):1078-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688089" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aorta/enzymology ; Binding Sites ; Cattle ; Chromatography, High Pressure Liquid ; Lysine/*analogs & derivatives/chemistry/metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Protein-Lysine 6-Oxidase/*chemistry/genetics/isolation & purification/metabolism ; Quinones/*chemistry/metabolism ; Spectrophotometry, Ultraviolet ; Spectrum Analysis, Raman
    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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  • 9
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    Interaction of a peptidomimetic aminimide inhibitor with elastase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peisach, E -- Casebier, D -- Gallion, S L -- Furth, P -- Petsko, G A -- Hogan, J C Jr -- Ringe, D -- T32GMO7596/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):66-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Biophysics, Brandeis University, Waltham, MA 02254, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604279" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anilides/chemistry/*metabolism ; Binding Sites ; Crystallography, X-Ray ; Dipeptides/chemistry/*metabolism ; Hydrazines/chemistry/*metabolism ; Hydrogen Bonding ; Molecular Sequence Data ; Pancreatic Elastase/*antagonists & inhibitors/chemistry/metabolism
    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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  • 10
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    In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-12
    Description: A retroviral vector system based on the human immunodeficiency virus (HIV) was developed that, in contrast to a murine leukemia virus-based counterpart, transduced heterologous sequences into HeLa cells and rat fibroblasts blocked in the cell cycle, as well as into human primary macrophages. Additionally, the HIV vector could mediate stable in vivo gene transfer into terminally differentiated neurons. The ability of HIV-based viral vectors to deliver genes in vivo into nondividing cells could increase the applicability of retroviral vectors in human gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naldini, L -- Blomer, U -- Gallay, P -- Ory, D -- Mulligan, R -- Gage, F H -- Verma, I M -- Trono, D -- AG08514/AG/NIA NIH HHS/ -- AG10435/AG/NIA NIH HHS/ -- AI37510/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):263-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602510" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/cytology/virology ; Cell Division ; Cells, Cultured ; Female ; *Gene Transfer Techniques ; Genetic Therapy ; *Genetic Vectors ; HIV/*genetics/physiology ; HeLa Cells ; Humans ; Macrophages/cytology/virology ; Molecular Sequence Data ; Neurons/cytology/virology ; Plasmids ; Rats ; Transfection ; Virus Integration
    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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