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  • Transfection  (21)
  • Adult
  • American Association for the Advancement of Science (AAAS)  (27)
  • 1995-1999  (27)
  • 1980-1984
  • 1940-1944
  • 1995  (27)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (27)
  • Springer  (1)
Years
  • 1995-1999  (27)
  • 1980-1984
  • 1940-1944
Year
  • 1
    Publication Date: 1995-11-10
    Description: A blood donor infected with human immunodeficiency virus-type 1 (HIV-1) and a cohort of six blood or blood product recipients infected from this donor remain free of HIV-1-related disease with stable and normal CD4 lymphocyte counts 10 to 14 years after infection. HIV-1 sequences from either virus isolates or patient peripheral blood mononuclear cells had similar deletions in the nef gene and in the region of overlap of nef and the U3 region of the long terminal repeat (LTR). Full-length sequencing of one isolate genome and amplification of selected HIV-1 genome regions from other cohort members revealed no other abnormalities of obvious functional significance. These data show that survival after HIV infection can be determined by the HIV genome and support the importance of nef or the U3 region of the LTR in determining the pathogenicity of HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deacon, N J -- Tsykin, A -- Solomon, A -- Smith, K -- Ludford-Menting, M -- Hooker, D J -- McPhee, D A -- Greenway, A L -- Ellett, A -- Chatfield, C -- Lawson, V A -- Crowe, S -- Maerz, A -- Sonza, S -- Learmont, J -- Sullivan, J S -- Cunningham, A -- Dwyer, D -- Dowton, D -- Mills, J -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):988-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉AIDS Molecular Biology Unit, Macfarlane Burnet Centre for Medical Research, Fairfield, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481804" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Base Composition ; Base Sequence ; *Blood Donors ; Blood Transfusion ; CD4 Lymphocyte Count ; Cohort Studies ; Disease Progression ; Female ; Gene Rearrangement ; *Genes, nef ; Genome, Viral ; HIV Infections/immunology/transmission/*virology ; *HIV Long Terminal Repeat ; HIV-1/*genetics/*pathogenicity/physiology ; Humans ; Male ; Middle Aged ; Molecular Sequence Data ; Multigene Family ; Sequence Deletion ; Virulence ; Virus Replication
    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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    American Association for the Advancement of Science (AAAS)
    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
    Publication Date: 1995-08-18
    Description: A candidate gene for the chromosome 1 Alzheimer's disease (AD) locus was identified (STM2). The predicted amino acid sequence for STM2 is homologous to that of the recently cloned chromosome 14 AD gene (S182). A point mutation in STM2, resulting in the substitution of an isoleucine for an asparagine (N141l), was identified in affected people from Volga German AD kindreds. This N141l mutation occurs at an amino acid residue that is conserved in human S182 and in the mouse S182 homolog. The presence of missense mutations in AD subjects in two highly similar genes strongly supports the hypothesis that mutations in both are pathogenic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy-Lahad, E -- Wasco, W -- Poorkaj, P -- Romano, D M -- Oshima, J -- Pettingell, W H -- Yu, C E -- Jondro, P D -- Schmidt, S D -- Wang, K -- AG0513C/AG/NIA NIH HHS/ -- R01-AG11762/AG/NIA NIH HHS/ -- R01-AG11899/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geriatric Research Education, and Clinical Center (182B), Veterans Affairs Medical Center, Seattle, WA 98108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638622" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/ethnology/*genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Cloning, Molecular ; DNA, Complementary/genetics ; Female ; Gene Expression ; Germany/ethnology ; Humans ; Lod Score ; Male ; Membrane Proteins/chemistry/*genetics ; Middle Aged ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Presenilin-2
    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
    Publication Date: 1995-08-18
    Description: The Volga German kindreds are a group of seven related families with autosomal dominant early-onset Alzheimer's disease (AD). Linkage to known AD-related loci on chromosomes 21 and 14 has been excluded. Significant evidence for linkage to AD in these families was obtained with D1S479 and there was also positive evidence for linkage with other markers in the region. A 112-base pair allele of D1S479 co-segregated with the disease in five of seven families, which is consistent with a common genetic founder. This study demonstrates the presence of an AD locus on chromosome 1q31-42.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy-Lahad, E -- Wijsman, E M -- Nemens, E -- Anderson, L -- Goddard, K A -- Weber, J L -- Bird, T D -- Schellenberg, G D -- AG05136/AG/NIA NIH HHS/ -- F32 AG05635/AG/NIA NIH HHS/ -- HG00835/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):970-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geriatric Research, Education, and Clinical Center (182B), Veterans Affairs Medical Center, Seattle, WA 98108-1597, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638621" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Age of Onset ; Aged ; Aged, 80 and over ; Alleles ; Alzheimer Disease/ethnology/*genetics ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Female ; Genetic Markers ; Genotype ; Germany/ethnology ; Haplotypes ; Humans ; Lod Score ; Male ; Middle Aged ; Pedigree
    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
    Publication Date: 1995-03-24
    Description: Congenital lipoid adrenal hyperplasia is an autosomal recessive disorder that is characterized by impaired synthesis of all adrenal and gonadal steroid hormones. In three unrelated individuals with this disorder, steroidogenic acute regulatory protein, which enhances the mitochondrial conversion of cholesterol into pregnenolone, was mutated and nonfunctional, providing genetic evidence that this protein is indispensable normal adrenal and gonadal steroidogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, D -- Sugawara, T -- Strauss, J F 3rd -- Clark, B J -- Stocco, D M -- Saenger, P -- Rogol, A -- Miller, W L -- HD 06274/HD/NICHD NIH HHS/ -- HD 07688/HD/NICHD NIH HHS/ -- HD 28825/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1828-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892608" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/*metabolism ; Adrenal Hyperplasia, Congenital/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport/physiology ; Cell Line ; Cholesterol/*metabolism ; Female ; Gonads/*metabolism ; Haplorhini ; Hormones/*biosynthesis ; Humans ; Male ; Mitochondria/metabolism ; Molecular Sequence Data ; Phosphoproteins/genetics/*physiology ; Point Mutation ; Steroids/*biosynthesis ; 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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  • 6
    Publication Date: 1995-01-13
    Description: The cyclin-dependent kinase 4 (CDK4) regulates progression through the G1 phase of the cell cycle. The activity of CDK4 is controlled by the opposing effects of the D-type cyclin, an activating subunit, and p16INK4, an inhibitory subunit. Ectopic expression of p16INK4 blocked entry into S phase of the cell cycle induced by oncogenic Ha-Ras, and this block was relieved by coexpression of a catalytically inactive CDK4 mutant. Expression of p16INK4 suppressed cellular transformation of primary rat embryo fibroblasts by oncogenic Ha-Ras and Myc, but not by Ha-Ras and E1a. Together, these observations provide direct evidence that p16INK4 can inhibit cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Serrano, M -- Gomez-Lahoz, E -- DePinho, R A -- Beach, D -- Bar-Sagi, D -- CA55360/CA/NCI NIH HHS/ -- EY09300-01/EY/NEI NIH HHS/ -- HD28317-02/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809631" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/genetics/physiology ; Animals ; Carrier Proteins/genetics/*physiology ; *Cell Division ; *Cell Transformation, Neoplastic ; Cells, Cultured ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p16 ; *Cyclin-Dependent Kinases ; Genes, Reporter ; Genes, Retinoblastoma ; Genes, myc ; Genes, ras ; Plasmids ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; *Proto-Oncogene Proteins ; Rats ; Retinoblastoma Protein/physiology ; S Phase ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; ras Proteins/genetics/*physiology
    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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  • 7
    Publication Date: 1995-11-03
    Description: A heptadecapeptide was identified and purified from porcine brain tissue as a ligand for an orphan heterotrimeric GTP-binding protein (G protein)-coupled receptor (LC132) that is similar in sequence to opioid receptors. This peptide, orphanin FQ, has a primary structure reminiscent of that of opioid peptides. Nanomolar concentrations of orphanin FQ inhibited forskolin-stimulated adenylyl cyclase activity in cells transfected with LC132. This inhibitory activity was not affected by the addition of opioid ligands, nor did the peptide activate opioid receptors. Orphanin FQ bound to its receptor in a saturable manner and with high affinity. When injected intracerebroventricularly into mice, orphanin FQ caused a decrease in locomotor activity but did not induce analgesia in the hot-plate test. However, the peptide produced hyperalgesia in the tail-flick assay. Thus, orphanin FQ may act as a transmitter in the brain by modulating nociceptive and locomotor behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinscheid, R K -- Nothacker, H P -- Bourson, A -- Ardati, A -- Henningsen, R A -- Bunzow, J R -- Grandy, D K -- Langen, H -- Monsma, F J Jr -- Civelli, O -- DA 08562/DA/NIDA NIH HHS/ -- DA 09620/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):792-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharma Division, Hoffmann-La Roche AG, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481766" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Amino Acid Sequence ; Analgesics/pharmacology ; Animals ; CHO Cells ; Colforsin/pharmacology ; Cricetinae ; GTP-Binding Proteins/*metabolism ; Hypothalamus/chemistry ; Injections, Intraventricular ; Injections, Spinal ; Ligands ; Mice ; Molecular Sequence Data ; Motor Activity/drug effects ; Opioid Peptides/chemistry/*isolation & purification/*metabolism/pharmacology ; Pain Measurement ; Receptors, Neuropeptide/*metabolism ; Receptors, Opioid/*metabolism ; Swine ; 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
    Publication Date: 1995-07-14
    Description: CD1 molecules are distantly related to the major histocompatibility complex (MHC) class I proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids. Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castano, A R -- Tangri, S -- Miller, J E -- Holcombe, H R -- Jackson, M R -- Huse, W D -- Kronenberg, M -- Peterson, P A -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542403" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigen Presentation ; Antigens, CD/chemistry/*immunology/metabolism ; Antigens, CD1 ; Cell Line ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptides/chemistry/*immunology/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; 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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  • 9
    Publication Date: 1995-09-01
    Description: Eukaryotic chromosomes are capped with repetitive telomere sequences that protect the ends from damage and rearrangements. Telomere repeats are synthesized by telomerase, a ribonucleic acid (RNA)-protein complex. Here, the cloning of the RNA component of human telomerase, termed hTR, is described. The template region of hTR encompasses 11 nucleotides (5'-CUAACCCUAAC) complementary to the human telomere sequence (TTAGGG)n. Germline tissues and tumor cell lines expressed more hTR than normal somatic cells and tissues, which have no detectable telomerase activity. Human cell lines that expressed hTR mutated in the template region generated the predicted mutant telomerase activity. HeLa cells transfected with an antisense hTR lost telomeric DNA and began to die after 23 to 26 doublings. Thus, human telomerase is a critical enzyme for the long-term proliferation of immortal tumor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, J -- Funk, W D -- Wang, S S -- Weinrich, S L -- Avilion, A A -- Chiu, C P -- Adams, R R -- Chang, E -- Allsopp, R C -- Yu, J -- AG09383/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1236-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geron Corporation, Menlo Park, CA 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7544491" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Death ; *Cell Division ; Cell Line ; Cloning, Molecular ; DNA Nucleotidylexotransferase/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Polymerase Chain Reaction ; RNA/chemistry/genetics/*metabolism ; Templates, Genetic ; Transfection ; Tumor Cells, Cultured
    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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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1995-04-28
    Description: Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2) is a transcriptional activator that is essential for EBV-driven B cell immortalization. EBNA2 is targeted to responsive promoters through interaction with a cellular DNA binding protein, C promoter binding factor 1 (CBF1). A transcriptional repression domain has been identified within CBF1. This domain also interacts with EBNA2, and repression is masked by EBNA2 binding. Thus, EBNA2 acts by countering transcriptional repression. Mutation at amino acid 233 of CBF1 abolishes repression and correlates with a loss-of-function mutation in the Drosophila homolog Su(H).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsieh, J J -- Hayward, S D -- CA42245/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725102" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/chemistry/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Epstein-Barr Virus Nuclear Antigens ; *Gene Expression Regulation ; HeLa Cells ; Humans ; Immunoglobulin J Recombination Signal Sequence-Binding Protein ; Models, Genetic ; Mutation ; *Nuclear Proteins ; Promoter Regions, Genetic ; Trans-Activators/chemistry/*metabolism ; *Transcription, Genetic ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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