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  • American Association for the Advancement of Science (AAAS)
  • 1995-1999  (10)
  • 1985-1989  (6)
  • 1
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    Regulated delivery of therapeutic proteins after in vivo somatic cell gene transfer (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999
    Description: Stable delivery of a therapeutic protein under pharmacologic control was achieved through in vivo somatic gene transfer. This system was based on the expression of two chimeric, human-derived proteins that were reconstituted by rapamycin into a transcription factor complex. A mixture of two adeno-associated virus vectors, one expressing the transcription factor chimeras and one containing erythropoietin (Epo) under the control of a promoter responsive to the transcription factor, was injected into skeletal muscle of immune-competent mice. Administration of rapamycin resulted in 200-fold induction of plasma Epo. Stable engraftment of this humanized system in immune-competent mice was achieved for 6 months with similar results for at least 3 months in a rhesus monkey.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ye, X -- Rivera, V M -- Zoltick, P -- Cerasoli, F Jr -- Schnell, M A -- Gao, G -- Hughes, J V -- Gilman, M -- Wilson, J M -- P01 AR/NS43648-03/AR/NIAMS NIH HHS/ -- P30 DK47757-05/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1999 Jan 1;283(5398):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Human Gene Therapy, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9872748" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytomegalovirus/genetics ; Dependovirus/genetics ; Erythropoietin/administration & dosage/blood/*genetics ; Female ; Gene Expression Regulation ; *Gene Transfer Techniques ; Genetic Therapy/*methods ; Genetic Vectors ; Hematocrit ; Injections, Intramuscular ; Macaca mulatta ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Muscle, Skeletal ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Recombinant Proteins ; Sirolimus/*pharmacology ; Transcription Factors/*genetics
    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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    Emerging infectious diseases: public health issues for the 21st century (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-21
    Description: Infectious diseases are the third leading cause of death in the United States and the leading cause worldwide. As the new millennium approaches, the public health community must replenish capacity depleted during years of inadequate funding while simultaneously incorporating new technologies and planning for the longer term. Among the challenges facing the public health community is the need for coordinated, global, multisectoral approaches to preventing and controlling complex infectious disease problems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Binder, S -- Levitt, A M -- Sacks, J J -- Hughes, J M -- New York, N.Y. -- Science. 1999 May 21;284(5418):1311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Parasitic Diseases, National Center for Infectious Diseases (NCID), Centers for Disease Control and Prevention (CDC), F-22, 4770 Buford Highway, NE, Atlanta, GA 30341, USA. scb1@cdc.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10334978" target="_blank"〉PubMed〈/a〉
    Keywords: *Communicable Disease Control/trends ; *Communicable Diseases/diagnosis/epidemiology/mortality ; Drug Resistance, Microbial ; Environmental Health ; Global Health ; Humans ; Population Surveillance ; *Public Health Practice ; Socioeconomic Factors ; United States/epidemiology ; Vaccination
    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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  • 3
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    Genetic selection of peptide inhibitors of biological pathways (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-27
    Description: Genetic selections were used to find peptides that inhibit biological pathways in budding yeast. The peptides were presented inside cells as peptamers, surface loops on a highly expressed and biologically inert carrier protein, a catalytically inactive derivative of staphylococcal nuclease. Peptamers that inhibited the pheromone signaling pathway, transcriptional silencing, and the spindle checkpoint were isolated. Putative targets for the inhibitors were identified by a combination of two-hybrid analysis and genetic dissection of the target pathways. This analysis identified Ydr517w as a component of the spindle checkpoint and reinforced earlier indications that Ste50 has both positive and negative roles in pheromone signaling. Analysis of transcript arrays showed that the peptamers were highly specific in their effects, which suggests that they may be useful reagents in organisms that lack sophisticated genetics as well as for identifying components of existing biological pathways that are potential targets for drug discovery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norman, T C -- Smith, D L -- Sorger, P K -- Drees, B L -- O'Rourke, S M -- Hughes, T R -- Roberts, C J -- Friend, S H -- Fields, S -- Murray, A W -- P41-RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 23;285(5427):591-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of California, San Francisco, CA 94143-0444, USA. tnorman@microbia.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10417390" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Fungal Proteins/metabolism ; G1 Phase ; Galactose/metabolism ; Lipoproteins/metabolism ; Micrococcal Nuclease ; Mitosis ; Molecular Sequence Data ; Peptide Library ; Peptides/genetics/metabolism/*pharmacology ; Pheromones/*metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases ; Protein-Tyrosine Kinases ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; *Selection, Genetic ; *Signal Transduction ; Spindle Apparatus/drug effects/*metabolism ; Transcription, Genetic
    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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    Direct observation of heterogeneous chemistry in the atmosphere (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-04
    Description: The heterogeneous replacement of chloride by nitrate in individual sea-salt particles was monitored continuously over time in the troposphere with the use of aerosol time-of-flight mass spectrometry. Modeling calculations show that the observed chloride displacement process is consistent with a heterogeneous chemical reaction between sea-salt particles and gas-phase nitric acid, leading to sodium nitrate production in the particle phase accompanied by liberation of gaseous HCl from the particles. Such single-particle measurements, combined with a single-particle model, make it possible to monitor and explain heterogeneous gas/particle chemistry as it occurs in the atmosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gard -- Kleeman -- Gross -- Hughes -- Allen -- Morrical -- Fergenson -- Dienes -- E Galli M -- Johnson -- Cass -- Prather -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1184-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. E. Gard, D. S. Gross, B. D. Morrical, D. P. Fergenson, T. Dienes, M. E. Galli, K. A. Prather, Department of Chemistry, University of California, Riverside, CA 92521, USA. M. J. Kleeman, L. S. Hughes, J. O. Allen, R. J. Johnson, G. R. Cass, Departme.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469803" target="_blank"〉PubMed〈/a〉
    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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    Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-26
    Description: The SWI/SNF complex participates in the restructuring of chromatin for transcription. The function of the yeast SWI/SNF complex in the remodeling of a nucleosome array has now been analyzed in vitro. Binding of the purified SWI/SNF complex to a nucleosome array disrupted multiple nucleosomes in an adenosine triphosphate-dependent reaction. However, removal of SWI/SNF left a deoxyribonuclease I-hypersensitive site specifically at a nucleosome that was bound by derivatives of the transcription factor Gal4p. Analysis of individual nucleosomes revealed that the SWI/SNF complex catalyzed eviction of histones from the Gal4-bound nucleosomes. Thus, the transient action of the SWI/SNF complex facilitated irreversible disruption of transcription factor-bound nucleosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen-Hughes, T -- Utley, R T -- Cote, J -- Peterson, C L -- Workman, J L -- GM47867/GM/NIGMS NIH HHS/ -- R01 GM049650/GM/NIGMS NIH HHS/ -- R37 GM049650/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 26;273(5274):513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology and Center for Gene Regulation, Pennsylvania State University, University Park, PA 16802-4500, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; DNA, Fungal/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; Fungal Proteins/*metabolism ; Histones/metabolism ; Molecular Sequence Data ; *Nuclear Proteins ; Nucleosomes/*metabolism/ultrastructure ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*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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  • 6
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    Population diversity: its extent and extinction (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: Genetically distinct populations are an important component of biodiversity. This work estimates the number of populations per area of a sample of species from literature on population differentiation and the average range area of a species from a sample of distribution maps. This yields an estimate of about 220 populations per species, or 1.1 to 6.6 billion populations globally. Assuming that population extinction is a linear function of habitat loss, approximately 1800 populations per hour (16 million annually) are being destroyed in tropical forests alone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, J B -- Daily, G C -- Ehrlich, P R -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):689-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381179" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ecosystem ; *Genetics, Population ; Mathematics ; Plants ; Polymorphism, Restriction Fragment Length ; Population Density
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  • 7
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    Genetic relatedness in colonies of tropical wasps with multiple queens (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-25
    Description: The evolution of worker behavior in the social insects is usually explained by kin selection: although workers do not produce offspring, they do reproduce their genes by aiding the reproduction of relatives. The most difficult case for kin selection theory would be species in which workers are fully capable of reproducing but instead opt to rear brood of low relatedness. These conditions are perhaps best fulfilled by the swarm-founding wasps because they have little caste differentiation and their colonies usually have multiple queens, which should lower relatedness. Estimates of within-colony relatedness for three species in this group confirm that it is sometimes (but not always) very low. Inbreeding is negligible in these species, so the hypothesis that inbreeding may raise relatedness is not supported. The maintenance of worker behavior in such species is a significant challenge for kin selection theory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Queller, D C -- Strassmann, J E -- Hughes, C R -- New York, N.Y. -- Science. 1988 Nov 25;242(4882):1155-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17799732" target="_blank"〉PubMed〈/a〉
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  • 8
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    The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-03
    Description: A complementary DNA (cDNA) for ubiquitin carboxyl-terminal hydrolase isozyme L3 was cloned from human B cells. The cDNA encodes a protein of 230 amino acids with a molecular mass of 26.182 daltons. The human protein is very similar to the bovine homolog, with only three amino acids differing in over 100 residues compared. The amino acid sequence deduced from the cDNA was 54% identical to that of the neuron-specific protein PGP 9.5. Purification of bovine PGP 9.5 confirmed that it is also a ubiquitin carboxyl-terminal hydrolase. These results suggest that a family of such related proteins exists and that their expression is tissue-specific.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkinson, K D -- Lee, K M -- Deshpande, S -- Duerksen-Hughes, P -- Boss, J M -- Pohl, J -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):670-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2530630" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/enzymology ; Base Sequence ; Cattle ; DNA/genetics ; Humans ; Isoenzymes/genetics ; Molecular Sequence Data ; Neuropeptides/*genetics/isolation & purification ; Sequence Homology, Nucleic Acid ; Thiolester Hydrolases/*genetics/isolation & purification ; Ubiquitin Thiolesterase
    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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    "Future shock" (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, F P -- New York, N.Y. -- Science. 1995 May 19;268(5213):957.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17774209" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
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  • 10
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    Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: The CDC13 gene has previously been implicated in the maintenance of telomere integrity in Saccharomyces cerevisiae. With the use of two classes of mutations, here it is shown that CDC13 has two discrete roles at the telomere. The cdc13-2est mutation perturbs a function required in vivo for telomerase regulation but not in vitro for enzyme activity, whereas cdc13-1ts defines a separate essential role at the telomere. In vitro, purified Cdc13p binds to single-strand yeast telomeric DNA. Therefore, Cdc13p is a telomere-binding protein required to protect the telomere and mediate access of telomerase to the chromosomal terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nugent, C I -- Hughes, T R -- Lue, N F -- Lundblad, V -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics and Cell and Molecular Biology Program, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824190" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cloning, Molecular ; Cyclin B ; Cyclins/genetics/*metabolism ; DNA, Fungal/metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/genetics ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Phenotype ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/*metabolism ; Telomere/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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