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  • Humans  (26)
  • American Association for the Advancement of Science (AAAS)  (26)
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  • 1
    Publication Date: 2013-07-03
    Description: The textbook description of mitochondrial respiratory complexes (RCs) views them as free-moving entities linked by the mobile carriers coenzyme Q (CoQ) and cytochrome c (cyt c). This model (known as the fluid model) is challenged by the proposal that all RCs except complex II can associate in supercomplexes (SCs). The proposed SCs are the respirasome (complexes I, III, and IV), complexes I and III, and complexes III and IV. The role of SCs is unclear, and their existence is debated. By genetic modulation of interactions between complexes I and III and III and IV, we show that these associations define dedicated CoQ and cyt c pools and that SC assembly is dynamic and organizes electron flux to optimize the use of available substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lapuente-Brun, Esther -- Moreno-Loshuertos, Raquel -- Acin-Perez, Rebeca -- Latorre-Pellicer, Ana -- Colas, Carmen -- Balsa, Eduardo -- Perales-Clemente, Ester -- Quiros, Pedro M -- Calvo, Enrique -- Rodriguez-Hernandez, M A -- Navas, Placido -- Cruz, Raquel -- Carracedo, Angel -- Lopez-Otin, Carlos -- Perez-Martos, Acisclo -- Fernandez-Silva, Patricio -- Fernandez-Vizarra, Erika -- Enriquez, Jose Antonio -- New York, N.Y. -- Science. 2013 Jun 28;340(6140):1567-70. doi: 10.1126/science.1230381.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23812712" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Cytochromes c/*metabolism ; Electron Transport ; Electron Transport Complex I/genetics/*metabolism ; Electron Transport Complex III/genetics/*metabolism ; Electron Transport Complex IV/genetics/*metabolism ; Gene Knockdown Techniques ; HEK293 Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Mitochondria/*enzymology ; Molecular Sequence Data ; Ubiquinone/*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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  • 2
    Publication Date: 1999-09-08
    Description: A fundamental question about human memory is which brain structures are involved, and when, in transforming experiences into memories. This experiment sought to identify neural correlates of memory formation with the use of intracerebral electrodes implanted in the brains of patients with temporal lobe epilepsy. Event-related potentials (ERPs) were recorded directly from the medial temporal lobe (MTL) as the patients studied single words. ERPs elicited by words subsequently recalled in a memory test were contrasted with ERPs elicited by unrecalled words. Memory formation was associated with distinct but interrelated ERP differences within the rhinal cortex and the hippocampus, which arose after about 300 and 500 milliseconds, respectively. These findings suggest that declarative memory formation is dissociable into subprocesses and sequentially organized within the MTL.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, G -- Effern, A -- Grunwald, T -- Pezer, N -- Lehnertz, K -- Dumpelmann, M -- Van Roost, D -- Elger, C E -- New York, N.Y. -- Science. 1999 Sep 3;285(5433):1582-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Epileptology, University of Bonn, 53105 Bonn, Germany. gf@mailer.meb.uni-bonn.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10477525" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Analysis of Variance ; Brain Mapping ; Electrodes, Implanted ; Epilepsy, Temporal Lobe/physiopathology ; Evoked Potentials ; Female ; Hippocampus/*physiology ; Humans ; Magnetic Resonance Imaging ; Male ; Memory/*physiology ; Mental Recall/*physiology ; Middle Aged ; Neurons/physiology ; Temporal Lobe/*physiology ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2001-08-11
    Description: The power of placebos has long been recognized for improving numerous medical conditions such as Parkinson's disease (PD). Little is known, however, about the mechanism underlying the placebo effect. Using the ability of endogenous dopamine to compete for [11C]raclopride binding as measured by positron emission tomography, we provide in vivo evidence for substantial release of endogenous dopamine in the striatum of PD patients in response to placebo. Our findings indicate that the placebo effect in PD is powerful and is mediated through activation of the damaged nigrostriatal dopamine system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de la Fuente-Fernandez, R -- Ruth, T J -- Sossi, V -- Schulzer, M -- Calne, D B -- Stoessl, A J -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1164-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurodegenerative Disorders Centre, TRIUMF, University of British Columbia, Vancouver, BC, Canada V6T 2B5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498597" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Antiparkinson Agents/administration & dosage/*therapeutic use ; Apomorphine/administration & dosage/*therapeutic use ; Corpus Striatum/*metabolism/radionuclide imaging ; Dopamine/*metabolism ; Female ; Humans ; Male ; Middle Aged ; Parkinson Disease/*drug therapy/metabolism ; *Placebo Effect ; Placebos/administration & dosage ; Raclopride/metabolism ; Synapses/metabolism ; Tomography, Emission-Computed
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2001-09-15
    Description: Infections with Plasmodium falciparum during pregnancy lead to the accumulation of parasitized red blood cells (infected erythrocytes, IEs) in the placenta. IEs of P. falciparum isolates that infect the human placenta were found to bind immunoglobulin G (IgG). A strain of P. falciparum cloned for IgG binding adhered massively to placental syncytiotrophoblasts in a pattern similar to that of natural infections. Adherence was inhibited by IgG-binding proteins, but not by glycosaminoglycans or enzymatic digestion of chondroitin sulfate A or hyaluronic acid. Normal, nonimmune IgG that is bound to a duffy binding-like domain beta of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) might at the IE surface act as a bridge to neonatal Fc receptors of the placenta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flick, K -- Scholander, C -- Chen, Q -- Fernandez, V -- Pouvelle, B -- Gysin, J -- Wahlgren, M -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2098-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology and Tumor Biology Center (MTC), Karolinska Institutet and Swedish Institute for Infectious Disease Control, Box 280, S-171 77 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11557894" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Adhesion ; Chondroitin ABC Lyase/metabolism ; Chondroitin Sulfates/metabolism/pharmacology ; Cloning, Molecular ; Erythrocytes/metabolism/*parasitology ; Female ; Humans ; Hyaluronic Acid/pharmacology ; Hyaluronoglucosaminidase/metabolism ; Immunoglobulin G/immunology/*metabolism ; Malaria, Falciparum/immunology/*parasitology ; Placenta/blood supply/immunology/*parasitology ; Placenta Diseases/immunology/parasitology ; Plasmodium falciparum/genetics/immunology/metabolism ; Pregnancy ; Pregnancy Complications, Parasitic/immunology/*parasitology ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/immunology/*metabolism ; Receptors, Fc/*metabolism ; Recombinant Fusion Proteins ; Staphylococcal Protein A/metabolism/pharmacology ; Trophoblasts/immunology/parasitology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1998-06-26
    Description: Type IV bundle-forming pili of enteropathogenic Escherichia coli are required for the localized adherence and autoaggregation phenotypes. Whether these pili are also required for virulence was tested in volunteers by inactivating bfpA or bfpT (perA) encoding, respectively, the pilus subunit and the bfp operon transcriptional activator. Both mutants caused significantly less diarrhea. Mutation of the bfpF nucleotide-binding domain caused increased piliation, enhanced localized adherence, and abolished the twitching motility-dispersal phase of the autoaggregation phenotype. The bfpF mutant colonized the human intestine but was about 200-fold less virulent. Thus, BfpF is required for dispersal from the bacterial aggregate and for full virulence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bieber, D -- Ramer, S W -- Wu, C Y -- Murray, W J -- Tobe, T -- Fernandez, R -- Schoolnik, G K -- 1RO1-AI39521/AI/NIAID NIH HHS/ -- 1RO3-DK52038/DK/NIDDK NIH HHS/ -- MO1-RR00070/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 26;280(5372):2114-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Division of Infectious Diseases and Geographical Medicine, Stanford Program for Vaccine Research, Stanford University Medical Center, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9641917" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Agglutination ; Bacterial Adhesion ; Cell Membrane/ultrastructure ; Diarrhea/*microbiology ; Epithelial Cells/microbiology ; Escherichia coli/genetics/*pathogenicity/physiology/ultrastructure ; Escherichia coli Infections/*microbiology ; Fimbriae, Bacterial/genetics/*physiology/ultrastructure ; Humans ; Intestinal Mucosa/microbiology ; Middle Aged ; Mutation ; Operon ; Phenotype ; Tumor Cells, Cultured ; Virulence
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1990-06-01
    Description: An amyloid protein that precipitates in the cerebral vessel walls of Dutch patients with hereditary cerebral hemorrhage with amyloidosis is similar to the amyloid protein in vessel walls and senile plaques in brains of patients with Alzheimer's disease, Down syndrome, and sporadic cerebral amyloid angiopathy. Cloning and sequencing of the two exons that encode the amyloid protein from two patients with this amyloidosis revealed a cytosine-to-guanine transversion, a mutation that caused a single amino acid substitution (glutamine instead of glutamic acid) at position 22 of the amyloid protein. The mutation may account for the deposition of this amyloid protein in the cerebral vessel walls of these patients, leading to cerebral hemorrhages and premature death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, E -- Carman, M D -- Fernandez-Madrid, I J -- Power, M D -- Lieberburg, I -- van Duinen, S G -- Bots, G T -- Luyendijk, W -- Frangione, B -- AG 05891/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1124-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2111584" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Alleles ; Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; Amyloid beta-Protein Precursor ; Amyloidosis/complications/*genetics ; Base Sequence ; Brain Chemistry ; Cerebral Hemorrhage/etiology/*genetics ; Cerebrovascular Disorders/complications/*genetics ; Dna ; Deoxyribonucleases, Type II Site-Specific ; Exons ; Female ; Genes, Dominant ; Humans ; Middle Aged ; Molecular Sequence Data ; *Mutation ; Netherlands ; Polymerase Chain Reaction ; Protein Precursors/*genetics
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  • 7
    Publication Date: 2007-05-15
    Description: In this millennium, global drylands face a myriad of problems that present tough research, management, and policy challenges. Recent advances in dryland development, however, together with the integrative approaches of global change and sustainability science, suggest that concerns about land degradation, poverty, safeguarding biodiversity, and protecting the culture of 2.5 billion people can be confronted with renewed optimism. We review recent lessons about the functioning of dryland ecosystems and the livelihood systems of their human residents and introduce a new synthetic framework, the Drylands Development Paradigm (DDP). The DDP, supported by a growing and well-documented set of tools for policy and management action, helps navigate the inherent complexity of desertification and dryland development, identifying and synthesizing those factors important to research, management, and policy communities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reynolds, James F -- Smith, D Mark Stafford -- Lambin, Eric F -- Turner, B L 2nd -- Mortimore, Michael -- Batterbury, Simon P J -- Downing, Thomas E -- Dowlatabadi, Hadi -- Fernandez, Roberto J -- Herrick, Jeffrey E -- Huber-Sannwald, Elisabeth -- Jiang, Hong -- Leemans, Rik -- Lynam, Tim -- Maestre, Fernando T -- Ayarza, Miguel -- Walker, Brian -- New York, N.Y. -- Science. 2007 May 11;316(5826):847-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nicholas School of the Environment and Earth Sciences and Department of Biology, Post Office Box 90328, Duke University, Durham, NC 27708, USA. james.f.reynolds@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17495163" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Desert Climate ; Ecology ; *Ecosystem ; *Environment ; Humans ; Public Policy ; Soil
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  • 8
    Publication Date: 2003-04-12
    Description: DNA sequence and annotation of the entire human chromosome 7, encompassing nearly 158 million nucleotides of DNA and 1917 gene structures, are presented. To generate a higher order description, additional structural features such as imprinted genes, fragile sites, and segmental duplications were integrated at the level of the DNA sequence with medical genetic data, including 440 chromosome rearrangement breakpoints associated with disease. This approach enabled the discovery of candidate genes for developmental diseases including autism.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2882961/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2882961/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scherer, Stephen W -- Cheung, Joseph -- MacDonald, Jeffrey R -- Osborne, Lucy R -- Nakabayashi, Kazuhiko -- Herbrick, Jo-Anne -- Carson, Andrew R -- Parker-Katiraee, Layla -- Skaug, Jennifer -- Khaja, Razi -- Zhang, Junjun -- Hudek, Alexander K -- Li, Martin -- Haddad, May -- Duggan, Gavin E -- Fernandez, Bridget A -- Kanematsu, Emiko -- Gentles, Simone -- Christopoulos, Constantine C -- Choufani, Sanaa -- Kwasnicka, Dorota -- Zheng, Xiangqun H -- Lai, Zhongwu -- Nusskern, Deborah -- Zhang, Qing -- Gu, Zhiping -- Lu, Fu -- Zeesman, Susan -- Nowaczyk, Malgorzata J -- Teshima, Ikuko -- Chitayat, David -- Shuman, Cheryl -- Weksberg, Rosanna -- Zackai, Elaine H -- Grebe, Theresa A -- Cox, Sarah R -- Kirkpatrick, Susan J -- Rahman, Nazneen -- Friedman, Jan M -- Heng, Henry H Q -- Pelicci, Pier Giuseppe -- Lo-Coco, Francesco -- Belloni, Elena -- Shaffer, Lisa G -- Pober, Barbara -- Morton, Cynthia C -- Gusella, James F -- Bruns, Gail A P -- Korf, Bruce R -- Quade, Bradley J -- Ligon, Azra H -- Ferguson, Heather -- Higgins, Anne W -- Leach, Natalia T -- Herrick, Steven R -- Lemyre, Emmanuelle -- Farra, Chantal G -- Kim, Hyung-Goo -- Summers, Anne M -- Gripp, Karen W -- Roberts, Wendy -- Szatmari, Peter -- Winsor, Elizabeth J T -- Grzeschik, Karl-Heinz -- Teebi, Ahmed -- Minassian, Berge A -- Kere, Juha -- Armengol, Lluis -- Pujana, Miguel Angel -- Estivill, Xavier -- Wilson, Michael D -- Koop, Ben F -- Tosi, Sabrina -- Moore, Gudrun E -- Boright, Andrew P -- Zlotorynski, Eitan -- Kerem, Batsheva -- Kroisel, Peter M -- Petek, Erwin -- Oscier, David G -- Mould, Sarah J -- Dohner, Hartmut -- Dohner, Konstanze -- Rommens, Johanna M -- Vincent, John B -- Venter, J Craig -- Li, Peter W -- Mural, Richard J -- Adams, Mark D -- Tsui, Lap-Chee -- 38103/Canadian Institutes of Health Research/Canada -- P01 GM061354/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Genomic Biology, The Hospital for Sick Children, Toronto, Ontario, Canada, M5G 1X8. steve@genet.sickkids.on.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690205" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autistic Disorder/genetics ; Chromosome Aberrations ; Chromosome Fragile Sites ; Chromosome Fragility ; Chromosome Mapping ; Chromosomes, Human, Pair 7/*genetics ; Computational Biology ; Congenital Abnormalities/genetics ; CpG Islands ; DNA, Complementary ; Databases, Genetic ; Euchromatin/genetics ; Expressed Sequence Tags ; Gene Duplication ; Genes, Overlapping ; Genetic Diseases, Inborn/genetics ; Genomic Imprinting ; Humans ; In Situ Hybridization, Fluorescence ; Limb Deformities, Congenital/genetics ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasms/genetics ; Pseudogenes ; RNA/genetics ; Retroelements ; *Sequence Analysis, DNA ; Williams Syndrome/genetics
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  • 9
    Publication Date: 2004-07-27
    Description: Glycoconjugate vaccines provide effective prophylaxis against bacterial infections. To date, however, no commercial vaccine has been available in which the key carbohydrate antigens are produced synthetically. We describe the large-scale synthesis, pharmaceutical development, and clinical evaluation of a conjugate vaccine composed of a synthetic capsular polysaccharide antigen of Haemophilus influenzae type b (Hib). The vaccine was evaluated in clinical trials in Cuba and showed long-term protective antibody titers that compared favorably to licensed products prepared with the Hib polysaccharide extracted from bacteria. This demonstrates that access to synthetic complex carbohydrate-based vaccines is feasible and provides a basis for further development of similar approaches for other human pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verez-Bencomo, V -- Fernandez-Santana, V -- Hardy, Eugenio -- Toledo, Maria E -- Rodriguez, Maria C -- Heynngnezz, Lazaro -- Rodriguez, Arlene -- Baly, Alberto -- Herrera, Luis -- Izquierdo, Mabel -- Villar, Annette -- Valdes, Yury -- Cosme, Karelia -- Deler, Mercedes L -- Montane, Manuel -- Garcia, Ernesto -- Ramos, Alexis -- Aguilar, Aristides -- Medina, Ernesto -- Torano, Gilda -- Sosa, Ivan -- Hernandez, Ibis -- Martinez, Raydel -- Muzachio, Alexis -- Carmenates, Ania -- Costa, Lourdes -- Cardoso, Felix -- Campa, Concepcion -- Diaz, Manuel -- Roy, Rene -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):522-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for the Study of Synthetic Antigens, Facultad de Quimica, Universidad de la Habana, Ciudad Habana, Cuba, 10400. vicente@fq.uh.cu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273395" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antibodies, Bacterial/biosynthesis/blood ; Child, Preschool ; Double-Blind Method ; Glycoconjugates/immunology ; Haemophilus Vaccines/administration & dosage/*chemical synthesis/*immunology ; Haemophilus influenzae type b/*immunology ; Humans ; Immunization Schedule ; Immunoglobulin G/blood ; Infant ; Polysaccharides/*chemical synthesis/*immunology/isolation & purification ; Polysaccharides, Bacterial/*immunology/isolation & purification ; Tetanus Toxoid/immunology ; Vaccines, Conjugate/administration & dosage/immunology
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  • 10
    Publication Date: 2004-09-28
    Description: Most acquired immunodeficiency syndrome (AIDS) service providers are in countries with little access to scientific developments relevant to their programs. It is critical to transfer advances from the scientific arena to service providers on a global scale. Human immunodeficiency virus (HIV) prevention organizations in 78 countries were randomized to receive either a control condition or a technology transfer condition with an interactive distance learning computer training curriculum and individualized distance consultation. Of 42 nongovernmental organizations in the technology transfer condition, 29 adopted the science-based program in their communities or trained other agencies to also use it. Advanced communication technologies can create a cost-effective infrastructure to disseminate new intervention models to service providers worldwide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, Jeffrey A -- Somlai, Anton M -- Benotsch, Eric G -- McAuliffe, Timothy L -- Amirkhanian, Yuri A -- Brown, Kevin D -- Stevenson, L Yvonne -- Fernandez, M Isa -- Sitzler, Cheryl -- Gore-Felton, Cheryl -- Pinkerton, Steven D -- Weinhardt, Lance S -- Opgenorth, Karen M -- P30-MH52776/MH/NIMH NIH HHS/ -- R01-MH62982/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 24;305(5692):1953-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for AIDS Intervention Research (CAIR), Department of Psychiatry and Behavioral Medicine, Medical College of Wisconsin, Milwaukee, WI 53226, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15448268" target="_blank"〉PubMed〈/a〉
    Keywords: *Communication ; Community Health Services ; Compact Disks ; Computer-Assisted Instruction ; *Education, Distance ; Follow-Up Studies ; HIV Infections/*prevention & control ; *Health Education ; *Health Personnel ; Health Promotion ; Humans ; Information Dissemination ; Organizations ; *Technology Transfer
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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