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{userid:"tjakkovanham", "articletype":"article","pages":"601-612","author":"Tjakko J van Ham, Mats A Holmberg, Annemieke T van der Goot, Eva Teuling, Moises Garcia-Arencibia, Hyun-eui Kim, Deguo Du, Karen L Thijssen, Marit Wiersma, Rogier Burggraaff, Petra van Bergeijk, Jeroen van Rheenen, G Jerre van Veluw, Robert M W Hofstra, David C Rubinsztein, Ellen A A Nollen","year":"2010","title":"Identification of MOAG-4\/SERF as a regulator of age-related proteotoxicity.","month":"Aug","journal":"Cell","publisher":"","volume":"142","number":"4","note":"","tags":"Amyloid beta-Peptides,Animals,Caenorhabditis elegans,Caenorhabditis elegans Proteins,Cell Aging,Cell Line,Cell Line, Tumor,Humans,Mice,Nerve Tissue Proteins,Neurodegenerative Diseases,Peptides,Proteins,alpha-Synuclein","booktitle":"","editor":"","abstract":"Fibrillar protein aggregates are the major pathological hallmark of several incurable, age-related, neurodegenerative disorders. These aggregates typically contain aggregation-prone pathogenic proteins, such as amyloid-beta in Alzheimer's disease and alpha-synuclein in Parkinson's disease. It is, however, poorly understood how these aggregates are formed during cellular aging. Here we identify an evolutionarily highly conserved modifier of aggregation, MOAG-4, as a positive regulator of aggregate formation in C. elegans models for polyglutamine diseases. Inactivation of MOAG-4 suppresses the formation of compact polyglutamine aggregation intermediates that are required for aggregate formation. The role of MOAG-4 in driving aggregation extends to amyloid-beta and alpha-synuclein and is evolutionarily conserved in its human orthologs SERF1A and SERF2. MOAG-4\/SERF appears to act independently from HSF-1-induced molecular chaperones, proteasomal degradation, and autophagy. Our results suggest that MOAG-4\/SERF regulates age-related proteotoxicity through a previously unexplored pathway, which will open up new avenues for research on age-related, neurodegenerative diseases.","address":"","school":"","issn":"1097-4172","doi":"10.1016\/j.cell.2010.07.020","isi":"","pubmed":"20723760","key":"vanHam2010","howpublished":"","urllink":"","refid":6}
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{userid:"mariana.emerenciano", "articletype":"article","pages":"1811-1819","author":"Bruno Alves de Aguiar Gon\u00e7alves, Gisele M Vasconcelos, Luiz Claudio Santos Thuler, Camilla Andrade, Alessandra Faro, Maria S Pombo-de-Oliveira,  , Mariana Emerenciano, Beatriz de Camargo, Luna Bernstain, Cynthia Curvello Neves, Jozina Maria de Andrade Agareno, Lilian Maria Burlacchini de Carvalho, Fl\u00e1via Nogueira Serafim Ara\u00fajo, Nilma Pimentel de Brito, Isis Q Magalh\u00e3es, Jos\u00e9 Carlos Cordoba, Fl\u00e1via Pimenta, Andreia Gadelha, Elo\u00edsa Cartaxo, Rosania Maria Basegio, Atalla Mnayarji, Marcelo S Souza, Alejandro Arencibia, Renato Melaragno, Virg\u00ednia Maria C\u00f3ser, Thereza Christina Lafayete, Sergio Koifman","year":"2012","title":"NQO1 rs1800566 (C609T), PON1 rs662 (Q192R), and PON1 rs854560 (L55M) polymorphisms segregate the risk of childhood acute leukemias according to age range distribution.","month":"Nov","journal":"Cancer causes & control : CCC","publisher":"","volume":"23","number":"11","note":"","tags":"Age Distribution,Alleles,Aryldialkylphosphatase,Brazil,Child,Child, Preschool,Genotype,Humans,NAD(P)H Dehydrogenase (Quinone),Polymorphism, Genetic,Precursor Cell Lymphoblastic Leukemia-Lymphoma,Risk Factors","booktitle":"","editor":"","abstract":"The risk of developing childhood leukemia has been associated with gene polymorphisms that decrease the activity of detoxifying metabolic enzymes and enzymes involved in systemic oxidative stress. We investigated the NQO1 and PON1 polymorphisms for associations with susceptibility to childhood leukemia.","address":"","school":"","issn":"1573-7225","doi":"10.1007\/s10552-012-0060-5","isi":"","pubmed":"22976839","key":"deAguiarGon\u00e7alves2012","howpublished":"","urllink":"","refid":20}
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