Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 3, 2013, Pages 966-971

  Yang, Chunzhang ^a   Rahimpour, Shervin ^a   Lu, Jie ^a   Pacak, Karel ^b   Ikejiri, Barbara ^a   Brady, Roscoe O ^a   Zhuang, Zhengping ^a  

^a NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE   (United States)

^b EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN CONTAINING TCP1; GLUCOSYLCERAMIDASE; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE INHIBITOR; MESSENGER RNA;

ACETYLATION; ARTICLE; DEACETYLATION; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVITY; ENZYME DEGRADATION; GAUCHER DISEASE; GENETIC DISORDER; HUMAN; HUMAN CELL; HUMAN TISSUE; MODULATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROCESSING; UBIQUITINATION;

ACETYLATION; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; GAUCHER DISEASE; GLUCOSYLCERAMIDASE; HISTONE DEACETYLASE INHIBITORS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION; PROTEIN FOLDING; RECOMBINANT PROTEINS;

EID: 84872541302     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1221046110     Document Type: Article

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