Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease. | J Biol Chem;285(2): 1404-13, 2010 Jan 08. | MEDLINE

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Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease.

Rao, Sudheendra N R; Sharma, Jaiprakash; Maity, Ranjan; Jana, Nihar Ranjan.

Affiliation

Rao SN; Cellular and Molecular Neuroscience Laboratory, National Brain Research Centre, Manesar, Gurgaon-122 050, India.

J Biol Chem ; 285(2): 1404-13, 2010 Jan 08.

Article in En | MEDLINE | ID: mdl-19892702

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carrier Proteins / Protein Folding / Lafora Disease / Ubiquitin-Protein Ligases / Proteasome Endopeptidase Complex Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 2010 Document type: Article Affiliation country:

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carrier Proteins / Protein Folding / Lafora Disease / Ubiquitin-Protein Ligases / Proteasome Endopeptidase Complex Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 2010 Document type: Article Affiliation country: