Chaperone molecules concentrate together with the ubiquitin-proteasome system inside particulate cytoplasmic structures: possible role in metabolism of misfolded proteins.

Vanoli, Alessandro; Necchi, Vittorio; Barozzi, Serena; Manca, Rachele; Pecci, Alessandro; Solcia, Enrico

Vanoli, Alessandro; Necchi, Vittorio; Barozzi, Serena; Manca, Rachele; Pecci, Alessandro; Solcia, Enrico.

Affiliation

Vanoli A; Pathologic Anatomy Section, Department of Diagnostic Medicine, Fondazione IRCCS Policlinico San Matteo, Pavia, Italy.

Histochem Cell Biol ; 144(2): 179-84, 2015 Aug.

Article in En | MEDLINE | ID: mdl-25952156

Subject(s)

Cytoplasmic Structures/metabolism; Heat-Shock Proteins/analysis; Molecular Chaperones/analysis; Proteasome Endopeptidase Complex/metabolism; Protein Folding; Ubiquitin/metabolism; Cell Line, Tumor; Cytoplasmic Structures/chemistry; Heat-Shock Proteins/metabolism; Humans; Immunohistochemistry; Infant; Molecular Chaperones/metabolism

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Folding / Molecular Chaperones / Cytoplasmic Structures / Ubiquitin / Proteasome Endopeptidase Complex / Heat-Shock Proteins Type of study: Prognostic_studies Limits: Humans / Infant Language: En Journal: Histochem Cell Biol Journal subject: CITOLOGIA / HISTOCITOQUIMICA Year: 2015 Document type: Article Affiliation country: Italy Country of publication: Germany

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