Pressure-temperature folding landscape in proteins involved in neurodegenerative diseases and cancer.

Cordeiro, Yraima; Foguel, Debora; Silva, Jerson L

Cordeiro, Yraima; Foguel, Debora; Silva, Jerson L.

Affiliation

Cordeiro Y; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.

Biophys Chem ; 183: 9-18, 2013 Dec 15.

Article in En | MEDLINE | ID: mdl-23849959

Subject(s)

Amyloid/chemistry; Hydrostatic Pressure; Prealbumin/chemistry; Prions/chemistry; Tumor Suppressor Protein p53/chemistry; alpha-Synuclein/chemistry; Animals; Humans; Neoplasms/physiopathology; Neurodegenerative Diseases; Nuclear Magnetic Resonance, Biomolecular; Prealbumin/genetics; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Quaternary; Thermodynamics; Tumor Suppressor Protein p53/genetics; alpha-Synuclein/genetics

Key words

1-anilino 8-naphthalene sulfonate; 4, 4'-bis(1-anilinonaphthalene 8-sulfonate); ANS; Amyloid; DA; Degenerative disease; FTIR; Fourier transform infrared; HHP; High pressure; I state; LB; Lewy bodies; NMR; PD; Parkinson's disease; PrP; Protein aggregation; Protein misfolding; TEM; TTR; alpha-synuclein; bis-ANS; dopamine; high hydrostatic pressure; intermediate state; nuclear magnetic resonance; p53; p53 tumor suppressor protein; prion protein; rPrP; recombinant prion protein; transmission electron microscopy; transthyretin; α-syn

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Prions / Prealbumin / Tumor Suppressor Protein p53 / Alpha-Synuclein / Amyloid / Hydrostatic Pressure Limits: Animals / Humans Language: En Journal: Biophys Chem Year: 2013 Document type: Article Affiliation country: Brazil Country of publication: Netherlands

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