Thiol-disulfide interchange a potential key to conformational change associated with amyloid fibril formation [1]

Journal of Theoretical Biology

Volumn 206, Issue 2, 2000, Pages 313-315

  Feughelman, M ^a   Willis, B K ^b  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b Reckitt & Colman   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; DISULFIDE; HOMOCYSTEINE; PRION PROTEIN; THIOL;

ALPHA HELIX; AMYLOIDOSIS; CONFORMATIONAL TRANSITION; DEGENERATIVE DISEASE; DISULFIDE BOND; LETTER; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN STABILITY;

EID: 0034699419     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1006/jtbi.2000.2112     Document Type: Editorial

References (11)

1. Folate, vitamin B12 and serum total homocysteine levels in confirmed Alzheimer disease
2. The prion diseases
3. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
4. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform
5. Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of tau protein in vitro
6. Scrapie prions, brain amyloid, and senile dementia
7. Prions
8. The molecular basis of amyloidosis
9. Prion domain initiation of amyloid formation in vitro from native Ure2p
10. Purification and properties of the cellular and scrapie hamster prion proteins