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Article

Amyloid fibril formation by a helical cytochrome.

FEBS letters - 27 Apr 2001

Pertinhez T A, Bouchard M, Tomlinson E J, Wain R, Ferguson S J, Dobson C M, Smith L J

Abstract excerpt

The substitution of alanines for the two cysteines which form thioether linkages to the haem group in cytochrome c(552) from Hydogenobacter thermophilus destabilises the native protein fold. The holo form of this variant slowly converts into a partially folded apo state that over prolonged periods of time aggregates into fibrillar structures. Characterisation of these structures by electron microscopy and...

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Identifiers

PMID: 11334888
DOI: 10.1016/s0014-5793(01)02384-5

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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