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Structural insights into functional amyloid inhibition in Gram −ve bacteria
Author(s) -
William Hawthorne,
Sarah L. Rouse,
Lee Sewell,
Stephen Matthews
Publication year - 2016
Publication title -
biochemical society transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.562
H-Index - 144
eISSN - 1470-8752
pISSN - 0300-5127
DOI - 10.1042/bst20160245
Subject(s) - amyloid (mycology) , bacteria , chemistry , amyloid β , biochemistry , biology , computational biology , medicine , disease , genetics , pathology , inorganic chemistry
Amyloids are proteinaceous aggregates known for their role in debilitating degenerative diseases involving protein dysfunction. Many forms of functional amyloid are also produced in nature and often these systems require careful control of their assembly to avoid the potentially toxic effects. The best-characterised functional amyloid system is the bacterial curli system. Three natural inhibitors of bacterial curli amyloid have been identified and recently characterised structurally. Here, we compare common structural features of CsgC, CsgE and CsgH and discuss the potential implications for general inhibition of amyloid.

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