In this section
@article{Hawthorne:2016:10.1042/BST20160245,
author = {Hawthorne, W and Rouse, S and Sewell, L and Matthews, SJ},
doi = {10.1042/BST20160245},
journal = {Biochemical Society Transactions},
pages = {1643--1649},
title = {Structural insights into functional amyloid inhibition in Gram –ve bacteria},
url = {http://dx.doi.org/10.1042/BST20160245},
volume = {44},
year = {2016}
}
TY - JOUR
AB - 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.
AU - Hawthorne,W
AU - Rouse,S
AU - Sewell,L
AU - Matthews,SJ
DO - 10.1042/BST20160245
EP - 1649
PY - 2016///
SN - 1470-8752
SP - 1643
TI - Structural insights into functional amyloid inhibition in Gram –ve bacteria
T2 - Biochemical Society Transactions
UR - http://dx.doi.org/10.1042/BST20160245
UR - http://hdl.handle.net/10044/1/40630
VL - 44
ER -
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