Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation

MR Chapman, LS Robinson, JS Pinkner, R Roth… - Science, 2002 - science.org
Amyloid is associated with debilitating human ailments including Alzheimer's and prion
diseases. Biochemical, biophysical, and imaging analyses revealed that fibers produced by …

[HTML][HTML] The molecular basis of functional bacterial amyloid polymerization and nucleation

X Wang, ND Hammer, MR Chapman - Journal of Biological Chemistry, 2008 - ASBMB
Amyloid fibers are filamentous proteinaceous structures commonly associated with
mammalian neurodegenerative diseases. Nucleation is the rate-limiting step of amyloid …

Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis

X Wang, Y Zhou, JJ Ren… - Proceedings of the …, 2010 - National Acad Sciences
Amyloid fibers are filamentous protein structures commonly associated with
neurodegenerative diseases. Unlike disease-associated amyloids, which are the products of …

The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization

ND Hammer, JC Schmidt… - Proceedings of the …, 2007 - National Acad Sciences
Curli are functional amyloid fibers assembled by enteric bacteria such as Escherichia coli
and Salmonella spp. In E. coli, the polymerization of the major curli fiber subunit protein …

The C-terminal repeating units of CsgB direct bacterial functional amyloid nucleation

ND Hammer, BA McGuffie, Y Zhou, MP Badtke… - Journal of molecular …, 2012 - Elsevier
Curli are functional amyloids produced by enteric bacteria. The major curli fiber subunit,
CsgA, self-assembles into an amyloid fiber in vitro. The minor curli subunit protein, CsgB, is …

[HTML][HTML] In vitro polymerization of a functional Escherichia coli amyloid protein

X Wang, DR Smith, JW Jones, MR Chapman - Journal of Biological …, 2007 - ASBMB
Amyloid formation is characterized by the conversion of soluble proteins into biochemically
and structurally distinct fibers. Although amyloid formation is traditionally associated with …

[HTML][HTML] The bacterial curli system possesses a potent and selective inhibitor of amyloid formation

ML Evans, E Chorell, JD Taylor, J Åden, A Götheson… - Molecular cell, 2015 - cell.com
Curli are extracellular functional amyloids that are assembled by enteric bacteria during
biofilm formation and host colonization. An efficient secretion system and chaperone …

A bacterial export system for generating extracellular amyloid aggregates

V Sivanathan, A Hochschild - Nature protocols, 2013 - nature.com
Here we describe a protocol for the generation of amyloid aggregates of target
amyloidogenic proteins using a bacteria-based system called curli-dependent amyloid …

Fibrillation of the major curli subunit CsgA under a wide range of conditions implies a robust design of aggregation

MS Dueholm, SB Nielsen, KL Hein, P Nissen… - Biochemistry, 2011 - ACS Publications
The amyloid fold is usually considered a result of protein misfolding. However, a number of
studies have recently shown that the amyloid structure is also used in nature for functional …

Sequence determinants of bacterial amyloid formation

X Wang, MR Chapman - Journal of molecular biology, 2008 - Elsevier
Amyloids are proteinaceous fibers commonly associated with neurodegenerative diseases
and prion-based encephalopathies. Many different polypeptides can form amyloid fibers …