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 …

CsgE is a curli secretion specificity factor that prevents amyloid fibre aggregation

AA Nenninger, LS Robinson, ND Hammer… - Molecular …, 2011 - Wiley Online Library
Curli are extracellular amyloid fibres produced by Escherichia coli that are critical for biofilm
formation and adhesion to biotic and abiotic surfaces. CsgA and CsgB are the major and …

Inhibition of curli assembly and Escherichia coli biofilm formation by the human systemic amyloid precursor transthyretin

N Jain, J Ådén, K Nagamatsu… - Proceedings of the …, 2017 - National Acad Sciences
During biofilm formation, Escherichia coli and other Enterobacteriaceae produce an
extracellular matrix consisting of curli amyloid fibers and cellulose. The precursor of curli …

Atomic resolution insights into curli fiber biogenesis

JD Taylor, Y Zhou, PS Salgado, A Patwardhan… - Structure, 2011 - cell.com
Bacteria produce functional amyloid fibers called curli in a controlled, noncytotoxic manner.
These extracellular fimbriae enable biofilm formation and promote pathogenicity …

Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts

E Chorell, E Andersson, ML Evans, N Jain… - PloS one, 2015 - journals.plos.org
Amyloid formation is historically associated with cytotoxicity, but many organisms produce
functional amyloid fibers (eg, curli) as a normal part of cell biology. Two E. coli genes in the …

Utilizing selenocysteine for expressed protein ligation and bioconjugations

J Liu, Q Chen, S Rozovsky - Journal of the American Chemical …, 2017 - ACS Publications
Employing selenocysteine-containing protein fragments to form the amide bond between
respective protein fragments significantly extends the current capabilities of the widely used …

Enhanced crystallizability by protein engineering approaches: a general overview

A Ruggiero, G Smaldone, F Squeglia… - Protein and peptide …, 2012 - ingentaconnect.com
The limiting step in macromolecular crystallography is the preparation protein crystals
suitable for X-ray diffraction studies. A strong prerequisite for the success of crystallization …

[HTML][HTML] Pushing the limits of sulfur SAD phasing: de novo structure solution of the N-terminal domain of the ectodomain of HCV E1

K El Omari, O Iourin, J Kadlec, R Fearn… - … Section D: Biological …, 2014 - scripts.iucr.org
Single-wavelength anomalous dispersion of S atoms (S-SAD) is an elegant phasing method
to determine crystal structures that does not require heavy-atom incorporation or …

77Se enrichment of proteins expands the biological NMR toolbox

SA Schaefer, M Dong, RP Rubenstein… - Journal of molecular …, 2013 - Elsevier
Sulfur, a key contributor to biological reactivity, is not amendable to investigations by
biological NMR spectroscopy. To utilize selenium as a surrogate, we have developed a …

Tuning functional amyloid formation through disulfide engineering

A Balistreri, E Kahana, S Janakiraman… - Frontiers in …, 2020 - frontiersin.org
Many organisms produce “functional” amyloid fibers, which are stable protein polymers that
serve many roles in cellular biology. Certain Enterobacteriaceae assemble functional …