Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association

Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: What have we learned to date?

(2014) Lindsay M. McMorran et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Antiparallel  -sheet architecture in Iowa-mutant  -amyloid fibrils

(2012) W. Qiang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Dissecting theEscherichia coliperiplasmic chaperone network using differential proteomics

(2012) Katleen Denoncin et al.   PROTEOMICS

The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel

(2011) Emily J. Danoff et al.   BIOPHYSICAL CHEMISTRY

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

(2010) Matthew Biancalana et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Self-Association of Unfolded Outer Membrane Proteins

(2010) Alexandra Ebie Tan et al.   MACROMOLECULAR BIOSCIENCE

Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

(2010) V. L. Anderson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution

(2010) Harry Levine   PROTEIN SCIENCE

Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin

(2008) Thuzar M Shin et al.   Molecular Neurodegeneration