Related references
Note: Only part of the references are listed.Identifying the amylome, proteins capable of forming amyloid-like fibrils
Lukasz Goldschmidt et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies
Matthew Biancalana et al.
JOURNAL OF MOLECULAR BIOLOGY (2009)
Binding Modes of Thioflavin-T to the Single-Layer β-Sheet of the Peptide Self-Assembly Mimics
Chun Wu et al.
JOURNAL OF MOLECULAR BIOLOGY (2009)
Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils
Eri Chatani et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Amyloid nucleation triggered by agitation of β2-microglobulin under acidic and neutral pH conditions
Kenji Sasahara et al.
BIOCHEMISTRY (2008)
Thiol compounds inhibit the formation of amyloid fibrils by β2-microglobulin at neutral pH
Kaori Yamamoto et al.
JOURNAL OF MOLECULAR BIOLOGY (2008)
The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity
Matthias J. Feige et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's Aβ(1-40) amyloid fibrils
Karolin Klement et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Clustal W and clustal X version 2.0
M. A. Larkin et al.
BIOINFORMATICS (2007)
Heat-triggered conversion of protofibrils into mature amyloid fibrils of β2-microglobulin
Kenji Sasahara et al.
BIOCHEMISTRY (2007)
Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain
Matthias J. Feige et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
Paula Saa et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Mechanism by which the amyloid-like fibrils of a β2-microglobulin fragment are induced by fluorine-substituted alcohols
Kei-ichi Yamaguchi et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
Ultrasonication-induced amyloid fibril formation of β2-microglobulin
Y Ohhashi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains
Y Hagihara et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Seeding-dependent maturation of ß2-microglobulin amyloid fibrils at neutral pH
M Kihara et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Critical balance of electrostatic and hydrophobic interactions is required for β2-microglobulin amyloid fibril growth and stability
B Raman et al.
BIOCHEMISTRY (2005)
Low concentrations of sodium dodecyl sulfate induce the extension of β2-microglobulin-related amyloid fibrils at a neutral pH
S Yamamoto et al.
BIOCHEMISTRY (2004)
Glycosaminoglycans enhance the trifluoroethanol-induced extensionof beta(2)-microglobulin-related amyloid fibrils at a neutral pH
S Yamamoto et al.
JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY (2004)
Therapeutic approaches to protein-misfolding diseases
FE Cohen et al.
NATURE (2003)
Amyloid fibril formation in the context of full-length protein -: Effects of proline mutations on the amyloid fibril formation of β2-microglobulin
T Chiba et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
GP Saborio et al.
NATURE (2001)
Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
R Khurana et al.
BIOCHEMISTRY (2001)
Review: Immunoglobulin light chain amyloidosis - The archetype of structural and pathogenic variability
V Bellotti et al.
JOURNAL OF STRUCTURAL BIOLOGY (2000)