Related references
Note: Only part of the references are listed.Protein Misfolded Oligomers: Experimental Approaches, Mechanism of Formation, and Structure-Toxicity Relationships
Francesco Bemporad et al.
CHEMISTRY & BIOLOGY (2012)
The Monomer-Seed Interaction Mechanism in the Formation of the β2-Microglobulin Amyloid Fibril Clarified by Solution NMR Techniques
Kotaro Yanagi et al.
JOURNAL OF MOLECULAR BIOLOGY (2012)
Oligomeric Intermediates in Amyloid Formation: Structure Determination and Mechanisms of Toxicity
Marcus Faendrich
JOURNAL OF MOLECULAR BIOLOGY (2012)
Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation
Yuichi Yoshimura et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2012)
What Drives Amyloid Molecules To Assemble into Oligomers and Fibrils?
Jeremy D. Schmit et al.
BIOPHYSICAL JOURNAL (2011)
Kinetic Intermediates of β2-Microglobulin Fibril Elongation Probed by Pulse-Labeling H/D Exchange Combined with NMR Analysis
Tsuyoshi Konuma et al.
JOURNAL OF MOLECULAR BIOLOGY (2011)
Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation
Stuart A. Sievers et al.
NATURE (2011)
Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
Christian Bleiholder et al.
NATURE CHEMISTRY (2011)
The Mechanism of Enhanced Insulin Amyloid Fibril Formation by NaCl Is Better Explained by a Conformational Change Model
Mahvish Muzaffar et al.
PLOS ONE (2011)
Detection of Populations of Amyloid-Like Protofibrils with Different Physical Properties
Annalisa Relini et al.
BIOPHYSICAL JOURNAL (2010)
Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid β but Do Not Seed Fibril Formation
Jessica W. Wu et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
Mutation-dependent Polymorphism of Cu,Zn-Superoxide Dismutase Aggregates in the Familial Form of Amyotrophic Lateral Sclerosis
Yoshiaki Furukawa et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
Role of Small Oligomers on the Amyloidogenic Aggregation Free-Energy Landscape
Xianglan He et al.
JOURNAL OF MOLECULAR BIOLOGY (2010)
Pre-Steady-State Kinetic Analysis of the Elongation of Amyloid Fibrils of β2-Microglobulin with Tryptophan Mutagenesis
Eri Chatani et al.
JOURNAL OF MOLECULAR BIOLOGY (2010)
Amyloid Gels: Precocious Appearance of Elastic Properties during the Formation of an Insulin Fibrillar Network
Mauro Manno et al.
LANGMUIR (2010)
Differences in prion strain conformations result from non-native interactions in a nucleus
Yumiko Ohhashi et al.
NATURE CHEMICAL BIOLOGY (2010)
A causative link between the structure of aberrant protein oligomers and their toxicity
Silvia Campioni et al.
NATURE CHEMICAL BIOLOGY (2010)
Structural conversion of neurotoxic amyloid-β1-42 oligomers to fibrils
Mahiuddin Ahmed et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2010)
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)
Prion-like aggregates: infectious agents in human disease
Gunilla T. Westermark et al.
TRENDS IN MOLECULAR MEDICINE (2010)
Amyloid Protofibrils of Lysozyme Nucleate and Grow Via Oligomer Fusion
Shannon E. Hill et al.
BIOPHYSICAL JOURNAL (2009)
Formation Mechanism of Insulin Fibrils and Structural Aspects of the Insulin Fibrillation Process
M. Groenning et al.
CURRENT PROTEIN & PEPTIDE SCIENCE (2009)
A SAXS Study of Glucagon Fibrillation
Cristiano Luis Pinto Oliveira et al.
JOURNAL OF MOLECULAR BIOLOGY (2009)
Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation
Vito Fodera et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2009)
Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation
Natalia Carullaa et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Dynamics of locking of peptides onto growing amyloid fibrils
Govardhan Reddy et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Molecular basis for insulin fibril assembly
Magdalena I. Ivanova et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
A primer of amyloid nomenclature
Per Westermark et al.
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS (2007)
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Michael R. Sawaya et al.
NATURE (2007)
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
Bente Vestergaard et al.
PLOS BIOLOGY (2007)
A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis
Leanne M. Wilson et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
Yuequan Shen et al.
NATURE (2006)
Kinetics and thermodynamics of amyloid fibril assembly
Ronald Wetzel
ACCOUNTS OF CHEMICAL RESEARCH (2006)
A systematic screen of β2-microglobulin and insulin for amyloid-like segments
MI Ivanova et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Solvation-assisted pressure tuning of insulin fibrillation: From novel aggregation pathways to biotechnological applications
S Grudzielanek et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core
OV Bocharova et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Early events in the fibrillation of monomeric insulin
A Ahmad et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Limited proteolysis in the investigation of β2-microglobulin amyloidogenic and fibrillar states
M Monti et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2005)
Capturing intermediate structures of Alzheimer's β-amyloid, Aβ(1-40), by solid-state NMR spectroscopy
S Chimon et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (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)
Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
R Jansen et al.
BIOPHYSICAL JOURNAL (2005)
Conformational constraints for amyloid fibrillation: the importance of being unfolded
VN Uversky et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2004)
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
R Kayed et al.
SCIENCE (2003)
The protofilament structure of insulin amyloid fibrils
JL Jimenez et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2002)
Conformation of β2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond
DP Hong et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Insulin at pH 2: Structural analysis of the conditions promoting insulin fibre formation
JL Whittingham et al.
JOURNAL OF MOLECULAR BIOLOGY (2002)
Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
L Nielsen et al.
BIOCHEMISTRY (2001)
Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: A site-specific investigation by mass spectrometry
P Tito et al.
JOURNAL OF MOLECULAR BIOLOGY (2000)
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
M Bouchard et al.
PROTEIN SCIENCE (2000)
Nucleated conformational conversion and the replication of conformational information by a prion determinant
TR Serio et al.
SCIENCE (2000)
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
WP Esler et al.
BIOCHEMISTRY (2000)