The Amyloid Phenomenon and Its Links with Human Disease

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

(2016) Paolo Arosio et al.   Nature Communications

A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins

(2016) Priyanka Joshi et al.   ACS Combinatorial Science

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic A 42 aggregates linked with Alzheimers disease

(2016) J. Habchi et al.   Science Advances

2015 Alzheimer's disease facts and figures

(2015)   Alzheimers & Dementia

Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates

(2015) Maya A. Wright et al.   CHEMICAL COMMUNICATIONS

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

(2015) Céline Galvagnion et al.   Nature Chemical Biology

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

(2015) Samuel I A Cohen et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases

(2015) Prajwal Ciryam et al.   TRENDS IN PHARMACOLOGICAL SCIENCES

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

(2015) Samuel I A Cohen et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Health care: Bring microbial sequencing to hospitals

(2014) Sharon Peacock   NATURE

The amyloid state and its association with protein misfolding diseases

(2014) Tuomas P. J. Knowles et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Spatial Propagation of Protein Polymerization

(2014) S. I. A. Cohen et al.   PHYSICAL REVIEW LETTERS

Solution conditions determine the relative importance of nucleation and growth processes in  -synuclein aggregation

(2014) A. K. Buell et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Chemical kinetics for drug discovery to combat protein aggregation diseases

(2014) Paolo Arosio et al.   TRENDS IN PHARMACOLOGICAL SCIENCES

Atomic structure and hierarchical assembly of a cross-  amyloid fibril

(2013) A. W. P. Fitzpatrick et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism

(2013) S. I. A. Cohen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

(2012) Nunilo Cremades et al.   CELL

A Unifying Role for Prions in Neurodegenerative Diseases

(2012) S. B. Prusiner   SCIENCE

Metastability of Native Proteins and the Phenomenon of Amyloid Formation

(2011) Andrew J. Baldwin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Observation of spatial propagation of amyloid assembly from single nuclei

(2011) T. P. J. Knowles et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Converging concepts of protein folding in vitro and in vivo

(2009) F Ulrich Hartl et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

An Analytical Solution to the Kinetics of Breakable Filament Assembly

(2009) T. P. J. Knowles et al.   SCIENCE

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE

A Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates

(2008) Stefan Auer et al.   PLoS Computational Biology