P T Lansbury

Amyloid diseases: abnormal protein aggregation in neurodegeneration.

P. Lansbury, J. Kelly, E. Koo, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.

P. Lansbury, J. Rochet, M. J. Volles, 2001, Biochemistry.

Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB.

P. Lansbury, J. Jarrett, P T Lansbury, 1992, Biochemistry.

Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins.

P. Lansbury, J. Harper, P T Lansbury, 1997, Annual review of biochemistry.

The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease?

P. Lansbury, P. Weinreb, P T Lansbury, 1995, Chemistry & biology.

A kinetic model for amyloid formation in the prion diseases: importance of seeding.

P E Fraser, P. Lansbury, P. Fraser, 1993, Proceedings of the National Academy of Sciences of the United States of America.

An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.

R G Griffin, R. G. Spencer, P. Lansbury, 1991, Biochemistry.

Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.

P. Lansbury, J. Rochet, K. Conway, 2000, Proceedings of the National Academy of Sciences of the United States of America.