P. Lansbury

Molecular Biology · 2000–2008

A researcher in the Science corpus: 12 papers; trusts 1 researcher and is trusted by 19 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 26 citations into it; #5,320 of 17,773 by trust here, #6,338 by citations
• Cell Biology — 11 citations into it

Whom P. Lansbury trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. Christopher M. Dobson

Who trusts P. Lansbury overall

1. Christopher M. Dobson
2. P. Muchowski
3. Vladimir N Uversky
4. I. Hamley
5. D. Selkoe
6. Tuomas P. J. Knowles
7. Christian Haass
8. Ò. Conchillo-Solé
9. Jennifer L. Wacker
10. H. Lashuel

Papers from P. Lansbury's perspective

Ordered by how strongly the researchers P. Lansbury trusts endorse each paper. Same corpus, a different order for every researcher.

1. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death (Nature)
2. Amyloid fibrillogenesis: themes and variations. (Current Opinion in Structural Biology)
3. Opposing Activities Protect Against Age-Onset Proteotoxicity (Science)
4. Loss of autophagy in the central nervous system causes neurodegeneration in mice (Nature)
5. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice (Nature)
6. A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly* (Journal of Biological Chemistry)
7. Protein folding and misfolding
8. Impairment of the ubiquitin-proteasome system by protein aggregation. (Science)
9. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis (Science)
10. Aggresomes, inclusion bodies and protein aggregation. (Trends in Cell Biology)

Their papers

• Amyloid fibrillogenesis: themes and variations. (2000) — 1,015 citations
• Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. (2003) — 1,735 citations
• Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. (2008) — 604 citations
• A century-old debate on protein aggregation and neurodegeneration enters the clinic (2006) — 680 citations
• Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. (2004) — 1,033 citations
• Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy (2004) — 1,846 citations
• Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. (2002) — 828 citations
• The UCH-L1 gene encodes two opposing enzymatic activities that affect-synuclein degradation and Park (2002) — 789 citations
• Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. (2001) — 709 citations
• Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct (2001) — 895 citations
• Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. (2000) — 785 citations
• 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. (2000) — 1,612 citations