H. Lashuel
Molecular Biology · 2002–2017
A researcher in the Science corpus: 5 papers; trusts 1 researcher and is trusted by 0 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 16 citations into it
- Cell Biology — 7 citations into it
Whom H. Lashuel trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts H. Lashuel overall
Papers from H. Lashuel's perspective
Ordered by how strongly the researchers H. Lashuel trusts endorse each paper. Same corpus, a different order for every researcher.
- 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. (Proceedings of the National Academy of Sciences of the United States of America)
- Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. (Science)
- Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death (Nature)
- Opposing Activities Protect Against Age-Onset Proteotoxicity (Science)
- Loss of autophagy in the central nervous system causes neurodegeneration in mice (Nature)
- Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice (Nature)
- Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. (Biochemistry)
- Amyloid fibrillogenesis: themes and variations. (Current Opinion in Structural Biology)
- A Drosophila model of Parkinson's disease (Nature)
- Protein folding and misfolding
Their papers
- Combined multi-plane phase retrieval and super-resolution optical fluctuation imaging for 4D cell microscopy (2017) — 116 citations
- The many faces of α-synuclein: from structure and toxicity to therapeutic target (2012) — 1,544 citations
- A century-old debate on protein aggregation and neurodegeneration enters the clinic (2006) — 680 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