Peter T. Jr. Lansbury
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Peter T. Jr. Lansburybiology Degrees
Biology
#9942
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#13212
Historical Rank
Neuroscience
#1494
World Rank
#1545
Historical Rank
Biochemistry
#1542
World Rank
#1672
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Biology
Peter T. Jr. Lansbury's Degrees
- Doctorate Medicine Harvard University
Why Is Peter T. Jr. Lansbury Influential?
(Suggest an Edit or Addition)Peter T. Jr. Lansbury's Published Works
Number of citations in a given year to any of this author's works
Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author
Published Works
- Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? (1993) (2130)
- The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. (1993) (1906)
- Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. (2003) (1684)
- Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy (2004) (1661)
- Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. (1997) (1579)
- 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) (1538)
- Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease (1998) (1468)
- NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. (1996) (1454)
- Neurodegenerative disease: Amyloid pores from pathogenic mutations (2002) (1266)
- Amyloid fibrillogenesis: themes and variations. (2000) (1006)
- Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. (2004) (999)
- Cell-free formation of protease-resistant prion protein (1994) (885)
- Kinetic Stabilization of the α-Synuclein Protofibril by a Dopamine-α-Synuclein Adduct (2001) (849)
- The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility (2002) (816)
- Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. (2002) (796)
- Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. (2000) (765)
- Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. (2001) (697)
- A century-old debate on protein aggregation and neurodegeneration enters the clinic (2006) (656)
- Observation of metastable Aβ amyloid protofibrils by atomic force microscopy (1997) (638)
- Amyloid diseases: abnormal protein aggregation in neurodegeneration. (1999) (623)
- Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. (2008) (570)
- Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. (1999) (530)
- Non-genetic propagation of strain-specific properties of scrapie prion protein (1995) (521)
- Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. (2002) (492)
- Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. (2003) (445)
- Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's Disease† (1999) (433)
- Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? (2006) (400)
- Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease? (2000) (400)
- A kinetic model for amyloid formation in the prion diseases: importance of seeding. (1993) (398)
- Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide (1995) (398)
- Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. (1997) (395)
- Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. (2002) (370)
- Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease. (1995) (358)
- Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. (1995) (345)
- A detergent-insoluble membrance compartment contains Aβ in vivo (1998) (327)
- Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein* (2008) (313)
- Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. (1992) (300)
- Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. (2002) (287)
- 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? (1995) (282)
- The C‐Terminus of the β Protein is Critical in Amyloidogenesis a (1993) (272)
- Carbon Nanotube Tips: High-Resolution Probes for Imaging Biological Systems (1998) (272)
- Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments. (1990) (272)
- Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? (2002) (269)
- Molecular assessment of the potential transmissibilities of BSE and scrapie to humans (1997) (259)
- Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line. (2003) (246)
- Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores. (2003) (241)
- The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states. (2007) (232)
- Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. (2000) (230)
- Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. (2007) (219)
- Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. (1995) (203)
- A detergent-insoluble membrane compartment contains A beta in vivo. (1998) (191)
- Accelerated Oligomerization by Parkinson's Disease Linked α‐Synuclein Mutants (2000) (189)
- Structural Neurology: Are Seeds at the Root of Neuronal Degeneration? (1997) (184)
- Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. (1997) (179)
- Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. (2004) (177)
- Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1. (2006) (169)
- Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease. (2003) (167)
- The chemistry of scrapie infection: implications of the 'ice 9' metaphor. (1995) (167)
- Dissociation of amyloid fibrils of α-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities (2003) (160)
- Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. (2005) (152)
- In pursuit of the molecular structure of amyloid plaque: new technology provides unexpected and critical information. (1992) (142)
- The C-terminus of the beta protein is critical in amyloidogenesis. (1993) (133)
- Abeta protofibrils possess a stable core structure resistant to hydrogen exchange. (2003) (128)
- The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast. (2009) (127)
- An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. (2004) (126)
- Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies (1997) (123)
- Membrane-associated farnesylated UCH-L1 promotes α-synuclein neurotoxicity and is a therapeutic target for Parkinson's disease (2009) (117)
- Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. (1999) (114)
- A chemical approach to elucidate tin mechanism of transthyretin and β-protein amyloid fibril formation (1994) (112)
- Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain. (1996) (109)
- Accelerated oligomerization by Parkinson's disease linked alpha-synuclein mutants. (2000) (107)
- Genetics of Parkinson's disease and biochemical studies of implicated gene products. (2002) (104)
- Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR (1991) (103)
- The N-Terminal Repeat Domain of α-Synuclein Inhibits β-Sheet and Amyloid Fibril Formation† (2003) (99)
- Reversible Monoubiquitination Regulates the Parkinson Disease-associated Ubiquitin Hydrolase UCH-L1*♦ (2007) (97)
- An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. (1991) (91)
- Back to the future: the 'old-fashioned' way to new medications for neurodegeneration (2004) (84)
- Synthesis and amyloid binding properties of rhenium complexes: preliminary progress toward a reagent for SPECT imaging of Alzheimer's disease brain. (1999) (83)
- Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides. (1996) (74)
- Genetics of Parkinson's disease and biochemical studies of implicated gene products. (2002) (72)
- Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation : peptide models of pancreatic amyloid (1993) (59)
- The structural basis of pancreatic amyloid formation : isotope-edited spectroscopy in the solid state (1992) (59)
- Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein. (2007) (48)
- Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods. (2010) (42)
- The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation. (2003) (42)
- Substrate recognition and catalysis by UCH-L1. (2006) (36)
- A novel solvent system for solid-phase synthesis of protected peptides: the disaggregation of resin-bound antiparallel .beta.-sheet (1990) (36)
- Stress-Induced Cellular Clearance Is Mediated by the SNARE Protein ykt6 and Disrupted by α-Synuclein (2019) (34)
- A possible therapeutic target for Lou Gehrig's disease. (2004) (31)
- Interactions among α-synuclein, dopamine, and biomembranes (2007) (29)
- A computer program for the estimation of protein and nucleic acid sequence diversity in random point mutagenesis libraries (2005) (28)
- Predisposition of prion protein homozygotes to Creutzfeldt-Jakob disease can be explained by a nucleation-dependent polymerization mechanism (1994) (27)
- Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form (2017) (26)
- Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems (1999) (20)
- Peptide Models of a Hydrophobic Cluster at the C-Terminus of the Beta-Amyloid Protein (1994) (17)
- The double life of the prion protein (1996) (17)
- Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems. An update. (1999) (16)
- Following nature's anti-amyloid strategy (2001) (14)
- Improving Synaptic Function in a Mouse Model of AD (2006) (14)
- Importance of seeding (2005) (14)
- Consequences of the molecular mechanism of amyloid formation for the understanding of the pathogenesis of Alzheimer's disease and the development of therapeutic strategies. (1995) (13)
- Yeast prions: Inheritance by seeded protein polymerization? (1997) (7)
- Observation of metastable Ap amyloid protofibrils by atomic force microscopy (2004) (2)
- Yeast prions: Bungee cord domains' balancing act (1999) (1)
- Morphology, conformation and stability of Alzheimer β-amyloid peptide fibrils (1991) (1)
- The Role of α-Synuclein in Parkinson’s Disease: A Biophysical Analogy to Aβ and Alzheimer’s Disease (2000) (1)
- Farnesyltransferase inhibitor LNK-754 attenuates axonal dystrophy and reduces amyloid pathology in mice (2022) (1)
- Farnesyltransferase inhibitor LNK-754 attenuates axonal dystrophy and reduces amyloid pathology in mice (2022) (0)
- The Formation of Scrapie-Associated Prion Protein In Vitro (1996) (0)
- Development of Drugs That Target Proteopathic Seeds Will Require Measurement of Drug Mechanism in Human Brain (2013) (0)
- Rapid, large-scale synthesis and solubility studies of the amyloid β protein of Alzheimer’s disease (1994) (0)
- Crystal Structure of Ubiquitin Carboxy-terminal Hydrolase L1 (UCH-L1) (2006) (0)
- Synthesis and aggregation of C-terminal analogs of β-amyloid (1994) (0)
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What Schools Are Affiliated With Peter T. Jr. Lansbury?
Peter T. Jr. Lansbury is affiliated with the following schools:
