| Year |
Citation |
Score |
| 2019 |
Cuddy LK, Wani WY, Morella ML, Pitcairn C, Tsutsumi K, Fredriksen K, Justman CJ, Grammatopoulos TN, Belur NR, Zunke F, Subramanian A, Affaneh A, Lansbury PT, Mazzulli JR. Stress-Induced Cellular Clearance Is Mediated by the SNARE Protein ykt6 and Disrupted by α-Synuclein. Neuron. PMID 31648898 DOI: 10.1016/J.Neuron.2019.09.001 |
0.316 |
|
| 2017 |
Collier TJ, Srivastava KR, Justman C, Grammatopoulous T, Hutter-Paier B, Prokesch M, Havas D, Rochet JC, Liu F, Jock K, de Oliveira P, Stirtz GL, Dettmer U, Sortwell CE, Feany MB, ... Lansbury P, et al. Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form. Neurobiology of Disease. PMID 28711409 DOI: 10.1016/J.Nbd.2017.07.007 |
0.358 |
|
| 2009 |
Vamvaca K, Volles MJ, Lansbury PT. The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast. Journal of Molecular Biology. 389: 413-24. PMID 19285989 DOI: 10.1016/J.Jmb.2009.03.021 |
0.328 |
|
| 2008 |
Paleologou KE, Schmid AW, Rospigliosi CC, Kim HY, Lamberto GR, Fredenburg RA, Lansbury PT, Fernandez CO, Eliezer D, Zweckstetter M, Lashuel HA. Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein. The Journal of Biological Chemistry. 283: 16895-905. PMID 18343814 DOI: 10.1074/Jbc.M800747200 |
0.309 |
|
| 2008 |
Martinez-Vicente M, Talloczy Z, Kaushik S, Massey AC, Mazzulli J, Mosharov EV, Hodara R, Fredenburg R, Wu DC, Follenzi A, Dauer W, Przedborski S, Ischiropoulos H, Lansbury PT, Sulzer D, et al. Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. The Journal of Clinical Investigation. 118: 777-88. PMID 18172548 DOI: 10.1172/Jci32806 |
0.315 |
|
| 2007 |
Fredenburg RA, Rospigliosi C, Meray RK, Kessler JC, Lashuel HA, Eliezer D, Lansbury PT. The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states. Biochemistry. 46: 7107-18. PMID 17530780 DOI: 10.1021/Bi7000246 |
0.351 |
|
| 2007 |
Volles MJ, Lansbury PT. Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. Journal of Molecular Biology. 366: 1510-22. PMID 17222866 DOI: 10.1016/J.Jmb.2006.12.044 |
0.343 |
|
| 2007 |
Follmer C, Romão L, Einsiedler CM, Porto TC, Lara FA, Moncores M, Weissmüller G, Lashuel HA, Lansbury P, Neto VM, Silva JL, Foguel D. Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein. Biochemistry. 46: 472-82. PMID 17209557 DOI: 10.1021/Bi061871+ |
0.311 |
|
| 2006 |
Lansbury PT, Lashuel HA. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature. 443: 774-9. PMID 17051203 DOI: 10.1038/Nature05290 |
0.353 |
|
| 2006 |
Lashuel HA, Lansbury PT. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Quarterly Reviews of Biophysics. 39: 167-201. PMID 16978447 DOI: 10.1017/S0033583506004422 |
0.362 |
|
| 2006 |
Lansbury PT. Improving synaptic function in a mouse model of AD. Cell. 126: 655-7. PMID 16923386 DOI: 10.1016/J.Cell.2006.08.011 |
0.3 |
|
| 2004 |
Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science (New York, N.Y.). 305: 1292-5. PMID 15333840 DOI: 10.1126/Science.1101738 |
0.316 |
|
| 2004 |
Rochet JC, Outeiro TF, Conway KA, Ding TT, Volles MJ, Lashuel HA, Bieganski RM, Lindquist SL, Lansbury PT. Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. Journal of Molecular Neuroscience : Mn. 23: 23-34. PMID 15126689 DOI: 10.1385/Jmn:23:1-2:023 |
0.33 |
|
| 2004 |
Ray SS, Nowak RJ, Strokovich K, Brown RH, Walz T, Lansbury PT. An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Biochemistry. 43: 4899-905. PMID 15109247 DOI: 10.1021/Bi030246R |
0.335 |
|
| 2004 |
Ray SS, Lansbury PT. A possible therapeutic target for Lou Gehrig's disease. Proceedings of the National Academy of Sciences of the United States of America. 101: 5701-2. PMID 15079068 DOI: 10.1073/Pnas.0401934101 |
0.32 |
|
| 2003 |
Kheterpal I, Lashuel HA, Hartley DM, Walz T, Lansbury PT, Wetzel R. Abeta protofibrils possess a stable core structure resistant to hydrogen exchange. Biochemistry. 42: 14092-8. PMID 14640676 DOI: 10.1021/Bi0357816 |
0.37 |
|
| 2003 |
Lashuel HA, Hartley DM, Petre BM, Wall JS, Simon MN, Walz T, Lansbury PT. Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores. Journal of Molecular Biology. 332: 795-808. PMID 12972252 DOI: 10.1016/S0022-2836(03)00927-6 |
0.338 |
|
| 2003 |
Foguel D, Suarez MC, Ferrão-Gonzales AD, Porto TC, Palmieri L, Einsiedler CM, Andrade LR, Lashuel HA, Lansbury PT, Kelly JW, Silva JL. Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities. Proceedings of the National Academy of Sciences of the United States of America. 100: 9831-6. PMID 12900507 DOI: 10.1073/Pnas.1734009100 |
0.394 |
|
| 2003 |
Volles MJ, Lansbury PT. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry. 42: 7871-8. PMID 12834338 DOI: 10.1021/Bi030086J |
0.384 |
|
| 2003 |
Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annual Review of Neuroscience. 26: 267-98. PMID 12704221 DOI: 10.1146/Annurev.Neuro.26.010302.081142 |
0.376 |
|
| 2003 |
Park JY, Lansbury PT. Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease. Biochemistry. 42: 3696-700. PMID 12667059 DOI: 10.1021/Bi020604A |
0.34 |
|
| 2003 |
Kessler JC, Rochet JC, Lansbury PT. The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation. Biochemistry. 42: 672-8. PMID 12534279 DOI: 10.1021/Bi020429Y |
0.34 |
|
| 2002 |
Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT. Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. Journal of Molecular Biology. 322: 1089-102. PMID 12367530 DOI: 10.1016/S0022-2836(02)00735-0 |
0.323 |
|
| 2002 |
Anguiano M, Nowak RJ, Lansbury PT. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry. 41: 11338-43. PMID 12234175 DOI: 10.1021/Bi020314U |
0.376 |
|
| 2002 |
Ding TT, Lee SJ, Rochet JC, Lansbury PT. Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry. 41: 10209-17. PMID 12162735 DOI: 10.1021/Bi020139H |
0.339 |
|
| 2002 |
Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature. 418: 291. PMID 12124613 DOI: 10.1038/418291A |
0.404 |
|
| 2002 |
Volles MJ, Lansbury PT. Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry. 41: 4595-602. PMID 11926821 DOI: 10.1021/Bi0121353 |
0.333 |
|
| 2002 |
Shtilerman MD, Ding TT, Lansbury PT. Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry. 41: 3855-60. PMID 11900526 DOI: 10.1021/Bi0120906 |
0.37 |
|
| 2001 |
Conway KA, Rochet JC, Bieganski RM, Lansbury PT. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science (New York, N.Y.). 294: 1346-9. PMID 11701929 DOI: 10.1126/Science.1063522 |
0.306 |
|
| 2001 |
Volles MJ, Lee SJ, Rochet JC, Shtilerman MD, Ding TT, Kessler JC, Lansbury PT. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry. 40: 7812-9. PMID 11425308 DOI: 10.1021/Bi0102398 |
0.35 |
|
| 2000 |
Conway KA, Lee SJ, Rochet JC, Ding TT, Harper JD, Williamson RE, Lansbury PT. Accelerated oligomerization by Parkinson's disease linked alpha-synuclein mutants. Annals of the New York Academy of Sciences. 920: 42-5. PMID 11193175 DOI: 10.1111/J.1749-6632.2000.Tb06903.X |
0.321 |
|
| 2000 |
Rochet JC, Conway KA, Lansbury PT. Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. Biochemistry. 39: 10619-26. PMID 10978144 DOI: 10.1021/Bi001315U |
0.352 |
|
| 2000 |
Goldberg MS, Lansbury PT. Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nature Cell Biology. 2: E115-9. PMID 10878819 DOI: 10.1038/35017124 |
0.327 |
|
| 2000 |
Rochet JC, Lansbury PT. Amyloid fibrillogenesis: themes and variations. Current Opinion in Structural Biology. 10: 60-8. PMID 10679462 DOI: 10.1016/S0959-440X(99)00049-4 |
0.353 |
|
| 2000 |
Lansbury PT, Kosik KS. Neurodegeneration: new clues on inclusions. Chemistry & Biology. 7: R9-R12. PMID 10662685 DOI: 10.1016/S1074-5521(00)00068-5 |
0.352 |
|
| 2000 |
Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, Lansbury PT. 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. 97: 571-6. PMID 10639120 DOI: 10.1073/Pnas.97.2.571 |
0.342 |
|
| 1999 |
Koo EH, Lansbury PT, Kelly JW. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proceedings of the National Academy of Sciences of the United States of America. 96: 9989-90. PMID 10468546 DOI: 10.1073/Pnas.96.18.9989 |
0.386 |
|
| 1999 |
Zhen W, Han H, Anguiano M, Lemere CA, Cho CG, Lansbury PT. Synthesis and amyloid binding properties of rhenium complexes: preliminary progress toward a reagent for SPECT imaging of Alzheimer's disease brain. Journal of Medicinal Chemistry. 42: 2805-15. PMID 10425090 DOI: 10.1021/Jm990103W |
0.624 |
|
| 1999 |
Harper JD, Wong SS, Lieber CM, Lansbury PT. Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38: 8972-80. PMID 10413470 DOI: 10.1021/Bi9904149 |
0.334 |
|
| 1999 |
Lansbury PT. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proceedings of the National Academy of Sciences of the United States of America. 96: 3342-4. PMID 10097040 DOI: 10.1073/Pnas.96.7.3342 |
0.359 |
|
| 1998 |
Conway KA, Harper JD, Lansbury PT. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nature Medicine. 4: 1318-20. PMID 9809558 DOI: 10.1038/3311 |
0.325 |
|
| 1998 |
Lee SJ, Liyanage U, Bickel PE, Xia W, Lansbury PT, Kosik KS. A detergent-insoluble membrane compartment contains A beta in vivo. Nature Medicine. 4: 730-4. PMID 9623986 DOI: 10.1038/Nm0698-730 |
0.31 |
|
| 1997 |
Lansbury PT. Inhibition of amyloid formation: a strategy to delay the onset of Alzheimer's disease. Current Opinion in Chemical Biology. 1: 260-7. PMID 9667848 DOI: 10.1016/S1367-5931(97)80018-X |
0.366 |
|
| 1997 |
Harper JD, Lieber CM, Lansbury PT. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chemistry & Biology. 4: 951-9. PMID 9427660 DOI: 10.1016/S1074-5521(97)90303-3 |
0.373 |
|
| 1997 |
Lansbury PT. Structural neurology: are seeds at the root of neuronal degeneration? Neuron. 19: 1151-4. PMID 9427238 DOI: 10.1016/S0896-6273(00)80406-7 |
0.325 |
|
| 1997 |
Lansbury PT. Yeast prions: inheritance by seeded protein polymerization? Current Biology : Cb. 7: R617-9. PMID 9368740 DOI: 10.1016/S0960-9822(06)00316-2 |
0.315 |
|
| 1997 |
Harper JD, Lansbury PT. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annual Review of Biochemistry. 66: 385-407. PMID 9242912 DOI: 10.1146/Annurev.Biochem.66.1.385 |
0.403 |
|
| 1997 |
Harper JD, Wong SS, Lieber CM, Lansbury PT. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chemistry & Biology. 4: 119-25. PMID 9190286 DOI: 10.1016/S1074-5521(97)90255-6 |
0.346 |
|
| 1997 |
Costa PR, Kocisko DA, Sun BQ, Lansbury PT, Griffin RG. Determination of peptide amide configuration in a model amyloid fibril by solid-state NMR Journal of the American Chemical Society. 119: 10487-10493. DOI: 10.1021/Ja971494B |
0.356 |
|
| 1996 |
Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry. 35: 13709-15. PMID 8901511 DOI: 10.1021/Bi961799N |
0.38 |
|
| 1996 |
Kocisko DA, Lansbury PT, Caughey B. Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain. Biochemistry. 35: 13434-42. PMID 8873612 DOI: 10.1021/Bi9610562 |
0.302 |
|
| 1996 |
Ashburn TT, Han H, McGuinness BF, Lansbury PT. Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides. Chemistry & Biology. 3: 351-8. PMID 8807864 DOI: 10.1016/S1074-5521(96)90118-0 |
0.348 |
|
| 1996 |
Lansbury PT, Caughey B. The double life of the prion protein. Current Biology : Cb. 6: 914-6. PMID 8805340 DOI: 10.1016/S0960-9822(02)00624-3 |
0.316 |
|
| 1996 |
Cho CG, Lansbury PT. Synthesis of two bicyclic surfactants which form reversed micelles capable of selective protein extraction Journal of Organic Chemistry. 61: 1920-1921. DOI: 10.1021/Jo9600518 |
0.597 |
|
| 1995 |
Han H, Weinreb PH, Lansbury PT. 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? Chemistry & Biology. 2: 163-9. PMID 9383418 DOI: 10.1016/1074-5521(95)90071-3 |
0.409 |
|
| 1995 |
Caughey B, Kocisko DA, Raymond GJ, Lansbury PT. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chemistry & Biology. 2: 807-17. PMID 8807814 DOI: 10.1016/1074-5521(95)90087-X |
0.311 |
|
| 1995 |
Evans KC, Berger EP, Cho CG, Weisgraber KH, Lansbury PT. Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease. Proceedings of the National Academy of Sciences of the United States of America. 92: 763-7. PMID 7846048 DOI: 10.1073/Pnas.92.3.763 |
0.645 |
|
| 1995 |
Lansbury PT, Costa PR, Griffiths JM, Simon EJ, Auger M, Halverson KJ, Kocisko DA, Hendsch ZS, Ashburn TT, Spencer RG. Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nature Structural Biology. 2: 990-8. PMID 7583673 DOI: 10.1038/Nsb1195-990 |
0.329 |
|
| 1994 |
Kocisko DA, Come JH, Priola SA, Chesebro B, Raymond GJ, Lansbury PT, Caughey B. Cell-free formation of protease-resistant prion protein. Nature. 370: 471-4. PMID 7913989 DOI: 10.1038/370471A0 |
0.313 |
|
| 1994 |
Kelly JW, Lansbury PT. A chemical approach to elucidate tin mechanism of transthyretin and βprotein amyloid fibril formation Amyloid. 1: 186-205. DOI: 10.3109/13506129409148451 |
0.377 |
|
| 1994 |
Weinreb PH, Jarrett JT, Lansbury PT. Peptide Models of a Hydrophobic Cluster at the C-Terminus of the .beta.-Amyloid Protein Journal of the American Chemical Society. 116: 10835-10836. DOI: 10.1021/Ja00102A079 |
0.307 |
|
| 1994 |
Jarrett JT, Costa PR, Griffin RG, Lansbury PT. Models of the .beta. Protein C-Terminus: Differences in Amyloid Structure May Lead to Segregation of "Long" and "Short" Fibrils Journal of the American Chemical Society. 116: 9741-9742. DOI: 10.1021/Ja00100A046 |
0.326 |
|
| 1994 |
Come JH, Lansbury PT. Predisposition of prion protein homozygotes to Creutzfeldt-Jakob disease can be explained by a nucleation-dependent polymerization mechanism Journal of the American Chemical Society. 116: 4109-4110. DOI: 10.1021/Ja00088A069 |
0.316 |
|
| 1993 |
Jarrett JT, Lansbury PT. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell. 73: 1055-8. PMID 8513491 DOI: 10.1016/0092-8674(93)90635-4 |
0.381 |
|
| 1993 |
Jarrett JT, Berger EP, Lansbury PT. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry. 32: 4693-7. PMID 8490014 DOI: 10.1021/Bi00069A001 |
0.302 |
|
| 1993 |
Come JH, Fraser PE, Lansbury PT. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proceedings of the National Academy of Sciences of the United States of America. 90: 5959-63. PMID 8327467 DOI: 10.1073/Pnas.90.13.5959 |
0.394 |
|
| 1993 |
Jarrett JT, Berger EP, Lansbury PT. The C-terminus of the beta protein is critical in amyloidogenesis. Annals of the New York Academy of Sciences. 695: 144-8. PMID 8239273 DOI: 10.1111/J.1749-6632.1993.Tb23043.X |
0.327 |
|
| 1993 |
Ashburn TT, Lansbury PT. Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation: Peptide models of pancreatic amyloid Journal of the American Chemical Society. 115: 11012-11013. DOI: 10.1021/Ja00076A078 |
0.316 |
|
| 1993 |
Cohen-Anisfeld ST, Lansbury PT. A practical, convergent method for glycopeptide synthesis Journal of the American Chemical Society. 115: 10531-10537. DOI: 10.1021/Ja00076A010 |
0.306 |
|
| 1992 |
Jarrett JT, Lansbury PT. Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry. 31: 12345-52. PMID 1463722 DOI: 10.1021/Bi00164A008 |
0.353 |
|
| 1992 |
Hendrix JC, Lansbury PT. Synthesis of a protected peptide corresponding to residues 1-25 of the .beta.-amyloid protein of Alzheimer's disease Journal of Organic Chemistry. 57: 3421-3426. DOI: 10.1021/Jo00038A034 |
0.378 |
|
| 1992 |
Hendrix JC, Jarrett JT, Anisfeld ST, Lansbury PT. Studies related to a convergent fragment-coupling approach to peptide synthesis using the Kaiser oxime resin Journal of Organic Chemistry. 57: 3414-3420. DOI: 10.1021/Jo00038A033 |
0.341 |
|
| 1992 |
Hendrix JC, Halverson KJ, Lansbury PT. A Convergent Synthesis of the Amyloid Protein of Alzheimer′s Disease. Journal of the American Chemical Society. 114: 7930-7931. DOI: 10.1021/Ja00046A060 |
0.373 |
|
| 1991 |
Spencer RG, Halverson KJ, Auger M, McDermott AE, Griffin RG, Lansbury PT. An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Biochemistry. 30: 10382-7. PMID 1931962 DOI: 10.1021/Bi00107A004 |
0.375 |
|
| 1991 |
Halverson KJ, Sucholeiki I, Ashburn TT, Lansbury PT. Location of .beta.-sheet-forming sequences in amyloid proteins by FTIR Journal of the American Chemical Society. 113: 6701-6703. DOI: 10.1021/Ja00017A068 |
0.319 |
|
| 1990 |
Halverson K, Fraser PE, Kirschner DA, Lansbury PT. Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments. Biochemistry. 29: 2639-44. PMID 2346740 DOI: 10.1021/Bi00463A003 |
0.326 |
|
| 1959 |
Lansbury PT, Letsinger RL. peri-Substituted naphthalenes. II. A rearrangement involving a 1,5-aryl migration Journal of the American Chemical Society. 81: 940-943. DOI: 10.1021/Ja01513A046 |
0.488 |
|
| 1959 |
Letsinger RL, Lansbury PT. Peri-substituted naphthalenes. I. New rearrangement reactions of substituted naphthopyrans Journal of the American Chemical Society. 81: 935-939. DOI: 10.1021/Ja01513A045 |
0.5 |
|
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