| Year |
Citation |
Score |
| 2020 |
Ivanova MI, Lin Y, Lee YH, Zheng J, Ramamoorthy A. Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology. Biophysical Chemistry. 269: 106507. PMID 33254009 DOI: 10.1016/j.bpc.2020.106507 |
0.452 |
|
| 2020 |
Cox SJ, Rodriguez Camargo DC, Lee YH, Dubini RCA, Rovó P, Ivanova MI, Padmini V, Reif B, Ramamoorthy A. Small molecule induced toxic human-IAPP species characterized by NMR. Chemical Communications (Cambridge, England). PMID 33006345 DOI: 10.1039/d0cc04803h |
0.443 |
|
| 2020 |
Lee HJ, Woo H, Lee HE, Jeon H, Ryu KY, Nam JH, Jeon SG, Park H, Lee JS, Han KM, Lee SM, Kim J, Kang RJ, Lee YH, Kim JI, et al. The novel DYRK1A inhibitor KVN93 regulates cognitive function, amyloid-beta pathology, and neuroinflammation. Free Radical Biology & Medicine. PMID 32896600 DOI: 10.1016/J.Freeradbiomed.2020.08.030 |
0.301 |
|
| 2019 |
Lin Y, Sahoo BR, Ozawa D, Kinoshita M, Kang J, Lim MH, Okumura M, Huh YH, Moon E, Jang JH, Lee HJ, Ryu KY, Ham S, Won HS, Ryu KS, ... ... Lee YH, et al. Diverse Structural Conversion and Aggregation Pathways of Alzheimer's Amyloid-β (1-40). Acs Nano. PMID 31310506 DOI: 10.1021/Acsnano.9B01578 |
0.539 |
|
| 2019 |
Sakurai K, Maeno A, Lee YH, Akasaka K. Conformational Properties Relevant to the Amyloidogenicity of β-Microglobulin Analyzed Using Pressure- and Salt-Dependent Chemical Shift Data. The Journal of Physical Chemistry. B. PMID 30604603 DOI: 10.1021/Acs.Jpcb.8B11408 |
0.312 |
|
| 2018 |
Lee YH, Lin Y, Cox SJ, Kinoshita M, Sahoo BR, Ivanova M, Ramamoorthy A. Zinc Boosts EGCG's hIAPP Amyloid Inhibition both in solution and Membrane. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30468883 DOI: 10.1016/J.Bbapap.2018.11.006 |
0.53 |
|
| 2018 |
Kinoshita M, Lin Y, Dai I, Okumura M, Markova N, Ladbury JE, Sterpone F, Lee YH. Energy landscape of polymorphic amyloid generation of β2-microglobulin revealed by calorimetry. Chemical Communications (Cambridge, England). PMID 29967909 DOI: 10.1039/C8Cc02718H |
0.328 |
|
| 2018 |
Negoro S, Shibata N, Lee YH, Takehara I, Kinugasa R, Nagai K, Tanaka Y, Kato DI, Takeo M, Goto Y, Higuchi Y. Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase. Scientific Reports. 8: 9725. PMID 29950566 DOI: 10.1038/S41598-018-27860-W |
0.316 |
|
| 2018 |
Terakawa MS, Lin Y, Kinoshita M, Kanemura S, Itoh D, Sugiki T, Okumura M, Ramamoorthy A, Lee YH. Impact of membrane curvature on amyloid aggregation. Biochimica Et Biophysica Acta. PMID 29709613 DOI: 10.1016/J.Bbamem.2018.04.012 |
0.545 |
|
| 2018 |
Lee YH, Ramamoorthy A. Semen-Derived Amyloidogenic Peptides - Key Players of HIV Infection. Protein Science : a Publication of the Protein Society. PMID 29493036 DOI: 10.1002/Pro.3395 |
0.505 |
|
| 2018 |
Cox SJ, Rodriguez Camargo DC, Lee Y, Reif B, Ivanova M, Ramamoorthy A. Amyloid Aggregation of hIAPP, Aβ, and Calcitonin Altered by a Curcumin Derivative Biophysical Journal. 114: 226a. DOI: 10.1016/J.Bpj.2017.11.1261 |
0.515 |
|
| 2017 |
Terakawa MS, Lee YH, Kinoshita M, Lin Y, Sugiki T, Fukui N, Ikenoue T, Kawata Y, Goto Y. Membrane-induced initial structure of α-synuclein control its amyloidogenesis on model membranes. Biochimica Et Biophysica Acta. PMID 29273335 DOI: 10.1016/J.Bbamem.2017.12.011 |
0.311 |
|
| 2017 |
Kinoshita M, Kakimoto E, Terakawa MS, Lin Y, Ikenoue T, So M, Sugiki T, Ramamoorthy A, Goto Y, Lee YH. Model membrane size-dependent amyloidogenesis of Alzheimer's amyloid-β peptides. Physical Chemistry Chemical Physics : Pccp. PMID 28608875 DOI: 10.1039/C6Cp07774A |
0.485 |
|
| 2017 |
Kinoshita M, Lin Y, Nakatsuji M, Inui T, Lee YH. Kinetics and polymorphs of yeast prion Sup35NM amyloidogenesis. International Journal of Biological Macromolecules. PMID 28476595 DOI: 10.1016/J.Ijbiomac.2017.05.001 |
0.399 |
|
| 2017 |
Korshavn KJ, Satriano C, Lin Y, Zhang R, Dulchavsky M, Bhunia A, Ivanova MI, Lee YH, La Rosa C, Lim MH, Ramamoorthy A. Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β. The Journal of Biological Chemistry. 292: 4638-4650. PMID 28154182 DOI: 10.1074/Jbc.M116.764092 |
0.478 |
|
| 2015 |
Yagi H, Mizuno A, So M, Hirano M, Adachi M, Akazawa-Ogawa Y, Hagihara Y, Ikenoue T, Lee YH, Kawata Y, Goto Y. Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils. Biochimica Et Biophysica Acta. 1854: 209-17. PMID 25528988 DOI: 10.1016/J.Bbapap.2014.12.014 |
0.379 |
|
| 2015 |
Terakawa MS, Yagi H, Adachi M, Lee YH, Goto Y. Small liposomes accelerate the fibrillation of amyloid β (1-40). The Journal of Biological Chemistry. 290: 815-26. PMID 25406316 DOI: 10.1074/Jbc.M114.592527 |
0.38 |
|
| 2012 |
Yoshimura Y, Lin Y, Yagi H, Lee YH, Kitayama H, Sakurai K, So M, Ogi H, Naiki H, Goto Y. Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation. Proceedings of the National Academy of Sciences of the United States of America. 109: 14446-51. PMID 22908252 DOI: 10.1073/Pnas.1208228109 |
0.37 |
|
| 2012 |
Lee YH, Goto Y. Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance. Biochimica Et Biophysica Acta. 1824: 1307-23. PMID 22885025 DOI: 10.1016/J.Bbapap.2012.07.013 |
0.383 |
|
| 2012 |
Yanagi K, Sakurai K, Yoshimura Y, Konuma T, Lee YH, Sugase K, Ikegami T, Naiki H, Goto Y. The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques. Journal of Molecular Biology. 422: 390-402. PMID 22683352 DOI: 10.1016/J.Jmb.2012.05.034 |
0.395 |
|
| 2010 |
Yoshimura Y, Sakurai K, Lee Y, Ikegami T, Chatani E, Naiki H, Goto Y. Direct observation of minimum‐sized amyloid fibrils using solution NMR spectroscopy Protein Science. 19: 2347-2355. PMID 20936689 DOI: 10.1002/Pro.515 |
0.328 |
|
| 2009 |
Lee Y, Chatani E, Sasahara K, Naiki H, Goto Y. A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of β2-Microglobulin Journal of Biological Chemistry. 284: 2169-2175. PMID 19017634 DOI: 10.1074/Jbc.M806939200 |
0.347 |
|
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