Year |
Citation |
Score |
2023 |
Zhao L, Meng F, Li Y, Liu S, Xu M, Chu F, Li C, Yang X, Luo L. Multivalent Nanobody Conjugate with Rigid, Reactive Oxygen Species Scavenging Scaffold for Multi-Target Therapy of Alzheimer's Disease. Advanced Materials (Deerfield Beach, Fla.). e2210879. PMID 36786375 DOI: 10.1002/adma.202210879 |
0.412 |
|
2022 |
Zhao L, Wang S, Hu Q, Jia H, Xin Y, Luo L, Meng F. Conformation-reconstructed multivalent antibody mimic for amplified mitigation of human islet amyloid polypeptide amyloidogenesis. Nanoscale. PMID 35133388 DOI: 10.1039/d1nr08090c |
0.316 |
|
2021 |
Xin Y, Wang S, Liu H, Ke H, Tian S, Cao Y, Huang Y, Shang Y, Jia H, Su L, Yang X, Meng F, Luo L. Hierarchical Vitalization of Oligotyrosine in Mitigating Islet Amyloid Polypeptide Amyloidogenesis through Multivalent Macromolecules with Conformation-Restrained Nanobody Ligands. Acs Nano. PMID 34293858 DOI: 10.1021/acsnano.1c03083 |
0.423 |
|
2021 |
Cao Y, He Z, Gao Y, Xin Y, Luo L, Meng F. Boosting the Photodynamic Degradation of Islet Amyloid Polypeptide Aggregates Via a "Bait-Hook-Devastate" Strategy. Acs Applied Materials & Interfaces. PMID 33764749 DOI: 10.1021/acsami.1c00082 |
0.515 |
|
2019 |
Xin Y, Zhang H, Hu Q, Tian S, Wang C, Luo L, Meng F. Oligotyrosines Inhibit Amyloid Formation of Human Islet Amyloid Polypeptide in a Tyrosine-Number-Dependent Manner. Acs Biomaterials Science & Engineering. 5: 1092-1099. PMID 33405799 DOI: 10.1021/acsbiomaterials.8b01384 |
0.594 |
|
2018 |
Zhao L, Xin Y, Li Y, Yang X, Luo L, Meng F. Ultraeffective Inhibition of Amyloid Fibril Assembly by Nanobody-Gold Nanoparticle Conjugates. Bioconjugate Chemistry. PMID 30585717 DOI: 10.1021/Acs.Bioconjchem.8B00797 |
0.431 |
|
2018 |
Xin Y, Wang X, Luo L, Meng F. Conformation-Dependent Manipulation of Human Islet Amyloid Polypeptide Fibrillation by Shiitake-Derived Lentinan. Acs Applied Materials & Interfaces. PMID 30148596 DOI: 10.1021/Acsami.8B11078 |
0.505 |
|
2018 |
Xin Y, Zhang H, Hu Q, Tian S, Wang C, Luo L, Meng F. Oligotyrosines Inhibit Amyloid Formation of Human Islet Amyloid Polypeptide in a Tyrosine-Number-Dependent Manner Acs Biomaterials Science & Engineering. 5: 1092-1099. DOI: 10.1021/Acsbiomaterials.8B01384 |
0.585 |
|
2016 |
Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, Tu LH, Middleton CT, Chao B, Sartori D, Meng F, Wang H, Wong AG, Zanni MT, Verchere CB, Raleigh DP, et al. Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics. Elife. 5. PMID 27213520 DOI: 10.7554/Elife.12977 |
0.677 |
|
2016 |
Abedini A, Plesner A, Cao P, Ridgway Z, Zhang J, Tu L, Middleton CT, Chao B, Sartori DJ, Meng F, Wang H, Wong AG, Zanni MT, Verchere CB, Raleigh DP, et al. Author response: Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics Elife. DOI: 10.7554/Elife.12977.045 |
0.629 |
|
2016 |
Meng F, Xin JY, Cao CY, Shao X, Shan BY, Xiao QF. Seasonal variations in aerosol optical thickness over eastern China determined from VIIRS data and ground measurements International Journal of Remote Sensing. 37: 1868-1880. DOI: 10.1080/01431161.2016.1163750 |
0.377 |
|
2015 |
Lee CC, Julian MC, Tiller KE, Meng F, DuConge SE, Akter R, Raleigh DP, Tessier PM. Design and Optimization of Anti-Amyloid Domain Antibodies Specific for β-Amyloid and Islet Amyloid Polypeptide. The Journal of Biological Chemistry. PMID 26601942 DOI: 10.1074/Jbc.M115.682336 |
0.581 |
|
2011 |
Meng F, Raleigh DP. Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates. Journal of Molecular Biology. 406: 491-502. PMID 21195086 DOI: 10.1016/J.Jmb.2010.12.028 |
0.754 |
|
2010 |
Meng F, Raleigh DP, Abedini A. Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. Journal of the American Chemical Society. 132: 14340-2. PMID 20873820 DOI: 10.1021/Ja1046186 |
0.796 |
|
2010 |
Meng F, Abedini A, Plesner A, Verchere CB, Raleigh DP. The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry. 49: 8127-33. PMID 20707388 DOI: 10.1021/Bi100939A |
0.8 |
|
2010 |
Meng F, Abedini A, Plesner A, Middleton CT, Potter KJ, Zanni MT, Verchere CB, Raleigh DP. The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. Journal of Molecular Biology. 400: 555-66. PMID 20452363 DOI: 10.1016/J.Jmb.2010.05.001 |
0.794 |
|
2010 |
Cao P, Meng F, Abedini A, Raleigh DP. The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. Biochemistry. 49: 872-81. PMID 20028124 DOI: 10.1021/Bi901751B |
0.761 |
|
2010 |
Abedini A, Gupta R, Marek P, Meng F, Raleigh DP, Taskent H, Tracz S. Role of Posttranslational Modifications in Amyloid Formation Protein Misfolding Diseases: Current and Emerging Principles and Therapies. 131-144. DOI: 10.1002/9780470572702.ch7 |
0.662 |
|
2008 |
Meng F, Marek P, Potter KJ, Verchere CB, Raleigh DP. Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. Biochemistry. 47: 6016-24. PMID 18457428 DOI: 10.1021/Bi702518M |
0.799 |
|
2007 |
Meng F, Abedini A, Song B, Raleigh DP. Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry. 46: 12091-9. PMID 17924651 DOI: 10.1021/Bi7004834 |
0.783 |
|
2007 |
Abedini A, Meng F, Raleigh DP. A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. Journal of the American Chemical Society. 129: 11300-1. PMID 17722920 DOI: 10.1021/Ja072157Y |
0.787 |
|
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