Fernando L. Palhano, Ph.D.
Affiliations: | Biochemistry | Univ. Federal Rio de Janeiro, Brazil |
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"Fernando Palhano"Mean distance: 8.73
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Publications
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| Martins LDA, Ferreira PS, Leitão Dos Santos OA, et al. (2024) Structural and thermodynamic characterization of a highly amyloidogenic dimer of transthyretin involved in a severe cardiomyopathy. The Journal of Biological Chemistry. 107495 |
| Gonçalves PB, Palhano FL, Cordeiro Y, et al. (2023) How oxidized EGCG remodels α-synuclein fibrils into non-toxic aggregates: insights from computational simulations. Physical Chemistry Chemical Physics : Pccp. 25: 19182-19194 |
| Fernandes L, Cardim-Pires TR, Foguel D, et al. (2021) Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases. Frontiers in Neuroscience. 15: 718188 |
| Fernandes L, Messias B, Pereira-Neves A, et al. (2020) Green Tea Polyphenol Microparticles Based on the Oxidative Coupling of EGCG Inhibit Amyloid Aggregation/Cytotoxicity and Serve as a Platform for Drug Delivery. Acs Biomaterials Science & Engineering. 6: 4414-4423 |
| Fernandes L, Messias B, Pereira-Neves A, et al. (2020) Green Tea Polyphenol Microparticles Based on the Oxidative Coupling of EGCG Inhibit Amyloid Aggregation/Cytotoxicity and Serve as a Platform for Drug Delivery Acs Biomaterials Science & Engineering. 6: 4414-4423 |
| Moreira MH, Barros GC, Requião RD, et al. (2019) From reporters to endogenous genes: the impact of the first five codons on translation efficiency in . Rna Biology. 1-11 |
| Azevedo EP, Guimaraes-Costa AB, Bandeira-Melo C, et al. (2019) Inflammatory profiling of patients with familial amyloid polyneuropathy. Bmc Neurology. 19: 146 |
| Wreden AB, Fernandes L, Kelley M, et al. (2018) Selective and sensitive pull down of amyloid fibrils produced in vitro and in vivo by the use of pentameric-thiophene-coupled resins. Acs Chemical Neuroscience |
| Fernandes L, Moraes N, Sagrillo FS, et al. (2017) An ortho-Iminoquinone Compound Reacts with Lysine Inhibiting Aggregation while Remodeling Mature Amyloid Fibrils. Acs Chemical Neuroscience |
| Sant'Anna R, Almeida MR, Varejāo N, et al. (2017) Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation. Scientific Reports. 7: 44709 |