Detalhe da pesquisa
1.
A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers.
J Biol Chem
; 298(12): 102688, 2022 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-36370848
2.
Differential Effects of Lipid Bilayers on αPSM Peptide Functional Amyloid Formation.
Int J Mol Sci
; 25(1)2023 Dec 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-38203273
3.
Heparin promotes fibrillation of most phenol-soluble modulin virulence peptides from Staphylococcus aureus.
J Biol Chem
; 297(2): 100953, 2021 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-34270957
4.
Fabrication and Characterization of Reconstituted Silk Microgels for the Storage and Release of Small Molecules.
Macromol Rapid Commun
; 40(8): e1800898, 2019 Apr.
Artigo
em Inglês
| MEDLINE | ID: mdl-30840348
5.
Absolute Quantification of Amyloid Propagons by Digital Microfluidics.
Anal Chem
; 89(22): 12306-12313, 2017 11 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-28972786
6.
Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases?
Biochim Biophys Acta
; 1848(9): 1897-907, 2015 Sep.
Artigo
em Inglês
| MEDLINE | ID: mdl-25666871
7.
Scaffolded multimers of hIAPP(20-29) peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP(20-29) peptide fragment.
Biochim Biophys Acta
; 1854(12): 1890-1897, 2015 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-26284878
8.
Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.
Proc Natl Acad Sci U S A
; 110(8): 2798-803, 2013 Feb 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-23388629
9.
The importance of being capped: Terminal capping of an amyloidogenic peptide affects fibrillation propensity and fibril morphology.
Biochemistry
; 53(44): 6968-80, 2014 Nov 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-25334015
10.
High stability and cooperative unfolding of α-synuclein oligomers.
Biochemistry
; 53(39): 6252-63, 2014 Oct 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-25216651
11.
The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.
J Am Chem Soc
; 136(10): 3859-68, 2014 Mar 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-24527756
12.
Intrinsically disordered Pseudomonas chaperone FapA slows down the fibrillation of major biofilm-forming functional amyloid FapC.
FEBS J
; 291(9): 1925-1943, 2024 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-38349812
13.
Polymorphic fibrillation of the destabilized fourth fasciclin-1 domain mutant A546T of the Transforming growth factor-ß-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates.
J Biol Chem
; 287(41): 34730-42, 2012 Oct 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-22893702
14.
Modulation of fibrillation of hIAPP core fragments by chemical modification of the peptide backbone.
Biochim Biophys Acta
; 1824(2): 274-85, 2012 Feb.
Artigo
em Inglês
| MEDLINE | ID: mdl-22064122
15.
Preventing peptide and protein misbehavior.
Proc Natl Acad Sci U S A
; 112(17): 5267-8, 2015 Apr 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-25902542
16.
Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp.
J Biol Chem
; 286(7): 4951-8, 2011 Feb 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-21135107
17.
Functional amyloids from bacterial biofilms - structural properties and interaction partners.
Chem Sci
; 13(22): 6457-6477, 2022 Jun 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-35756505
18.
Uncovering the universality of self-replication in protein aggregation and its link to disease.
Sci Adv
; 8(32): eabn6831, 2022 Aug 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-35960802
19.
Modulating Kinetics of the Amyloid-Like Aggregation of S. aureus Phenol-Soluble Modulins by Changes in pH.
Microorganisms
; 9(1)2021 Jan 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-33430169
20.
Cross-talk between individual phenol-soluble modulins in Staphylococcus aureus biofilm enables rapid and efficient amyloid formation.
Elife
; 92020 12 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-33259287