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1.
p53 amyloid pathology is correlated with higher cancer grade irrespective of the mutant or wild-type form.
J Cell Sci
; 136(17)2023 09 01.
Article
in English
| MEDLINE | ID: mdl-37622400
2.
Protein misfolding and amyloid nucleation through liquid-liquid phase separation.
Chem Soc Rev
; 53(10): 4976-5013, 2024 May 20.
Article
in English
| MEDLINE | ID: mdl-38597222
3.
Oncogenic gain of function due to p53 amyloids occurs through aberrant alteration of cell cycle and proliferation.
J Cell Sci
; 135(15)2022 08 01.
Article
in English
| MEDLINE | ID: mdl-35796018
4.
Direct evidence of cellular transformation by prion-like p53 amyloid infection.
J Cell Sci
; 134(11)2021 06 01.
Article
in English
| MEDLINE | ID: mdl-34085695
5.
Role of non-specific interactions in the phase-separation and maturation of macromolecules.
PLoS Comput Biol
; 18(5): e1010067, 2022 05.
Article
in English
| MEDLINE | ID: mdl-35533203
6.
Modulating α-Synuclein Liquid-Liquid Phase Separation.
Biochemistry
; 60(48): 3676-3696, 2021 12 07.
Article
in English
| MEDLINE | ID: mdl-34431665
7.
Benzimidazole-based fluorophores for the detection of amyloid fibrils with higher sensitivity than Thioflavin-T.
J Neurochem
; 156(6): 1003-1019, 2021 03.
Article
in English
| MEDLINE | ID: mdl-32750740
8.
Biophysical characterization of p53 core domain aggregates.
Biochem J
; 477(1): 111-120, 2020 01 17.
Article
in English
| MEDLINE | ID: mdl-31841126
9.
Prion-like p53 Amyloids in Cancer.
Biochemistry
; 59(2): 146-155, 2020 01 21.
Article
in English
| MEDLINE | ID: mdl-31603660
10.
Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils.
J Biol Chem
; 293(34): 12975-12991, 2018 08 24.
Article
in English
| MEDLINE | ID: mdl-29959225
11.
α-Synuclein Spontaneously Adopts Stable and Reversible α-Helical Structure in Water-Less Environment.
Chemphyschem
; 20(21): 2783-2790, 2019 11 05.
Article
in English
| MEDLINE | ID: mdl-31515915
12.
Protein Nanofibrils as Storage Forms of Peptide Drugs and Hormones.
Adv Exp Med Biol
; 1174: 265-290, 2019.
Article
in English
| MEDLINE | ID: mdl-31713202
13.
The Familial α-Synuclein A53E Mutation Enhances Cell Death in Response to Environmental Toxins Due to a Larger Population of Oligomers.
Biochemistry
; 57(33): 5014-5028, 2018 08 21.
Article
in English
| MEDLINE | ID: mdl-30025458
14.
Complexation of NAC-Derived Peptide Ligands with the C-Terminus of α-Synuclein Accelerates Its Aggregation.
Biochemistry
; 57(5): 791-804, 2018 02 06.
Article
in English
| MEDLINE | ID: mdl-29286644
15.
Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation.
Biochemistry
; 57(35): 5183-5187, 2018 09 04.
Article
in English
| MEDLINE | ID: mdl-29771508
16.
Amyloid Fibrils: Versatile Biomaterials for Cell Adhesion and Tissue Engineering Applications.
Biomacromolecules
; 19(6): 1826-1839, 2018 06 11.
Article
in English
| MEDLINE | ID: mdl-29701992
17.
Amyloids Are Novel Cell-Adhesive Matrices.
Adv Exp Med Biol
; 1112: 79-97, 2018.
Article
in English
| MEDLINE | ID: mdl-30637692
18.
Cytotoxic Oligomers and Fibrils Trapped in a Gel-like State of α-Synuclein Assemblies.
Angew Chem Int Ed Engl
; 57(19): 5262-5266, 2018 05 04.
Article
in English
| MEDLINE | ID: mdl-29524323
19.
Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.
J Biol Chem
; 291(10): 5278-98, 2016 Mar 04.
Article
in English
| MEDLINE | ID: mdl-26742841
20.
Differential copper binding to alpha-synuclein and its disease-associated mutants affect the aggregation and amyloid formation.
Biochim Biophys Acta Gen Subj
; 1861(2): 365-374, 2017 Feb.
Article
in English
| MEDLINE | ID: mdl-27916677