Detalhe da pesquisa
1.
LUBAC assembles a ubiquitin signaling platform at mitochondria for signal amplification and transport of NF-κB to the nucleus.
EMBO J
; 41(24): e112006, 2022 12 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-36398858
2.
Biophysical evaluation of the oligomerization and conformational properties of the N-terminal domain of TDP-43.
Arch Biochem Biophys
; 737: 109533, 2023 03 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-36740035
3.
Selection of synthetic proteins to modulate the human frataxin function.
Biotechnol Bioeng
; 120(2): 409-425, 2023 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-36225115
4.
Thin-Plate Superstructures of the Immunogenic 33-mer Gliadin Peptide.
Chembiochem
; 23(22): e202200552, 2022 11 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-36161684
5.
Implementing Complementary Approaches to Shape the Mechanism of α-Synuclein Oligomerization as a Model of Amyloid Aggregation.
Molecules
; 27(1)2021 Dec 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-35011320
6.
Frataxin Structure and Function.
Subcell Biochem
; 93: 393-438, 2019.
Artigo
em Inglês
| MEDLINE | ID: mdl-31939159
7.
Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.
Molecules
; 25(20)2020 Oct 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-33096797
8.
Structure of the Human ACP-ISD11 Heterodimer.
Biochemistry
; 58(46): 4596-4609, 2019 11 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-31664822
9.
Modulating amyloid fibrillation in a minimalist model peptide by intermolecular disulfide chemical reduction.
Phys Chem Chem Phys
; 21(22): 11916-11923, 2019 Jun 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-31125036
10.
Molecular mechanisms of 33-mer gliadin peptide oligomerisation.
Phys Chem Chem Phys
; 21(40): 22539-22552, 2019 Oct 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-31588935
11.
Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages.
Nanomedicine
; 14(4): 1417-1427, 2018 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-29689371
12.
Insights on the conformational dynamics of human frataxin through modifications of loop-1.
Arch Biochem Biophys
; 636: 123-137, 2017 12 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-29097312
13.
Direct Cysteine Desulfurase Activity Determination by NMR and the Study of the Functional Role of Key Structural Elements of Human NFS1.
ACS Chem Biol
; 18(7): 1534-1547, 2023 07 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-37410592
14.
Gliadin proteolytical resistant peptides: the interplay between structure and self-assembly in gluten-related disorders.
Biophys Rev
; 13(6): 1147-1154, 2021 Dec.
Artigo
em Inglês
| MEDLINE | ID: mdl-35047092
15.
Pepsin Digest of Gliadin Forms Spontaneously Amyloid-Like Nanostructures Influencing the Expression of Selected Pro-Inflammatory, Chemoattractant, and Apoptotic Genes in Caco-2 Cells: Implications for Gluten-Related Disorders.
Mol Nutr Food Res
; 65(16): e2100200, 2021 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-34110092
16.
Structural conformation and self-assembly process of p31-43 gliadin peptide in aqueous solution. Implications for celiac disease.
FEBS J
; 287(10): 2134-2149, 2020 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-31659864
17.
Exploring iron-binding to human frataxin and to selected Friedreich ataxia mutants by means of NMR and EPR spectroscopies.
Biochim Biophys Acta Proteins Proteom
; 1867(11): 140254, 2019 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-31344531
18.
p31-43 Gliadin Peptide Forms Oligomers and Induces NLRP3 Inflammasome/Caspase 1- Dependent Mucosal Damage in Small Intestine.
Front Immunol
; 10: 31, 2019.
Artigo
em Inglês
| MEDLINE | ID: mdl-30761127
19.
Policy options and practical recommendations for determining priorities in public health research agendas in peripheral countries: insights from a collaborative work initiative in Argentina during the COVID-19 pandemic.
Front Med (Lausanne)
; 10: 1334194, 2023.
Artigo
em Inglês
| MEDLINE | ID: mdl-38274453
20.
Rescuing the Rescuer: On the Protein Complex between the Human Mitochondrial Acyl Carrier Protein and ISD11.
ACS Chem Biol
; 13(6): 1455-1462, 2018 06 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-29737835