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1.
TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models.
EMBO J
; 39(17): e104671, 2020 09 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-32757223
2.
Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM.
Proc Natl Acad Sci U S A
; 117(12): 6866-6874, 2020 03 24.
Artículo
en Inglés
| MEDLINE | ID: mdl-32161130
3.
Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils.
J Am Chem Soc
; 144(24): 10723-10735, 2022 06 22.
Artículo
en Inglés
| MEDLINE | ID: mdl-35679155
4.
Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau.
J Biol Chem
; 295(23): 7905-7922, 2020 06 05.
Artículo
en Inglés
| MEDLINE | ID: mdl-32341125
5.
Site-Specific Phosphorylation of Huntingtin Exonâ 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases.
Chembiochem
; 22(1): 217-231, 2021 01 05.
Artículo
en Inglés
| MEDLINE | ID: mdl-32805086
6.
A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of α-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α-synuclein research.
J Neurochem
; 153(1): 103-119, 2020 04.
Artículo
en Inglés
| MEDLINE | ID: mdl-31925956
7.
Phosphorylation of huntingtin at residue T3 is decreased in Huntington's disease and modulates mutant huntingtin protein conformation.
Proc Natl Acad Sci U S A
; 114(50): E10809-E10818, 2017 12 12.
Artículo
en Inglés
| MEDLINE | ID: mdl-29162692
8.
N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting.
J Biol Chem
; 293(48): 18540-18558, 2018 11 30.
Artículo
en Inglés
| MEDLINE | ID: mdl-30185623
9.
Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.
Angew Chem Int Ed Engl
; 56(19): 5202-5207, 2017 05 02.
Artículo
en Inglés
| MEDLINE | ID: mdl-28334491
10.
Elucidating the Role of Site-Specific Nitration of α-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis.
J Am Chem Soc
; 137(15): 5041-52, 2015 Apr 22.
Artículo
en Inglés
| MEDLINE | ID: mdl-25768729
11.
Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore.
ACS Nano
; 18(2): 1504-1515, 2024 Jan 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-38112538
12.
Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity.
NPJ Parkinsons Dis
; 8(1): 136, 2022 Oct 20.
Artículo
en Inglés
| MEDLINE | ID: mdl-36266318
13.
Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation.
Front Mol Biosci
; 8: 686086, 2021.
Artículo
en Inglés
| MEDLINE | ID: mdl-34381813
14.
The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1.
J Mol Biol
; 433(21): 167222, 2021 10 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-34492254
15.
Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates.
Sci Rep
; 11(1): 17977, 2021 09 09.
Artículo
en Inglés
| MEDLINE | ID: mdl-34504195
16.
Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity.
Nat Commun
; 11(1): 2820, 2020 06 04.
Artículo
en Inglés
| MEDLINE | ID: mdl-32499486
17.
Chronic corticosterone aggravates behavioral and neuronal symptomatology in a mouse model of alpha-synuclein pathology.
Neurobiol Aging
; 83: 11-20, 2019 11.
Artículo
en Inglés
| MEDLINE | ID: mdl-31585362
18.
Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy.
J Vis Exp
; (136)2018 06 27.
Artículo
en Inglés
| MEDLINE | ID: mdl-30010666
19.
Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding.
Protein Sci
; 27(7): 1262-1274, 2018 07.
Artículo
en Inglés
| MEDLINE | ID: mdl-29603451
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