Detalhe da pesquisa
1.
Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains.
Proc Natl Acad Sci U S A
; 120(21): e2216234120, 2023 05 23.
Artigo
Inglês
| MEDLINE | ID: mdl-37186840
2.
The Amyloid Fibril-Forming ß-Sheet Regions of Amyloid ß and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ.
Molecules
; 26(20)2021 Oct 11.
Artigo
Inglês
| MEDLINE | ID: mdl-34684701
3.
Short-term memory span in aphasia: Insights from speech-timing measures.
J Neurolinguistics
; 48: 176-189, 2018 Nov.
Artigo
Inglês
| MEDLINE | ID: mdl-30455550
4.
Small heat-shock proteins: important players in regulating cellular proteostasis.
Cell Mol Life Sci
; 72(3): 429-451, 2015 Feb.
Artigo
Inglês
| MEDLINE | ID: mdl-25352169
5.
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers.
Proc Natl Acad Sci U S A
; 109(31): 12479-84, 2012 Jul 31.
Artigo
Inglês
| MEDLINE | ID: mdl-22802614
6.
A radish seed antifungal peptide with a high amyloid fibril-forming propensity.
Biochim Biophys Acta
; 1834(8): 1615-23, 2013 Aug.
Artigo
Inglês
| MEDLINE | ID: mdl-23665069
7.
On alert for Ebola: public health risk assessment of travellers from Uganda to the U.S. during the 2022 outbreak.
J Travel Med
; 2024 Jun 11.
Artigo
Inglês
| MEDLINE | ID: mdl-38861425
8.
Single molecule characterization of the interactions between amyloid-ß peptides and the membranes of hippocampal cells.
J Am Chem Soc
; 135(4): 1491-8, 2013 Jan 30.
Artigo
Inglês
| MEDLINE | ID: mdl-23339742
9.
Amyloid-ß oligomers are sequestered by both intracellular and extracellular chaperones.
Biochemistry
; 51(46): 9270-6, 2012 Nov 20.
Artigo
Inglês
| MEDLINE | ID: mdl-23106396
10.
Iron promotes the toxicity of amyloid beta peptide by impeding its ordered aggregation.
J Biol Chem
; 286(6): 4248-56, 2011 Feb 11.
Artigo
Inglês
| MEDLINE | ID: mdl-21147772
11.
Twisting transition between crystalline and fibrillar phases of aggregated peptides.
Phys Rev Lett
; 109(15): 158101, 2012 Oct 12.
Artigo
Inglês
| MEDLINE | ID: mdl-23102370
12.
Binding of the molecular chaperone αB-crystallin to Aß amyloid fibrils inhibits fibril elongation.
Biophys J
; 101(7): 1681-9, 2011 Oct 05.
Artigo
Inglês
| MEDLINE | ID: mdl-21961594
13.
Metastability of native proteins and the phenomenon of amyloid formation.
J Am Chem Soc
; 133(36): 14160-3, 2011 Sep 14.
Artigo
Inglês
| MEDLINE | ID: mdl-21650202
14.
The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.
Biophys J
; 98(5): 843-51, 2010 Mar 03.
Artigo
Inglês
| MEDLINE | ID: mdl-20197038
15.
The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.
Mol Vis
; 16: 2446-56, 2010 Nov 18.
Artigo
Inglês
| MEDLINE | ID: mdl-21152271
16.
Effects of Verb Overlap on Structural Priming in Dialogue: Implications for Syntactic Learning in Aphasia.
J Speech Lang Hear Res
; 62(6): 1933-1950, 2019 06 19.
Artigo
Inglês
| MEDLINE | ID: mdl-31112446
17.
Priming sentence comprehension in aphasia: Effects of lexically independent and specific structural priming.
Aphasiology
; 33(7): 780-802, 2019.
Artigo
Inglês
| MEDLINE | ID: mdl-31814655
18.
Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.
J Mol Biol
; 372(2): 470-84, 2007 Sep 14.
Artigo
Inglês
| MEDLINE | ID: mdl-17662998
19.
The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.
FASEB J
; 21(10): 2312-22, 2007 Aug.
Artigo
Inglês
| MEDLINE | ID: mdl-17412999
20.
Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.
Biochem J
; 401(1): 129-41, 2007 Jan 01.
Artigo
Inglês
| MEDLINE | ID: mdl-16928191