Detalhe da pesquisa
1.
The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Mol Cell
; 81(17): 3496-3508.e5, 2021 09 02.
Artigo
Inglês
| MEDLINE | ID: mdl-34380015
2.
Mapping interactions of calmodulin and neuronal NO synthase by crosslinking and mass spectrometry.
J Biol Chem
; 300(1): 105464, 2024 Jan.
Artigo
Inglês
| MEDLINE | ID: mdl-37979917
3.
Structural insights of the p97/VCP AAA+ ATPase: How adapter interactions coordinate diverse cellular functionality.
J Biol Chem
; 299(11): 105182, 2023 11.
Artigo
Inglês
| MEDLINE | ID: mdl-37611827
4.
Polyphosphate: A Conserved Modifier of Amyloidogenic Processes.
Mol Cell
; 63(5): 768-80, 2016 09 01.
Artigo
Inglês
| MEDLINE | ID: mdl-27570072
5.
Chemical Features of Polyanions Modulate Tau Aggregation and Conformational States.
J Am Chem Soc
; 2023 Feb 08.
Artigo
Inglês
| MEDLINE | ID: mdl-36753572
6.
The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.
Mol Cell
; 56(1): 116-27, 2014 Oct 02.
Artigo
Inglês
| MEDLINE | ID: mdl-25242142
7.
Compromised function of the ESCRT pathway promotes endolysosomal escape of tau seeds and propagation of tau aggregation.
J Biol Chem
; 294(50): 18952-18966, 2019 12 13.
Artigo
Inglês
| MEDLINE | ID: mdl-31578281
8.
The full-length cytochrome P450 enzyme CYP102A1 dimerizes at its reductase domains and has flexible heme domains for efficient catalysis.
J Biol Chem
; 293(20): 7727-7736, 2018 05 18.
Artigo
Inglês
| MEDLINE | ID: mdl-29618513
9.
X-linked inhibitor of apoptosis protein (XIAP) is a client of heat shock protein 70 (Hsp70) and a biomarker of its inhibition.
J Biol Chem
; 293(7): 2370-2380, 2018 02 16.
Artigo
Inglês
| MEDLINE | ID: mdl-29255093
10.
Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.
Mol Cell
; 42(6): 771-81, 2011 Jun 24.
Artigo
Inglês
| MEDLINE | ID: mdl-21700222
11.
Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90ß in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery.
Mol Pharmacol
; 94(3): 984-991, 2018 09.
Artigo
Inglês
| MEDLINE | ID: mdl-29941666
12.
Switch I-dependent allosteric signaling in a G-protein chaperone-B12 enzyme complex.
J Biol Chem
; 292(43): 17617-17625, 2017 10 27.
Artigo
Inglês
| MEDLINE | ID: mdl-28882898
13.
Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.
Proc Natl Acad Sci U S A
; 112(7): E616-24, 2015 Feb 17.
Artigo
Inglês
| MEDLINE | ID: mdl-25646478
14.
Enhancement of dynamin polymerization and GTPase activity by Arc/Arg3.1.
Biochim Biophys Acta
; 1850(6): 1310-8, 2015 Jun.
Artigo
Inglês
| MEDLINE | ID: mdl-25783003
15.
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.
Mol Cell
; 32(5): 631-40, 2008 Dec 05.
Artigo
Inglês
| MEDLINE | ID: mdl-19061638
16.
Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.
Biochemistry
; 54(48): 7120-31, 2015 Dec 08.
Artigo
Inglês
| MEDLINE | ID: mdl-26565746
17.
Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain.
J Biol Chem
; 289(24): 16855-65, 2014 Jun 13.
Artigo
Inglês
| MEDLINE | ID: mdl-24737326
18.
The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.
J Biol Chem
; 289(5): 2908-17, 2014 Jan 31.
Artigo
Inglês
| MEDLINE | ID: mdl-24327656
19.
Cryo-EM Structures Reveal Tau Filaments from Down Syndrome Adopt Alzheimer's Disease Fold.
bioRxiv
; 2024 Apr 03.
Artigo
Inglês
| MEDLINE | ID: mdl-38617229
20.
Amyloid Accelerator Polyphosphate Implicated as the Mystery Density in α-Synuclein Fibrils.
bioRxiv
; 2024 May 02.
Artigo
Inglês
| MEDLINE | ID: mdl-38746133