212 related articles for article (PubMed ID: 37529680)
1. The unhappy chaperone.
Linse S; Thalberg K; Knowles TPJ
QRB Discov; 2021; 2():e7. PubMed ID: 37529680
[TBL] [Abstract][Full Text] [Related]
2. Mechanistic Insights into the Role of Molecular Chaperones in Protein Misfolding Diseases: From Molecular Recognition to Amyloid Disassembly.
Hervás R; Oroz J
Int J Mol Sci; 2020 Dec; 21(23):. PubMed ID: 33276458
[TBL] [Abstract][Full Text] [Related]
3. Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation.
Månsson C; Arosio P; Hussein R; Kampinga HH; Hashem RM; Boelens WC; Dobson CM; Knowles TP; Linse S; Emanuelsson C
J Biol Chem; 2014 Nov; 289(45):31066-76. PubMed ID: 25217638
[TBL] [Abstract][Full Text] [Related]
4. Proteostasis and the Regulation of Intra- and Extracellular Protein Aggregation by ATP-Independent Molecular Chaperones: Lens α-Crystallins and Milk Caseins.
Carver JA; Ecroyd H; Truscott RJW; Thorn DC; Holt C
Acc Chem Res; 2018 Mar; 51(3):745-752. PubMed ID: 29442498
[TBL] [Abstract][Full Text] [Related]
5. Mechanism of an ATP-independent protein disaggregase: I. structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone.
Nguyen TX; Jaru-Ampornpan P; Lam VQ; Cao P; Piszkiewicz S; Hess S; Shan SO
J Biol Chem; 2013 May; 288(19):13420-30. PubMed ID: 23525109
[TBL] [Abstract][Full Text] [Related]
6. HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.
Baughman HER; Clouser AF; Klevit RE; Nath A
J Biol Chem; 2018 Feb; 293(8):2687-2700. PubMed ID: 29298892
[TBL] [Abstract][Full Text] [Related]
7. Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome.
Huiting W; Dekker SL; van der Lienden JCJ; Mergener R; Musskopf MK; Furtado GV; Gerrits E; Coit D; Oghbaie M; Di Stefano LH; Schepers H; van Waarde-Verhagen MAWH; Couzijn S; Barazzuol L; LaCava J; Kampinga HH; Bergink S
Elife; 2022 Feb; 11():. PubMed ID: 35200138
[TBL] [Abstract][Full Text] [Related]
8. Distinct role of hydration water in protein misfolding and aggregation revealed by fluctuating thermodynamics analysis.
Chong SH; Ham S
Acc Chem Res; 2015 Apr; 48(4):956-65. PubMed ID: 25844814
[TBL] [Abstract][Full Text] [Related]
9. Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
Abelein A; Gräslund A; Danielsson J
Proc Natl Acad Sci U S A; 2015 Apr; 112(17):5407-12. PubMed ID: 25825723
[TBL] [Abstract][Full Text] [Related]
10. Alpha-crystallin-derived peptides as therapeutic chaperones.
Raju M; Santhoshkumar P; Krishna Sharma K
Biochim Biophys Acta; 2016 Jan; 1860(1 Pt B):246-51. PubMed ID: 26141743
[TBL] [Abstract][Full Text] [Related]
11. Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.
Garvey M; Ecroyd H; Ray NJ; Gerrard JA; Carver JA
Biomolecules; 2017 Sep; 7(3):. PubMed ID: 28895938
[TBL] [Abstract][Full Text] [Related]
12. Amyposomes, a nanotechnological chaperone with anti-amyloidogenic activity.
Re F; Giorgetti S; Biondi B; Scapin S; Mantegazza F; Cassina V; Sesana SM; Rizzi L; Eberini I; Palazzolo L; Beeg M; Gobbi M; Sardina M; Masserini M
Ann Med; 2023 Dec; 55(1):2205659. PubMed ID: 37143345
[TBL] [Abstract][Full Text] [Related]
13. Gold Nanoclusters Enhance the Efficacy of the Polymer-Based Chaperone in Restoring and Maintaining the Native Conformation of Human Islet Amyloid Polypeptide.
Zhou L; Gao G; Ma Z; Zhang Z; Gu Z; Yu L; Li X; Zhang N; Qian L; Tao Z; Sun T
ACS Appl Mater Interfaces; 2023 Jan; 15(2):3409-3419. PubMed ID: 36598876
[TBL] [Abstract][Full Text] [Related]
14. The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins.
Huang C; Lu J; Ma X; Qiang J; Wang C; Liu C; Fang Y; Zhang Y; Jiang L; Li D; Zhang S
J Biol Chem; 2022 May; 298(5):101912. PubMed ID: 35398355
[TBL] [Abstract][Full Text] [Related]
15. Thermodynamic phase diagram of amyloid-β (16-22) peptide.
Wang Y; Bunce SJ; Radford SE; Wilson AJ; Auer S; Hall CK
Proc Natl Acad Sci U S A; 2019 Feb; 116(6):2091-2096. PubMed ID: 30674664
[TBL] [Abstract][Full Text] [Related]
16. The molecular chaperone β-casein prevents amorphous and fibrillar aggregation of α-lactalbumin by stabilisation of dynamic disorder.
Sanders HM; Jovcevski B; Carver JA; Pukala TL
Biochem J; 2020 Feb; 477(3):629-643. PubMed ID: 31939601
[TBL] [Abstract][Full Text] [Related]
17. Hsp40s play complementary roles in the prevention of tau amyloid formation.
Irwin R; Faust O; Petrovic I; Wolf SG; Hofmann H; Rosenzweig R
Elife; 2021 Aug; 10():. PubMed ID: 34369377
[TBL] [Abstract][Full Text] [Related]
18. Molecular chaperones: guardians of the proteome in normal and disease states.
Jeng W; Lee S; Sung N; Lee J; Tsai FT
F1000Res; 2015; 4():. PubMed ID: 26918154
[TBL] [Abstract][Full Text] [Related]
19. The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.
Scheidt T; Carozza JA; Kolbe CC; Aprile FA; Tkachenko O; Bellaiche MMJ; Meisl G; Peter QAE; Herling TW; Ness S; Castellana-Cruz M; Benesch JLP; Vendruscolo M; Dobson CM; Arosio P; Knowles TPJ
Proc Natl Acad Sci U S A; 2021 Sep; 118(38):. PubMed ID: 34518228
[TBL] [Abstract][Full Text] [Related]
20. Chaperone-client complexes: A dynamic liaison.
Hiller S; Burmann BM
J Magn Reson; 2018 Apr; 289():142-155. PubMed ID: 29544626
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]