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245 related items for PubMed ID: 31600047
1. Interaction between Copper Chaperone Atox1 and Parkinson's Disease Protein α-Synuclein Includes Metal-Binding Sites and Occurs in Living Cells. Horvath I, Blockhuys S, Šulskis D, Holgersson S, Kumar R, Burmann BM, Wittung-Stafshede P. ACS Chem Neurosci; 2019 Nov 20; 10(11):4659-4668. PubMed ID: 31600047 [Abstract] [Full Text] [Related]
2. Crossroads between copper ions and amyloid formation in Parkinson's disease. Wittung-Stafshede P. Essays Biochem; 2022 Dec 16; 66(7):977-986. PubMed ID: 35757906 [Abstract] [Full Text] [Related]
3. Copper chaperone blocks amyloid formation via ternary complex. Horvath I, Werner T, Kumar R, Wittung-Stafshede P. Q Rev Biophys; 2018 Jan 16; 51():e6. PubMed ID: 30912493 [Abstract] [Full Text] [Related]
4. Oxidation of Human Copper Chaperone Atox1 and Disulfide Bond Cleavage by Cisplatin and Glutathione. Nardella MI, Rosato A, Belviso BD, Caliandro R, Natile G, Arnesano F. Int J Mol Sci; 2019 Sep 06; 20(18):. PubMed ID: 31500118 [Abstract] [Full Text] [Related]
5. Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein. Strausak D, Howie MK, Firth SD, Schlicksupp A, Pipkorn R, Multhaup G, Mercer JF. J Biol Chem; 2003 Jun 06; 278(23):20821-7. PubMed ID: 12679332 [Abstract] [Full Text] [Related]
6. An EPR Study on the Interaction between the Cu(I) Metal Binding Domains of ATP7B and the Atox1 Metallochaperone. Zaccak M, Qasem Z, Gevorkyan-Airapetov L, Ruthstein S. Int J Mol Sci; 2020 Aug 02; 21(15):. PubMed ID: 32748830 [Abstract] [Full Text] [Related]
7. Single-cell tracking demonstrates copper chaperone Atox1 to be required for breast cancer cell migration. Blockhuys S, Zhang X, Wittung-Stafshede P. Proc Natl Acad Sci U S A; 2020 Jan 28; 117(4):2014-2019. PubMed ID: 31932435 [Abstract] [Full Text] [Related]
8. The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. Walker JM, Huster D, Ralle M, Morgan CT, Blackburn NJ, Lutsenko S. J Biol Chem; 2004 Apr 09; 279(15):15376-84. PubMed ID: 14754885 [Abstract] [Full Text] [Related]
9. Novel interaction of antioxidant-1 with TRAF4: role in inflammatory responses in endothelial cells. Das A, Sudhahar V, Ushio-Fukai M, Fukai T. Am J Physiol Cell Physiol; 2019 Dec 01; 317(6):C1161-C1171. PubMed ID: 31553645 [Abstract] [Full Text] [Related]
10. A revised picture of the Cu(II)-α-synuclein complex: the role of N-terminal acetylation. Moriarty GM, Minetti CA, Remeta DP, Baum J. Biochemistry; 2014 May 06; 53(17):2815-7. PubMed ID: 24739028 [Abstract] [Full Text] [Related]
11. Bioinorganic Chemistry of Parkinson's Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length β-Synuclein Protein. Miotto MC, Pavese MD, Quintanar L, Zweckstetter M, Griesinger C, Fernández CO. Inorg Chem; 2017 Sep 05; 56(17):10387-10395. PubMed ID: 28820253 [Abstract] [Full Text] [Related]
12. Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant α-synuclein variants. Lorentzon E, Kumar R, Horvath I, Wittung-Stafshede P. Biometals; 2020 Jun 05; 33(2-3):97-106. PubMed ID: 32170541 [Abstract] [Full Text] [Related]
13. Copper ion incorporation in α-synuclein amyloids. Walke G, Kumar R, Wittung-Stafshede P. Protein Sci; 2024 Apr 05; 33(4):e4956. PubMed ID: 38511511 [Abstract] [Full Text] [Related]
14. The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics. Yu CH, Yang N, Bothe J, Tonelli M, Nokhrin S, Dolgova NV, Braiterman L, Lutsenko S, Dmitriev OY. J Biol Chem; 2017 Nov 03; 292(44):18169-18177. PubMed ID: 28900031 [Abstract] [Full Text] [Related]
15. Applying chaperones to protein-misfolding disorders: molecular chaperones against α-synuclein in Parkinson's disease. Chaari A, Hoarau-Véchot J, Ladjimi M. Int J Biol Macromol; 2013 Sep 03; 60():196-205. PubMed ID: 23748003 [Abstract] [Full Text] [Related]
16. Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts. Chorell E, Andersson E, Evans ML, Jain N, Götheson A, Åden J, Chapman MR, Almqvist F, Wittung-Stafshede P. PLoS One; 2015 Sep 03; 10(10):e0140194. PubMed ID: 26465894 [Abstract] [Full Text] [Related]
17. Arylsulfatase A, a genetic modifier of Parkinson's disease, is an α-synuclein chaperone. Lee JS, Kanai K, Suzuki M, Kim WS, Yoo HS, Fu Y, Kim DK, Jung BC, Choi M, Oh KW, Li Y, Nakatani M, Nakazato T, Sekimoto S, Funayama M, Yoshino H, Kubo SI, Nishioka K, Sakai R, Ueyama M, Mochizuki H, Lee HJ, Sardi SP, Halliday GM, Nagai Y, Lee PH, Hattori N, Lee SJ. Brain; 2019 Sep 01; 142(9):2845-2859. PubMed ID: 31312839 [Abstract] [Full Text] [Related]
18. The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteins. Rekas A, Ahn KJ, Kim J, Carver JA. Proteins; 2012 May 01; 80(5):1316-25. PubMed ID: 22274962 [Abstract] [Full Text] [Related]
19. Copper Dependent Modulation of α-Synuclein Phosphorylation in Differentiated SHSY5Y Neuroblastoma Cells. Greco M, Spinelli CC, De Riccardis L, Buccolieri A, Di Giulio S, Musarò D, Pagano C, Manno D, Maffia M. Int J Mol Sci; 2021 Feb 18; 22(4):. PubMed ID: 33670800 [Abstract] [Full Text] [Related]
20. Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro. Palm ME, Weise CF, Lundin C, Wingsle G, Nygren Y, Björn E, Naredi P, Wolf-Watz M, Wittung-Stafshede P. Proc Natl Acad Sci U S A; 2011 Apr 26; 108(17):6951-6. PubMed ID: 21482801 [Abstract] [Full Text] [Related] Page: [Next] [New Search]