These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
4. The intrinsic amyloidogenic propensity of cofilin-1 is aggravated by Cys-80 oxidation: A possible link with neurodegenerative diseases. Kaushik V, Brünnert D, Hanschmann EM, Sharma PK, Anand BG, Kar K, Kateriya S, Goyal P. Biochem Biophys Res Commun; 2021 Sep 10; 569():187-192. PubMed ID: 34256187 [Abstract] [Full Text] [Related]
10. Structural insights into a yeast prion illuminate nucleation and strain diversity. Krishnan R, Lindquist SL. Nature; 2005 Jun 09; 435(7043):765-72. PubMed ID: 15944694 [Abstract] [Full Text] [Related]
11. Mechanisms and consequences of protein cysteine oxidation: the role of the initial short-lived intermediates. Turell L, Zeida A, Trujillo M. Essays Biochem; 2020 Feb 17; 64(1):55-66. PubMed ID: 31919496 [Abstract] [Full Text] [Related]
13. Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast. MacLea KS, Paul KR, Ben-Musa Z, Waechter A, Shattuck JE, Gruca M, Ross ED. Mol Cell Biol; 2015 Mar 17; 35(5):899-911. PubMed ID: 25547291 [Abstract] [Full Text] [Related]
14. Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues. Bao R, Zhang Y, Zhou CZ, Chen Y. Biochim Biophys Acta; 2009 Apr 17; 1794(4):716-21. PubMed ID: 19166985 [Abstract] [Full Text] [Related]
16. Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein. Gianni S, Camilloni C, Giri R, Toto A, Bonetti D, Morrone A, Sormanni P, Brunori M, Vendruscolo M. Proc Natl Acad Sci U S A; 2014 Sep 30; 111(39):14141-6. PubMed ID: 25228761 [Abstract] [Full Text] [Related]
17. Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase. Osváth S, Jäckel M, Agócs G, Závodszky P, Köhler G, Fidy J. Proteins; 2006 Mar 01; 62(4):909-17. PubMed ID: 16353200 [Abstract] [Full Text] [Related]
18. Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation. Taler-Verčič A, Hasanbašić S, Berbić S, Stoka V, Turk D, Žerovnik E. Int J Mol Sci; 2017 Mar 07; 18(3):. PubMed ID: 28272335 [Abstract] [Full Text] [Related]
19. Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system. Zhu L, Zhang XJ, Wang LY, Zhou JM, Perrett S. J Mol Biol; 2003 Apr 18; 328(1):235-54. PubMed ID: 12684011 [Abstract] [Full Text] [Related]