Kardos J - Search Results

1

Cold denaturation of α-synuclein amyloid fibrils.

Ikenoue T, Lee YH, Kardos J, Saiki M, Yagi H, Kawata Y, Goto Y. Ikenoue T, et al. Among authors: kardos j. Angew Chem Int Ed Engl. 2014 Jul 21;53(30):7799-804. doi: 10.1002/anie.201403815. Epub 2014 Jun 11. Angew Chem Int Ed Engl. 2014. PMID: 24920162

2

Protein folding: could hydrophobic collapse be coupled with hydrogen-bond formation?

Fernández A, Kardos J, Goto Y. Fernández A, et al. Among authors: kardos j. FEBS Lett. 2003 Feb 11;536(1-3):187-92. doi: 10.1016/s0014-5793(03)00056-5. FEBS Lett. 2003. PMID: 12586361 Free article.

3

Structural defects and the diagnosis of amyloidogenic propensity.

Fernández A, Kardos J, Scott LR, Goto Y, Berry RS. Fernández A, et al. Among authors: kardos j. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6446-51. doi: 10.1073/pnas.0731893100. Epub 2003 May 12. Proc Natl Acad Sci U S A. 2003. PMID: 12743379 Free PMC article.

4

Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.

Villanueva J, Hoshino M, Katou H, Kardos J, Hasegawa K, Naiki H, Goto Y. Villanueva J, et al. Among authors: kardos j. Protein Sci. 2004 Mar;13(3):797-809. doi: 10.1110/ps.03445704. Epub 2004 Feb 6. Protein Sci. 2004. PMID: 14767076 Free PMC article.

5

Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH.

Yamamoto S, Hasegawa K, Yamaguchi I, Tsutsumi S, Kardos J, Goto Y, Gejyo F, Naiki H. Yamamoto S, et al. Among authors: kardos j. Biochemistry. 2004 Aug 31;43(34):11075-82. doi: 10.1021/bi049262u. Biochemistry. 2004. PMID: 15323566

6

Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry.

Kardos J, Yamamoto K, Hasegawa K, Naiki H, Goto Y. Kardos J, et al. J Biol Chem. 2004 Dec 31;279(53):55308-14. doi: 10.1074/jbc.M409677200. Epub 2004 Oct 19. J Biol Chem. 2004. PMID: 15494406 Free article.

7

Structural studies reveal that the diverse morphology of beta(2)-microglobulin aggregates is a reflection of different molecular architectures.

Kardos J, Okuno D, Kawai T, Hagihara Y, Yumoto N, Kitagawa T, Závodszky P, Naiki H, Goto Y. Kardos J, et al. Biochim Biophys Acta. 2005 Nov 10;1753(1):108-20. doi: 10.1016/j.bbapap.2005.08.013. Epub 2005 Sep 9. Biochim Biophys Acta. 2005. PMID: 16185940

8

Mechanism of lysophosphatidic acid-induced amyloid fibril formation of beta(2)-microglobulin in vitro under physiological conditions.

Pál-Gábor H, Gombos L, Micsonai A, Kovács E, Petrik E, Kovács J, Gráf L, Fidy J, Naiki H, Goto Y, Liliom K, Kardos J. Pál-Gábor H, et al. Among authors: kardos j. Biochemistry. 2009 Jun 23;48(24):5689-99. doi: 10.1021/bi900356r. Biochemistry. 2009. PMID: 19432419

9

The amyloid fibrils of the constant domain of immunoglobulin light chain.

Yamamoto K, Yagi H, Lee YH, Kardos J, Hagihara Y, Naiki H, Goto Y. Yamamoto K, et al. Among authors: kardos j. FEBS Lett. 2010 Aug 4;584(15):3348-53. doi: 10.1016/j.febslet.2010.06.019. Epub 2010 Jun 18. FEBS Lett. 2010. PMID: 20580354 Free article.

10

Reversible heat-induced dissociation of β2-microglobulin amyloid fibrils.

Kardos J, Micsonai A, Pál-Gábor H, Petrik É, Gráf L, Kovács J, Lee YH, Naiki H, Goto Y. Kardos J, et al. Biochemistry. 2011 Apr 19;50(15):3211-20. doi: 10.1021/bi2000017. Epub 2011 Mar 24. Biochemistry. 2011. PMID: 21388222

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