Thorn DC - Search Results

1

Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein.

Thorn DC, Meehan S, Sunde M, Rekas A, Gras SL, MacPhee CE, Dobson CM, Wilson MR, Carver JA. Thorn DC, et al. Biochemistry. 2005 Dec 27;44(51):17027-36. doi: 10.1021/bi051352r. Biochemistry. 2005. PMID: 16363816

2

Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?

Carver JA, Rekas A, Thorn DC, Wilson MR. Carver JA, et al. Among authors: thorn dc. IUBMB Life. 2003 Dec;55(12):661-8. doi: 10.1080/15216540310001640498. IUBMB Life. 2003. PMID: 14769002 Free article. Review.

3

Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.

Rekas A, Jankova L, Thorn DC, Cappai R, Carver JA. Rekas A, et al. Among authors: thorn dc. FEBS J. 2007 Dec;274(24):6290-304. doi: 10.1111/j.1742-4658.2007.06144.x. Epub 2007 Nov 12. FEBS J. 2007. PMID: 18005258 Free article.

4

Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein.

Ecroyd H, Koudelka T, Thorn DC, Williams DM, Devlin G, Hoffmann P, Carver JA. Ecroyd H, et al. Among authors: thorn dc. J Biol Chem. 2008 Apr 4;283(14):9012-22. doi: 10.1074/jbc.M709928200. Epub 2008 Feb 1. J Biol Chem. 2008. PMID: 18245081 Free PMC article.

5

Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein.

Thorn DC, Ecroyd H, Sunde M, Poon S, Carver JA. Thorn DC, et al. Biochemistry. 2008 Mar 25;47(12):3926-36. doi: 10.1021/bi701278c. Epub 2008 Feb 27. Biochemistry. 2008. PMID: 18302322

6

The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.

Ecroyd H, Thorn DC, Liu Y, Carver JA. Ecroyd H, et al. Among authors: thorn dc. Biochem J. 2010 Jul 15;429(2):251-60. doi: 10.1042/BJ20091949. Biochem J. 2010. PMID: 20441567

7

The chaperone action of bovine milk αS1- and αS2-caseins and their associated form αS-casein.

Treweek TM, Thorn DC, Price WE, Carver JA. Treweek TM, et al. Among authors: thorn dc. Arch Biochem Biophys. 2011 Jun 1;510(1):42-52. doi: 10.1016/j.abb.2011.03.012. Epub 2011 Mar 30. Arch Biochem Biophys. 2011. PMID: 21457703

8

Amyloid fibrils from readily available sources: milk casein and lens crystallin proteins.

Ecroyd H, Garvey M, Thorn DC, Gerrard JA, Carver JA. Ecroyd H, et al. Among authors: thorn dc. Methods Mol Biol. 2013;996:103-17. doi: 10.1007/978-1-62703-354-1_6. Methods Mol Biol. 2013. PMID: 23504420

9

Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods.

Holt C, Carver JA, Ecroyd H, Thorn DC. Holt C, et al. Among authors: thorn dc. J Dairy Sci. 2013 Oct;96(10):6127-46. doi: 10.3168/jds.2013-6831. Epub 2013 Aug 16. J Dairy Sci. 2013. PMID: 23958008 Free article. Review.

10

The Effect of Milk Constituents and Crowding Agents on Amyloid Fibril Formation by κ-Casein.

Liu J, Dehle FC, Liu Y, Bahraminejad E, Ecroyd H, Thorn DC, Carver JA. Liu J, et al. Among authors: thorn dc. J Agric Food Chem. 2016 Feb 17;64(6):1335-43. doi: 10.1021/acs.jafc.5b04977. Epub 2016 Feb 4. J Agric Food Chem. 2016. PMID: 26807595

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