Wilson MR - Search Results

1

Dabbs RA, Wyatt AR, Yerbury JJ, Ecroyd H, Wilson MR. Dabbs RA, et al. Among authors: wilson mr. Top Curr Chem. 2013;328:241-68. doi: 10.1007/128_2011_262. Top Curr Chem. 2013. PMID: 22076079 Review.

2

Clusterin has chaperone-like activity similar to that of small heat shock proteins.

Humphreys DT, Carver JA, Easterbrook-Smith SB, Wilson MR. Humphreys DT, et al. Among authors: wilson mr. J Biol Chem. 1999 Mar 12;274(11):6875-81. doi: 10.1074/jbc.274.11.6875. J Biol Chem. 1999. PMID: 10066740 Free article.

3

Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway.

Poon S, Treweek TM, Wilson MR, Easterbrook-Smith SB, Carver JA. Poon S, et al. Among authors: wilson mr. FEBS Lett. 2002 Feb 27;513(2-3):259-66. doi: 10.1016/s0014-5793(02)02326-8. FEBS Lett. 2002. PMID: 11904161 Free article.

4

Mildly acidic pH activates the extracellular molecular chaperone clusterin.

Poon S, Rybchyn MS, Easterbrook-Smith SB, Carver JA, Pankhurst GJ, Wilson MR. Poon S, et al. Among authors: wilson mr. J Biol Chem. 2002 Oct 18;277(42):39532-40. doi: 10.1074/jbc.M204855200. Epub 2002 Aug 9. J Biol Chem. 2002. PMID: 12176985 Free article.

5

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: wilson mr. IUBMB Life. 2003 Dec;55(12):661-8. doi: 10.1080/15216540310001640498. IUBMB Life. 2003. PMID: 14769002 Free article. Review.

6

The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin.

Yerbury JJ, Rybchyn MS, Easterbrook-Smith SB, Henriques C, Wilson MR. Yerbury JJ, et al. Among authors: wilson mr. Biochemistry. 2005 Aug 16;44(32):10914-25. doi: 10.1021/bi050764x. Biochemistry. 2005. PMID: 16086594

7

Quality control of protein folding in extracellular space.

Yerbury JJ, Stewart EM, Wyatt AR, Wilson MR. Yerbury JJ, et al. Among authors: wilson mr. EMBO Rep. 2005 Dec;6(12):1131-6. doi: 10.1038/sj.embor.7400586. EMBO Rep. 2005. PMID: 16319958 Free PMC article. Review.

8

Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.

Stewart EM, Aquilina JA, Easterbrook-Smith SB, Murphy-Durland D, Jacobsen C, Moestrup S, Wilson MR. Stewart EM, et al. Among authors: wilson mr. Biochemistry. 2007 Feb 6;46(5):1412-22. doi: 10.1021/bi062082v. Biochemistry. 2007. PMID: 17260971

9

The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM. Kumita JR, et al. Among authors: wilson mr. J Mol Biol. 2007 May 25;369(1):157-67. doi: 10.1016/j.jmb.2007.02.095. Epub 2007 Mar 7. J Mol Biol. 2007. PMID: 17407782 Free article.

10

The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.

Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR. Yerbury JJ, et al. Among authors: wilson mr. FASEB J. 2007 Aug;21(10):2312-22. doi: 10.1096/fj.06-7986com. Epub 2007 Apr 5. FASEB J. 2007. PMID: 17412999

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