Poon S - Search Results

1

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. 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.

2

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. 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.

3

Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.

Poon S, Easterbrook-Smith SB, Rybchyn MS, Carver JA, Wilson MR. Poon S, et al. Biochemistry. 2000 Dec 26;39(51):15953-60. doi: 10.1021/bi002189x. Biochemistry. 2000. PMID: 11123922

4

Evidence that clusterin has discrete chaperone and ligand binding sites.

Lakins JN, Poon S, Easterbrook-Smith SB, Carver JA, Tenniswood MP, Wilson MR. Lakins JN, et al. Among authors: poon s. Biochemistry. 2002 Jan 8;41(1):282-91. doi: 10.1021/bi0157666. Biochemistry. 2002. PMID: 11772027

5

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: poon s. FASEB J. 2007 Aug;21(10):2312-22. doi: 10.1096/fj.06-7986com. Epub 2007 Apr 5. FASEB J. 2007. PMID: 17412999

6

Chapter 6: The chaperone action of Clusterin and its putative role in quality control of extracellular protein folding.

Wyatt A, Yerbury J, Poon S, Dabbs R, Wilson M. Wyatt A, et al. Among authors: poon s. Adv Cancer Res. 2009;104:89-114. doi: 10.1016/S0065-230X(09)04006-8. Adv Cancer Res. 2009. PMID: 19878774 Review.

7

Therapeutic targets in extracellular protein deposition diseases.

Wyatt AR, Yerbury JJ, Poon S, Wilson MR. Wyatt AR, et al. Among authors: poon s. Curr Med Chem. 2009;16(22):2855-66. doi: 10.2174/092986709788803187. Curr Med Chem. 2009. PMID: 19689268 Review.

8

Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity.

Wilson MR, Yerbury JJ, Poon S. Wilson MR, et al. Among authors: poon s. Mol Biosyst. 2008 Jan;4(1):42-52. doi: 10.1039/b712728f. Epub 2007 Nov 19. Mol Biosyst. 2008. PMID: 18075673 Review.

9

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. Among authors: poon s. Biochemistry. 2008 Mar 25;47(12):3926-36. doi: 10.1021/bi701278c. Epub 2008 Feb 27. Biochemistry. 2008. PMID: 18302322

10

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: poon s. 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.

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My Custom Filters

Publication date

Text availability

Article attribute

Article type

Article Language

Species

Sex

Age

Other

566 results

Search Page

Filters