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Items: 1 to 20 of 102

1.

Expression and purification of chaperone-active recombinant clusterin.

Dabbs RA, Wilson MR.

PLoS One. 2014 Jan 23;9(1):e86989. doi: 10.1371/journal.pone.0086989. eCollection 2014.

2.

The chaperone activity of clusterin is dependent on glycosylation and redox environment.

Rohne P, Prochnow H, Wolf S, Renner B, Koch-Brandt C.

Cell Physiol Biochem. 2014;34(5):1626-39. doi: 10.1159/000366365. Epub 2014 Nov 3.

PMID:
25402950
3.

Evidence that clusterin has discrete chaperone and ligand binding sites.

Lakins JN, Poon S, Easterbrook-Smith SB, Carver JA, Tenniswood MP, Wilson MR.

Biochemistry. 2002 Jan 8;41(1):282-91.

PMID:
11772027
4.

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.

Biochemistry. 2007 Feb 6;46(5):1412-22.

PMID:
17260971
5.

Identification of human plasma proteins as major clients for the extracellular chaperone clusterin.

Wyatt AR, Wilson MR.

J Biol Chem. 2010 Feb 5;285(6):3532-9. doi: 10.1074/jbc.M109.079566. Epub 2009 Dec 7.

6.

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

Humphreys DT, Carver JA, Easterbrook-Smith SB, Wilson MR.

J Biol Chem. 1999 Mar 12;274(11):6875-81.

7.

Human cellular prion protein interacts directly with clusterin protein.

Xu F, Karnaukhova E, Vostal JG.

Biochim Biophys Acta. 2008 Nov;1782(11):615-20. doi: 10.1016/j.bbadis.2008.08.004. Epub 2008 Aug 22.

8.
9.

Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils.

Matsuda A, Itoh Y, Koshikawa N, Akizawa T, Yana I, Seiki M.

J Biol Chem. 2003 Sep 19;278(38):36350-7. Epub 2003 Jul 14.

10.
11.

Mildly acidic pH activates the extracellular molecular chaperone clusterin.

Poon S, Rybchyn MS, Easterbrook-Smith SB, Carver JA, Pankhurst GJ, Wilson MR.

J Biol Chem. 2002 Oct 18;277(42):39532-40. Epub 2002 Aug 9. Erratum in: J Biol Chem 2002 Dec 6;277(49):47964.

12.

High-yield expression in Escherichia coli of soluble human alpha-hemoglobin complexed with its molecular chaperone.

Vasseur-Godbillon C, Hamdane D, Marden MC, Baudin-Creuza V.

Protein Eng Des Sel. 2006 Mar;19(3):91-7. Epub 2006 Jan 3.

13.

The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.

Narayan P, Orte A, Clarke RW, Bolognesi B, Hook S, Ganzinger KA, Meehan S, Wilson MR, Dobson CM, Klenerman D.

Nat Struct Mol Biol. 2011 Dec 18;19(1):79-83. doi: 10.1038/nsmb.2191.

PMID:
22179788
14.

Clusterin facilitates in vivo clearance of extracellular misfolded proteins.

Wyatt AR, Yerbury JJ, Berghofer P, Greguric I, Katsifis A, Dobson CM, Wilson MR.

Cell Mol Life Sci. 2011 Dec;68(23):3919-31. doi: 10.1007/s00018-011-0684-8). Epub 2011 Apr 20.

PMID:
21505792
15.

Structural characterization of clusterin-chaperone client protein complexes.

Wyatt AR, Yerbury JJ, Wilson MR.

J Biol Chem. 2009 Aug 14;284(33):21920-7. doi: 10.1074/jbc.M109.033688. Epub 2009 Jun 17.

16.
17.

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.

Biochemistry. 2000 Dec 26;39(51):15953-60.

PMID:
11123922
18.

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.

FEBS Lett. 2002 Feb 27;513(2-3):259-66.

19.

pH-dependent changes in the in vitro ligand-binding properties and structure of human clusterin.

Hochgrebe T, Pankhurst GJ, Wilce J, Easterbrook-Smith SB.

Biochemistry. 2000 Feb 15;39(6):1411-9.

PMID:
10684622
20.

Expression, purification, and molecular analysis of the Necator americanus glutathione S-transferase 1 (Na-GST-1): a production process developed for a lead candidate recombinant hookworm vaccine antigen.

Goud GN, Deumic V, Gupta R, Brelsford J, Zhan B, Gillespie P, Plieskatt JL, Tsao EI, Hotez PJ, Bottazzi ME.

Protein Expr Purif. 2012 Jun;83(2):145-51. doi: 10.1016/j.pep.2012.03.013. Epub 2012 Apr 4.

PMID:
22503665
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