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Items: 1 to 20 of 91

1.

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

Wilson MR, Yerbury JJ, Poon S.

Mol Biosyst. 2008 Jan;4(1):42-52. Review.

PMID:
18075673
2.

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.

Adv Cancer Res. 2009;104:89-114. doi: 10.1016/S0065-230X(09)04006-8. Review.

PMID:
19878774
3.

Therapeutic targets in extracellular protein deposition diseases.

Wyatt AR, Yerbury JJ, Poon S, Wilson MR.

Curr Med Chem. 2009;16(22):2855-66. Review.

PMID:
19689268
4.

Do extracellular chaperone proteins in plasma have potential as Alzheimer's disease biomarkers?

Thambisetty M.

Biomark Med. 2010 Dec;4(6):831-4. doi: 10.2217/bmm.10.108. No abstract available.

5.

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.

Biochemistry. 2005 Aug 16;44(32):10914-25.

PMID:
16086594
6.

Quality control of protein folding in extracellular space.

Yerbury JJ, Stewart EM, Wyatt AR, Wilson MR.

EMBO Rep. 2005 Dec;6(12):1131-6. Review.

7.

Chaperones in control of protein disaggregation.

Liberek K, Lewandowska A, Zietkiewicz S.

EMBO J. 2008 Jan 23;27(2):328-35. doi: 10.1038/sj.emboj.7601970. Review.

8.

Roles of extracellular chaperones in amyloidosis.

Wyatt AR, Yerbury JJ, Dabbs RA, Wilson MR.

J Mol Biol. 2012 Aug 24;421(4-5):499-516. doi: 10.1016/j.jmb.2012.01.004. Review.

PMID:
22248589
9.

Influence of molecular and chemical chaperones on protein folding.

Welch WJ, Brown CR.

Cell Stress Chaperones. 1996 Jun;1(2):109-15. Review. Erratum in: Cell Stress Chaperones 1996 Sep;1(3):207.

10.

Protein folding and diseases.

Lee C, Yu MH.

J Biochem Mol Biol. 2005 May 31;38(3):275-80. Review.

PMID:
15943901
11.

The role of chaperone-assisted folding and quality control in inborn errors of metabolism: protein folding disorders.

Gregersen N, Bross P, Andrese BS, Pedersen CB, Corydon TJ, Bolund L.

J Inherit Metab Dis. 2001 Apr;24(2):189-212. Review.

PMID:
11405340
12.
13.

Extracellular chaperones.

Dabbs RA, Wyatt AR, Yerbury JJ, Ecroyd H, Wilson MR.

Top Curr Chem. 2013;328:241-68. doi: 10.1007/128_2011_262. Review.

PMID:
22076079
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).

PMID:
21505792
15.

Protein misfolding disorders: pathogenesis and intervention.

Gregersen N.

J Inherit Metab Dis. 2006 Apr-Jun;29(2-3):456-70. Review.

PMID:
16763918
16.

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.

17.

Molecular roles of chaperones in assisted folding and assembly of proteins.

Fisher MT.

Genet Eng (N Y). 2006;27:191-229. Review. No abstract available.

PMID:
16382878
18.

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity.

Butterfield S, Hejjaoui M, Fauvet B, Awad L, Lashuel HA.

J Mol Biol. 2012 Aug 10;421(2-3):204-36. doi: 10.1016/j.jmb.2012.01.051. Review.

PMID:
22342932
19.

The role of chaperones in polyglutamine disease.

Opal P, Zoghbi HY.

Trends Mol Med. 2002 May;8(5):232-6. Review.

PMID:
12067633
20.

Structure, formation and propagation of amyloid fibrils.

Goto Y, Yagi H, Yamaguchi K, Chatani E, Ban T.

Curr Pharm Des. 2008;14(30):3205-18. Review.

PMID:
19075701

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