Treweek TM - Search Results

1

Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.

Meehan S, Knowles TP, Baldwin AJ, Smith JF, Squires AM, Clements P, Treweek TM, Ecroyd H, Tartaglia GG, Vendruscolo M, Macphee CE, Dobson CM, Carver JA. Meehan S, et al. Among authors: treweek tm. J Mol Biol. 2007 Sep 14;372(2):470-84. doi: 10.1016/j.jmb.2007.06.060. Epub 2007 Jun 29. J Mol Biol. 2007. PMID: 17662998

2

Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation.

Treweek TM, Ecroyd H, Williams DM, Meehan S, Carver JA, Walker MJ. Treweek TM, et al. PLoS One. 2007 Oct 17;2(10):e1046. doi: 10.1371/journal.pone.0001046. PLoS One. 2007. PMID: 17940610 Free PMC article.

3

Small heat-shock proteins: important players in regulating cellular proteostasis.

Treweek TM, Meehan S, Ecroyd H, Carver JA. Treweek TM, et al. Cell Mol Life Sci. 2015 Feb;72(3):429-451. doi: 10.1007/s00018-014-1754-5. Epub 2014 Oct 29. Cell Mol Life Sci. 2015. PMID: 25352169 Free PMC article. Review.

4

R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable.

Treweek TM, Rekas A, Lindner RA, Walker MJ, Aquilina JA, Robinson CV, Horwitz J, Perng MD, Quinlan RA, Carver JA. Treweek TM, et al. FEBS J. 2005 Feb;272(3):711-24. doi: 10.1111/j.1742-4658.2004.04507.x. FEBS J. 2005. PMID: 15670152 Free article.

5

Casein proteins as molecular chaperones.

Morgan PE, Treweek TM, Lindner RA, Price WE, Carver JA. Morgan PE, et al. Among authors: treweek tm. J Agric Food Chem. 2005 Apr 6;53(7):2670-83. doi: 10.1021/jf048329h. J Agric Food Chem. 2005. PMID: 15796610

6

A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.

Treweek TM, Rekas A, Walker MJ, Carver JA. Treweek TM, et al. Exp Eye Res. 2010 Nov;91(5):691-9. doi: 10.1016/j.exer.2010.08.015. Epub 2010 Aug 21. Exp Eye Res. 2010. PMID: 20732317

7

The small heat-shock chaperone protein, alpha-crystallin, does not recognize stable molten globule states of cytosolic proteins.

Treweek TM, Lindner RA, Mariani M, Carver JA. Treweek TM, et al. Biochim Biophys Acta. 2000 Aug 31;1481(1):175-88. doi: 10.1016/s0167-4838(00)00109-6. Biochim Biophys Acta. 2000. PMID: 10962105

8

The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.

Lindner RA, Treweek TM, Carver JA. Lindner RA, et al. Among authors: treweek tm. Biochem J. 2001 Feb 15;354(Pt 1):79-87. doi: 10.1042/0264-6021:3540079. Biochem J. 2001. PMID: 11171082 Free PMC article.

9

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: treweek tm. 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.

10

Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity.

Morris AM, Treweek TM, Aquilina JA, Carver JA, Walker MJ. Morris AM, et al. Among authors: treweek tm. FEBS J. 2008 Dec;275(23):5885-98. doi: 10.1111/j.1742-4658.2008.06719.x. FEBS J. 2008. PMID: 19021764 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

13 results

Search Page

Filters