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Teresa M Treweek

Showing results (1-10 of 9) with videos related to

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Cellular and Molecular Life Sciences : CMLS|October 30, 2014
Small heat-shock proteins: important players in regulating cellular proteostasisTeresa M Treweek, Sarah Meehan, Heath Ecroyd, et al.
Experimental Eye Research|August 25, 2010
A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallinTeresa M Treweek, Agata Rekas, Mark J Walker, et al.
Archives of Biochemistry and Biophysics|April 5, 2011
The chaperone action of bovine milk αS1- and αS2-caseins and their associated form αS-caseinTeresa M Treweek, David C Thorn, William E Price, et al.
Journal of Agricultural and Food Chemistry|March 31, 2005
Casein proteins as molecular chaperonesPhilip E Morgan, Teresa M Treweek, Robyn A Lindner, et al.
The FEBS Journal|November 22, 2008
Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrityAmie M Morris, Teresa M Treweek, J A Aquilina, et al.
FEBS Letters|March 21, 2002
Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathwayStephen Poon, Teresa M Treweek, Mark R Wilson, et al.
Plos One|October 18, 2007
Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationTeresa M Treweek, Heath Ecroyd, Danielle M Williams, et al.
The FEBS Journal|January 27, 2005
R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstableTeresa M Treweek, Agata Rekas, Robyn A Lindner, et al.
Journal of Molecular Biology|July 31, 2007
Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallinsSarah Meehan, Tuomas P J Knowles, Andrew J Baldwin, et al.
Pageof 1

Showing results (1-10 of 9) with videos related to

Sort By:
Pageof 1
Cellular and Molecular Life Sciences : CMLS|October 30, 2014
Small heat-shock proteins: important players in regulating cellular proteostasisTeresa M Treweek, Sarah Meehan, Heath Ecroyd, et al.
Experimental Eye Research|August 25, 2010
A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallinTeresa M Treweek, Agata Rekas, Mark J Walker, et al.
Archives of Biochemistry and Biophysics|April 5, 2011
The chaperone action of bovine milk αS1- and αS2-caseins and their associated form αS-caseinTeresa M Treweek, David C Thorn, William E Price, et al.
Journal of Agricultural and Food Chemistry|March 31, 2005
Casein proteins as molecular chaperonesPhilip E Morgan, Teresa M Treweek, Robyn A Lindner, et al.
The FEBS Journal|November 22, 2008
Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrityAmie M Morris, Teresa M Treweek, J A Aquilina, et al.
FEBS Letters|March 21, 2002
Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathwayStephen Poon, Teresa M Treweek, Mark R Wilson, et al.
Plos One|October 18, 2007
Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationTeresa M Treweek, Heath Ecroyd, Danielle M Williams, et al.
The FEBS Journal|January 27, 2005
R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstableTeresa M Treweek, Agata Rekas, Robyn A Lindner, et al.
Journal of Molecular Biology|July 31, 2007
Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallinsSarah Meehan, Tuomas P J Knowles, Andrew J Baldwin, et al.
Pageof 1