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Cellular and Molecular Life Sciences : CMLS
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October 30, 2014
Small heat-shock proteins: important players in regulating cellular proteostasis
Teresa 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-crystallin
Teresa 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-casein
Teresa M Treweek, David C Thorn, William E Price, et al.
Journal of Agricultural and Food Chemistry
|
March 31, 2005
Casein proteins as molecular chaperones
Philip 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 integrity
Amie 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 pathway
Stephen 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 formation
Teresa 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 unstable
Teresa 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-crystallins
Sarah Meehan, Tuomas P J Knowles, Andrew J Baldwin, et al.
Page
of 1
Search research articles
Search
Showing results (1-10 of 9) with videos related to
Sort By:
Page
of 1
Cellular and Molecular Life Sciences : CMLS
|
October 30, 2014
Small heat-shock proteins: important players in regulating cellular proteostasis
Teresa 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-crystallin
Teresa 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-casein
Teresa M Treweek, David C Thorn, William E Price, et al.
Journal of Agricultural and Food Chemistry
|
March 31, 2005
Casein proteins as molecular chaperones
Philip 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 integrity
Amie 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 pathway
Stephen 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 formation
Teresa 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 unstable
Teresa 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-crystallins
Sarah Meehan, Tuomas P J Knowles, Andrew J Baldwin, et al.
Page
of 1