1
|
Alteration of protein-protein interactions of congenital cataract crystallin mutants.
|
Invest Ophthalmol Vis Sci
|
2003
|
1.28
|
2
|
Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay.
|
J Biol Chem
|
2001
|
1.26
|
3
|
Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant.
|
Mol Vis
|
2005
|
1.09
|
4
|
Domain interaction sites of human lens betaB2-crystallin.
|
J Biol Chem
|
2005
|
1.04
|
5
|
Unfolding of human lens recombinant betaB2- and gammaC-crystallins.
|
J Struct Biol
|
2002
|
1.00
|
6
|
Confocal fluorescence resonance energy transfer microscopy study of protein-protein interactions of lens crystallins in living cells.
|
Mol Vis
|
2007
|
0.97
|
7
|
Protein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching.
|
Mol Vis
|
2008
|
0.94
|
8
|
Protein-protein interactions among human lens acidic and basic beta-crystallins.
|
FEBS Lett
|
2007
|
0.90
|
9
|
Protein-protein interactions involving congenital cataract T5P gammaC-crystallin mutant: a confocal fluorescence microscopy study.
|
Exp Eye Res
|
2008
|
0.88
|
10
|
Enhanced stability of alpha B-crystallin in the presence of small heat shock protein Hsp27.
|
Biochem Biophys Res Commun
|
2003
|
0.88
|