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Biophysical Journal|March 22, 2001
Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamilyS Abgar, J Vanhoudt, T Aerts, et al.
Biochemistry|April 12, 2000
Native quaternary structure of bovine alpha-crystallinJ Vanhoudt, S Abgar, T Aerts, et al.
European Journal of Biochemistry|June 10, 2000
A small-angle X-ray solution scattering study of bovine alpha-crystallinJ Vanhoudt, S Abgar, T Aerts, et al.
International Journal of Biological Macromolecules|July 3, 1998
Quaternary structure of bovine alpha-crystallin: influence of temperatureJ Vanhoudt, T Aerts, S Abgar, et al.
European Journal of Biochemistry|September 21, 2000
The structural differences between bovine lens alphaA- and alphaB-crystallinS Abgar, J Backmann, T Aerts, et al.
Biochemical and Biophysical Research Communications|October 12, 2000
Chaperone-like activity of bovine lens alpha-crystallin in the presence of dithiothreitol-destabilized proteins: characterization of the formed complexesS Abgar, N Yevlampieva, T Aerts, et al.
Biophysical Journal|March 1, 1994
Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interactionJ Z Xia, T Aerts, K Donceel, et al.
Biological Signals and Receptors|February 25, 2000
Purification of rat C6 glioma plasma membranes by affinity partitioningQ Wang, Y Wu, T Aerts, et al.
Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology|February 9, 1999
Expression of IGF-I and IGF-II receptors in rat C6 glioma cells as a function of the growth phaseQ Wang, Y Wu, T Aerts, et al.
Biophysical Journal|November 1, 1996
Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteinsJ Z Xia, Q Wang, S Tatarkova, et al.
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