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Acta Crystallographica. Section D, Biological Crystallography|November 1, 1995
On the solution of the molecular-replacement problem at very low resolution: application to large complexesA Urzhumtsev, A Podjarny
Cellular and Molecular Life Sciences : CMLS|May 15, 2007
Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sitesO El-Kabbani, A Podjarny
Biochemistry|April 5, 1977
Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozymeA Yonath, A Podjarny, B Honig, et al.
Biochemistry|April 5, 1977
Crystallographic studies of protein denaturation and renaturation. 1. Effects of denaturants on volume and X-ray pattern of cross-linked triclinic lysozyme crystalsA Yonath, A Sielecki, J Moult, et al.
Acta Crystallographica. Section D, Biological Crystallography|March 1, 1993
Structure determination of aldose reductase: joys and traps of local symmetry averagingF Tête-Favier, J M Rondeau, A Podjarny, et al.
Cellular and Molecular Life Sciences : CMLS|April 20, 2004
Subatomic and atomic crystallographic studies of aldose reductase: implications for inhibitor bindingA Podjarny, R E Cachau, T Schneider, et al.
Biophysics of Structure and Mechanism|December 27, 1977
Structural analysis of denaturant-protein interactions: comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozymeA Yonath, A Podjarny, B Honig, et al.
European Biophysics Journal : EBJ|April 20, 2006
Comparison of hydrogen determination with X-ray and neutron crystallography in a human aldose reductase-inhibitor complexM P Blakeley, A Mitschler, I Hazemann, et al.
Nature|January 30, 1992
Novel NADPH-binding domain revealed by the crystal structure of aldose reductaseJ M Rondeau, F Tête-Favier, A Podjarny, et al.
Proteins|October 12, 2000
Aldose and aldehyde reductases: correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active siteO El-Kabbani, H Rogniaux, P Barth, et al.
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