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  1. 1.   The RIO kinases: An atypical protein kinase family required for ribosome biogenesis and cell cycle progression
  2. Laronde-Leblanc, N.; Wlodawer, A.
  3. Biochimica Et Biophysica Acta-Proteins and Proteomics. 2005, DEC 30; 1754(1-2, Sp. Iss.): 14-24.
  1. 2.   Multifunctional roles of the conserved arg residues in the second region of homology of p97/valosin-containing protein
  2. Wang, Q.; Song, C. C.; Irizarry, L.; Dai, R. M.; Zhang, X. D.; Li, C. C. H.
  3. Journal of Biological Chemistry. 2005, DEC 9; 280(49): 40515-40523.
  1. 3.   A family portrait of the RIO kinases
  2. Laronde-Leblanc, N.; Wlodawer, A.
  3. Journal of Biological Chemistry. 2005, NOV 11; 280(45): 37297-37300.
  1. 4.   Is the critical role of loop 3 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase in catalysis due to loop-3 residues arginine-84 and tryptophan-89? Site-directed mutagenesis, biochemical, and crystallographic studies
  2. Li, Y.; Blaszczyk, J.; Wu, Y.; Shi, G. B.; Ji, X. H.; Yan, H. G.
  3. Biochemistry. 2005, JUN 21; 44(24): 8590-8599.
  1. 5.   Comparison of the substrate specificity of two potyvirus proteases
  2. Tozser, J.; Tropea, J. E.; Cherry, S.; Bagossi, P.; Copeland, T.; Wlodawer, A.; Waugh, D. S.
  3. Febs Journal. 2005, JAN; 272(2): 514-523.
  1. 6.   Substrate-induced conformational changes in glycosyltransferases
  2. Qasba, P. K.; Ramakrishnan, B.; Boeggeman, E.
  3. Trends in Biochemical Sciences. 2005, JAN; 30(1): 53-62.
  1. 7.   Crystal structure of A-fulgidus Rio2 defines a new family of serine protein kinases
  2. Laronde-Leblanc, N.; Wlodawer, A.
  3. Structure. 2004, SEP; 12(9): 1585-1594.
  1. 8.   The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
  2. Botos, I.; Melnikov, E. E.; Cherry, S.; Tropea, J. E.; Khalatova, A. G.; Rasulova, F.; Dauter, Z.; Maurizi, M. R.; Rotanova, T. V.; Wlodawer, A.; Gustchina, A.
  3. Journal of Biological Chemistry. 2004 279(9): 8140-8148.
  1. 9.   Modulating functional loop movements: The role of highly conserved residues in the correlated loop motions
  2. Gunasekaran, K.; Nussinov, R.
  3. Chembiochem. 2004 5(2): 224-230.
  1. 10.   The role of tryptophan 314 in the conformational changes of beta 1,4-galactosyltransferase-I
  2. Ramasamy, V.; Ramakrishnan, B.; Boeggeman, E.; Qasba, P. K.
  3. Journal of Molecular Biology. 2003 331(5): 1065-1076.
  1. 11.   Studies on the metal binding sites in the catalytic domain of beta 1,4-galactosyltransferase
  2. Boeggeman, E.; Qasba, P. K.
  3. Glycobiology. 2002 12(7): 395-407.
  1. 12.   Thermal unfolding molecular dynamics simulation of Escherichia coli dihydrofolate reductase: Thermal stability of protein domains and unfolding pathway
  2. Sham, Y. Y.; Ma, B. Y.; Tsai, C. J.; Nussinov, R.
  3. Proteins-Structure Function and Genetics. 2002 46(3): 308-320.
  1. 13.   Molecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: Relative stabilities in experiment and simulations
  2. Sham, Y. Y.; Ma, B. Y.; Tsai, C. J.; Nussinov, R.
  3. Protein Science. 2001 10(1): 135-148.
  1. 14.   Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta 1,4- galactosyltransferase-1
  2. Ramakrishnan, B.; Qasba, P. K.
  3. Journal of Molecular Biology. 2001 310(1): 205-218.
  1. 15.   Mapping the effects of metal ion reduction and substrate analog binding to Fe-superoxide dismutase by NMR spectroscopy
  2. Vathyam, S.; Byrd, R. A.; Miller, A. F.
  3. Magnetic Resonance in Chemistry. 2000 38(7): 536-542.
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