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  1. 1.   How Does the Reductase Help To Regulate the Catalytic Cycle of Cytochrome P450 3A4 Using the Conserved Water Channel?
  2. Fishelovitch, D.; Shaik, S.; Wolfson, H. J.; Nussinov, R.
  3. Journal of Physical Chemistry B. 2010, May; 114(17): 5964-5970.
  1. 2.   Residues crucial for maintaining short paths in network communication mediate signaling in proteins
  2. del Sol, A.; Fujihashi, H.; Amoros, D.; Nussinov, R.
  3. Molecular Systems Biology. 2006
  1. 3.   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. 4.   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. 5.   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. 6.   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. 7.   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. 8.   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. 9.   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. 10.   Crystal structure of the AAA(+) alpha domain of E-coli Lon protease at 1.9 angstrom resolution
  2. Botos, I.; Melnikov, E. E.; Cherry, S.; Khalatova, A. G.; Rasulova, F. S.; Tropea, J. E.; Maurizi, M. R.; Rotanova, T. V.; Gustchina, A.; Wlodawer, A.
  3. Journal of Structural Biology. 2004, APR-MAY; 146(1-2): 113-122.
  1. 11.   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. 12.   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. 13.   Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and mGSTA2-2 toward benzo a pyrene-(7R,8S)-diol- (9S,10R)-epoxide
  2. Gu, Y. J.; Xiao, B.; Wargo, H. L.; Bucher, M. H.; Singh, S. V.; Ji, X. H.
  3. Biochemistry. 2003 42(4): 917-921.
  1. 14.   Molecular mechanisms of chaperonin GroEL-GroES function
  2. Keskin, O.; Bahar, I.; Flatow, D.; Covell, D. G.; Jernigan, R. L.
  3. Biochemistry. 2002 41(2): 491-501.
  1. 15.   Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins
  2. Fox, J. D.; Kapust, R. B.; Waugh, D. S.
  3. Protein Science. 2001 10(3): 622-630.
  1. 16.   Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S),10(R)-epoxide
  2. Gu, Y. J.; Singh, S. V.; Ji, X. H.
  3. Biochemistry. 2000 39(41): 12552-12557.
  1. 17.   Structural and biochemical studies of retroviral proteases
  2. Wlodawer, A.; Gustchina, A.
  3. Biochimica et Biophysica Acta - Protein Structure & Molecular Enzymology. 2000 1477(1-2): 16-34.
  1. 18.   Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution
  2. Bertelsen, E. B.; Zhou, H. J.; Lowry, D. F.; Flynn, G. C.; Dahlquist, F. W.
  3. Protein Science. 1999 8(2): 343-354.
  1. 19.   Studies On the Symmetry and Sequence Context Dependence of the Hiv-1 Proteinase Specificity
  2. Tozser, J.; Bagossi, P.; Weber, I. T.; Louis, J. M.; Copeland, T. D.; Oroszlan, S.
  3. Journal of Biological Chemistry. 1997 272(27): 16807-16814.
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