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I Schlichting

Showing results (21-30 of 63) with videos related to

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Nature Structural Biology|December 10, 1998
Iron center, substrate recognition and mechanism of peptide deformylaseA Becker, I Schlichting, W Kabsch, et al.
Biochemical and Biophysical Research Communications|June 4, 1998
Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active siteD Groche, A Becker, I Schlichting, et al.
Biochemistry|April 2, 1998
Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activationA Lavie, M Konrad, R Brundiers, et al.
Nature Structural Biology|August 1, 1997
Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activationA Lavie, I R Vetter, M Konrad, et al.
Nature Medicine|August 1, 1997
The bottleneck in AZT activationA Lavie, I Schlichting, I R Vetter, et al.
Proteins|January 1, 1996
Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complexE M Jacoby, I Schlichting, C B Lantwin, et al.
Biochemistry|January 16, 1990
Proton NMR studies of transforming and nontransforming H-ras p21 mutantsI Schlichting, J John, M Frech, et al.
Nature|March 8, 2000
Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobinK Chu, J Vojtchovský, B H McMahon, et al.
Biological Chemistry Hoppe-Seyler|August 1, 1986
31P-NMR studies on ATP X Mg2+, p21 X nucleotide, and adenylate kinase X nucleotide complexes. Chemical shifts, rate and equilibrium constantsW Klaus, I Schlichting, R S Goody, et al.
The Journal of Biological Chemistry|October 28, 1994
Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthaseI Schlichting, X J Yang, E W Miles, et al.
Pageof 7

Showing results (21-30 of 63) with videos related to

Sort By:
Pageof 7
Nature Structural Biology|December 10, 1998
Iron center, substrate recognition and mechanism of peptide deformylaseA Becker, I Schlichting, W Kabsch, et al.
Biochemical and Biophysical Research Communications|June 4, 1998
Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active siteD Groche, A Becker, I Schlichting, et al.
Biochemistry|April 2, 1998
Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activationA Lavie, M Konrad, R Brundiers, et al.
Nature Structural Biology|August 1, 1997
Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activationA Lavie, I R Vetter, M Konrad, et al.
Nature Medicine|August 1, 1997
The bottleneck in AZT activationA Lavie, I Schlichting, I R Vetter, et al.
Proteins|January 1, 1996
Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complexE M Jacoby, I Schlichting, C B Lantwin, et al.
Biochemistry|January 16, 1990
Proton NMR studies of transforming and nontransforming H-ras p21 mutantsI Schlichting, J John, M Frech, et al.
Nature|March 8, 2000
Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobinK Chu, J Vojtchovský, B H McMahon, et al.
Biological Chemistry Hoppe-Seyler|August 1, 1986
31P-NMR studies on ATP X Mg2+, p21 X nucleotide, and adenylate kinase X nucleotide complexes. Chemical shifts, rate and equilibrium constantsW Klaus, I Schlichting, R S Goody, et al.
The Journal of Biological Chemistry|October 28, 1994
Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthaseI Schlichting, X J Yang, E W Miles, et al.
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