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D Ringe

Showing results (171-180 of 316) with videos related to

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Biochemistry|August 21, 1990
Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitorsK Brady, A Z Wei, D Ringe, et al.
Current Medical Research and Opinion|December 14, 2004
Comment on Putting evidence-based medicine into clinical practice: comparing anti-resorptive agents for the treatment of osteoporosisHans-Peter Kruse, Johann D Ringe, Johannes Pfeilschifter, et al.
Biochemistry|August 9, 1994
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastaseX Ding, B F Rasmussen, G A Petsko, et al.
Biochemistry|March 21, 1995
Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complexK N Allen, A Lavie, G A Petsko, et al.
Biochemistry|May 10, 1994
X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysisA Lavie, K N Allen, G A Petsko, et al.
Biochemistry|March 14, 1995
Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitorsC Mattos, D A Giammona, G A Petsko, et al.
Protein Engineering|February 1, 1991
Insertion of an elastase-binding loop into interleukin-1 betaA J Wolfson, M Kanaoka, F T Lau, et al.
Biochemistry|September 23, 1986
X-ray diffraction analysis of the inactivation of chymotrypsin by 3-benzyl-6-chloro-2-pyroneD Ringe, J M Mottonen, M H Gelb, et al.
Nature Structural Biology|April 1, 1996
Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysisX Ding, H Zeng, N Schiering, et al.
Protein Engineering|March 10, 2000
The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferaseC J Jeffery, L M Gloss, G A Petsko, et al.
Pageof 32

Showing results (171-180 of 316) with videos related to

Sort By:
Pageof 32
Biochemistry|August 21, 1990
Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitorsK Brady, A Z Wei, D Ringe, et al.
Current Medical Research and Opinion|December 14, 2004
Comment on Putting evidence-based medicine into clinical practice: comparing anti-resorptive agents for the treatment of osteoporosisHans-Peter Kruse, Johann D Ringe, Johannes Pfeilschifter, et al.
Biochemistry|August 9, 1994
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastaseX Ding, B F Rasmussen, G A Petsko, et al.
Biochemistry|March 21, 1995
Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complexK N Allen, A Lavie, G A Petsko, et al.
Biochemistry|May 10, 1994
X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysisA Lavie, K N Allen, G A Petsko, et al.
Biochemistry|March 14, 1995
Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitorsC Mattos, D A Giammona, G A Petsko, et al.
Protein Engineering|February 1, 1991
Insertion of an elastase-binding loop into interleukin-1 betaA J Wolfson, M Kanaoka, F T Lau, et al.
Biochemistry|September 23, 1986
X-ray diffraction analysis of the inactivation of chymotrypsin by 3-benzyl-6-chloro-2-pyroneD Ringe, J M Mottonen, M H Gelb, et al.
Nature Structural Biology|April 1, 1996
Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysisX Ding, H Zeng, N Schiering, et al.
Protein Engineering|March 10, 2000
The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferaseC J Jeffery, L M Gloss, G A Petsko, et al.
Pageof 32