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European Journal of Biochemistry|October 15, 1993
Structural flexibility of the calmodulin-binding locus in Bordetella pertussis adenylate cyclase. Reconstitution of catalytically active species from fragments or inactive forms of the enzymeH Munier, A Bouhss, A M Gilles, et al.
The Journal of Biological Chemistry|May 15, 1992
The role of histidine 63 in the catalytic mechanism of Bordetella pertussis adenylate cyclaseH Munier, A Bouhss, E Krin, et al.
European Journal of Biochemistry|March 14, 1991
Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclaseH Munier, A M Gilles, P Glaser, et al.
Acta Crystallographica. Section D, Biological Crystallography|February 10, 2000
Crystallization and preliminary X-ray analysis of the thymidylate kinase from Mycobacterium tuberculosisI Li de la Sierra, H Munier-Lehmann, A M Gilles, et al.
The Journal of Biological Chemistry|January 25, 1993
Cooperative phenomena in binding and activation of Bordetella pertussis adenylate cyclase by calmodulinA Bouhss, E Krin, H Munier, et al.
Biochemistry|May 22, 1990
Characterization of ATP and calmodulin-binding properties of a truncated form of Bacillus anthracis adenylate cyclaseE Labruyère, M Mock, D Ladant, et al.
Archives of Biochemistry and Biophysics|July 10, 1995
Structural characterization by nuclear magnetic resonance spectroscopy of a genetically engineered high-affinity calmodulin-binding peptide derived from Bordetella pertussis adenylate cyclaseH Munier, A Bouhss, A M Gilles, et al.
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|July 1, 1989
Investigation of adenylate kinase from Escherichia coli and its interaction with nucleotides by Fourier transform infrared spectroscopyJ L Arrondo, A M Gilles, O Bárzu, et al.
Biochemistry|September 4, 1990
Intrinsic fluorescence of a truncated Bordetella pertussis adenylate cyclase expressed in Escherichia coliA M Gilles, H Munier, T Rose, et al.
Biochemistry|March 31, 1992
Zinc, a novel structural element found in the family of bacterial adenylate kinasesP Glaser, E Presecan, M Delepierre, et al.
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