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Structural flexibility of the calmodulin-binding locus in Bordetella pertussis adenylate cyclase. Reconstitution of catalytically active species from fragments or inactive forms of the enzyme.
Hélène Munier
,
Ahmed Bouhss
,
A. M. Gilles
,
Evelyne Krin
,
Philippe Glaser
,
et al.
Journal articles
pasteur-00167090v1
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Cooperative phenomena in binding and activation of Bordetella pertussis adenylate cyclase by calmodulin.
Ahmed Bouhss
,
Evelyne Krin
,
Hélène Munier
,
Anne-Marie Gilles
,
Antoine Danchin
,
et al.
Journal of Biological Chemistry, 1993, 268 (3), pp.1690-4
Journal articles
pasteur-00167092v1
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The role of histidine 63 in the catalytic mechanism of Bordetella pertussis adenylate cyclase.
Hélène Munier
,
Ahmed Bouhss
,
Evelyne Krin
,
Antoine Danchin
,
Anne-Marie Gilles
,
et al.
Journal of Biological Chemistry, 1992, 267 (14), pp.9816-20
Journal articles
pasteur-00167093v1
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Conformational transitions within the calmodulin-binding site of Bordetella pertussis adenylate cyclase studied by time-resolved fluorescence of Trp242 and circular dichroism.
Ahmed Bouhss
,
Michel Vincent
,
Hélène Munier
,
Anne-Marie Gilles
,
Masayuchi Takahashi
,
et al.
Journal articles
pasteur-00167087v1
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Structural characterization by nuclear magnetic resonance spectroscopy of a genetically engineered high-affinity calmodulin-binding peptide derived from Bordetella pertussis adenylate cyclase.
Hélène Munier
,
A. Bouhss
,
A. M. Gilles
,
Nicolae Palibroda
,
O. Bârzu
,
et al.
Journal articles
istex
pasteur-00167088v1
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