about
Crystal structures of the class D beta-lactamase OXA-13 in the native form and in complex with meropenemCrystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptideGenetic and Structural Insights into the Dissemination Potential of the Extremely Broad-Spectrum Class A -Lactamase KPC-2 Identified in an Escherichia coli Strain and an Enterobacter cloacae Strain Isolated from the Same Patient in FranceDifferent mutations in the HHV-6 DNA polymerase gene accounting for resistance to foscarnetDNA gyrase inhibition assays are necessary to demonstrate fluoroquinolone resistance secondary to gyrB mutations in Mycobacterium tuberculosis.Extending the definition of the GyrB quinolone resistance-determining region in Mycobacterium tuberculosis DNA gyrase for assessing fluoroquinolone resistance in M. tuberculosis.Description of compensatory gyrA mutations restoring fluoroquinolone susceptibility in Mycobacterium tuberculosis.Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase CTDNew mutations in the mycobacterial ATP synthase: new insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure.Purification, crystallization and preliminary X-ray diffraction experiments on the breakage-reunion domain of the DNA gyrase from Mycobacterium tuberculosis.Crystallization and preliminary X-ray diffraction study of the class A beta-lactamase SED-1 and its mutant SED-G238C from Citrobacter sedlakii.Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.Comparative study of enzymatic activities of new KatG mutants from low- and high-level isoniazid-resistant clinical isolates of Mycobacterium tuberculosis.Conservation of HHV-6 DNA polymerase processivity factor sequence and predicted structure suggests it as a target for antiviral developmentOverall Structures of Mycobacterium tuberculosis DNA Gyrase Reveal the Role of a Corynebacteriales GyrB-Specific Insert in ATPase Activity
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description
researcher ORCID: 0000-0001-6641-5901
@en
wetenschapper
@nl
name
Stéphanie Petrella
@ast
Stéphanie Petrella
@en
Stéphanie Petrella
@es
Stéphanie Petrella
@nl
type
label
Stéphanie Petrella
@ast
Stéphanie Petrella
@en
Stéphanie Petrella
@es
Stéphanie Petrella
@nl
prefLabel
Stéphanie Petrella
@ast
Stéphanie Petrella
@en
Stéphanie Petrella
@es
Stéphanie Petrella
@nl
P106
P21
P31
P496
0000-0001-6641-5901