about
Structural and functional analyses of disease-causing missense mutations in Bloom syndrome proteinStructural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicaseThe structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactisvSDC: a method to improve early recognition in virtual screening when limited experimental resources are availableOxidative stress in mammalian cells impinges on the cysteines redox state of human XRCC3 protein and on its cellular localization.The arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling.Multiple Escherichia coli RecQ helicase monomers cooperate to unwind long DNA substrates: a fluorescence cross-correlation spectroscopy study.A new binding site involving the C-terminal domain to design specific inhibitors of PepX.The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding.Structure of influenza virus haemagglutinin complexed with a neutralizing antibody.The structural comparison of the bacterial PepX and human DPP-IV reveals sites for the design of inhibitors of PepX activity.Crystallization and Preliminary X-ray Analysis of PepC, a Thiol Aminopeptidase from Lactoccocus lactis Homologous to Bleomycin Hydrolase
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description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Pascal Rigolet
@ast
Pascal Rigolet
@en
Pascal Rigolet
@es
Pascal Rigolet
@nl
type
label
Pascal Rigolet
@ast
Pascal Rigolet
@en
Pascal Rigolet
@es
Pascal Rigolet
@nl
prefLabel
Pascal Rigolet
@ast
Pascal Rigolet
@en
Pascal Rigolet
@es
Pascal Rigolet
@nl
P106
P21
P31
P496
0000-0001-6868-4953