Author

Marie-France Langelier

Université de MontréalORCID 0000-0001-9815-1840Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:protein structure· 2 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

John M. PascaliD· 2 shared Ben E. BlackiD· 1 shared David NeuhausiD· 1 shared Elizabeth Underwood· 1 shared Emily S. Smith-Pillet· 1 shared Ji‐Chun YangiD· 1 shared Kevin J. Embrey· 1 shared Laura E. Easton· 1 shared

Activity by Year

2021-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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2 shared papersBiochemistry

John M. PascalORCID

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2 papers

Recent·Most cited

BiochemistryMolecular CellPeer-reviewedJan 30, 2025

A PARP2-specific active site alpha-helix melts to permit DNA damage-induced enzymatic activation

Emily S. Smith-Pillet, Ramya Billur, Marie-France Langelier…·Ben E. Black

This study identifies structural differences in PARP1 and PARP2 activation mechanisms, showing that PARP2 requires an active site alpha-helix to be unfolded for DNA damage-induced activation, unlike PARP1.

11 citationstop 4%

protein structureexperimental assay

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Molecular BiologyNucleic Acids ResearchPeer-reviewedJan 9, 2021

Dynamics of the HD regulatory subdomain of PARP 1; substrate access and allostery in PARP activation and inhibition.

Tom E. H. Ogden, Ji‐Chun Yang, Marianne Schimpl…·David Neuhaus

This study investigates the dynamics of the HD subdomain in PARP-1 using NMR and crystal structures to understand its role in activation and inhibition.

74 citationstop 4%

humanprotein structure

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