Author

K. DEGUILLEN

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 1 Microbiology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Organism:fungi (other)· 1 Organism:plant (other)· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Padilla· 2 shared L. Mammri· 2 shared P. BARTHE· 2 shared A. Hecker· 1 shared B. Petre· 1 shared C. Henriquet· 1 shared C. Lorrain· 1 shared C. ROUMESTAND· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersPlant Biology

A. Padilla

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Author profile →

3 papers

Recent·Most cited

Design of a new effector recognition specificity in a plant NLR immune receptor by molecular engineering of its integrated decoy domain

S. Cesari, Y. Xi, N. Declerck, V. Chalvon-Poulier, L. Mammri, M. Pugniere, C. Henriquet, K. Deguillen, A. Padilla, T. Kroj

This study demonstrates that molecular engineering of the integrated decoy domain of an NLR can expand its effector recognition spectrum to a new effector.

bioRxiv · Apr 24, 2021 · PreprintPlant Biology

Structural genomic applied on the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine-knot and nuclear transport factor 2-like protein folds

K. DEGUILLEN, C. Lorrain, P. Tsan, P. BARTHE, B. Petre, N. Saveleva, N. Rouhier, S. Duplessis, A. PADILLA, A. Hecker

The paper identifies two effector proteins from the rust fungus Melampsora larici-populina that adopt structural folds similar to knottin and nuclear transport factor 2-like proteins despite lacking sequence similarity.

bioRxiv · Aug 7, 2019Microbiology

Monitoring Unfolding of Titin I27 single- and bi-Domain with High-Pressure NMR Spectroscopy.

C. ROUMESTAND, I. HERRADA, M. VAN HEUSDEN, P. BARTHE, K. DEGUILLEN, L. MAMMRI, S. DELBECQ, F. Rico

This study uses high-pressure NMR to analyze the unfolding of titin I27 domains, confirming the AG β-sheet as a critical structural element and revealing differences from previous MD simulation findings.

bioRxiv · Mar 31, 2018Biophysics