Author

W. Vranken

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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Biochemistry· 2 Evolutionary Biology· 1 Microbiology· 1 Scientific Communication & Education· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Approach:benchmark study· 1 Research Focus:benchmarking· 1 Assay:CRISPR screen· 1 Assay:cryo-EM· 1 Research Focus:database / resource· 1

Frequent Co-Authors

A. Clark-ElSayed· 1 shared A. Diaz· 1 shared A. Economou· 1 shared A. Fernandez· 1 shared A. Hatos· 1 shared A. N. Brooks· 1 shared A. Portaliou· 1 shared A. Quesada-Ganuza· 1 shared

Activity by Year

2019-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 8 mutual co-author links

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Curved chords = mutual co-authorship

1 shared paperMicrobiology

A. Clark-ElSayed

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

MIADE metadata guidelines: Minimum Information About a Disorder Experiment

B. Meszaros, A. Hatos, N. Palopoli, F. Quaglia, E. Salladini, K. Van Roey, H. Arthanari, Z. Dosztanyi, I. C. Felli, P. D. Fischer, J. Hoch, C. M. Jeffries, S. Longhi, E. Maiani, S. Orchard, , N. E. Davey

The paper introduces MIADE guidelines to standardize metadata for experiments studying intrinsically disordered proteins, improving data interpretation and reproducibility.

bioRxiv · Jul 12, 2022 · PreprintScientific Communication & Education

Deep mutational scanning of essential bacterial proteins can guide antibiotic development

L. Dewachter, A. N. Brooks, K. Noon, C. Cialek, A. Clark-ElSayed, T. Schalck, N. Krishnamurthy, W. Versees, W. Vranken, J. Michiels

This study uses deep mutational scanning on E. coli proteins to identify antimicrobial targets and guide drug development by analyzing mutation effects and resistance potential.

bioRxiv · May 23, 2022Microbiology

Evolutionary adaptation of the folding pathway for secretability

D. Smets, A. Tsirigotaki, J. H. Smit, S. Krishnamurthy, A. Portaliou, A. Vorobieva, W. Vranken, S. Karamanou, A. Economou

This study identifies structural features that delay folding in secretory proteins, enabling their translocation, by comparing PpiA and PpiB.

bioRxiv · Apr 3, 2022 · PreprintBiochemistry

Evolution of CRISPR-associated Endonucleases as Inferred from Resurrected Proteins

B. Alonso-Lerma, Y. Jabalera, M. Morin, A. Fernandez, S. Samperio, A. Quesada-Ganuza, A. Reifs, S. Fernandez-Penalver, Y. Benitez, L. Soletto, J. A. Gavira, A. Diaz, W. Vranken, B. P. Kleinstiver, A. Sanchez-Mejias, , R. Perez-Jimenez

This study resurrects ancient CRISPR-Cas9 nucleases to show their greater flexibility in PAM and gRNA requirements and their evolution toward double-strand break activity.

bioRxiv · Mar 30, 2022Evolutionary Biology

Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM

T. Uchanski, S. Masiulis, B. Fischer, V. Kalichuk, A. Wohlkonig, T. Zogg, H. Remaut, W. Vranken, A. R. Aricescu, E. Pardon, J. Steyaert

The paper introduces megabodies, engineered nanobodies that improve cryo-EM resolution by addressing particle size and orientation issues, and demonstrates their application in solving a membrane protein structure.

bioRxiv · Oct 22, 2019Biochemistry