Author

A. El Sahili

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 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:structural biology· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Organism:plant (other)· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. Lescar· 4 shared B. C. Goh· 2 shared J. Lin· 2 shared A. Marquardt· 1 shared A. Partridge· 1 shared B. Colley· 1 shared C. F. Liu· 1 shared C. W. Liew· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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4 shared papersBiochemistry

J. Lescar

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural basis for substrate recognition, ligation and activation by a hyperactive Asn peptide ligase from Viola yedoensis

J. Lescar, S. Hu, A. El Sahili, S. Kishore, X. Hemu, C. F. Liu, J. P. Tam, B. C. Goh, Y. H. Wong, Z. Wang

The paper captures VyPAL2, a plant peptide ligase with a bound substrate, revealing the molecular basis for substrate recognition and ligation.

bioRxiv · Dec 9, 2021 · PreprintBiochemistry

Identification of an inhibitory pocket in falcilysin provides a new avenue for malaria drug development

G. Wirjanata, J. Lin, J. Dziekan, A. El Sahili, Z. Chung, S. Tjia, N. E. B. Zulkifli, J. Boentoro, R. Tham, S. J. Lai, K. Go, Y. Han, A. Partridge, D. Olsen, N. Prabhu, , Z. Bozdech

This study identifies falcilysin as a target of anti-malaria drugs and reveals a shared inhibitory pocket that could guide new drug development.

bioRxiv · Apr 8, 2021Microbiology

The SiaABC threonine phosphorylation pathway controls biofilm formation in response to carbon availability in Pseudomonas aeruginosa

W.-H. Poh, J. Lin, B. Colley, N. Müller, B. C. Goh, D. Schleheck, A. El Sahili, A. Marquardt, Y. Liang, S. Kjelleberg, J. Lescar, S. A. Rice, J. Klebensberger

This study identifies the SiaABC threonine phosphorylation pathway as a regulator of biofilm formation in Pseudomonas aeruginosa in response to carbon availability and surfactant stress.

bioRxiv · Apr 16, 2020Microbiology

Crystal structures of full length DENV4 NS2B-NS3 reveal the dynamic interaction between NS2B and NS3 upon binding to protease inhibitors

W. W. Phoo, A. El Sahili, C. W. Liew, J. Lescar, S. Vasudevan, D. Luo, M. W. Chen

The paper reports crystal structures of DENV4 NS2B-NS3 constructs with and without protease inhibitors, showing how different linkers affect the enzyme's conformation and activity.

bioRxiv · Jan 27, 2020Biochemistry