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Acta Crystallographica. Section D, Biological Crystallography|September 21, 2007
Structure of an aliphatic amidase from Geobacillus pallidus RAPc8Serah W Kimani, Vinod B Agarkar, Donald A Cowan, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|December 5, 2006
The quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packingVinod B Agarkar, Serah W Kimani, Donald A Cowan, et al.
The Journal of Biological Chemistry|August 16, 2013
The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioningBrandon W Weber, Serah W Kimani, Arvind Varsani, et al.
Communications Biology|December 16, 2023
The co-crystal structure of Cbl-b and a small-molecule inhibitor reveals the mechanism of Cbl-b inhibitionSerah W Kimani, Sumera Perveen, Magdalena Szewezyk, et al.
Communications Biology|July 24, 2024
A ligand discovery toolbox for the WWE domain family of human E3 ligasesLena Münzker, Serah W Kimani, Milan M Fowkes, et al.
RSC Chemical Biology|September 10, 2025
Discovery of an exquisitely selective WDR5 chemical probe accelerated by a high-quality DEL-ML HitLasse Hoffmann, Christopher Lenz, Frederic Farges, et al.
Journal of Chemical Information and Modeling|June 23, 2023
Discovery of a Novel DCAF1 Ligand Using a Drug-Target Interaction Prediction Model: Generalizing Machine Learning to New Drug TargetsSerah W Kimani, Julie Owen, Stuart R Green, et al.
Communications Biology|July 19, 2025
OICR-41103 as a chemical probe for the DCAF1 WD40 domainSerah W Kimani, Mahmoud Noureldin, Brian Wilson, et al.
Nature Communications|November 23, 2024
Crystal structures of DCAF1-PROTAC-WDR5 ternary complexes provide insight into DCAF1 substrate specificityMark F Mabanglo, Brian Wilson, Mahmoud Noureldin, et al.
Journal of Medicinal Chemistry|November 4, 2024
A Target Class Ligandability Evaluation of WD40 Repeat-Containing ProteinsSuzanne Ackloo, Fengling Li, Magda Szewczyk, et al.
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