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Proceedings of the National Academy of Sciences of the United States of America|August 22, 2012
Structural insights into Helicobacter pylori oncoprotein CagA interaction with β1 integrinBurcu Kaplan-Türköz, Luisa F Jiménez-Soto, Cyril Dian, et al.
Nature Chemical Biology|June 20, 2017
Nucleation and growth of a bacterial functional amyloid at single-fiber resolutionMike Sleutel, Imke Van den Broeck, Nani Van Gerven, et al.
Infection and Immunity|August 19, 2009
Structural determinants of autoproteolysis of the Haemophilus influenzae Hap autotransporterRoma Kenjale, Guoyu Meng, Doran L Fink, et al.
Cell|May 2, 2017
Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial ConjugationAravindan Ilangovan, Christopher W M Kay, Sandro Roier, et al.
Biochemical and Biophysical Research Communications|April 19, 2017
Structural analysis of the interaction between spiroisoxazoline SMARt-420 and the Mycobacterium tuberculosis repressor EthR2Alexandre Wohlkönig, Han Remaut, Martin Moune, et al.
Nature Communications|June 1, 2017
Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extensionLéa Marie, Chiara Rapisarda, Violette Morales, et al.
The Journal of Biological Chemistry|March 26, 2013
dNTP-dependent conformational transitions in the fingers subdomain of Klentaq1 DNA polymerase: insights into the role of the "nucleotide-binding" statePaul J Rothwell, William J Allen, Evangelos Sisamakis, et al.
Nature Communications|August 29, 2024
Helical ultrastructure of the L-ENA spore aggregation factor of a Bacillus paranthracis foodborne outbreak strainMike Sleutel, Ephrem Debebe Zegeye, Ann-Katrin Llarena, et al.
Elife|October 2, 2014
Allosteric signalling in the outer membrane translocation domain of PapC usherIrene Farabella, Thieng Pham, Nadine S Henderson, et al.
Cell|September 10, 2016
Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid ComplexTiago R D Costa, Aravindan Ilangovan, Marta Ukleja, et al.
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