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Structural Investigations on the SH3b Domains of Clostridium perfringens Autolysin through NMR Spectroscopy and Structure Simulation Enlighten the Cell Wall Binding Function

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Endo-N-Acetyl-β-D-Glucosaminidases and Peptide-N4-(N-acetyl-β-D-Glucosaminyl) Asparagine Amidases: More Than Just Tools

Karamanos, Y. (2013) · Advances in Biochemistry · doi:10.11648/j.ab.20130105.12 · Cited by 4 · see citing works

A LysR-like Transcriptional Regulator DsfB Is Required for the Daughter Cell Separation in Bacillus cereus 0–9

Liu, Q., Wang, Y., Wang, J., Zhang, J., Liu, F., & Wang, G. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c07307 · Cited by 3 · see citing works

Autolysin as a fibronectin receptor on the cell surface of Clostridium perfringens

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Enzybiotics, a Promising Era in Confronting Bacteria in the Poultry Industry

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Characterisation and functional analysis of the putative agr system in Clostridium acetobutylicum

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X-ray structure and mutagenesis analyses of Clostridioides difficile endolysin Ecd09610 glucosaminidase domain

Sekiya, H., Nonaka, Y., Kamitori, S., Miyaji, T., & Tamai, E. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.149957

Identification of genes involved in extracellular DNA release during biofilm formation in Clostridium perfringens

Ando, T., Nomura, N., & Obana, N. (2026) · Anaerobe · doi:10.1016/j.anaerobe.2026.103052

Study of two autolysins with N-acetylglucosaminidase activity of Clostridium perfringens and Clostridium difficile

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Étude de deux autolysines à activité N-acétylglucosaminidase chez Clostridium perfringens et Clostridium difficile

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Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain

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Acd, a peptidoglycan hydrolase of Clostridium difficile with N-acetylglucosaminidase activity

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Extraction, purification and characterization of a peptidoglycan hydrolase from vegetative cells of Clostridium perfringens type A.

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