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Feinberg, H., Taylor, M.E., Razi, N., McBride, R., Knirel, Y.A., Graham, S.A., et al. (2011) Structural Basis for Langerin Recognition of Diverse Pathogen and Mammalian Glycans Through a Single Binding Site. Journal of Molecular Biology, 405, 1027-1039.
https://doi.org/10.1016/j.jmb.2010.11.039

has been cited by the following article:

• TITLE: Recombinant Human REG Iα Aggregates Staphylococcus aureus—Exhibits a Lectin-Like Function

  AUTHORS: Nausheen Jamal, Yuichiro Kezuka, Takamasa Nonaka, Kazuaki Ohashi, Koji Nata

  KEYWORDS: Reg Proteins, Lectin-Like Activity, Bacterial Aggregation

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.8 No.3, March 16, 2017

  ABSTRACT: Staphylococcus aureus is pathogenic to humans with worldwide health care concern due to its ability to evade the immune system and develop resistance to multiple drugs. Reg family proteins are C-type lectins with antimicrobial properties. Bacterial aggregation through binding to microbial cell surface sugar and/or lipid moieties is key mechanism employed in the process. In the present study we have analysed the antimicrobial effect of human REG Iα on S. aureus. Aggregation of mid-log phase culture of S. aureus was observed in presence of purified recombinant REG Iα. Therefore REG Iα can be applied in eliminating S. aureus infections in humans.