Chen Chen
Medical College of Wisconsin
20 Papers
97 Citations
Chen Chen is an academic researcher from Medical College of Wisconsin. The author has contributed to research in topics: Biology & Medicine. The author has an hindex of 9, co-authored 14 publications. Previous affiliations of Chen Chen include University of Chicago.
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Papers
Gangliosides as High Affinity Receptors for Tetanus Neurotoxin
TL;DR: Glycan array and solid phase binding analyses and crystal structure of a ternary complex of HCR/T with sugar components of two gangliosides bound to the W and R supported the binding of ganglioides to both carbohydrate pockets, showing that gang liosides are functional dual receptors for TeNT.
136
Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus.
Chen Chen,Vengadesan Krishnan,Kevin Macon,Kartik Manne,Sthanam V.L. Narayana,Olaf Schneewind +5 more
TL;DR: It is shown here that Esp cleaves autolysin (Atl)-derived murein hydrolases and prevents staphylococcal release of DNA, which serves as extracellular matrix in biofilms and appears to be perturbed by the Esp protease of S. aureus.
100
Tetanus toxin and botulinum toxin a utilize unique mechanisms to enter neurons of the central nervous system.
TL;DR: Assessment of TeNT entry into CNS neurons, using the prototypic BoNT serotype A as a reference for SV2-mediated entry into synaptic vesicles, shows that TeNT and BoNT/A enter neurons by unique mechanisms.
68
Molecular basis for tetanus toxin coreceptor interactions.
TL;DR: A solid phase assay characterized the ganglioside binding specificity and functional properties of both carbohydrate binding pockets of TeNT and provided a model for how tetanus toxin utilizes coreceptors for high-affinity binding to neurons.
66
A Heterologous Reporter Defines the Role of the Tetanus Toxin Interchain Disulfide in Light-Chain Translocation
TL;DR: βlac-TeNT(RY) is the first reporter system to measure translocation by an AB single-chain toxin in intact cells and implies that disulfide reduction is a prerequisite for LC delivery into the host cytosol.
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