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Structure
Article . 2012
License: Elsevier Non-Commercial
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Structure
Article . 2012 . Peer-reviewed
License: Elsevier Non-Commercial
Data sources: Crossref
Structure
Article . 2012
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Host Glycan Recognition by a Pore Forming Toxin

Authors: Bouyain, Samuel; Geisbrecht, Brian V.;

Host Glycan Recognition by a Pore Forming Toxin

Abstract

An exposed F-type lectin domain fused to the N-terminus of a cholesterol-dependent cytolysin scaffold allows Streptococcus mitis lectinolysin to cluster at fucose-rich sites on target cell membranes, thereby leading to increased pore-forming toxin activity. In this issue of Structure, Feil and coworkers define the structural basis for lectinolysin glycan-binding specificity.

Related Organizations
Keywords

Pore Forming Cytotoxic Proteins, Lewis Blood Group Antigens, Bacterial Proteins, Structural Biology, Lectins, Streptococcus mitis, Molecular Biology

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
7
Average
Average
Average
hybrid
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