The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells

Overview of attention for article published in PLoS Pathogens, September 2016

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So far, Altmetric has seen 17 tweets from 8 users, with an upper bound of 23,756 followers.

#PLOSPathogens: Crystal structure of syphilis pathogen adhesin Tp0751 (Pallilysin) https://t.co/cbBh7BNaNX

RT @micro_papers: The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhes… https…

RT @PLOSPathogens: New Research from Cameron, Boulanger et al: Structural Basis for Tp0751 Interaction with Endothelial Cells https://t.co/…

RT @UofTDentLib: #PLOSPathogens: The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fol ... https://…

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