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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In the top 25% of all research outputs scored by Altmetric
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Above-average Attention Score compared to outputs of the same age and source (57th percentile)

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facebook: 3 Facebook pages

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So far, Altmetric has seen 33 tweets from 13 users, with an upper bound of 41,398 followers.

#PLOSPathogens: The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold that Mediates Adhesion to Extracellular Matrix Components & Interactions with Host Cells https://t.co/17J0vqt65P

03 May 2019

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RT @MoriartyLab: #Syphilis Tp0751 (Pallilysin) Structure Reveals a Non-canonical Lipocalin Fold Mediating Adhesion to Extracellular Matrix…

29 Dec 2018

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RT @MoriartyLab: #Syphilis Tp0751 (Pallilysin) Structure Reveals a Non-canonical Lipocalin Fold Mediating Adhesion to Extracellular Matrix…

29 Dec 2018

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#Syphilis Tp0751 (Pallilysin) Structure Reveals a Non-canonical Lipocalin Fold Mediating Adhesion to Extracellular Matrix Components & Interactions with Host Cells. https://t.co/17J0vqbveh https://t.co/cKJS7ZbFGD

29 Dec 2018

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