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 (54th percentile)

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twitter: 11 tweeters

facebook: 3 Facebook pages

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So far, Altmetric has seen 28 tweets from 11 users, with an upper bound of 34,222 followers.

RT @MoriartyLab: #PLOSPathogens: The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediat…

27 Sep 2018

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RT @MoriartyLab: #PLOSPathogens: The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediat…

27 Sep 2018

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#PLOSPathogens: 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. https://t.co/17J0vqt65P https://t.co/CKZgujV7Jo

27 Sep 2018

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

17 Jun 2018

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