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
Good Attention Score compared to outputs of the same age (74th percentile)
Average Attention Score compared to outputs of the same age and source

Mentioned by

twitter: 10 tweeters

facebook: 3 Facebook pages

Readers on

mendeley: 17 Mendeley

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So far, Altmetric has seen 25 tweets from 10 users, with an upper bound of 31,622 followers.

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

17 Jun 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

16 Jun 2018

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

27 Apr 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

15 Apr 2018

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