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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facebook: 3 Facebook pages

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So far, Altmetric has seen 22 tweets from 9 users, with an upper bound of 30,419 followers.

#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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RT @MoriartyLab: #PLOSPathogens: The Structure of #Syphilis Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesi…

20 Mar 2018

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

20 Mar 2018

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12 Feb 2018

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