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

Altmetric Badge

About this Attention Score

In the top 25% of all research outputs scored by Altmetric
Good Attention Score compared to outputs of the same age (79th percentile)
Above-average Attention Score compared to outputs of the same age and source (57th percentile)

Mentioned by

twitter: 13 tweeters

facebook: 3 Facebook pages

Citations

dimensions_citation: 13 Dimensions

Readers on

mendeley: 26 Mendeley

Summary Twitter Facebook Dimensions citations

So far, Altmetric has seen 33 tweets from 13 users, with an upper bound of 46,557 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

Reply Retweet Favourite

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

29 Dec 2018

Reply Retweet Favourite

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

29 Dec 2018

Reply Retweet Favourite

#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

Reply Retweet Favourite

This page shows the most recent tweets that mention this research output.

Click here to find out how to access more activity, including 29 additional tweets.