E2ESL7
Uniprot
Fold
Class
Family
Origin
Species
Related proteins
> 50% identity

PubMed
Baier M, Rustmeier N, Harr J, Cyrus N, Reiss G, Grafmüller A, Blaum B, Stehle T, Hartmann L.
Divalent Sialylated Precision Glycooligomers Binding to Polyomaviruses and the Effect of Different Linkers. Macromolecular bioscience 2019

PubMed
Baier M, Rustmeier N, Harr J, Cyrus N, Reiss G, Grafmüller A, Blaum B, Stehle T, Hartmann L.
Divalent Sialylated Precision Glycooligomers Binding to Polyomaviruses and the Effect of Different Linkers. Macromolecular bioscience 2019

PubMed
Ströh L, Gee G, Blaum B, Dugan A, Feltkamp M, Atwood W, Stehle T.
Trichodysplasia spinulosa-Associated Polyomavirus Uses a Displaced Binding Site on VP1 to Engage Sialylated Glycolipids. PLoS pathogens 2015

PubMed
Ströh L, Gee G, Blaum B, Dugan A, Feltkamp M, Atwood W, Stehle T.
Trichodysplasia spinulosa-Associated Polyomavirus Uses a Displaced Binding Site on VP1 to Engage Sialylated Glycolipids. PLoS pathogens 2015

PubMed
Ströh L, Gee G, Blaum B, Dugan A, Feltkamp M, Atwood W, Stehle T.
Trichodysplasia spinulosa-Associated Polyomavirus Uses a Displaced Binding Site on VP1 to Engage Sialylated Glycolipids. PLoS pathogens 2015

PubMed
Ströh L, Gee G, Blaum B, Dugan A, Feltkamp M, Atwood W, Stehle T.
Trichodysplasia spinulosa-Associated Polyomavirus Uses a Displaced Binding Site on VP1 to Engage Sialylated Glycolipids. PLoS pathogens 2015
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