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Q34421772-42AB5371-5A4C-48DB-A81C-ACBFD990965A
Q34421772-42AB5371-5A4C-48DB-A81C-ACBFD990965A
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http://www.wikidata.org/entity/statement/Q34421772-42AB5371-5A4C-48DB-A81C-ACBFD990965A
The active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation
P2860
Q34421772-42AB5371-5A4C-48DB-A81C-ACBFD990965A
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34421772-42AB5371-5A4C-48DB-A81C-ACBFD990965A
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fec1144ba56f8ad2f3498bb94023a574ce20e752
P2860
Zonula occludens toxin structure-function analysis. Identification of the fragment biologically active on tight junctions and of the zonulin receptor binding domain.