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Q34594866-FADFAF17-8F3A-4ECE-858A-DBE17B5F4082
Q34594866-FADFAF17-8F3A-4ECE-858A-DBE17B5F4082
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34594866-FADFAF17-8F3A-4ECE-858A-DBE17B5F4082
Different roles of the three loops forming the adhesive interface of nectin-4 in measles virus binding and cell entry, nectin-4 homodimerization, and heterodimerization with nectin-1
P2860
Q34594866-FADFAF17-8F3A-4ECE-858A-DBE17B5F4082
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34594866-FADFAF17-8F3A-4ECE-858A-DBE17B5F4082
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Statement
wasDerivedFrom
a1e64c9e21609a96c3b67827d398d5be48526298
P2860
Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.