Open AccessProximity biotinylation identifies a set of conformation-specific interactions between Merlin and cell junction proteins
Author(s) -
Robert F. Hennigan,
Jonathan S. Fletcher,
Steven Guard,
Nancy Ratner
Publication year - 2019
Publication title -
science signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.659
H-Index - 154
eISSN - 1937-9145
pISSN - 1945-0877
DOI - 10.1126/scisignal.aau8749
Subject(s) - merlin (protein) , neurofibromatosis type 2 , microbiology and biotechnology , biotinylation , mutant , biology , ferm domain , chemistry , suppressor , genetics , gene , membrane protein , neurofibromatosis , integral membrane protein , membrane
The tumor suppressor Merlin interacts with cell junction–associated proteins and with the proapoptotic protein ASPP2.
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