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Details on Person Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing

Class:IdLiteratureReference:381197
_displayNameStructure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
_timestamp2008-11-19 16:17:11
author[Person:381112] Lee, KP
[Person:381115] Dey, M
[Person:381120] Neculai, D
[Person:381069] Cao, C
[Person:72559] Dever, TE
[Person:178190] Sicheri, F
created[InstanceEdit:381159] May, B, 2008-11-19 16:17:44
journalCell
pages89-100
pubMedIdentifier18191223
titleStructure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
volume132
year2008
(literatureReference)[Complex:535501] p-3S,T844-IRE1 dimer:ADP (yeast) [endoplasmic reticulum membrane] [Saccharomyces cerevisiae]
[EntityWithAccessionedSequence:535555] p-3S,T844-IRE1 [endoplasmic reticulum membrane] [Saccharomyces cerevisiae]
[Complex:535590] p-3S,T844-IRE1 dimer (yeast) [endoplasmic reticulum membrane] [Saccharomyces cerevisiae]
[Summation:381014] Crystallographic evidence indicates that the IRE1 homodimer ...
[Summation:381028] The dissociation of the IRE1-alpha:BiP heterodimer liberates...
[Summation:381196] After juxtaposition of the luminal N-termini of IRE1 to form...
[Reaction:535524] Phosphorylated Ire1 Dimer Binds ADP [Saccharomyces cerevisiae]
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No pathways have been reviewed or authored by Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing (381197)