The endoplasmic reticulum remains functionally connected by vesicular transport after its fragmentation in cells expressing Z-α1-antitrypsin

FASEB Journal

Volumn 30, Issue 12, 2016, Pages 4083-4097

  Dickens, Jennifer A ^a,b   Ordóñez, Adriana ^a   Chambers, Joseph E ^a,b   Beckett, Alison J ^c   Patel, Vruti ^a   Malzer, Elke ^a   Dominicus, Caia S ^a   Bradley, Jayson ^a   Peden, Andrew A ^c   Prior, Ian A ^d   Lomas, David A ^e   Marciniak, Stefan J ^a,b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c UNIVERSITY OF SHEFFIELD   (United Kingdom)

^d UNIVERSITY OF LIVERPOOL   (United Kingdom)

^e UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

ER stress; Homotypic fusion; Serpin; SNARE

Indexed keywords

ALPHA 1 ANTITRYPSIN; N ETHYLMALEIMIDE; PROTEIN; SAR1 PROTEIN; SEC22B PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CELL COMMUNICATION; CELL FRACTIONATION; CELL FUSION; CELL INCLUSION; CELL PERMEABILIZATION; CELL VACUOLE; CHO CELL LINE; COMPARATIVE STUDY; CONTROLLED STUDY; CYTOSOL; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM MEMBRANE; ENDOPLASMIC RETICULUM STRESS; FEMALE; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; ANIMAL; CELL CULTURE; CRICETULUS; GENETICS; LIVER; METABOLISM; MUTATION; PHYSIOLOGY; TRANSPORT AT THE CELLULAR LEVEL;

ALPHA 1-ANTITRYPSIN; ANIMALS; BIOLOGICAL TRANSPORT; CELLS, CULTURED; CHO CELLS; CRICETULUS; ENDOPLASMIC RETICULUM; LIVER; MUTATION;

EID: 85002202584     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.201600430R     Document Type: Article

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