N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase

Neuroscience Letters

Volumn 523, Issue 1, 2012, Pages 71-75

  Chan, Wallace K B ^a   Chen, Vicky P ^a   Luk, Wilson K W ^a   Choi, Roy C Y ^a   Tsim, Karl W K ^a  

^a HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

Author keywords

AChE; Assembly; Glycosylation; PRiMA; Trafficking

Indexed keywords

ACETYLCHOLINESTERASE; ASPARAGINE; GLYCOPROTEIN; PROLINE RICH MEMBRANE ANCHOR; PROLINE RICH PROTEIN; STRUCTURAL PROTEIN; TETRAMER; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME GLYCOSYLATION; HUMAN; HUMAN TISSUE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; SITE DIRECTED MUTAGENESIS;

ACETYLCHOLINESTERASE; ANIMALS; DIMERIZATION; GLYCOSYLATION; HEK293 CELLS; HUMANS; MEMBRANE PROTEINS; MICE; MULTIPROTEIN COMPLEXES; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN TRANSPORT;

EID: 84864291399     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2012.06.045     Document Type: Article

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