Enhancing the secretion of recombinant proteins by engineering N-glycosylation sites

Biotechnology Progress

Volumn 25, Issue 5, 2009, Pages 1468-1475

  Liu, Yan ^a   Nguyen, Anton ^a   Wolfert, Robert L ^a   Zhuo, Shaoqiu ^a  

^a diaDexus Inc   (United States)

Author keywords

Mutagenesis; N glycosylation; Protein expression; Protein folding; Quality control; Secretion

Indexed keywords

ENDOPLASMIC RETICULUM; GLYCOSYLATED; HEK293 CELLS; HIGH RATE; N-GLYCOSYLATION; N-GLYCOSYLATION SITES; PROTEIN EXPRESSION; RECOMBINANT PROTEIN; SECRETION; SECRETION OF RECOMBINANT PROTEINS;

ESTERIFICATION; GLYCOSYLATION; MUTAGENESIS; OLIGOSACCHARIDES; QUALITY ASSURANCE; QUALITY CONTROL; QUALITY FUNCTION DEPLOYMENT; TOTAL QUALITY MANAGEMENT;

PROTEIN FOLDING;

POLYSACCHARIDE; RECOMBINANT PROTEIN;

ARTICLE; CELL CULTURE; GENETICS; GLYCOSYLATION; HUMAN; METABOLISM; METHODOLOGY; PROTEIN ENGINEERING; SECRETION; SITE DIRECTED MUTAGENESIS;

CELLS, CULTURED; GLYCOSYLATION; HUMANS; MUTAGENESIS, SITE-DIRECTED; POLYSACCHARIDES; PROTEIN ENGINEERING; RECOMBINANT PROTEINS;

EID: 70350146914     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1002/btpr.241     Document Type: Article

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