N-linked glycosylation of CD38 is required for its structure stabilization but not for membrane localization

Molecular and Cellular Biochemistry

Volumn 295, Issue 1-2, 2007, Pages 1-7

  Gao, Yin ^a   Mehta, Kapil ^a,b  

^a UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

^b UNIVERSITY OF TEXAS   (United States)

Author keywords

CD38; Glycolsylation; Membrane localization; Protein cross linking; Structure stability

Indexed keywords

ASPARAGINE; CD38 ANTIGEN; COMPLEMENTARY DNA; MUTANT PROTEIN; OLIGOMER; TUNICAMYCIN;

ARTICLE; CELL MEMBRANE; CELL STRAIN MCF 7; CONTROLLED STUDY; CROSS LINKING; DIMERIZATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE MUTATION; GENETIC TRANSFECTION; HELA CELL; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; MOLECULAR STABILITY; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; WESTERN BLOTTING; WILD TYPE;

ANTIGENS, CD38; CELL MEMBRANE; GLYCOSYLATION; HELA CELLS; HUMANS; MEMBRANE GLYCOPROTEINS; MUTANT PROTEINS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN TRANSPORT; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 33846538427     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-006-9265-9     Document Type: Article

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