Enhancement of the complement regulatory function of CD59 by site-directed mutagenesis at the N-glycosylation site.
Akami
T
T
Second Department of Surgery, Kyoto Prefectural University of Medicine, Japan.
Arakawa
K
K
Okamoto
M
M
Akioka
K
K
Fujiwara
I
I
Nakai
I
I
Mitsuo
M
M
Sawada
R
R
Naruto
M
M
Oka
T
T
D000595:Amino Acid Sequence; D000818:Animals; D015703:Antigens, CD / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D001483:Base Sequence; D001769:Blood; D015153:Blotting, Western; D018957:CD59 Antigens; D002460:Cell Line; D003169:Complement Inactivator Proteins / Q000378:metabolism*; D003165:Complement System Proteins / Q000502:physiology*; D017931:DNA Primers; D006031:Glycosylation; D000882:Haplorhini; D006801:Humans; D008562:Membrane Glycoproteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D051379:Mice; D008954:Models, Biological; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism; D013552:Swine; D014162:Transfection; D014183:Transplantation, Heterologous / Q000276:immunology
D015703:Antigens, CD; D018957:CD59 Antigens; D003169:Complement Inactivator Proteins; D017931:DNA Primers; D008562:Membrane Glycoproteins; D011994:Recombinant Proteins; D003165:Complement System Proteins