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Volumn 268, Issue 15, 1993, Pages 11152-11159
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N-linked glycosylation of the ligand-binding domain of the human urokinase receptor contributes to the affinity for its ligand
a
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Author keywords
[No Author keywords available]
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Indexed keywords
UROKINASE;
AMINO ACID SUBSTITUTION;
ANIMAL CELL;
ARTICLE;
CELLULAR DISTRIBUTION;
ENDOPLASMIC RETICULUM;
LIGAND BINDING;
MOUSE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN GLYCOSYLATION;
RECEPTOR AFFINITY;
RECEPTOR BINDING;
SITE DIRECTED MUTAGENESIS;
AMINO ACID SEQUENCE;
ANIMAL;
ASPARAGINE;
BINDING SITES;
CROSS-LINKING REAGENTS;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
GENTAMICINS;
GLYCOSYLATION;
HUMAN;
KINETICS;
L CELLS (CELL LINE);
LIGANDS;
MICE;
MOLECULAR WEIGHT;
MUTAGENESIS, SITE-DIRECTED;
PHOSPHORIC DIESTER HYDROLASES;
POINT MUTATION;
RECEPTORS, CELL SURFACE;
RECOMBINANT PROTEINS;
SUPPORT, NON-U.S. GOV'T;
TRANSFECTION;
TUNICAMYCIN;
URINARY PLASMINOGEN ACTIVATOR;
RICKETTSIA SP. PAR;
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EID: 0027200215
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: None Document Type: Article |
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Times cited : (73)
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References (0)
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