Transport of meprin subunits through the secretory pathway: Role of the transmembrane and cytoplasmic domains and oligomerization

Journal of Biological Chemistry

Volumn 279, Issue 33, 2004, Pages 34856-34864

  Hengst, Jeremy A ^a   Bond, Judith S ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; BIOSYNTHESIS; CELLS; CHEMICAL BONDS; DIMERS; ENZYMES; MUTAGENESIS; OLIGOMERS; SUBSTITUTION REACTIONS;

CELL SURFACES; ENDOPLASMIC RETICULUM (ER); MEMBRANE PROTEINS; PROTEOLYSIS;

CELL MEMBRANES;

ALANINE; CYTOPLASM PROTEIN; DIMER; GLYCINE; LEUCINE; MEMBRANE PROTEIN; MEPRIN; MUTANT PROTEIN; OLIGOMER; AZOCASEIN; CASEIN; COMPLEMENTARY DNA; DISULFIDE; GLYCOSIDASE; HYBRID PROTEIN; METALLOPROTEINASE; TIOPRONIN;

ALPHA CHAIN; AMINO ACID SEQUENCE; ARTICLE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE TRANSPORT; CELL SURFACE; CHIMERA; CONTROLLED STUDY; DISULFIDE BOND; EMBRYO; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; GENETIC TRANSFECTION; GOLGI COMPLEX; HUMAN; HUMAN CELL; KIDNEY CELL; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN TRANSPORT; ANIMAL; BIOLOGICAL MODEL; CELL LINE; CELL MEMBRANE; CHEMISTRY; CHROMATOGRAPHY; CULTURE MEDIUM; CYTOPLASM; DIMERIZATION; GENE DELETION; IMMUNOBLOTTING; METABOLISM; MOLECULAR GENETICS; MOUSE; MUTAGENESIS; MUTATION; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN TERTIARY STRUCTURE;

ALANINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CASEINS; CELL LINE; CELL MEMBRANE; CHROMATOGRAPHY; CULTURE MEDIA; CYTOPLASM; DIMERIZATION; DISULFIDES; DNA, COMPLEMENTARY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOPLASMIC RETICULUM; GENE DELETION; GLYCINE; GLYCOSIDE HYDROLASES; GOLGI APPARATUS; HUMANS; IMMUNOBLOTTING; LEUCINE; METALLOENDOPEPTIDASES; MICE; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECOMBINANT FUSION PROTEINS; THIOPRONINE;

EID: 4544377845     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M405774200     Document Type: Article

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