Functional characterization of two secreted SEL1L isoforms capable of exporting unassembled substrate

Journal of Biological Chemistry

Volumn 284, Issue 17, 2009, Pages 11405-11415

  Cattaneo, Monica ^a   Lotti, Lavinia Vittoria ^b   Martino, Simone ^b   Cardano, Marina ^c   Orlandi, Rosaria ^d   Mariani Costantini, Renato ^e   Biunno, Ida ^a,c  

^a INSTITUTE OF BIOMEDICAL TECHNOLOGIES   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c Integrated Systems Engineering   (Italy)

^d Molecular Targeting Unit   (Italy)

^e UNIVERSITY OF CHIETI   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ALTERNATIVE SPLICING; ANTITRYPSIN; BIOCHEMICAL TESTS; CELL-CELL CONTACT; CELLULAR COMPARTMENTS; DISULFIDE BONDS; ENDOPLASMIC RETICULUM; ER STRESS; FUNCTIONAL CHARACTERISTICS; FUNCTIONAL CHARACTERIZATION; HONG-KONG; HUMAN CELLS; INTERCELLULAR SPACES; ISOFORMS; MOLECULAR PATHWAYS; MONOMERIC FORMS; PROTEIN INTERACTION; SOLUBLE PROTEINS; TRANSIENT TRANSFECTION; TRANSMEMBRANE GLYCOPROTEINS; UNFOLDED PROTEIN RESPONSE; WILD TYPES;

DEGRADATION; GLYCOPROTEINS; NUCLEIC ACIDS; PROTEINS; SIGNAL TRANSDUCTION; SUBSTRATES;

CELL MEMBRANES;

ALPHA 1 ANTITRYPSIN; CELL MEMBRANE PROTEIN; IMMUNOGLOBULIN MU CHAIN; PROTEIN SEL1L A; PROTEIN SEL1L B; PROTEIN SEL1L C; UNCLASSIFIED DRUG; DISULFIDE; ISOPROTEIN; PROTEIN; SEL1L PROTEIN, HUMAN;

ARTICLE; CELL ACTIVATION; CELL COMMUNICATION; CELL COMPARTMENTALIZATION; CELL MEMBRANE; CELLULAR DISTRIBUTION; CHEMICAL ANALYSIS; CONTROLLED STUDY; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; HUMAN; HUMAN CELL; INTRACELLULAR SPACE; MOLECULAR INTERACTION; PEROXISOME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN TARGETING; PROTEIN TRANSPORT; TRANSIENT TRANSFECTION; WILD TYPE; CHEMISTRY; ENZYME SPECIFICITY; GENETIC TRANSFECTION; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SECRETION;

ALPHA 1-ANTITRYPSIN; BASE SEQUENCE; DISULFIDES; ENDOPLASMIC RETICULUM; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PEROXISOMES; PROTEIN DENATURATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEINS; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 66449112759     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M805408200     Document Type: Article

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