Elucidation of the molecular logic by which misfolded α1-antitrypsin is preferentially selected for degradation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 14, 2003, Pages 8229-8234

  Wu, Ying ^a   Swulius, Matthew T ^a   Morement, Kelley W ^b   Sifers, Richard N ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; ALPHA 1 ANTITRYPSIN; GLYCAN; GLYCOPROTEIN; LACTACYSTIN; MANNOSIDASE; MONOMER; PROTEASOME; TRANSFERRIN;

ANIMAL CELL; ARTICLE; CELL LINE; CHEMICAL MODIFICATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME MODIFICATION; ENZYME SUBUNIT; HEPATOMA CELL; INTRACELLULAR SPACE; MOLECULAR DYNAMICS; MOUSE; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN METABOLISM; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; QUALITY CONTROL; STOCHASTIC MODEL; WILD TYPE;

ACETYLCYSTEINE; ALBUMINS; ALPHA 1-ANTITRYPSIN; AMINO ACID SEQUENCE; ANIMALS; CARBOHYDRATE SEQUENCE; ENDOPLASMIC RETICULUM, SMOOTH; ENZYME INHIBITORS; EXOCYTOSIS; GLYCOPROTEINS; GLYCOSYLATION; LIVER NEOPLASMS, EXPERIMENTAL; MANNANS; MANNOSIDASES; MICE; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT FUSION PROTEINS; STOCHASTIC PROCESSES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRANSFECTION; TRANSFERRIN; TUMOR CELLS, CULTURED;

ANIMALIA; EUKARYOTA; MURINAE;

EID: 0037816258     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.1430537100     Document Type: Article

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