A giant protease with potential to substitute for some functions of the proteasome

Science

Volumn 283, Issue 5404, 1999, Pages 978-981

  Geier, Elke ^a   Pfeifer, Günter ^b   Wilm, Matthias ^c   Lucchiari Hartz, Maria ^a   Baumeister, Wolfgang ^b   Eichmann, Klaus ^a   Niedermann, Gabriele ^a  

^a MAX PLANCK INSTITUTE OF IMMUNOBIOLOGY AND EPIGENETICS   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; PEPTIDASE; POLYPEPTIDE; PROTEASOME; PROTEINASE;

ANIMAL CELL; ARTICLE; CHEMICAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME SPECIFICITY; EUKARYOTIC CELL; ISOLATION PROCEDURE; MAJOR HISTOCOMPATIBILITY COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ACETYLCYSTEINE; ALLELES; AMINO ACID CHLOROMETHYL KETONES; ANIMALS; CELL SURVIVAL; COUMARINS; CYSTEINE ENDOPEPTIDASES; CYTOSOL; EPITOPES; GENES, MHC CLASS I; HYDROLYSIS; MICE; MOLECULAR WEIGHT; MULTIENZYME COMPLEXES; OLIGOPEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; SUBSTRATE SPECIFICITY; TUMOR CELLS, CULTURED;

EID: 0033548055     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.283.5404.978     Document Type: Article

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32. We thank S. Gaedicke for technical assistance, E. J. Corey for supplying lactacystin, K. Peters and A. Würch for helpful discussions, and I. Haidl for critical reading of the manuscript. Supported by a grant of the Deutsche Forschungsgemeinschaft (Nl 368/2-1) to G.N.