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

Geier, E., Pfeifer, G., Wilm, M., Lucchiari-Hartz, M., Baumeister, W., Eichmann, K., et al. (1999). A giant protease with potential to substitute for some functions of the proteasome. Science, 283(5404), 978-981.

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Genre: Zeitschriftenartikel
Alternativer Titel : Science

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Geier, E., Autor
Pfeifer, G.1, Autor           
Wilm, M., Autor
Lucchiari-Hartz, M., Autor
Baumeister, W.1, Autor           
Eichmann, K., Autor
Niedermann, G., Autor
Affiliations:
1External Organizations, ou_persistent22              

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Schlagwörter: Tripeptidyl-peptidase-ii; Rat-liver; Inhibition; Lactacystin; Proteins; Cells.; Multidisciplinary in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Multidisciplinary in Current Contents(R)/Life Sciences. Multidisciplinary in Current Contents(R)/Physical, Chemical & Earth Sciences.
 Zusammenfassung: An alanyl-alanyl-phenylalanyl-7-amino-4-methylcoumarin-hydrolyzing protease particle copurifying with 265 proteasomes was isolated and identified as tripeptidyl peptidase II(TPPII), a cytosolic subtilisin-like peptidase of unknown function. The particle is larger than the 265 proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like endoproteolytic cleavage. TPPII may thus participate in extralysosomal polypeptide degradation and may in part account for nonproteasomal epitope generation as postulated for certain major histocompatibility complex class I alleles, In addition, TPPII may be able to substitute for some metabolic functions of the proteasome. [References: 28]

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 Datum: 1999
 Publikationsstatus: Erschienen
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 Identifikatoren: eDoc: 318389
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Titel: Science
  Alternativer Titel : Science
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 283 (5404) Artikelnummer: - Start- / Endseite: 978 - 981 Identifikator: -