Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

 
 
DownloadE-Mail
  Eubacterial proteasomes

Lupas, A., Zühl, F., Tamura, T., Wolf, S., Nagy, I., Demot, R., et al. (1997). Eubacterial proteasomes. Molecular Biology Reports, 24(1-2), 125-131.

Item is

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Lupas, A.1, Autor           
Zühl, F.1, Autor           
Tamura, T., Autor
Wolf, S.1, Autor           
Nagy, I.1, Autor           
Demot, R., Autor
Baumeister, W.1, Autor           
Affiliations:
1External Organizations, ou_persistent22              

Inhalt

einblenden:
ausblenden:
Schlagwörter: Proteasome; Hslvu; Clp; Multicatalytic protease; Atp-dependent proteolysis; Rhodococcus erythropolis.; Multicatalytic proteinase; Thermoplasma-acidophilum; Structural features; Electron-microscopy; Escherichia-coli; 20s proteasome; Complex dimer; 26-s protease; 26s protease; Subunit.; Molecular biology & genetics.
 Zusammenfassung: Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependentpathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease of about 700 kDa, which has also been detected in archaebacteria and, more recently, in eubacteria. Currently, the distribution of 20S proteasomes in eubacteria appears limited to the actinomycetes, while most other eubacteria contain a related complex of simpler structure. [References: 50]

Details

einblenden:
ausblenden:
Sprache(n):
 Datum: 1997-03
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 318360
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Molecular Biology Reports
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 24 (1-2) Artikelnummer: - Start- / Endseite: 125 - 131 Identifikator: -