Literature for peptidase S33.005: tricorn interacting factor F1
(Topics flags: S Structure, V Review. To select only the references relevant to a single topic, click the link above. See explanation.)
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Goettig,P., Brandstetter,H., Groll,M., Gohring,W., Konarev,P.V., Svergun,D.I., Huber,R. and Kim,J.S.
X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum
J Biol Chem280, 33387-33396. PubMed Europe PubMed DOI S -
Kitazono,A.A., Ito,K. and Yoshimoto,T.
Prolyl aminopeptidase
[ISSN:0-12-079610-4]2, 1943-1947. V -
[YEAR:15-10-2002]Goettig,P., Groll,M., Kim,J.S., Huber,R. and Brandstetter,H.
Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism
EMBO J21, 5343-5352. PubMed Europe PubMed DOI S -
[YEAR:25-11-1998]Tamura,N., Lottspeich,F., Baumeister,W. and Tamura,T.
The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation
Cell95, 637-648. PubMed Europe PubMed -
[YEAR:25-11-1996]Tamura,T., Tamura,N., Lottspeich,F. and Baumeister,W.
Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum is a proline iminopeptidase
FEBS Lett398, 101-105. PubMed Europe PubMed DOI
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1996
