Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Christiana Cicicopol"'
Autor:
Ralph Golbik, Christiana Cicicopol, Andrei N. Lupas, Andreas Engel, Jürgen Peters, Günter Pfeifer, Hauke Lilie, Shirley A. Müller, Wolfgang Baumeister, Zdenka Cejka
Publikováno v:
Journal of Molecular Biology. 290:347-361
The phosphoenolpyruvate (PEP)-synthases belong to the family of structurally and functionally related PEP-utilizing enzymes. The only archaeal member of this family characterized thus far is the Multimeric Archaeal PEP-Synthase homologue from Staphyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::02688bb3fa95e5b908006ad774d6ed55
https://doi.org/10.1006/jmbi.1999.2878
https://doi.org/10.1006/jmbi.1999.2878
Autor:
Reiner Hegerl, Christiana Cicicopol, George Harauz, Wolfgang Baumeister, Zdenka Cejka, Kenneth N. Goldie, Andreas Engel, Ute Santarius
Publikováno v:
Journal of Structural Biology. 116:290-301
The phosphoenolpyruvate synthase of the hyperthermophilic archaeon Staphylothermus marinus forms an unusually large homomultimeric complex of 93 kDa subunits. Electron image analysis of negatively stained and low-dose unstained preparations showed th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dce10e9bc6a54b8af9767b9f53fb348
https://doi.org/10.1006/jsbi.1996.0044
https://doi.org/10.1006/jsbi.1996.0044
Publikováno v:
FEBS letters. 356(2-3)
A large protein complex (approx. 2000 kDa) was found in the cytosol of the hyperthermophilic archaebacterium Staphylothermus marinus. The purified protein was shown to be a homomultimer of 93 kDa subunits, the primary structure of which was determine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8bd5d80909db56c92e34c94d5efb421
https://pubmed.ncbi.nlm.nih.gov/7805870
https://pubmed.ncbi.nlm.nih.gov/7805870