Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Zdenka Cejka"'
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:
Andrei N. Lupas, Zdenka Cejka, Günter Pfeifer, Wolfgang Baumeister, István Nagy, Shirley A. Müller, Andreas Engel, René De Mot, Stefan Wolf
Publikováno v:
Journal of Molecular Biology. 277:13-25
A gene encoding a AAA ATPase was discovered in the 5′ region of the second operon of 20 S proteasome subunits in the nocardioform actinomycete Rhodococcus erythropolis NI86/21. The gene was cloned and expressed in Escherichia coli. The protein, ARC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79b12e9a2045e8b73d1697c3d86dd655
https://doi.org/10.1006/jmbi.1997.1589
https://doi.org/10.1006/jmbi.1997.1589
Autor:
Zdenka Cejka, Jürgen Peters, Vashu Pamnani, Andrei N. Lupas, Tomohiro Tamura, William Ashraf, Wolfgang Baumeister
Publikováno v:
FEBS Letters. 404:263-268
A member of the AAA family of Mg 2+ -ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli . The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0248f2578763495ab22d651805c7500a
https://doi.org/10.1016/s0014-5793(97)00138-5
https://doi.org/10.1016/s0014-5793(97)00138-5
Autor:
Zdenka Cejka, Reiner Hegerl, Friedrich Lottspeich, Noriko Tamura, Tomohiro Tamura, Wolfgang Baumeister
Publikováno v:
Science. 274:1385-1389
Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcd2ce1561f01c7df06583fb6f5cafa5
https://doi.org/10.1126/science.274.5291.1385
https://doi.org/10.1126/science.274.5291.1385
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
Autor:
Istvén Nagy, Tomohiro Tamura, Zdenka Cejka, Wolfgang Baumeister, René De Mot, Andrei N. Lupas, Friedrich Lottspeich, Keiji Tanaka, Geert Schoofs
Publikováno v:
Current Biology. 5(7):766-774
Background: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation. The proteolytic core of the complex is formed by the 20S proteasome, a cylinder-shaped particle that in archaebacteria contains two diff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea335553a16cb1c973a67b6254c39c1b
Publikováno v:
Journal of Molecular Biology. 234:932-937
Proteasomes play a key role in the degradation of abnormal proteins, of short-lived regulatory proteins and in antigen processing. Evidence is accumulating that the 20 S proteasome represents the proteolytic core of the 26 S protease complex (26 S pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebfd79001b3f20ce8d471dfc415ff7f6
https://doi.org/10.1006/jmbi.1993.1646
https://doi.org/10.1006/jmbi.1993.1646
Autor:
Tetsuro Yoshimura, Keiichi Kameyama, Toshio Takagi, Atsushi Ikai, Fuminori Tokunaga, Takehiko Koide, Nobuyuki Tanahashi, Tomohiro Tamura, Zdenka Cejka, Wolfgang Baumeister, Keiji Tanaka, Akira Ichihara
Publikováno v:
Journal of Structural Biology. 111:200-211
The molecular properties of an ATP/ubiquitin-dependent "26S" proteasome complex purified from rat liver were examined by physicochemical, biochemical, and morphological analyses. On ultracentrifugation, the proteasome complex sedimented as almost a s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2500099b00365a09528041c8399442c7
https://doi.org/10.1006/jsbi.1993.1050
https://doi.org/10.1006/jsbi.1993.1050
Publikováno v:
Journal of Structural Biology. 111:34-38
Image processing has revealed the attachment site of antibody 54G8 on chaperonin 60 (cpn60) from Bordetella pertussis. This antibody, previously shown to affect the ability of chaperonin 10 (cpn10) to inhibit the ATPase activity of cpn60, is attached
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73de397bdb60b10e930c9ed72a57fb0f
https://doi.org/10.1006/jsbi.1993.1033
https://doi.org/10.1006/jsbi.1993.1033
Publikováno v:
Journal of Structural Biology. 110:196-204
The mechanism by which bacteriorhodopsin (BR), the light-driven proton pump from the purple membrane (PM) of Halobacterium halobium, arranges in a 2D hexagonal array has been studied by reconstitution of BR in complexes of two types of bilayer made e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59a872f4ec958882dd77c27d01578bfb
https://doi.org/10.1006/jsbi.1993.1022
https://doi.org/10.1006/jsbi.1993.1022