Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Peter Zwickl"'
Autor:
Jörg Martin, Andrei N. Lupas, Sergej Djuranovic, Marcus D. Hartmann, Astrid Ursinus, Kornelius Zeth, Michael Habeck, Peter Zwickl
Publikováno v:
Molecular Cell. 34(5):580-590
The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4232a0d2345df3300450649751044190
Publikováno v:
Israel Journal of Chemistry. 46:225-229
The membrane-bound Lon protease from Thermoplasma acidophilum (Ta Lon) was shown to unfold and degrade a fusion of the green fluorescent protein with calmodulin (GFP—CaM). Unfolding and degradation were ATP-dependent reactions and could be inhibite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2bc51a2be118d091e329e22fa8a9f5f5
https://doi.org/10.1560/0env-nq8b-2wg6-nh8r
https://doi.org/10.1560/0env-nq8b-2wg6-nh8r
Autor:
Yune Z. Kunes, Nadine S. Weich, Ping Li, Zhiqiang Chen, Huilin Li, Gang Lin, Lawrence Dick, Peter Zwickl, Thomas F. Parsons, Christopher Tsu, Carl Nathan, Guiqing Hu
Publikováno v:
Molecular Microbiology. 59:1405-1416
Genes predicted to be associated with the putative proteasome of Mycobacterium tuberculosis (Mtb) play a critical role in defence of the bacillus against nitrosative stress. However, proteasomes are uncommon in eubacteria and it remains to be establi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::888bb5c992a398b5a3e92c2011904238
https://doi.org/10.1111/j.1365-2958.2005.05035.x
https://doi.org/10.1111/j.1365-2958.2005.05035.x
Autor:
Beate Rockel, Tomohiro Tamura, Peter Zwickl, Jürgen Peters, Alexandra Gerega, Wolfgang Baumeister
Publikováno v:
Journal of Biological Chemistry. 280:42856-42862
The Thermoplasma VCP-like ATPase from Thermoplasma acidophilum (VAT) ATPase is a member of the two-domain AAA ATPases and homologous to the mammalian p97/VCP and NSF proteins. We show here that the VAT ATPase complex unfolds green fluorescent protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df579dc097958d11207faf33e9a8b825
https://doi.org/10.1074/jbc.m510592200
https://doi.org/10.1074/jbc.m510592200
Publikováno v:
Journal of Biological Chemistry. 274:26008-26014
In eukaryotes, the 20 S proteasome is the proteolytic core of the 26 S proteasome, which degrades ubiquitinated proteins in an ATP-dependent process. Archaebacteria lack ubiquitin and 26 S proteasomes but do contain 20 S proteasomes. Many archaebacte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b63749e18e5c7d6beb449d3387753279
https://doi.org/10.1074/jbc.274.37.26008
https://doi.org/10.1074/jbc.274.37.26008
Publikováno v:
Annual Review of Biochemistry. 68:1015-1068
▪ Abstract In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built from ∼31 different subunits, which catalyzes protein degradation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22aeabce83d999c4bc67ae1fff9e56b4
https://doi.org/10.1146/annurev.biochem.68.1.1015
https://doi.org/10.1146/annurev.biochem.68.1.1015
Autor:
Peter Zwickl, Wolfgang Baumeister
This volume gives an overview of pro tea some-mediated protein degradation and the regulatory role of the ubiquitin system in cellular proteolysis. The first chapter describes the molecular evolution of the proteasome and its associated activators, i
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 60:515-524
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::264ceae84d5be4302a077b75d05915c8
https://doi.org/10.1101/sqb.1995.060.01.055
https://doi.org/10.1101/sqb.1995.060.01.055
Publikováno v:
Nature Structural Biology. 1:765-770
Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assembled and proteolytically active proteasomes. Post-translational processing of the beta-subunit occurs in E. coli as it does in Thermoplasma. Coexpressi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c71cf9281c7784ed26386d0265c40f
https://doi.org/10.1038/nsb1194-765
https://doi.org/10.1038/nsb1194-765
Publikováno v:
Systematic and Applied Microbiology. 16:734-741
We have examined a large number of archaea from all the major lineages and some bacteria with respect to the occurrence of proteasomes. Using three different assays for detection, the data we obtained suggest that proteasomes occur exclusively in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::517c92e0e950f4f58a3913ed0151a3fc
https://doi.org/10.1016/s0723-2020(11)80347-4
https://doi.org/10.1016/s0723-2020(11)80347-4