Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Regina Zahn"'
Autor:
Chi-ting Ho, Tomas Grousl, Oren Shatz, Areeb Jawed, Carmen Ruger-Herreros, Marije Semmelink, Regina Zahn, Karsten Richter, Bernd Bukau, Axel Mogk
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
The sequestration of misfolded proteins into large assemblies by sequestrases is now considered as the third pillar in protein quality control besides chaperones and proteases. Here the authors characterise the functions of the sequestrases Hsp42 and
Externí odkaz:
https://doaj.org/article/046a4baa20df4aac872c48bb40ab57d6
Autor:
Regina Zahn, Axel Mogk, Karsten Richter, Chi-Ting Ho, Areeb Jawed, Tomas Grousl, Bernd Bukau, Marije Semmelink, Oren Shatz, Carmen Ruger-Herreros
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Nature Communications
Nature Communications
Maintenance of cellular proteostasis is achieved by a multi-layered quality control network, which counteracts the accumulation of misfolded proteins by refolding and degradation pathways. The organized sequestration of misfolded proteins, actively p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5403397a7c76960f6f9b0422c56f0e8
https://doaj.org/article/046a4baa20df4aac872c48bb40ab57d6
https://doaj.org/article/046a4baa20df4aac872c48bb40ab57d6
Autor:
Jimena Weibezahn, Regina Zahn, Tobias Haslberger, Bernd Bukau, Francis T.F. Tsai, Axel Mogk, Sukyeong Lee
Publikováno v:
Molecular Cell. 25(2):247-260
The AAA(+) chaperone ClpB mediates the reactivation of aggregated proteins in cooperation with the DnaK chaperone system. ClpB consists of two AAA domains that drive the ATP-dependent threading of substrates through a central translocation channel. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::418536264f41c800d15d24278a263156
Autor:
Peisze Wong, Victoria J. Boulton, Sebastian C. L. Yeo, Alan L. Munn, Cong Liu, Mahendra Wagle, Regina Zahn, Gang Ren, Robert C. Piper, Linghui Xu, Piriya Sasajala, Hongyuan Yang, Jihui Ren
Publikováno v:
Journal of Cell Science. 116:3957-3970
Vps4p (End13p) is an AAA-family ATPase that functions in membrane transport through endosomes, sorting of soluble vacuolar proteins to the vacuole, and multivesicular body (MVB) sorting of membrane proteins to the vacuole lumen. In a yeast two-hybrid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66903c92402b0d031b3c8e0e27f5c3b8
https://doi.org/10.1242/jcs.00751
https://doi.org/10.1242/jcs.00751
Publikováno v:
Traffic. 2:189-201
Vrp1p/verprolin/End5p is a Saccharomyces cerevisiae proline-rich protein, structurally and functionally related to human Wiskott–Aldrich syndrome protein-interacting protein. Vrp1p is required for viability at 37°C, but not 24°C. Here, we show th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80f983bbecc4e08546a98d1dbf00c2a9
https://doi.org/10.1034/j.1600-0854.2001.020305.x
https://doi.org/10.1034/j.1600-0854.2001.020305.x
Publikováno v:
Molecular Medicine. 2:712-724
Bm2325, a major IgE-inducing antigen of the filarial parasite Brugia malayi has been implicated in the pathology of tropical pulmonary eosinophilia (TPE), a pulmonary syndrome thought to result from hypersensitivity to microfilariae. Affinity-purifie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::856c21d006b445af3d1e1f9c9a781f32
https://doi.org/10.1007/bf03401655
https://doi.org/10.1007/bf03401655
Publikováno v:
Biol Chem
TPR proteins modulate the activity of molecular chaperones. Here, we describe the S. cerevisiae TPR protein Sgt2 as interaction partner of Ssa1 and Hsp104 and as a component of the GET pathway by interacting with Get5. The GET pathway mediates the so
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b05ab91f57116dfd4522a62c10c148c8
https://pubmed.ncbi.nlm.nih.gov/21619481
https://pubmed.ncbi.nlm.nih.gov/21619481
Publikováno v:
Molecular microbiology. 72(2)
The N-end rule degradation pathway states that the half-life of a protein is determined by the nature of its N-terminal residue. In Escherichia coli the adaptor protein ClpS directly interacts with destabilizing N-terminal residues and transfers them
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bfe2a809d523c3f562cf9a7a9d23912
https://pubmed.ncbi.nlm.nih.gov/19317833
https://pubmed.ncbi.nlm.nih.gov/19317833
Autor:
Regina Zahn, Bernd Bukau, David A. Dougan, Annette H. Erbse, T. Bornemann, Jens Schneider-Mergener, R. W. Schmidt, Axel Mogk
Publikováno v:
Nature. 439(7077)
The N-end rule states that the half-life of a protein is determined by the nature of its amino-terminal residue1. Eukaryotes and prokaryotes use N-terminal destabilizing residues as a signal to target proteins for degradation by the N-end rule pathwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::802b5f4638cebb444e98490869fed50a
https://pubmed.ncbi.nlm.nih.gov/16467841
https://pubmed.ncbi.nlm.nih.gov/16467841
Autor:
Thorsten Kohl, Holger Ottleben, Simone Schleeger, Martina Schnölzer, Regina Zahn, Annemarie Poustka, Hans van der Zandt, Stefan Wiemann, Stephanie Bechtel, Ulrike Korf, Silke Wandschneider, Barbara Ueberle
Publikováno v:
Proteomics. 5(14)
Access to pure and soluble recombinant proteins is essential for numerous applications in proteome research, such as the production of antibodies, structural characterization of proteins, and protein microarrays. Through the German cDNA Consortium we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2e9861e337ee8052041968896a48b5b
https://pubmed.ncbi.nlm.nih.gov/16127724
https://pubmed.ncbi.nlm.nih.gov/16127724