Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Antje Schäfer"'
Autor:
Daniel Andreas Orlando Rotter, Christoph Heger, Christian Kühm, Nina Schmidt, Antje Schäfer, Thomas Heimerl, Matthias Mack, Peter L. Graumann
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
Flavins are ubiquitous molecules in life as they serve as important enzyme cofactors. In the Gram-positive, soil-dwelling bacterium Bacillus subtilis, four well-characterized gene products (the enzymes RibDG, RibE, RibAB, and RibH) catalyze the biosy
Externí odkaz:
https://doaj.org/article/7c617dd5d6d0420fa7d8deb3abe24cec
Publikováno v:
Traffic. 11:1363-1369
Proteins imported into the endoplasmic reticulum (ER) are scanned for their folding status. Those that do not reach their native conformation are degraded via the ubiquitin-proteasome system. This process is called ER-associated degradation (ERAD). D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81d971f0a4ffeef60f2d8b4e360f1363
https://doi.org/10.1111/j.1600-0854.2010.01093.x
https://doi.org/10.1111/j.1600-0854.2010.01093.x
Autor:
Dieter H. Wolf, Antje Schäfer
Publikováno v:
The EMBO Journal. 28:2874-2884
Endoplasmic reticulum-associated degradation (ERAD) is a cellular pathway for the disposal of misfolded secretory proteins. This process comprises recognition of the misfolded proteins followed by their retro-translocation across the ER membrane into
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b873cae8145f363281ae61f7f5ccd78
https://doi.org/10.1038/emboj.2009.231
https://doi.org/10.1038/emboj.2009.231
Publikováno v:
Journal of Biological Chemistry. 284:16082-16089
Misfolded proteins of the secretory pathway are recognized in the endoplasmic reticulum (ER), retrotranslocated into the cytoplasm, and degraded by the ubiquitin-proteasome system. Right after retrotranslocation and polyubiquitination, they are extra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbeec2ae117fa069852a5bd32322a284
https://doi.org/10.1074/jbc.m809282200
https://doi.org/10.1074/jbc.m809282200
Autor:
Wolf-H. Kunau, Antje Schäfer, Karsten Niederhoff, Nadja M. Meindl-Beinker, Uta Perband, Daniela Kerssen, Wolfgang Schliebs
Publikováno v:
Journal of Biological Chemistry. 280:35571-35578
Current evidence favors a cycling receptor model for the import of peroxisomal matrix proteins. The yeast Pex14 protein together with Pex13p and Pex17p form the docking subcomplex at the peroxisomal membrane and interact in this cycle with both solub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86490b5d53c400db66b5082b934e5ace
https://doi.org/10.1074/jbc.m502460200
https://doi.org/10.1074/jbc.m502460200
Publikováno v:
Molecular and Cellular Biology, 24(20), 8895-8906. AMER SOC MICROBIOLOGY
Within the extended receptor cycle of peroxisomal matrix import, the function of the import receptor Pex5p comprises cargo recognition and transport. While the C-terminal half (Pex5p-C) is responsible for PTS1 binding, the contribution of the N-termi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad0b5b905164f029ce1e4e3a9ae047fb
https://doi.org/10.1128/mcb.24.20.8895-8906.2004
https://doi.org/10.1128/mcb.24.20.8895-8906.2004
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 70(Pt 5)
The activation of ubiquitin by the ubiquitin-activating enzyme Uba1 (E1) constitutes the first step in the covalent modification of target proteins with ubiquitin. This activation is a three-step process in which ubiquitin is adenylated at its C-term
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21943d1c1ba5c337bd922e22baf1851d
https://pubmed.ncbi.nlm.nih.gov/24816100
https://pubmed.ncbi.nlm.nih.gov/24816100
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 832
The conjugation of ubiquitin and related modifiers to selected proteins represents a general mechanism to alter the function of these protein targets, thereby increasing the complexity of the cellular proteome. Ubiquitylation is catalyzed by a hierar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f1240a560f9363e3a4811ac356428195
https://pubmed.ncbi.nlm.nih.gov/22350912
https://pubmed.ncbi.nlm.nih.gov/22350912
Publikováno v:
Methods in Molecular Biology ISBN: 9781617794735
The conjugation of ubiquitin and related modifiers to selected proteins represents a general mechanism to alter the function of these protein targets, thereby increasing the complexity of the cellular proteome. Ubiquitylation is catalyzed by a hierar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23bfd69ff6119c7e77729b932bfa7327
https://doi.org/10.1007/978-1-61779-474-2_39
https://doi.org/10.1007/978-1-61779-474-2_39
Autor:
Mohamed A. Marahiel, Olaf Burghaus, Leif Flühe, Michael J. Gattner, Thomas A. Knappe, Uwe Linne, Antje Schäfer
Publikováno v:
Nature chemical biology. 8(4)
Subtilosin A is a 35-residue, ribosomally synthesized bacteriocin encoded by the sbo-alb operon of Bacillus subtilis. It is composed of a head-to-tail circular peptide backbone that is additionally restrained by three unusual thioether bonds between
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f470e721493d2bc885fd3a9ad771c05c
https://pubmed.ncbi.nlm.nih.gov/22366720
https://pubmed.ncbi.nlm.nih.gov/22366720