Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Jessica Klümper"'
Autor:
Mausumi Ghosh, Niels Denkert, Maren Reuter, Jessica Klümper, Katharina Reglinski, Rebecca Peschel, Wolfgang Schliebs, Ralf Erdmann, Michael Meinecke
Publikováno v:
Biological Chemistry. 404:169-178
Peroxisomal matrix proteins are synthesized on cytosolic ribosomes and imported in a posttranslational manner. Intricate protein import machineries have evolved that catalyze the different stages of translocation. In humans, PEX5L was found to be an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dac26896965470aea85436536e90288
https://doi.org/10.1515/hsz-2022-0170
https://doi.org/10.1515/hsz-2022-0170
Autor:
Malayko Montilla-Martinez, Sabrina Beck, Jessica Klümper, Michael Meinecke, Wolfgang Schliebs, Richard Wagner, Ralf Erdmann
Publikováno v:
Cell Reports, Vol 13, Iss 10, Pp 2126-2134 (2015)
Two peroxisomal targeting signals, PTS1 and PTS2, recognized by cytosolic receptors Pex5 and cooperating Pex7/Pex18, direct folded proteins to the peroxisomal matrix. A pore consisting of the PTS1 receptor Pex5 and the docking protein Pex14 imports P
Externí odkaz:
https://doaj.org/article/c0f96660e87f4cc9850c4a6da37d3340
Publikováno v:
Sub-cellular biochemistry. 89
Different pull-down strategies were successfully applied to gain novel insight into the interactome of human membrane-associated proteins. Here, we compare the outcome, efficiency and potential of pull-down strategies applied to human peroxisomal mem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b31e6c6ce8a999f8e472213ae5bc4171
https://pubmed.ncbi.nlm.nih.gov/30378027
https://pubmed.ncbi.nlm.nih.gov/30378027
Autor:
Malayko Montilla-Martinez, Sabrina Beck, Jessica Klümper, Michael Meinecke, Wolfgang Schliebs, Richard Wagner, Ralf Erdmann
Publikováno v:
Cell Reports, Vol 13, Iss 10, Pp 2126-2134 (2015)
Two peroxisomal targeting signals, PTS1 and PTS2, recognized by cytosolic receptors Pex5 and cooperating Pex7/Pex18, direct folded proteins to the peroxisomal matrix. A pore consisting of the PTS1 receptor Pex5 and the docking protein Pex14 imports P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1138e16528f44ef3b9f67d0ca367e964
Autor:
Ghosh, Mausumi, Denkert, Niels, Reuter, Maren, Klümper, Jessica, Reglinski, Katharina, Peschel, Rebecca, Schliebs, Wolfgang, Erdmann, Ralf, Meinecke, Michael
Publikováno v:
Biological Chemistry; Feb2023, Vol. 404 Issue 2/3, p169-178, 10p
Autor:
Luis A. del Río, Michael Schrader
This new edited volume in the Springer Subcellular Biochemistry Series presents a comprehensive, state-of-the-art overview of the proteomics of peroxisomes derived from mammalian, Drosophila, fungal, and plant origin, and contains contributions from
