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of 10
pro vyhledávání: '"Ruth, Menssen"'
Autor:
Thorsten Pfirrmann, Pablo Villavicencio-Lorini, Abinash K Subudhi, Ruth Menssen, Dieter H Wolf, Thomas Hollemann
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0120342 (2015)
In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis. In higher organisms six conserved Gid proteins form the CTLH protein-complex with unknown
Externí odkaz:
https://doaj.org/article/32f1bce80ac44ac7a9bd8d19e17b5f2c
Publikováno v:
FEBS Letters. 592:3286-3294
Glucose consumption via glycolysis and its biosynthesis via gluconeogenesis are central reciprocal pathways controlled by a set of different enzymes. In the yeast Saccharomyces cerevisiae, expression of gluconeogenic enzymes is induced when cells are
Autor:
Dieter H, Wolf, Ruth, Menssen
Publikováno v:
FEBS letters. 592(15)
Precise regulation of cellular processes is essential for life. Regarding proteins, many regulatory mechanisms were explored over the years, such as posttranslational modifications (e.g., phosphorylation), enzyme activation or inhibition by small mol
Autor:
Dieter H. Wolf, Ruth Menssen
Publikováno v:
BIOspektrum. 21:608-611
Protein degradation by the ubiquitin-proteasome system (UPS) is essential for life. Degradation of enzymes and other regulatory proteins like activators or inhibitors is crucial for a multitude of cellular processes. Prominent examples are cell cycle
Publikováno v:
Current Biology. 11:345-350
The inactivation of mitotic cyclin-dependent kinases (CDKs) during anaphase is a prerequisite for the completion of nuclear division and the onset of cytokinesis [1, 2]. In the budding yeast Saccharomyces cerevisiae , the essential protein kinase Cdc
Publikováno v:
Journal of Molecular Biology. 285:645-653
The N and C termini of peptides presented by major histocompatibility complex (MHC) class I molecules are held within the peptide binding groove by a network of hydrogen bonds to conserved MHC residues. However, the published structure of the human a
Autor:
Denis Kusevic, Bernhard Braun, Jörg Schweiggert, Jens Schreiner, Ruth Menssen, Dieter H. Wolf, Julia Reuther
In the yeast Saccharomyces cerevisiae, key regulatory enzymes of gluconeogenesis such as fructose-1,6-bisphosphatase are degraded via the ubiquitin proteasome system when cells are replenished with glucose. Polyubiquitination is carried out by the Gi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d69e359b9e88d94e2909a5e11b6b5d
https://europepmc.org/articles/PMC3408164/
https://europepmc.org/articles/PMC3408164/
Publikováno v:
Proceedings of the National Academy of Sciences. 91:903-907
On the basis of mutational analyses in yeast, the highly conserved ACAGAGA sequence of U6 small nuclear RNA (snRNA) and the adjacent U6-U2 helix I have been proposed to be part of the active center of the spliceosome. We report here a detailed analys
Autor:
Dieter H. Wolf, Bernhard Braun, Ruth Menssen, Kay Hofmann, Thorsten Pfirrmann, Hartmut Scheel
Publikováno v:
FEBS letters. 585(24)
The two major antagonistic pathways of carbon metabolism in cells, glycolysis and gluconeogenesis, are tightly regulated. In the eukaryotic model organism Saccharomyces cerevisiae the switch from gluconeogenesis to glycolysis is brought about by prot
Publikováno v:
Biochemical and biophysical research communications. 397(3)
Fructose-1,6-bisphosphatase (FBPase) is a key regulatory enzyme of gluconeogenesis. In the yeast Saccharomyces cerevisiae, it is only expressed when cells are grown in medium with nonfermentable carbon sources. Addition of glucose to cells leads to i