Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Daili J A Netz"'
Autor:
Lea Weinisch, Steffen Kühner, Robin Roth, Maria Grimm, Tamara Roth, Daili J A Netz, Antonio J Pierik, Sabine Filker
Publikováno v:
PLoS Biology, Vol 16, Iss 1, p e2003892 (2018)
Hypersaline environments pose major challenges to their microbial residents. Microorganisms have to cope with increased osmotic pressure and low water activity and therefore require specific adaptation mechanisms. Although mechanisms have already bee
Externí odkaz:
https://doaj.org/article/9685780c25614757843fb2000395b280
Autor:
Christina S. Müller, Carina Greth, Edward J. Reijerse, Kathrin Stegmaier, Catharina M. Blinn, Antonio J. Pierik, Volker Schünemann, Dominique F. Bechtel, Daili J. A. Netz, Valentin Jakob, Hendrik Auerbach
Publikováno v:
Journal of the American Chemical Society. 141(14)
Apd1, a cytosolic yeast protein, and Aim32, its counterpart in the mitochondrial matrix, have a C-terminal thioredoxin-like ferredoxin (TLF) domain and a widely divergent N-terminal domain. These proteins are found in bacteria, plants, fungi, and uni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc8dee35fee808013569170701fc8e35
https://pubmed.ncbi.nlm.nih.gov/30879301
https://pubmed.ncbi.nlm.nih.gov/30879301
Autor:
Valentin Jakob, Hendrik Auerbach, Dominique F. Bechtel, Volker Schünemann, Daili J. A. Netz, Antonio J. Pierik, Catharina M. Blinn, Christina S. Müller, Carina Greth, Kathrin Stegmaier
Apd1, a cytosolic yeast protein, and Aim32, its counterpart in the mitochondrial matrix, have a C-terminal thioredoxinlike ferredoxin domain and a widely divergent N-terminal domain. These proteins are found in bacteria, plants, fungi and unicellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b7a4a151bf4339e93fcf35749ef7de5
https://doi.org/10.26434/chemrxiv.7443971.v1
https://doi.org/10.26434/chemrxiv.7443971.v1
Autor:
Torsten Heidenreich, Nadine Richter, Antonio J. Pierik, Rafal Dutkiewicz, Judita Mascarenhas, Sven A. Freibert, Daili J. A. Netz, Roland Lill, Vasundara Srinivasan, Viktoria Désirée Paul, Martin Stümpfig, Ulrich Mühlenhoff, Oliver Stehling
Publikováno v:
European Journal of Cell Biology. 94:280-291
Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of eukaryotes. Numerous bacterial functions have been maintained inside the organelles including fatty acid degradation, citric acid cycle, oxidative phosphorylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::354952d1177f403b94895d63871ba1ab
https://doi.org/10.1016/j.ejcb.2015.05.002
https://doi.org/10.1016/j.ejcb.2015.05.002
Autor:
Maria Grimm, Robin Roth, Antonio J. Pierik, Steffen Kühner, Daili J. A. Netz, Sabine Filker, Lea Weinisch, Tamara Roth
Publikováno v:
PLoS Biology
PLoS Biology, Vol 16, Iss 1, p e2003892 (2018)
PLoS Biology, Vol 16, Iss 1, p e2003892 (2018)
Hypersaline environments pose major challenges to their microbial residents. Microorganisms have to cope with increased osmotic pressure and low water activity and therefore require specific adaptation mechanisms. Although mechanisms have already bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b958175f89cad2bc5a69183d1a0a9447
http://europepmc.org/articles/PMC5794333
http://europepmc.org/articles/PMC5794333
Autor:
Roland Lill, Christoph W. Müller, Vladimir Rybin, Daili J. A. Netz, Karin D. Breunig, Anne-Claude Gavin, Antonio J. Pierik, Sebastian Glatt, Ivana Vonkova, Amit Kumar, Rene Zabel, Jochen Balbach
Publikováno v:
Structure, Vol. 23, No 1 (2015) pp. 149-160
SummaryThe small, highly conserved Kti11 alias Dph3 protein encoded by the Kluyveromyces lactis killer toxin insensitive gene KTI11/DPH3 is involved in the diphthamide modification of eukaryotic elongation factor 2 and, together with Kti13, in Elonga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc308f7b7cc0318c2013e2a4853574a7
https://doi.org/10.1016/j.str.2014.11.008
https://doi.org/10.1016/j.str.2014.11.008
Autor:
Thibaut J. Lagny, Daili J. A. Netz, Somsuvro Basu, Nils Herlerth, Julius Lukeš, Antonio J. Pierik, Alexander C. Haindrich, Roland Lill
Publikováno v:
Molecular Microbiology. 93:897-910
Summary Cytosolic and nuclear iron-sulphur (Fe/S) proteins include essential components involved in protein translation, DNA synthesis and DNA repair. In yeast and human cells, assembly of their Fe/S cofactor is accomplished by the CIA (cytosolic iro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2b575e789d6a3fcdbf1709edd513ccd
https://doi.org/10.1111/mmi.12706
https://doi.org/10.1111/mmi.12706
Autor:
Tanu Sharma, Roland Lill, Daili J. A. Netz, Antonio J. Pierik, Oliver Stehling, Ajay A. Vashisht, James A. Wohlschlegel, Zophonías O. Jónsson, Judita Mascarenhas
Publikováno v:
Science. 337:195-199
MMS19 Joins the CIA Iron-sulfur (Fe-S) proteins play a critical role in cell metabolism and particularly in DNA repair and replication. Mutants in eukaryotic gene MMS19 are particularly sensitive to DNA damaging agents, suggesting that it is involved
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e8fcaa48187465a25afa676cac680307
https://doi.org/10.1126/science.1219723
https://doi.org/10.1126/science.1219723
Autor:
Roland Lill, Daili J. A. Netz, Martin Stümpfig, William E. Walden, Eckhard Bill, Anil K. Sharma, Leif J. Pallesen, Antonio J. Pierik
Publikováno v:
Journal of Biological Chemistry. 287:12365-12378
The essential P-loop NTPases Cfd1 and Nbp35 of the cytosolic iron-sulfur (Fe-S) protein assembly machinery perform a scaffold function for Fe-S cluster synthesis. Both proteins contain a nucleotide binding motif of unknown function and a C-terminal m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f436502159b7891e59b8489134b02862
https://doi.org/10.1074/jbc.m111.328914
https://doi.org/10.1074/jbc.m111.328914
Autor:
Daili J. A. Netz, Antonio J. Pierik, Ulrich Mühlenhoff, Roland Lill, Carole Doré, Martin Stümpfig
Publikováno v:
Nature Chemical Biology. 6:758-765
Iron-sulfur clusters are essential components of many proteins and are assembled in a hierarchical pathway. Tah18 is a diflavin reductase that transfers electrons to the [2Fe-2S] cluster of Dre2 in an early step of iron-sulfur cluster biogenesis in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60000d01e50a3a8cef9d1775e5ce7c1e
https://doi.org/10.1038/nchembio.432
https://doi.org/10.1038/nchembio.432