Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Jann-Patrick Pelz"'
Autor:
Christoph Lübbert, Igor Dykukha, Jann-Patrick Pelz, Helen Yearley, Wolfgang Junker, Nina Gruber, Sibyll Escher, Katrin Biereth, Sima Melnik, Julia Puschmann
Publikováno v:
Drugs in Context, Vol 12, Pp 1-12 (2023)
Background: Nirmatrelvir/ritonavir is authorized for the treatment of COVID-19 but has several contraindications and potential drug–drug interactions (pDDIs) due to ritonavir-induced irreversible inhibition of cytochrome P450 3A4. We aimed to asses
Externí odkaz:
https://doaj.org/article/74464b32825a40e0af5c09b21a20de0e
Publikováno v:
Biomolecules, Vol 10, Iss 6, p 872 (2020)
Eukaryotic cells determine the protein output of their genetic program by regulating mRNA transcription, localization, translation and turnover rates. This regulation is accomplished by an ensemble of RNA-binding proteins (RBPs) that bind to any give
Externí odkaz:
https://doaj.org/article/aec2e167836247c9863bf0036100ee75
Publikováno v:
'Biomolecules ', vol: 10, pages: 872-1-872-12 (2020)
Biomolecules
Biomolecules, Vol 10, Iss 872, p 872 (2020)
Volume 10
Issue 6
Biomolecules
Biomolecules, Vol 10, Iss 872, p 872 (2020)
Volume 10
Issue 6
Eukaryotic cells determine the protein output of their genetic program by regulating mRNA transcription, localization, translation and turnover rates. This regulation is accomplished by an ensemble of RNA-binding proteins (RBPs) that bind to any give
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a315d03dc71e65574e7b3cdebc1392e7
https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-207800
https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-207800
Autor:
Jochen Kuper, Katharina van Pee, Jann Patrick Pelz, Utz Fischer, Clemens Grimm, Hermann Schindelin, Kay Diederichs, Caroline Kisker
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 71(Pt 10)
The small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/6 and U5 are major constituents of the pre-mRNA processing spliceosome. They contain a common RNP core that is formed by the ordered binding of Sm proteins onto the single-stranded Sm site of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2754f9b62704f84c3ac610ca05b9dba8
https://pubmed.ncbi.nlm.nih.gov/26457428
https://pubmed.ncbi.nlm.nih.gov/26457428