Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ashley D. Easter"'
Autor:
Carlo Baejen, Juan B. Rodríguez-Molina, Patrick Cramer, Ana Casañal, Kerstin C. Maier, Sofia Battaglia, Ashley D. Easter, Pawel Grzechnik, Manuel Carminati, Lori A. Passmore, Michael Lidschreiber
Publikováno v:
Nucleic Acids Research
Lidschreiber, M, Easter, A D, Battaglia, S, Rodríguez-Molina, J B, Casanal, A, Carminati, M, Baejen, C, Grzechnik, P, Maier, K C, Cramer, P & Passmore, L A 2018, ' The APT complex is involved in non-coding RNA transcription and is distinct from CPF ', Nucleic acids research, vol. 46, no. 21, pp. 11528-11538 . https://doi.org/10.1093/nar/gky845
Lidschreiber, M, Easter, A D, Battaglia, S, Rodríguez-Molina, J B, Casanal, A, Carminati, M, Baejen, C, Grzechnik, P, Maier, K C, Cramer, P & Passmore, L A 2018, ' The APT complex is involved in non-coding RNA transcription and is distinct from CPF ', Nucleic acids research, vol. 46, no. 21, pp. 11528-11538 . https://doi.org/10.1093/nar/gky845
The 3′-ends of eukaryotic pre-mRNAs are processed in the nucleus by a large multiprotein complex, the cleavage and polyadenylation factor (CPF). CPF cleaves RNA, adds a poly(A) tail and signals transcription termination. CPF harbors four enzymatic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe274f18820bafe74e6c9fa40fa3f179
https://pubmed.ncbi.nlm.nih.gov/30247719
https://pubmed.ncbi.nlm.nih.gov/30247719
Autor:
Vickery L. Arcus, Joanne K. Hobbs, Louis A. Schipper, Ashley D. Easter, Wanting Jiao, Emily J. Parker
Publikováno v:
ACS chemical biology. 12(3)
The increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This accou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a74017b8213e3374b764f0025af9568b
https://pubmed.ncbi.nlm.nih.gov/24015933
https://pubmed.ncbi.nlm.nih.gov/24015933
Autor:
Nicholas Sofos, Lori A. Passmore, Ditlev E. Brodersen, Kasper R. Andersen, Andreas Bøggild, Ashley D. Easter, Ane Feddersen
Publikováno v:
Structure(London, England:1993)
Bøggild, A, Sofos, N, Andersen, K R, Feddersen, A, Easter, A D, Passmore, L A & Brodersen, D 2012, ' The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity ', Structure, vol. 20, no. 10, pp. 1641–1648 . https://doi.org/10.1016/j.str.2012.08.017
Bøggild, A, Sofos, N, Andersen, K R, Feddersen, A, Easter, A D, Passmore, L A & Brodersen, D 2012, ' The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity ', Structure, vol. 20, no. 10, pp. 1641–1648 . https://doi.org/10.1016/j.str.2012.08.017
Summary The bacterial relBE locus encodes a toxin-antitoxin complex in which the toxin, RelE, is capable of cleaving mRNA in the ribosomal A site cotranslationally. The antitoxin, RelB, both binds and inhibits RelE, and regulates transcription throug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1862102152c7ed66d307cd4a409f623e
http://europepmc.org/articles/PMC3507626
http://europepmc.org/articles/PMC3507626
Autor:
Ashley D. Easter, Patrick Cramer, Lori A. Passmore, Amelie Schreieck, Katrin Wiederhold, Stefanie Etzold, Michael Lidschreiber
Publikováno v:
Nature Structural and Molecular Biology
At the 3' ends of protein-coding genes, RNA polymerase (Pol) II is dephosphorylated at tyrosine residues (Tyr1) of its C-terminal domain (CTD). In addition, the associated cleavage-and-polyadenylation factor (CPF) cleaves the transcript and adds a po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9524387cab3a9e8ccca18802176947d