ANGEL2 is a member of the CCR4 family of deadenylases with 2′, 3′-cyclic phosphatase activity
RNA molecules are frequently modified with a terminal 2′,3′-cyclic phosphate group as a
result of endonuclease cleavage, exonuclease trimming, or de novo synthesis. During pre-…
result of endonuclease cleavage, exonuclease trimming, or de novo synthesis. During pre-…
Molecular architecture of the human tRNA ligase complex
A Kroupova, F Ackle, I Asanović, S Weitzer… - Elife, 2021 - elifesciences.org
RtcB enzymes are RNA ligases that play essential roles in tRNA splicing, unfolded protein
response, and RNA repair. In metazoa, RtcB functions as part of a five-subunit tRNA ligase …
response, and RNA repair. In metazoa, RtcB functions as part of a five-subunit tRNA ligase …
Structural basis for acceptor RNA substrate selectivity of the 3′ terminal uridylyl transferase Tailor
A Kroupova, A Ivaşcu, MM Reimao-Pinto… - Nucleic acids …, 2019 - academic.oup.com
Non-templated 3′-uridylation of RNAs has emerged as an important mechanism for regulating
the processing, stability and biological function of eukaryotic transcripts. In Drosophila, …
the processing, stability and biological function of eukaryotic transcripts. In Drosophila, …
[PDF][PDF] The oxidoreductase PYROXD1 uses NAD (P)+ as an antioxidant to sustain tRNA ligase activity in pre-tRNA splicing and unfolded protein response
I Asanović, E Strandback, A Kroupova, D Pasajlic… - Molecular Cell, 2021 - cell.com
The tRNA ligase complex (tRNA-LC) splices precursor tRNAs (pre-tRNA), and Xbp1-mRNA
during the unfolded protein response (UPR). In aerobic conditions, a cysteine residue bound …
during the unfolded protein response (UPR). In aerobic conditions, a cysteine residue bound …
Mechanistic basis for oxidative stress protection of the human tRNA ligase complex by the oxidoreductase PYROXD1
L Loeff, A Kroupova, I Asanović, F Boneberg… - bioRxiv, 2023 - biorxiv.org
RTCB is the catalytic subunit of the metazoan tRNA ligase complex (tRNA-LC) that plays
essential roles in tRNA biogenesis and unfolded protein response. The catalytic center of RTCB …
essential roles in tRNA biogenesis and unfolded protein response. The catalytic center of RTCB …
Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders
A Kroupova, VA Spiteri, H Furihata, D Darren… - bioRxiv, 2024 - biorxiv.org
The ubiquitin E3 ligase cereblon (CRBN) is the target of therapeutic drugs thalidomide and
lenalidomide and is recruited by most targeted protein degraders (PROTACs and molecular …
lenalidomide and is recruited by most targeted protein degraders (PROTACs and molecular …
Molecular architecture of the human tRNA ligase complex
K Alena, A Fabian, A Igor, S Weitzer, FM Boneberg… - eLife, 2021 - search.proquest.com
RtcB enzymes are RNA ligases that play essential roles in tRNA splicing, unfolded protein
response, and RNA repair. In metazoa, RtcB functions as part of a five-subunit tRNA ligase …
response, and RNA repair. In metazoa, RtcB functions as part of a five-subunit tRNA ligase …
The Oxidoreductase PYROXD1 Utilizes NAD (P)+ As an Antioxidant to Sustain tRNA Ligase Activity in Pre-tRNA Splicing and Unfolded Protein Response
I Asanovic, E Strandback, A Kroupova, D Pasajlic… - papers.ssrn.com
The tRNA ligase complex (tRNA-LC) mediates splicing of pre-tRNAs, and the Xbp1-mRNA
during the unfolded protein response (UPR). The presence of a cysteine residue and two …
during the unfolded protein response (UPR). The presence of a cysteine residue and two …
[BOOK][B] The impact of the United Nations human rights treaties on the domestic level
C Heyns, F Viljoen - 2021 - books.google.com
The six main United Nations human rights treaties enjoy almost universal ratification today.
Almost 80 per cent of the possible ratifications have been made, and every Member State of …
Almost 80 per cent of the possible ratifications have been made, and every Member State of …
[CITATION][C] Convention on the Rights of the Child: Education for the 21st Century
A Kroupová - Monitoring Children's Rights, 1996 - brill.com