Rajiv Kumar Bedi
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Explore the profile of Rajiv Kumar Bedi including associated specialties, affiliations and a list of published articles.
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Articles
8
Citations
139
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Recent Articles
1.
Corbeski I, Vargas-Rosales P, Bedi R, Deng J, Coelho D, Braud E, et al.
Elife
. 2024 Mar;
12.
PMID: 38470714
The complex of methyltransferase-like proteins 3 and 14 (METTL3-14) is the major enzyme that deposits N-methyladenosine (mA) modifications on messenger RNA (mRNA) in humans. METTL3-14 plays key roles in various...
2.
Corbeski I, Vargas-Rosales P, Bedi R, Deng J, Coelho D, Braud E, et al.
bioRxiv
. 2023 Sep;
PMID: 37732228
The complex of methyltransferase-like proteins 3 and 14 (METTL3-14) is the major enzyme that deposits N6-methyladenosine (m6A) modifications on mRNA in humans. METTL3-14 plays key roles in various biological processes...
3.
Bedi R, Huang D, Li Y, Caflisch A
ACS Bio Med Chem Au
. 2023 Aug;
3(4):359-370.
PMID: 37599794
Methyltransferase-like 3 (METTL3) and METTL14 form a heterodimeric complex that catalyzes the most abundant internal mRNA modification, -methyladenosine (mA). METTL3 is the catalytic subunit that binds the co-substrate -adenosyl methionine...
4.
Moroz-Omori E, Huang D, Bedi R, Cheriyamkunnel S, Bochenkova E, Dolbois A, et al.
ChemMedChem
. 2021 Jul;
16(19):3035-3043.
PMID: 34237194
The methylase METTL3 is the writer enzyme of the N -methyladenosine (m A) modification of RNA. Using a structure-based drug discovery approach, we identified a METTL3 inhibitor with potency in...
5.
Li Y, Bedi R, Wiedmer L, Sun X, Huang D, Caflisch A
J Chem Theory Comput
. 2021 Jan;
17(2):1240-1249.
PMID: 33472367
N6-Methyladenosine (mA) is the most frequent modification in eukaryotic messenger RNA (mRNA) and its cellular processing and functions are regulated by the reader proteins YTHDCs and YTHDFs. However, the mechanism...
6.
Bedi R, Huang D, Wiedmer L, Li Y, Dolbois A, Wojdyla J, et al.
ACS Chem Biol
. 2020 Feb;
15(3):618-625.
PMID: 32101404
We report a crystallographic analysis of small-molecule ligands of the human YTHDC1 domain that recognizes N6-methylated adenine (mA) in RNA. The 30 binders are fragments (molecular weight < 300 g...
7.
Li Y, Bedi R, Wiedmer L, Huang D, Sledz P, Caflisch A
J Chem Theory Comput
. 2019 Nov;
15(12):7004-7014.
PMID: 31670957
-Methyladenosine (mA) is the most prevalent chemical modification in human mRNAs. Its recognition by reader proteins enables many cellular functions, including splicing and translation of mRNAs. However, the binding mechanisms...
8.
Wiedmer L, Eberle S, Bedi R, Sledz P, Caflisch A
Anal Chem
. 2019 Feb;
91(4):3078-3084.
PMID: 30715855
We have developed a homogeneous time-resolved fluorescence (HTRF)-based enzyme assay to measure the catalytic activity of N-methyladenosine (mA) methyltransferases and demethylases. The assay detects mA modifications using the natural mA-binding...