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Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain

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metacan-v1-d91a1de5be90

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Bench or experimentalTheoretical or conceptualNot applicable
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Codex

Bench or experimental0.970
Other design0.028
Theoretical or conceptual0.009
Observational0.004
Not applicable0.003
Open science0.001
Metaresearch0.000
Scholarly communication0.000
Bibliometrics0.000
Research integrity0.000
Simulation or modelling0.000
Science and technology studies0.000
Randomized trial0.000
Meta-epidemiology (narrow)0.000
Case report0.000
Qualitative0.000
Meta-epidemiology (broad)0.000
Non-randomized trial0.000
Systematic review0.000
Meta-analysis0.000

Gemma

Bench or experimental0.993
Not applicable0.115
Theoretical or conceptual0.019
Observational0.001
Research integrity0.000
Metaresearch0.000
Simulation or modelling0.000
Open science0.000
Science and technology studies0.000
Bibliometrics0.000
Non-randomized trial0.000
Case report0.000
Qualitative0.000
Meta-epidemiology (narrow)0.000
Meta-epidemiology (broad)0.000
Randomized trial0.000
Scholarly communication0.000
Systematic review0.000
Meta-analysis0.000

Machine scores (provisional)

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

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Opus teacher head0.005
GPT teacher head0.262
Teacher spread
0.257 how far apart the two teachers sit on this one work
Validation status
score_only:v0-immature-baseline verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Abstract

N(6)-methyladenosine (m(6)A) is the most abundant internal modification of nearly all eukaryotic mRNAs and has recently been reported to be recognized by the YTH domain family proteins. Here we present the crystal structures of the YTH domain of YTHDC1, a member of the YTH domain family, and its complex with an m(6)A-containing RNA. Our structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m(6)A-YTH binding but also explain the preferential recognition of the GG(m(6)A)C sequences by YTHDC1.

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