Mapping close RNA–protein contacts by crosslinking, immunoprecipitation of a selected protein and analysis of attached RNA fragments. Input abundance, antibody specificity and crosslinking bias constrain the interpretation of an apparent binding peak.
Sequencing-based mapping after crosslinking and immunoprecipitation. Stabilizing RNA–protein contacts before isolation can improve positional evidence, while crosslinking and recovery biases affect which interactions are observed.
A crosslinking approach using photoactivatable nucleoside analogues to mark RNA–protein contacts. Characteristic sequence changes help localize contacts, connecting chemical labeling with transcriptome-wide binding maps.[ref]
An enhanced crosslinking-and-immunoprecipitation method for mapping RNA-binding protein contacts. Its controls and library design improve interpretation of enriched sites, without making every recovered sequence a functional regulatory target.[ref]
An individual-nucleotide-resolution crosslinking-and-immunoprecipitation method. Recovering information from reverse-transcription termination helps locate RNA–protein contacts, linking a biochemical event with a sequence position.[ref]

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