We are analyzing https://link.springer.com/article/10.1007/s00044-024-03342-9.

Title:
Targeting RNA-protein interactions with small molecules: promise and therapeutic potential | Medicinal Chemistry Research
Description:
The therapeutic potential of targeting protein-RNA interactions has not been fully explored. While several approaches to block the interactions between various RNA and protein partners have been developed, rational efforts to target pre-assembled complexes have not been broadly pursued. This is despite the recent commercial success of risdiplam, and the high-resolution structure of the EIF4A-polypurine-Rocaglamide A ternary complex, which elucidates how compounds may recognize these pockets. These prominent examples indicate the viability of this approach, but important questions remain. For example, how abundant are these pockets in other protein-RNA complexes? Do such pockets have properties suitable for small molecule recognition? A broad analysis of 160 previously published RNP complexes confirmed that interfacial pockets in RNA-protein complexes are both abundant and have favorable properties that would make them good candidates for rational screening campaigns. These conclusions are expected to have important implications especially for those working on developing small molecules that bind directly to RNA structural elements.
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Keywords {🔍}

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Topics {✒️}

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Questions {❓}

For example, how abundant are these pockets in other protein-RNA complexes?

Schema {🗺️}

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         headline:Targeting RNA-protein interactions with small molecules: promise and therapeutic potential
         description:The therapeutic potential of targeting protein-RNA interactions has not been fully explored. While several approaches to block the interactions between various RNA and protein partners have been developed, rational efforts to target pre-assembled complexes have not been broadly pursued. This is despite the recent commercial success of risdiplam, and the high-resolution structure of the EIF4A-polypurine-Rocaglamide A ternary complex, which elucidates how compounds may recognize these pockets. These prominent examples indicate the viability of this approach, but important questions remain. For example, how abundant are these pockets in other protein-RNA complexes? Do such pockets have properties suitable for small molecule recognition? A broad analysis of 160 previously published RNP complexes confirmed that interfacial pockets in RNA-protein complexes are both abundant and have favorable properties that would make them good candidates for rational screening campaigns. These conclusions are expected to have important implications especially for those working on developing small molecules that bind directly to RNA structural elements.
         datePublished:2024-11-23T00:00:00Z
         dateModified:2024-11-23T00:00:00Z
         pageStart:2050
         pageEnd:2065
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      description:The therapeutic potential of targeting protein-RNA interactions has not been fully explored. While several approaches to block the interactions between various RNA and protein partners have been developed, rational efforts to target pre-assembled complexes have not been broadly pursued. This is despite the recent commercial success of risdiplam, and the high-resolution structure of the EIF4A-polypurine-Rocaglamide A ternary complex, which elucidates how compounds may recognize these pockets. These prominent examples indicate the viability of this approach, but important questions remain. For example, how abundant are these pockets in other protein-RNA complexes? Do such pockets have properties suitable for small molecule recognition? A broad analysis of 160 previously published RNP complexes confirmed that interfacial pockets in RNA-protein complexes are both abundant and have favorable properties that would make them good candidates for rational screening campaigns. These conclusions are expected to have important implications especially for those working on developing small molecules that bind directly to RNA structural elements.
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         RNA
         RNA-protein interactions
         Medicinal chemistry
         Chemical biology
         Pharmacology/Toxicology
         Biochemistry
         general
         Medicinal Chemistry
         Bioorganic Chemistry
         Inorganic Chemistry
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               type:PostalAddress
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      affiliation:
            name:National Cancer Institute
            address:
               name:Chemical Biology Laboratory, National Cancer Institute, Frederick, USA
               type:PostalAddress
            type:Organization
      name:Kamyar Yazdani
      affiliation:
            name:National Cancer Institute
            address:
               name:Chemical Biology Laboratory, National Cancer Institute, Frederick, USA
               type:PostalAddress
            type:Organization
      name:Srinath Seshadri
      affiliation:
            name:National Cancer Institute
            address:
               name:Chemical Biology Laboratory, National Cancer Institute, Frederick, USA
               type:PostalAddress
            type:Organization
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      affiliation:
            name:National Cancer Institute
            address:
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               type:PostalAddress
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      name:Chemical Biology Laboratory, National Cancer Institute, Frederick, USA
      name:Chemical Biology Laboratory, National Cancer Institute, Frederick, USA
      name:Chemical Biology Laboratory, National Cancer Institute, Frederick, USA

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