{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Whitley JA"],"funding":["NEI NIH HHS","NIAID NIH HHS","NCI NIH HHS"],"pagination":["e12196"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8982324"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(4)"],"pubmed_abstract":["CRISPR/Cas9 genome editing is a very promising avenue for the treatment of a variety of genetic diseases. However, it is still very challenging to encapsulate CRISPR/Cas9 machinery for delivery. Protein N-myristoylation is an irreversible co/post-translational modification that results in the covalent attachment of the myristoyl-group to the N-terminus of a target protein. It serves as an anchor for a protein to associate with the cell membrane and determines its intracellular trafficking and activity. Extracellular vesicles (EVs) are secreted vesicles that mediate cell-cell communication. In this study, we demonstrate that myristoylated proteins were preferentially encapsulated into EVs. The octapeptide derived from the leading sequence of the N-terminus of Src kinase was a favourable sub"],"journal":["Journal of extracellular vesicles"],"pubmed_title":["Encapsulating Cas9 into extracellular vesicles by protein myristoylation."],"pmcid":["PMC8982324"],"funding_grant_id":["R21 EY028671","R01 EY031748","P30 EY005722","R21 AI171944","R21 AI157831","U01 CA225784"],"pubmed_authors":["Desrochers EG","Xie ZR","Ye C","Alsaidan OA","Sulejmani E","Cai J","Cai H","Kim S","Whitley JA","Liu Y","Beharry Z","Klingeborn M","Rickman CB","Lou L"],"additional_accession":[]},"is_claimable":false,"name":"Encapsulating Cas9 into extracellular vesicles by protein myristoylation.","description":"CRISPR/Cas9 genome editing is a very promising avenue for the treatment of a variety of genetic diseases. However, it is still very challenging to encapsulate CRISPR/Cas9 machinery for delivery. Protein N-myristoylation is an irreversible co/post-translational modification that results in the covalent attachment of the myristoyl-group to the N-terminus of a target protein. It serves as an anchor for a protein to associate with the cell membrane and determines its intracellular trafficking and activity. Extracellular vesicles (EVs) are secreted vesicles that mediate cell-cell communication. In this study, we demonstrate that myristoylated proteins were preferentially encapsulated into EVs. The octapeptide derived from the leading sequence of the N-terminus of Src kinase was a favourable sub","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-09T19:22:27.12Z","creation":"2025-04-06T03:58:39.81Z"},"accession":"S-EPMC8982324","cross_references":{"pubmed":["35384352"],"doi":["10.1002/jev2.12196"]}}