{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Terasawa K"],"funding":["Research Support Project for Life Science and Drug Discovery (Basis for Supporting Innovative Drug Discovery and Life Science Research [(BINDS])","MEXT program","Grants-in-Aid for Scientific Research","Grants-in-Aids for Scientific","Japan Agency for Medical Research and Development","Establishment of University Fellowships towards the Creation of Science Technology Innovation"],"pagination":["e4823"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10659947"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(12)"],"pubmed_abstract":["Genetic code expansion enables site-specific photo-crosslinking by introducing photo-reactive non-canonical amino acids into proteins at defined positions during translation. This technology is widely used for analyzing protein-protein interactions and is applicable in mammalian cells. However, the identification of the crosslinked region still remains challenging. Here, we developed a new method to identify the crosslinked region by pre-installing a site-specific cleavage site, an α-hydroxy acid (N<sup>ε</sup> -allyloxycarbonyl-α-hydroxyl-l-lysine acid, AllocLys-OH), into the target protein. Alkaline treatment cleaves the crosslinked complex at the position of the α-hydroxy acid residue and thus helps to identify which side of the cleavage site, either closer to the N-terminus or C-termin"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Site-specific photo-crosslinking/cleavage for protein-protein interface identification reveals oligomeric assembly of lysosomal-associated membrane protein type 2A in mammalian cells."],"pmcid":["PMC10659947"],"funding_grant_id":["JP17K12005","JP21K10063","JPMJFS2109","JP23ama121027"],"pubmed_authors":["Iwata T","Yokoyama S","Terasawa K","Sakamoto K","Terada T","Watabe T","Ohtake K","Seike T","Hara-Yokoyama M"],"additional_accession":[]},"is_claimable":false,"name":"Site-specific photo-crosslinking/cleavage for protein-protein interface identification reveals oligomeric assembly of lysosomal-associated membrane protein type 2A in mammalian cells.","description":"Genetic code expansion enables site-specific photo-crosslinking by introducing photo-reactive non-canonical amino acids into proteins at defined positions during translation. This technology is widely used for analyzing protein-protein interactions and is applicable in mammalian cells. However, the identification of the crosslinked region still remains challenging. Here, we developed a new method to identify the crosslinked region by pre-installing a site-specific cleavage site, an α-hydroxy acid (N<sup>ε</sup> -allyloxycarbonyl-α-hydroxyl-l-lysine acid, AllocLys-OH), into the target protein. Alkaline treatment cleaves the crosslinked complex at the position of the α-hydroxy acid residue and thus helps to identify which side of the cleavage site, either closer to the N-terminus or C-termin","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2026-06-27T03:13:22.483Z","creation":"2025-04-04T09:39:32.329Z"},"accession":"S-EPMC10659947","cross_references":{"pubmed":["37906694"],"doi":["10.1002/pro.4823"]}}