{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(1)"],"submitter":["Yu K"],"pubmed_abstract":["Vaults are naturally occurring ovoid nanoparticles constructed from a protein shell that is composed of multiple copies of major vault protein (MVP). The vault-interacting domain of vault poly(ADP-ribose)-polymerase (INT) has been used as a shuttle to pack biomolecular cargo in the vault lumen. However, the interaction between INT and MVP is poorly understood. It is hypothesized that the release rate of biomolecular cargo from the vault lumen is related to the interaction between MVP and INT. To tune the release of molecular cargos from the vault nanoparticles, we determined the interactions between the isolated INT-interacting MVP domains (iMVP) and wild-type INT and compared them to two structurally modified INT: 15-amino acid deletion at the C terminus (INTΔC15) and histidine substitute"],"journal":["Scientific reports"],"pagination":["14816"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5665922"],"repository":["biostudies-literature"],"pubmed_title":["Modulation of the Vault Protein-Protein Interaction for Tuning of Molecular Release."],"pmcid":["PMC5665922"],"pubmed_authors":["Rome LH","Sinha A","Lim S","Tan T","Yau YH","Kickhoefer VA","Lee H","Yu K","Shochat SG"],"additional_accession":[]},"is_claimable":false,"name":"Modulation of the Vault Protein-Protein Interaction for Tuning of Molecular Release.","description":"Vaults are naturally occurring ovoid nanoparticles constructed from a protein shell that is composed of multiple copies of major vault protein (MVP). The vault-interacting domain of vault poly(ADP-ribose)-polymerase (INT) has been used as a shuttle to pack biomolecular cargo in the vault lumen. However, the interaction between INT and MVP is poorly understood. It is hypothesized that the release rate of biomolecular cargo from the vault lumen is related to the interaction between MVP and INT. To tune the release of molecular cargos from the vault nanoparticles, we determined the interactions between the isolated INT-interacting MVP domains (iMVP) and wild-type INT and compared them to two structurally modified INT: 15-amino acid deletion at the C terminus (INTΔC15) and histidine substitute","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Nov","modification":"2026-04-30T09:25:35.337Z","creation":"2019-03-27T03:00:36Z"},"accession":"S-EPMC5665922","cross_references":{"pubmed":["29093465"],"doi":["10.1038/s41598-017-12870-x"]}}