ArticleScientific reports2017
Modulation of the Vault Protein-Protein Interaction for Tuning of Molecular Release.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- In Vitro Refolding of Vault-like Protein Nanocapsules with a Novel Scaffolding Mechanism.International journal of molecular sciences · 2025Article
- Structural insights into the roles of PARP4 and NADNature communications · 2025Article
- PARP4 interacts with hnRNPM to regulate splicing during lung cancer progression.Genome medicine · 2024Article
- An Efficient Method for Vault Nanoparticle Conjugation with Finely Adjustable Amounts of Antibodies and Small Molecules.International journal of molecular sciences · 2024Article
- Structure, Dynamics and Functional Implications of the Eukaryotic Vault Complex.Sub-cellular biochemistry · 2024Review
- Manufacturing of non-viral protein nanocages for biotechnological and biomedical applications.Frontiers in bioengineering and biotechnology · 2023Review
- Self-assembled peptide and protein nanostructures for anti-cancer therapy: Targeted delivery, stimuli-responsive devices and immunotherapy.Nano today · 2021Article
- Review
- Mutation-independent Proteomic Signatures of Pathological Progression in Murine Models of Duchenne Muscular Dystrophy.Molecular & cellular proteomics : MCP · 2020Article
- Bioengineered recombinant vault nanoparticles coupled with NY-ESO-1 glioma-associated antigens induce maturation of native dendritic cells.Journal of neuro-oncology · 2020Article
- Latest Advances in the Development of Eukaryotic Vaults as Targeted Drug Delivery Systems.Pharmaceutics · 2019Review
- Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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 substituted at the interaction surface (INT/DSA/3 H) to impart a pH-sensitive response. The apparent affinity constants determined using surface plasmon resonance (SPR) biosensor technology are 262 ± 4 nM for iMVP/INT, 1800 ± 160 nM for iMVP/INTΔC15 at pH 7.4. The INT/DSA/3 H exhibits stronger affinity to iMVP (K
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.