ArticlePloS one2013
An internal ribosome entry site (IRES) mutant library for tuning expression level of multiple genes in mammalian cells.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- IRES-Mediated Translation: Expanding the Toolkits of RNA Therapy.International journal of molecular sciences · 2025Review
- Structural and Functional Characterization of Anti-SARS-CoV-2 Spike Monoclonal Antibodies Produced via Bicistronic Expression in CHO Cells.Antibodies (Basel, Switzerland) · 2025Article
- Promoting the production of challenging proteins via induced expression in CHO cells and modified cell-free lysates harboring T7 RNA polymerase and mutant eIF2α.Synthetic and systems biotechnology · 2024Article
- SEMPER: Stoichiometric expression of mRNA polycistrons by eukaryotic ribosomes for compact, ratio-tunable multi-gene expression.Cell systems · 2024Article
- Near-Infrared Optogenetic Module for Conditional Protein Splicing.Journal of molecular biology · 2023Article
- Advancing personalized medicine in brain cancer: exploring the role of mRNA vaccines.Journal of translational medicine · 2023Review
- Compact Programmable Control of Protein Secretion in Mammalian Cells.bioRxiv : the preprint server for biology · 2023Article
- Optimizing effector functions of monoclonal antibodies via tailored N-glycan engineering using a dual landing pad CHO targeted integration platform.Scientific reports · 2023Article
- Reconstitution of Multi-Protein Complexes through Ribozyme-Assisted Polycistronic Co-Expression.ACS synthetic biology · 2023Article
- Vector design for enhancing expression level and assembly of knob-into-hole based FabscFv-Fc bispecific antibodies in CHO cells.Antibody therapeutics · 2022Article
- A Single Transcript Knockdown-Replacement Strategy Employing 5' UTR Secondary Structures to Precisely Titrate Rescue Protein Translation.Frontiers in genome editing · 2022Article
- Multiplexed engineering glycosyltransferase genes in CHO cells via targeted integration for producing antibodies with diverse complex-type N-glycans.Scientific reports · 2021Article
- Preparation, Assembly, and Transduction of Transgenic Elements Using Mosaic Analysis with Dual Recombinases (MADR).STAR protocols · 2020Article
- pHLuc, a Ratiometric Luminescent Reporter forFrontiers in bioengineering and biotechnology · 2020Article
- Mechanism of centromere recruitment of the CENP-A chaperone HJURP and its implications for centromere licensing.Nature communications · 2019Article
- Bicistronic Construct for Optogenetic Prosthesis of Ganglion Cell Receptive Field of Degenerative Retina.Doklady. Biochemistry and biophysics · 2019Article
- Programmable protein circuits in living cells.Science (New York, N.Y.) · 2018Article
- A bacterial phytochrome-based optogenetic system controllable with near-infrared light.Nature methods · 2016Article
- Balancing the Expression and Production of a Heterodimeric Protein: Recombinant Agkisacutacin as a Novel Antithrombotic Drug Candidate.Scientific reports · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A set of mutated Encephalomyocarditis virus (EMCV) internal ribosome entry site (IRES) elements with varying strengths is generated by mutating the translation initiation codons of 10(th), 11(th), and 12(th) AUG to non-AUG triplets. They are able to control the relative expression of multiple genes over a wide range in mammalian cells in both transient and stable transfections. The relative strength of each IRES mutant remains similar in different mammalian cell lines and is not gene specific. The expressed proteins have correct molecular weights. Optimization of light chain over heavy chain expression by these IRES mutants enhances monoclonal antibody expression level and quality in stable transfections. Uses of this set of IRES mutants can be extended to other applications such as synthetic biology, investigating interactions between proteins and its complexes, cell engineering, multi-subunit protein production, gene therapy, and reprogramming of somatic cells into stem cells.
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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.