ArticleMolecular biotechnology2026
Toward the Development of a Biosimilar Variant of Glucarpidase (Carboxypeptidase G2): Secretory Production, Optimization, and Immobilization.
Article in Molecular biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Non-Covalent Active Mixing as a Viable Alternative to Covalent Conjugation for the Intracellular Delivery of Biologics: The Case of Glucarpidase.Applied biochemistry and biotechnology · 2026Article
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.
Funding
Abstract
Carboxypeptidase G2 (CPG2) detoxifies high-dose methotrexate in cancer or autoimmune therapies. Additionally, CPG2 activates prodrugs at the tumor site in engineered CAR-T cell therapy. Since CPG2 cleaves glutamate from the substrate, it also has potential applications in enhancing food flavors and developing biosensors. However, cytoplasmic expression of recombinant CPG2 often leads to inclusion body formation, necessitating secretory production to improve product quality and streamline downstream industrial processes. This study aimed to perform a comprehensive in silico analysis to identify an optimal signal peptide for CPG2 secretion. The pelB leader sequence was selected for excretory production using the pET22b vector in Escherichia coli. The enzyme was successfully secreted into both the periplasmic space of bacterial cells and the culture medium with activities of about 0.038 UmL
Indexed as
Identifiers
40465023What OpenQuestion holds
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.