ArticleBioconjugate chemistry2018
Tailored Polyproteins Using Sequential Staple and Cut.
Article in Bioconjugate chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025Article
- Enzymatic Protein Immobilization on Amino-Functionalized Nanoparticles.Molecules (Basel, Switzerland) · 2023Article
- One-step asparaginyl endopeptidase (RSC chemical biology · 2022Article
- Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin.International journal of molecular sciences · 2022Article
- Designing Functional Bionanoconstructs for EffectiveBioconjugate chemistry · 2022Review
- Designed protein multimerization and polymerization for functionalization of proteins.Biotechnology letters · 2022Review
- Facile Synthesis of Peptide-Conjugated Gold Nanoclusters with Different Lengths.Nanomaterials (Basel, Switzerland) · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Structural basis of the strong cell-cell junction formed by cadherin-23.The FEBS journal · 2019Article
- Enzymatic biosynthesis and immobilization of polyprotein verified at the single-molecule level.Nature communications · 2019Article
- Broadening the scope of sortagging.RSC advances · 2019Review
- Recent progress in enzymatic protein labelling techniques and their applications.Chemical Society reviews · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Polyproteins, individual protein units joined covalently in tandem, have evolved as a promising tool for measuring the dynamic folding of biomacromolecules in single-molecule force spectroscopy. However, the synthetic routes to prepare polyproteins have been a bottleneck, and urge development of in vitro methods to knit individual protein units covalently into polyprotein. Employing two enzymes of orthogonal functionalities periodically in sequence, we synthesized monodispersed polyproteins on a solid surface. We used Sortase A (SrtA), the enzyme known for sequence specific transpeptidation, to staple protein units covalently through peptide bonds. Exploiting the sequence-specific peptide cleaving ability of TEV protease, we controlled the progress of the reaction to one attachment at a time. Finally, with unique design of the unit proteins we control the orientation of proteins in polyprotein. This simple conjugation has the potential to staple proteins with different functionalities and from different expression systems, in any number in the polyprotein and, above all, via irreversible peptide bonds. Multiple chimeric constructs can also be synthesized with interchangeable protein units.
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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.