ReviewNew biotechnology2017
Genetically encoding new bioreactivity.
Review in New biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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
45 citing papers in PubMed.
- Self-cleavage of the GAIN domain of adhesion G protein-coupled receptors requires multiple domain-extrinsic factors.Nature communications · 2025Article
- Genetic Code Expansion Approaches to Decipher the Ubiquitin Code.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Biospecific Chemistry for Covalent Linking of Biomacromolecules.Chemical reviews · 2024Review
- Advancing protein therapeutics through proximity-induced chemistry.Cell chemical biology · 2024Review
- Advances in Biosynthesis of Non-Canonical Amino Acids (ncAAs) and the Methods of ncAAs Incorporation into Proteins.Molecules (Basel, Switzerland) · 2023Review
- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Covalent Proteins as Targeted Radionuclide Therapies Enhance Antitumor Effects.ACS central science · 2023Article
- Residue selective crosslinking of proteins through photoactivatable or proximity-enabled reactivity.Current opinion in chemical biology · 2023Review
- Proximity-enhanced protein crosslinking through an alkene-tetrazine reaction.Bioorganic chemistry · 2023Article
- Orthogonal Crosslinking: A Strategy to Generate Novel Protein Topology and Function.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Genetically encoded chemical crosslinking of RNA in vivo.Nature chemistry · 2023Article
- Genetically encoded chemical crosslinking of carbohydrate.Nature chemistry · 2023Article
- Capture and mass spectrometry analysis of effector-substrate complexes using genetically incorporated photo-crosslinkers in host cells.STAR protocols · 2022Article
- Article
- Encoding latent SuFEx reactive meta-fluorosulfate tyrosine to expand covalent bonding of proteins.Chemical communications (Cambridge, England) · 2022Article
- Toward efficient multiple-site incorporation of unnatural amino acids using cell-free translation system.Synthetic and systems biotechnology · 2022Article
- New covalent bonding ability for proteins.Protein science : a publication of the Protein Society · 2022Review
- Genetic-code-expanded cell-based therapy for treating diabetes in mice.Nature chemical biology · 2022Article
- Uncover New Reactivity of Genetically Encoded Alkyl Bromide Non-Canonical Amino Acids.Frontiers in chemistry · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
The genetic code can be expanded to include unnatural amino acids (Uaas) by engineering orthogonal components involved in protein translation. To be compatible with live cells, side chains of Uaas have been limited to either chemically inert or bio-orthogonal (i.e., nonreactive toward biomolecules) functionalities. To introduce bioreactivity into live systems, the genetic code has recently been engineered to encode a new class of Uaas, the bioreactive Uaas. These Uaas, after being incorporated into proteins, specifically react with target natural amino acid residues via proximity-enabled bioreactivity, enabling the selective formation of new covalent linkages within and between proteins both in vitro and in live systems. The new covalent bonding ability has been harnessed within proteins to enhance photostability, increase thermostability, staple proteins recombinantly, and build optical nano-switches, and between proteins to pinpoint ligand-receptor interaction, target native receptors irreversibly, and generate covalent macromolecular inhibitors. These diverse bioreactivities, inaccessible to natural proteins, thus open doors to novel protein engineering and provide new avenues for biological studies, biotherapeutics and synthetic biology.
Indexed as
Identifiers
What 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.