Evidence map›Paper›PMID 24959531›Full record

ReviewFrontiers in chemistry2014

Non-standard amino acid incorporation into proteins using Escherichia coli cell-free protein synthesis.

Seok Hoon Hong, Yong-Chan Kwon, Michael C Jewett

Abstract readReview
In one paragraph

Review in Frontiers in chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Engineered mRNA-ribosome fusions for facile biosynthesis of selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Applications of synthetic biology in medical and pharmaceutical fields.Signal transduction and targeted therapy · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Simple Extract Preparation Methods for E. coli-Based Cell-Free Expression.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Additive CHARMM36 Force Field for Nonstandard Amino Acids.Journal of chemical theory and computation · 2021
    Article
  16. Review
  17. Review
  18. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Seok Hoon HongChemical and Biological Engineering, Northwestern University Evanston, IL, USA ; Chemistry of Life Processes Institute, Northwestern University Evanston, IL, USA.
Yong-Chan KwonChemical and Biological Engineering, Northwestern University Evanston, IL, USA ; Chemistry of Life Processes Institute, Northwestern University Evanston, IL, USA.
Michael C JewettChemical and Biological Engineering, Northwestern University Evanston, IL, USA ; Chemistry of Life Processes Institute, Northwestern University Evanston, IL, USA ; Robert H. Lurie Comprehensive Cancer Center, Northwestern University Chicago, IL, USA ; Institute of Bionanotechnology in Medicine, Northwestern University Chicago, IL, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Incorporating non-standard amino acids (NSAAs) into proteins enables new chemical properties, new structures, and new functions. In recent years, improvements in cell-free protein synthesis (CFPS) systems have opened the way to accurate and efficient incorporation of NSAAs into proteins. The driving force behind this development has been three-fold. First, a technical renaissance has enabled high-yielding (>1 g/L) and long-lasting (>10 h in batch operation) CFPS in systems derived from Escherichia coli. Second, the efficiency of orthogonal translation systems (OTSs) has improved. Third, the open nature of the CFPS platform has brought about an unprecedented level of control and freedom of design. Here, we review recent developments in CFPS platforms designed to precisely incorporate NSAAs. In the coming years, we anticipate that CFPS systems will impact efforts to elucidate structure/function relationships of proteins and to make biomaterials and sequence-defined biopolymers for medical and industrial applications.

Indexed as

cell-free protein synthesisgenome engineeringnon-standard amino acidssequence-defined polymerssynthetic biology

Identifiers

PMID24959531
PMCPMC4050362

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.