Evidence map›Paper›PMID 27797495›Full record

ArticleJournal of the American Chemical Society2016

Using Protein-Confined Proximity To Determine Chemical Reactivity.

Tomonori Kobayashi, Christian Hoppmann, Bing Yang, Lei Wang

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Shaping Antimalarials: A Geometry-First Approach toJournal of medicinal chemistry · 2026
    Article
  4. Recent advances in the expanding genetic code.Current opinion in chemical biology · 2024
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Genetically encoded crosslinkers to address protein-protein interactions.Protein science : a publication of the Protein Society · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. New covalent bonding ability for proteins.Protein science : a publication of the Protein Society · 2022
    Review
  18. Article
  19. Article
  20. Article
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

4 authors.

Tomonori KobayashiDepartment of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, San Francisco , 555 Mission Bay Boulevard South, San Francisco, California 94158, United States.
Christian HoppmannDepartment of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, San Francisco , 555 Mission Bay Boulevard South, San Francisco, California 94158, United States.
Bing YangDepartment of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, San Francisco , 555 Mission Bay Boulevard South, San Francisco, California 94158, United States.
Lei WangDepartment of Pharmaceutical Chemistry and the Cardiovascular Research Institute, University of California, San Francisco , 555 Mission Bay Boulevard South, San Francisco, California 94158, United States.

Funding

Adding New Covalent Bonds to Proteins in Live CellsR01GM118384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Lei Wang · 2016 to 2026
$3.0M
NIGMS NIH HHS R01 GM118384
6 · The paper itself

Abstract

Chemical reactivity is essential for functional modification of biomolecules with small molecules and the development of covalent drugs. The reactivity between a chemical functional group of a small molecule and that of a large biomolecule cannot be reliably predicted from the reactivity of the corresponding functional groups separately installed on two small molecules, because the proximity effect on reactivity resulting from the binding of the small molecule to the biomolecule is challenging to achieve by mixing two small molecules. Here we present a new strategy to determine the chemical reactivity of two functional groups in the context of close proximity afforded by proteins. The functional groups to be tested were separately installed at the interface of two interacting proteins in the format of amino acid side chains via the expansion of the genetic code. Reaction of the two functional groups resulted in covalent cross-linking of interacting proteins, readily detectable by gel electrophoresis. Using this strategy, we evolved new synthetases to genetically encode N

Indexed as

AcetylationAmino AcidsLigasesLysineMethanosarcinaMolecular ConformationAmino AcidsLigasesLysine

Identifiers

PMID27797495
PMCPMC5310709

What OpenQuestion holds

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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.