Evidence map›Paper›PMID 23913257›Full record

ArticleNature methods2013

Adding an unnatural covalent bond to proteins through proximity-enhanced bioreactivity.

Zheng Xiang, Haiyan Ren, Ying S Hu, Irene Coin, Jing Wei, Hu Cang, Lei Wang

Erratum issuedAbstract read
In one paragraph

Article in Nature methods, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing 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

81 citing papers in PubMed.

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21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors.

Zheng XiangThe Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies, La Jolla, California, USA.
Haiyan Ren
Ying S Hu
Irene Coin
Jing Wei
Hu Cang
Lei Wang

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Ye Zheng · 1985 to 2026
$82.8M
Genetically Encoding Novel Amino Acids to Investigate Wnt Signaling in C. elegansDP2OD004744 · OD · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI WANG, LEI · 2008 to 2009
$3.0M
NCI NIH HHS P30 CA014195NCI NIH HHS P30CA014195NIH HHS 1DP2OD004744-01NIH HHS DP2 OD004744
6 · The paper itself

Abstract

Natural proteins often rely on the disulfide bond to covalently link side chains. Here we genetically introduce a new type of covalent bond into proteins by enabling an unnatural amino acid to react with a proximal cysteine. We demonstrate the utility of this bond for enabling irreversible binding between an affibody and its protein substrate, capturing peptide-protein interactions in mammalian cells, and improving the photon output of fluorescent proteins.

Indexed as

Amino Acid SequenceAmino Acyl-tRNA SynthetasesAnimalsCRF Receptor, Type 1CysteineCysteine EndopeptidasesEscherichia coliFluorescenceMolecular Sequence DataMutationPhenylalaninePhotonsProtein ConformationProtein EngineeringProteinsRatsAmino Acyl-tRNA SynthetasesCRF Receptor, Type 1CysteineCysteine EndopeptidasesPhenylalanineProteinsReceptors, Corticotropin-Releasing HormoneRecombinant Proteins

Identifiers

PMID23913257
PMCPMC3882359

What OpenQuestion holds

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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.