Evidence map›Paper›PMID 34349951›Full record

ArticleChemical science2021

Diverse protein manipulations with genetically encoded glutamic acid benzyl ester.

Xiaochen Yang, Hui Miao, Ruotong Xiao, Luyao Wang, Yan Zhao, Qifan Wu, Yanli Ji, Juanjuan Du, Hongqiang Qin, Weimin Xuan

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 24% of its field
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

4 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
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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

10 authors at 3 institutions in 2 countries.

Xiaochen YangState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University Tianjin 300071 China wxuan@nankai.edu.cn.
Hui MiaoState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University Tianjin 300071 China wxuan@nankai.edu.cn.
Ruotong XiaoState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University Tianjin 300071 China wxuan@nankai.edu.cn.
Luyao WangSchool of Pharmaceutical Sciences, Tsinghua University 30 Shuangqing Rd. Beijing China.
Yan ZhaoSchool of Pharmaceutical Sciences, Tsinghua University 30 Shuangqing Rd. Beijing China.
Qifan WuState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University Tianjin 300071 China wxuan@nankai.edu.cn.ORCID https://orcid.org/0000-0002-6490-2180
Yanli JiState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University Tianjin 300071 China wxuan@nankai.edu.cn.
Juanjuan DuSchool of Pharmaceutical Sciences, Tsinghua University 30 Shuangqing Rd. Beijing China.
Hongqiang QinCAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences (CAS) Dalian, 116023 China.
Weimin XuanState Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University Tianjin 300071 China wxuan@nankai.edu.cn.ORCID https://orcid.org/0000-0001-9390-9923
Nankai University · CNTsinghua University · CNDalian Institute of Chemical Physics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Site-specific modification of proteins has significantly advanced the use of proteins in biological research and therapeutics development. Among various strategies aimed at this end, genetic code expansion (GCE) allows structurally and functionally distinct non-canonical amino acids (ncAAs) to be incorporated into specific sites of a protein. Herein, we genetically encode an esterified glutamic acid analogue (BnE) into proteins, and demonstrate that BnE can be applied in different types of site-specific protein modifications, including N-terminal pyroglutamation, caging Glu in the active site of a toxic protein, and endowing proteins with metal chelator hydroxamic acid and versatile reactive handle acyl hydrazide. Importantly, novel epigenetic mark Gln methylation is generated on histones

Identifiers

PMID34349951
PMCPMC8299518
OpenAlexW3173552891

What OpenQuestion holds

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LicenceCC BY-NC
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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.