Evidence map›Paper›PMID 33047860›Full record

ArticleAngewandte Chemie (International ed. in English)2021

One-Step Azolation Strategy for Site- and Chemo-Selective Labeling of Proteins with Mass-Sensitive Probes.

Kuei C Tang, Monika Raj

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. 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

2 authors.

Kuei C TangPresent address: Department of Chemistry, Emory University, Atlanta, GA, 30322, USA.ORCID 0000-0001-7733-6504
Monika RajPresent address: Department of Chemistry, Emory University, Atlanta, GA, 30322, USA.ORCID 0000-0002-9499-5947

Funding

Molecular Imaging Agents for Monitoring Lysine Demethylases in CellsR35GM133719 · NIGMS · EMORY UNIVERSITY · PI RAJ, MONIKA · 2019 to 2023
$2.1M
NIGMS NIH HHS 1R35GM133719-01NIGMS NIH HHS R35 GM133719
6 · The paper itself

Abstract

The chemical modification of proteins in a site-selective manner leads to many advances in various scientific fields. The major challenges with conventional N-terminal bioconjugation techniques are the lack of universal sequence compatibility and poor mass-detection sensitivity of the resulting bioconjugates. This approach efficiently analyzes proteolytic fragments and native proteins in a complex mixture. Multiple chemical steps are usually required for the site-selective synthesis of bioconjugates with enhanced mass-detection sensitivity. We present a single-step, versatile strategy for the selective modification of protein N-termini with mass boosters. The chemical tag enhances the peptide detection by multiple orders thus leading to the unambiguous analysis of the resulting bioconjugates. We demonstrate that tagging proteolytic fragments with mass sensitivity probes in a complex mixture improves the detection of resulting bioconjugates.

Indexed as

Amino Acid SequenceAzolesChromatography, High Pressure LiquidMolecular ProbesMyoglobinTandem Mass SpectrometryAzolesMolecular ProbesMyoglobinchemoselectivemass sensitivityN-terminal labelingoxazolationsite-selective

Identifiers

PMID33047860
PMCPMC10111340

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Registered trials

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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.