Evidence map›Paper›PMID 27813296›Full record

ArticleProtein science : a publication of the Protein Society2017

Simple method to introduce an ester infrared probe into proteins.

Ismail A Ahmed, Feng Gai

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. 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
0.5field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Site-Specific Interrogation of Protein Structure and Stability.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  4. Article
  5. 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

2 authors at 1 institution in 1 country.

Ismail A AhmedDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania, 19104.
Feng GaiDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, 19104.
University of Pennsylvania · US

Funding

Multidisciplinary Training in Cardiovascular BiologyT32HL007954 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI DAVIES, PETER FRANCIS · 2000 to 2019
$9.9M
ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
NHLBI NIH HHS T32 HL007954NIGMS NIH HHS P41 GM104605
6 · The paper itself

Abstract

The ester carbonyl stretching vibration has recently been shown to be a sensitive and convenient infrared (IR) probe of protein electrostatics due to the linear dependence of its frequency on local electric field. While an ester moiety can be easily incorporated into peptides via solid-phase synthesis, currently there is no method available to site-specifically incorporate it into a large protein. Herein, we show that it is possible to use a cysteine alkylation reaction to achieve this goal and demonstrate the feasibility of this simple method by successfully incorporating a methyl ester group (CH

Indexed as

Amyloid beta-PeptidesAnimalsCattleHumansInsulinMolecular ProbesSerum Albumin, BovineSpectrophotometry, InfraredAmyloid beta-PeptidesInsulinMolecular ProbesSerum Albumin, Bovineamyloidbovine serum albumincysteine alkylationinfrared probeprotein hydrationprotein modification

Identifiers

PMID27813296
PMCPMC5275736
OpenAlexW2547939282

What OpenQuestion holds

Textmetadata
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.