Evidence map›Paper›PMID 32191483›Full record

ArticleOrganic letters2020

Highly Stable Meldrum's Acid Derivatives for Irreversible Aqueous Covalent Modification of Amines.

Garrett J Davis, Holly A Sofka, John C Jewett

Open access · greenAbstract read
In one paragraph

Article in Organic letters, 2020. 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
1.3field-weighted citation impact, top 23% 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.

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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

3 authors at 1 institution in 1 country.

Garrett J DavisDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721, United States.
Holly A SofkaDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721, United States.
John C JewettDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721, United States.ORCID 0000-0001-5822-4080
University of Arizona · US

Funding

CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008804 · NIGMS · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2003 to 2023
$3.9M
NIGMS NIH HHS T32 GM008804
6 · The paper itself

Abstract

This work describes the development of a highly stable and pH-responsive probe for lysine modification. The scaffold has marked stability in the presence of several biological nucleophiles and across a wide pH range (2-12). Several functional analogs showed robust labeling of a protein at pH > 9. Taken together, our system displays versatility and can be easily adapted for variety of applications, while demonstrating stability suitable for a wide range of biologically compatible systems.

Indexed as

AminesDioxanesHydrogen-Ion ConcentrationLysineMolecular StructureWaterAminesDioxanesLysineMeldrum's acidWater

Identifiers

PMID32191483
PMCPMC7679203
OpenAlexW3010811366

What OpenQuestion holds

Textmetadata
LicenceTDM
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.