Evidence map›Paper›PMID 33817510›Full record

ArticleACS omega2021

Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface.

Matthew J McKay, Kelsey A Marr, Jake R Price, Denise V Greathouse, Roger E Koeppe

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

5 authors at 1 institution in 1 country.

Matthew J McKayDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, United States.
Kelsey A MarrDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, United States.
Jake R PriceDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, United States.
Denise V GreathouseDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, United States.
Roger E KoeppeDepartment of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, United States.
University of Arkansas at Fayetteville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ionization properties of protein side chains in lipid-bilayer membranes will differ from the canonical values of side chains exposed to an aqueous solution. While the propensities of positively charged side chains of His, Lys, and Arg to release a proton in lipid membranes have been rather well characterized, the propensity for a negatively charged Glu side chain to receive a proton and achieve the neutral state in a bilayer membrane has been less well characterized. Indeed, the ionization of the glutamic acid side chain has been predicted to depend on its depth of burial in a lipid membrane but has been difficult to verify experimentally. To address the issue, we incorporated an interfacial Glu residue at position 4 of a distinct 23-residue transmembrane helix and used

Identifiers

PMID33817510
PMCPMC8015139
OpenAlexW3139115415

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.