Evidence map›Paper›PMID 41552541›Full record

ArticleACS omega2026

Glutamine Substitution at Lysine

Mohammad Masood, Shadab Khan, Daraksha Yameen, Aleena Anwar, Faizya Khan, Saba Iqbal, Rupesh Chaturvedi, Anas Shamsi, Mohammad Mahfuzul Haque

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In one paragraph

Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Mohammad MasoodMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Shadab KhanMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Daraksha YameenMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Aleena AnwarMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Faizya KhanMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Saba IqbalMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.
Rupesh ChaturvediSchool of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India.
Anas ShamsiCentre for Medical and Bio-Allied Health Sciences Research, Ajman University, Ajman 346, United Arab Emirates.
Mohammad Mahfuzul HaqueMolecular Enzymology Laboratory, Department of Biotechnology, Jamia Millia Islamia, New Delhi 110025, India.ORCID https://orcid.org/0000-0003-0852-6368

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelial nitric oxide synthase (eNOS) is a critically important flavoheme enzyme that synthesizes nitric oxide (NO), a multifunctional signaling molecule essential to vascular homeostasis, immune modulation, and cardiovascular function. Post-translational modifications, such as acetylation, can affect eNOS activity by altering the charge state of lysine residues. However, we presently have little knowledge of how each lysine contributes to catalysis. In this study, we biochemically characterize two conserved lysine residues (Lys

Identifiers

PMID41552541
PMCPMC12809515

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.