Evidence map›Paper›PMID 41719409›Full record

ArticleScience advances2026

Structure and dynamics of a multidomain nitric oxide synthase regulated by a C2 domain.

Dhruva Nair, Brian R Crane

Abstract read
In one paragraph

Article in Science advances, 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

2 authors.

Dhruva NairWeill Institute for Cell and Molecular Biology, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Brian R CraneWeill Institute for Cell and Molecular Biology, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0001-8234-9991

Funding

Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
Acquisition of a Hybrid Quadrupole Time of Flight LC-MS/MS System for the CornellS10OD017992 · OD · CORNELL UNIVERSITY · PI ZHANG, SHENG · 2014 to 2014
$600k
NIGMS NIH HHS P30 GM124166NIH HHS S10 OD017992
6 · The paper itself

Abstract

Nitric oxide synthase (NOS) is a widely studied multidomain redox enzyme that produces the key signaling molecule and cytotoxic agent nitric oxide (NO) for functions that range from mammalian vasodilation to prokaryotic antibiotic resistance. NOS enzymes from metazoans and cyanobacteria rely on dynamic associations of their oxygenase and coupled diflavin reductase domains that have largely evaded detailed structural characterization. Cryo-electron microscopy studies of a representative dimeric six-domain

Indexed as

Nitric Oxide SynthaseSynechococcusCryoelectron MicroscopyHemeModels, MolecularProtein ConformationProtein DomainsHemeNitric Oxide Synthase

Identifiers

PMID41719409
PMCPMC12922734

What OpenQuestion holds

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LicenceCC BY
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.