Evidence map›Paper›PMID 40954389›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2025

Detection of a clamp-shaped conformation of a neuronal nitric oxide synthase construct by pulsed EPR.

Andrei V Astashkin, Yadav Prasad Gyawali, Ting Jiang, Huayu Zheng, Changjian Feng

Abstract read
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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

5 authors.

Andrei V AstashkinDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, 85721, USA.
Yadav Prasad GyawaliCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Ting JiangCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Huayu ZhengCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA.
Changjian FengCollege of Pharmacy, University of New Mexico, Albuquerque, NM, 87131, USA. cfeng@unm.edu.

Funding

University of New Mexico Center for Metals in Biology and Medicine - equipment supplementP20GM130422 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Sebastian Medina · 2020 to 2026
$20.4M
Pilot Project CoreP30ES032755 · NIEHS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI FENG, CHANGJIAN (JIM) · 2022 to 2025
$5.2M
Defining the conformational control of nitric oxide synthases by a multipronged approachR01GM133973 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI FENG, CHANGJIAN · 2020 to 2023
$1.5M
Defining Functional Dynamics of Multidomain Redox EnzymesR35GM156443 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Changjian (Jim) Feng · 2025 to 2026
$839k
Directorate for Biological Sciences 2041692NIEHS NIH HHS P30 ES032755NIGMS NIH HHS P20 GM130422NIGMS NIH HHS R01 GM133973NIGMS NIH HHS R35 GM156443NIH HHS P20GM130422
6 · The paper itself

Abstract

Nitric oxide synthase (NOS) is an enzyme responsible for the production of nitric oxide in living organisms. Structurally, it is a homodimer composed of multiple domains connected by random coil tethers. The resulting structural flexibility, along with the diverse conformational states it enables, is essential for NOS function and remains an active area of investigations. Here, we studied the docking interactions between the reductase domains of NOS subunits. To probe these interactions, a nitroxide-based bifunctional spin label was attached to each T34C/S38C calmodulin (CaM) molecule bound to the CaM-binding region of the tether, which connects the oxygenase and flavin mononucleotide (FMN) domains in each subunit of the homodimeric oxygenase/FMN (oxyFMN) construct of rat neuronal NOS (nNOS). The magnetic dipole interaction between the spin labels was detected by 2 + 1 electron spin echo (ESE) methods. The experimental 2 + 1 ESE traces were interpreted using the Monte Carlo calculations of NOS conformational distributions. The results unequivocally show that at the estimated effective temperature of the frozen conformational distribution, T

Indexed as

Nitric Oxide Synthase Type IAnimalsCalmodulinElectron Spin Resonance SpectroscopyFlavin MononucleotideProtein ConformationRatsSpin LabelsCalmodulinFlavin MononucleotideNitric Oxide Synthase Type INos1 protein, ratSpin LabelsCalmodulinConformational dynamicsKeywordsMonte Carlo calculationNitric oxide synthasePulsed EPRSpin label

Identifiers

PMID40954389
PMCPMC12746763

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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.