Evidence map›Paper›PMID 26311846›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics.

Yufan He, Mohammad Mahfuzul Haque, Dennis J Stuehr, H Peter Lu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  3. Analyzing the FMN-heme interdomain docking interactions in neuronal and inducible NOS isoforms by pulsed EPR experiments and conformational distribution modeling.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
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  11. Review
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  14. Exploring the conformations of nitric oxide synthase with fluorescence.Frontiers in bioscience (Landmark edition) · 2018
    Review
  15. Review
  16. Article
  17. A cryptophane-based "turn-on"Organic & biomolecular chemistry · 2017
    Article
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  20. Review
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

4 authors at 2 institutions in 1 country.

Yufan HeCenter for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403;
Mohammad Mahfuzul HaqueDepartment of Pathobiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195.
Dennis J StuehrDepartment of Pathobiology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195 stuehrd@ccf.org hplu@bgsu.edu.
H Peter LuCenter for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403; stuehrd@ccf.org hplu@bgsu.edu.
Bowling Green State University · USCleveland Clinic Lerner College of Medicine · US

Funding

Structural Determinants Of Ceruloplasmin Inflammatory ActivityP01HL076491 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 2004 to 2019
$27.3M
CONTROL MECHANISMS OF THE NITRIC OXIDE SYNTHASESR01GM051491 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI STUEHR, DENNIS J · 1994 to 2016
$5.1M
NHLBI NIH HHS HL076491NHLBI NIH HHS P01 HL076491NIGMS NIH HHS GM51491NIGMS NIH HHS R01 GM051491
6 · The paper itself

Abstract

Mechanisms that regulate the nitric oxide synthase enzymes (NOS) are of interest in biology and medicine. Although NOS catalysis relies on domain motions, and is activated by calmodulin binding, the relationships are unclear. We used single-molecule fluorescence resonance energy transfer (FRET) spectroscopy to elucidate the conformational states distribution and associated conformational fluctuation dynamics of the two electron transfer domains in a FRET dye-labeled neuronal NOS reductase domain, and to understand how calmodulin affects the dynamics to regulate catalysis. We found that calmodulin alters NOS conformational behaviors in several ways: It changes the distance distribution between the NOS domains, shortens the lifetimes of the individual conformational states, and instills conformational discipline by greatly narrowing the distributions of the conformational states and fluctuation rates. This information was specifically obtainable only by single-molecule spectroscopic measurements, and reveals how calmodulin promotes catalysis by shaping the physical and temporal conformational behaviors of NOS.

Indexed as

AnimalsCalmodulinCarbocyaninesCattleFluorescence Resonance Energy TransferNitric Oxide Synthase Type IProtein Structure, SecondaryProtein Structure, TertiarySpectrophotometry, UltravioletTime FactorsCalmodulinCarbocyaninescyanine dye 3cyanine dye 5Nitric Oxide Synthase Type Iconformational motiondomain–domain interactionelectron transferflavoproteinFRET

Identifiers

PMID26311846
PMCPMC4586839
OpenAlexW1963119831

What OpenQuestion holds

Textmetadata
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.