Evidence map›Paper›PMID 20211245›Full record

ArticleFree radical biology & medicine2010

Nitric oxide blocks cellular heme insertion into a broad range of heme proteins.

Syed Mohsin Waheed, Arnab Ghosh, Ritu Chakravarti, Ashis Biswas, Mohammad Mahfuzul Haque, Koustubh Panda, Dennis J Stuehr

Open access · greenAbstract read
In one paragraph

Article in Free radical biology & medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

42 citing papers in PubMed, 61 citations in OpenAlex.

  1. Loss of the ApJournal of bacteriology · 2026
    Article
  2. Review
  3. Review
  4. Key roles of GAPDH, Hsp90, and NO in heme trafficking.Journal of inorganic biochemistry · 2026
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Deletion ofAntimicrobial agents and chemotherapy · 2022
    Article
  16. NO rapidly mobilizes cellular heme to trigger assembly of its own receptor.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Review
  19. Review
  20. GAPDH delivers heme to soluble guanylyl cyclase.The Journal of biological chemistry · 2020
    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

7 authors at 3 institutions in 2 countries.

Syed Mohsin WaheedDepartment of Pathobiology, Lerner Research Institute, The Cleveland Clinic, Cleveland, OH 44195, USA.
Arnab Ghosh
Ritu Chakravarti
Ashis Biswas
Mohammad Mahfuzul Haque
Koustubh Panda
Dennis J Stuehr
Cleveland Clinic Lerner College of Medicine · USNational Institute of Technology Rourkela · INUniversity of Calcutta · IN

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
BIOCHEMISTRY OF NITRIC OXIDE SYNTHESISR01CA053914 · NCI · CLEVELAND CLINIC LERNER COM-CWRU · PI STUEHR, DENNIS J · 1996 to 2010
$3.1M
BIOCHEMISTRY OF MACROPHAGE NITRIC OXIDE SYNTHESISR29CA053914 · NCI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI STUEHR, DENNIS J · 1991 to 1995
–
NCI NIH HHS CA53914NCI NIH HHS R01 CA053914NHLBI NIH HHS HL076491NHLBI NIH HHS P01 HL076491NIGMS NIH HHS GM51491NIGMS NIH HHS R01 GM051491
6 · The paper itself

Abstract

Although the insertion of heme into proteins enables their function in bioenergetics, metabolism, and signaling, the mechanisms and regulation of this process are not fully understood. We developed a means to study cellular heme insertion into apo-protein targets over a 3-h period and then investigated how nitric oxide (NO) released from a chemical donor (NOC-18) might influence heme (protoporphyrin IX) insertion into seven targets that present a range of protein structures, heme ligation states, and functions (three NO synthases, two cytochrome P450's, catalase, and hemoglobin). NO blocked cellular heme insertion into all seven apo-protein targets. The inhibition occurred at relatively low (nM/min) fluxes of NO, was reversible, and did not involve changes in intracellular heme levels, activation of guanylate cyclase, or inhibition of mitochondrial ATP production. These aspects and the range of protein targets suggest that NO can act as a global inhibitor of heme insertion, possibly by inhibiting a common step in the process.

Indexed as

AnimalsCatalaseCell LineCytochrome P-450 CYP2D6Cytochrome P-450 CYP3AHemeHemeproteinsHumansK562 CellsMiceNitric OxideNitric Oxide Synthase Type INitric Oxide Synthase Type IINitroso CompoundsProtoporphyrinsCatalaseCYP3A4 protein, humanCytochrome P-450 CYP2D6Cytochrome P-450 CYP3AHemeHemeproteinsNitric OxideNitric Oxide Synthase Type INitric Oxide Synthase Type IINitroso CompoundsNOC 18protoporphyrin IXProtoporphyrins

Identifiers

PMID20211245
PMCPMC2866197
OpenAlexW2012685167

What OpenQuestion holds

Textmetadata
LicenceTDM
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.