Evidence map›Paper›PMID 10611283›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells.

H Zhu, H Qiu, H W Yoon, S Huang, H F Bunn

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
11.8field-weighted citation impact, top 1% 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

34 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Cytochrome bFree radical biology & medicine · 2026
    Article
  3. Article
  4. CytochromebioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Frontiers in molecular biosciences · 2022
    Article
  9. Crystal structures of the naturally fused CS and cytochrome bActa crystallographica. Section D, Structural biology · 2019
    Article
  10. Article
  11. Article
  12. Practicing biochemistry without a license.The Journal of biological chemistry · 2013
    Article
  13. Article
  14. Pulmonary endothelial cell NOX.American journal of respiratory cell and molecular biology · 2012
    Review
  15. Article
  16. Beta-Cell Injury in Ncb5or-null Mice is Exacerbated by Consumption of a High-Fat Diet.European journal of lipid science and technology : EJLST · 2012
    Article
  17. Review
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 1 country.

H ZhuHematology Division, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115, USA.
H Qiu
H W Yoon
S Huang
H F Bunn
Brigham and Women's Hospital · USScripps Research Institute · USHarvard University · US

Funding

REGULATION OF THE ERYTHROPOIETIN GENER01DK041234 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI BUNN, H. FRANKLIN · 1989 to 2003
$2.3M
Structural and Functional Analysis of Oxygen SensorK01DK059901 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI ZHU, HAO · 2001 to 2003
$272k
OXYGEN SENSOR--STRUCTURAL AND FUNCTIONAL STUDIESF32DK009678 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI ZHU, HAO · 1997 to 1999
–
NIDDK NIH HHS F32 DK009678NIDDK NIH HHS F32 DK09678NIDDK NIH HHS K01 DK059901NIDDK NIH HHS R01 DK041234NIDDK NIH HHS R01 DK41234
6 · The paper itself

Abstract

Cytochrome b-type NAD(P)H oxidoreductases are involved in many physiological processes, including iron uptake in yeast, the respiratory burst, and perhaps oxygen sensing in mammals. We have identified a cytosolic cytochrome b-type NAD(P)H oxidoreductase in mammals, a flavohemoprotein (b5+b5R) containing cytochrome b5 (b5) and b5 reductase (b5R) domains. A genetic approach, using BLAST searches against DBEST for FAD-, NAD(P)H-binding sequences followed by reverse transcription-PCR, was used to clone the complete cDNA sequence of human b5+b5R from the hepatoma cell line Hep 3B. Compared with the classical single-domain b5 and b5R proteins localized on endoplasmic reticulum membrane, b5+b5R also has binding motifs for heme, FAD, and NAD(P)H prosthetic groups but no membrane anchor. The human b5+b5R transcript was expressed at similar levels in all tissues and cell lines that were tested. The two functional domains b5* and b5R* are linked by an approximately 100-aa-long hinge bearing no sequence homology to any known proteins. When human b5+b5R was expressed as c-myc adduct in COS-7 cells, confocal microscopy revealed a cytosolic localization at the perinuclear space. The recombinant b5+b5R protein can be reduced by NAD(P)H, generating spectrum typical of reduced cytochrome b with alpha, beta, and Soret peaks at 557, 527, and 425 nm, respectively. Human b5+b5R flavohemoprotein is a NAD(P)H oxidoreductase, demonstrated by superoxide production in the presence of air and excess NAD(P)H and by cytochrome c reduction in vitro. The properties of this protein make it a plausible candidate oxygen sensor.

Indexed as

Amino Acid SequenceCell CompartmentationCytochrome-B(5) ReductaseCytochrome ReductasesCytochromes b5CytosolFlavoproteinsGene ExpressionHemeproteinsHumansModels, BiologicalMolecular Sequence DataNADH, NADPH OxidoreductasesNeoplasm ProteinsOxygenProtein Structure, TertiaryCytochrome-B(5) ReductaseCytochrome ReductasesCytochromes b5FlavoproteinsHemeproteinsNADH, NADPH OxidoreductasesNeoplasm ProteinsOxygenRecombinant Fusion Proteins

Identifiers

PMID10611283
PMCPMC24718
OpenAlexW2108554272

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.