Evidence map›Paper›PMID 9560218›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Transmembrane heme delivery systems.

B S Goldman, D L Beck, E M Monika, R G Kranz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The CcmC-CcmE interaction during cytochromeThe Journal of biological chemistry · 2018
    Article
  5. Article
  6. Regulation of intracellular heme trafficking revealed by subcellular reporters.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  7. Article
  8. Article
  9. TSPO Finds NOX2 in Microglia for Redox Homeostasis.Trends in pharmacological sciences · 2016
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

4 authors at 1 institution in 1 country.

B S GoldmanDepartment of Biology, Washington University, One Brookings Drive, St. Louis, MO 63130, USA.
D L Beck
E M Monika
R G Kranz
Washington University in St. Louis · US

Funding

MOLECULAR GENETIC ANALYSES OF CYTOCHROMES C BIOGENESISR01GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1994 to 2019
$6.0M
CYTOCHROMES C BIOGENESISR55GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1992 to 1992
–
NIGMS NIH HHS GM47909NIGMS NIH HHS R01 GM047909
6 · The paper itself

Abstract

Heme proteins play pivotal roles in a wealth of biological processes. Despite this, the molecular mechanisms by which heme traverses bilayer membranes for use in biosynthetic reactions are unknown. The biosynthesis of c-type cytochromes requires that heme is transported to the bacterial periplasm or mitochondrial intermembrane space where it is covalently ligated to two reduced cysteinyl residues of the apocytochrome. Results herein suggest that a family of integral membrane proteins in prokaryotes, protozoans, and plants act as transmembrane heme delivery systems for the biogenesis of c-type cytochromes. The complete topology of a representative from each of the three subfamilies was experimentally determined. Key histidinyl residues and a conserved tryptophan-rich region (designated the WWD domain) are positioned at the site of cytochrome c assembly for all three subfamilies. These histidinyl residues were shown to be essential for function in one of the subfamilies, an ABC transporter encoded by helABCD. We believe that a directed heme delivery pathway is vital for the synthesis of cytochromes c, whereby heme iron is protected from oxidation via ligation to histidinyl residues within the delivery proteins.

Indexed as

Plant ProteinsProtozoan ProteinsAmino Acid SequenceATP-Binding Cassette TransportersBacterial ProteinsBiological TransportCell MembraneChloroplastsHemeHemeproteinsHistidineMembrane ProteinsMolecular Sequence DataNuclear ProteinsProteinsRecombinant ProteinsATP-Binding Cassette TransportersBacterial ProteinsccsA protein, protozoanHelA protein, bacteriaHelB protein, Rhodobacter capsulatusHelC protein, bacteriaHelD protein, Rhodobacter capsulatusHemeHemeproteinsHistidineMembrane ProteinsNuclear ProteinsPlant ProteinsProteinsProtozoan ProteinsRecombinant ProteinsTryptophan

Identifiers

PMID9560218
PMCPMC20203
OpenAlexW2163990363

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.