Evidence map›Paper›PMID 25861988›Full record

ArticleThe Journal of biological chemistry2015

Isolation and Characterization of a Hybrid Respiratory Supercomplex Consisting of Mycobacterium tuberculosis Cytochrome bcc and Mycobacterium smegmatis Cytochrome aa3.

Mi-Sun Kim, Jichan Jang, Nurlilah Binte Ab Rahman, Kevin Pethe, Edward A Berry, Li-Shar Huang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Structure ofeLife · 2021
    Article
  6. Cryo-EM structures of engineered active bcNature communications · 2021
    Article
  7. Nitric Oxide Does Not Inhibit but Is Metabolized by the CytochromeInternational journal of molecular sciences · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Structure of a functional obligate complex IIINature structural & molecular biology · 2018
    Article
  13. The copper-deprivation stimulon ofThe Journal of biological chemistry · 2018
    Article
  14. CytochromeJournal of bacteriology · 2018
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. 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

6 authors at 3 institutions in 3 countries.

Mi-Sun KimFrom the State University of New York Upstate Medical University, Syracuse, New York 13210.
Jichan Jangthe Institut Pasteur Korea, Sampyeong-dong, Seongnam-si, Gyeonggi-do 463-400, Korea, and.
Nurlilah Binte Ab Rahmanthe Lee Kong Chian School of Medicine and School of Biological Sciences, Nanyang Technological University, Singapore 639798, Singapore.
Kevin Pethethe Institut Pasteur Korea, Sampyeong-dong, Seongnam-si, Gyeonggi-do 463-400, Korea, and the Lee Kong Chian School of Medicine and School of Biological Sciences, Nanyang Technological University, Singapore 639798, Singapore.ORCID http://orcid.org/0000-0003-0297-0150
Edward A BerryFrom the State University of New York Upstate Medical University, Syracuse, New York 13210, berrye@upstate.edu.ORCID http://orcid.org/0000-0001-8929-0259
Li-Shar HuangFrom the State University of New York Upstate Medical University, Syracuse, New York 13210, berryl@upstate.edu.
SUNY Upstate Medical University · USInstitut Pasteur Korea · KRNanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, energy production pathways have been shown to be viable antitubercular drug targets to combat multidrug-resistant tuberculosis and eliminate pathogen in the dormant state. One family of drugs currently under development, the imidazo[1,2-a]pyridine derivatives, is believed to target the pathogen's homolog of the mitochondrial bc1 complex. This complex, denoted cytochrome bcc, is highly divergent from mitochondrial Complex III both in subunit structure and inhibitor sensitivity, making it a good target for drug development. There is no soluble cytochrome c in mycobacteria to transport electrons from the bcc complex to cytochrome oxidase. Instead, the bcc complex exists in a "supercomplex" with a cytochrome aa3-type cytochrome oxidase, presumably allowing direct electron transfer. We describe here purification and initial characterization of the mycobacterial cytochrome bcc-aa3 supercomplex using a strain of M. smegmatis that has been engineered to express the M. tuberculosis cytochrome bcc. The resulting hybrid supercomplex is stable during extraction and purification in the presence of dodecyl maltoside detergent. It is hoped that this purification procedure will potentiate functional studies of the complex as well as crystallographic studies of drug binding and provide structural insight into a third class of the bc complex superfamily.

Indexed as

Bacterial ProteinsElectron TransportElectron Transport Complex IIIElectron Transport Complex IVHumansMycobacterium InfectionsMycobacterium smegmatisMycobacterium tuberculosisBacterial ProteinsElectron Transport Complex IIIElectron Transport Complex IVcytochrome bccelectron transfer complexenzyme purificationMycobacterium smegmatisMycobacterium tuberculosisQ203respiratory chainrespiratory supercomplex

Identifiers

PMID25861988
PMCPMC4505504
OpenAlexW1978869377

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.