Evidence map›Paper›PMID 23792964›Full record

ArticleThe Journal of biological chemistry2013

Efficient purification and reconstitution of ATP binding cassette transporter B6 (ABCB6) for functional and structural studies.

Hemantkumar Chavan, Mohiuddin Md Taimur Khan, George Tegos, Partha Krishnamurthy

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. TargetingZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Regulation of Heme Synthesis by Mitochondrial Homeostasis Proteins.Frontiers in cell and developmental biology · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. A heme-binding domain controls regulation of ATP-dependent potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Article
  16. TMEM14C is required for erythroid mitochondrial heme metabolism.The Journal of clinical investigation · 2014
    Article
  17. 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 3 institutions in 1 country.

Hemantkumar ChavanDepartment of Pharmacology, Toxicology and Therapeutics, University of Kansas Medical Center, Kansas City, Kansas 66160, USA.
Mohiuddin Md Taimur Khan
George Tegos
Partha Krishnamurthy
University of Kansas Medical Center · USPacific Northwest National Laboratory · USUniversity of New Mexico · US

Funding

THE ROLE OF HUMAN PXR IN ANTI-TUBERCULOSIS DRUG-INDUCED LIVER INJURYP20RR021940 · NCRR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI KLASSEN, CURTIS D · 2006 to 2011
$12.1M
Hight Throughput Screening for inhibitors of the ABC transporter ABCB6R03MH093193 · NIMH · UNIVERSITY OF KANSAS MEDICAL CENTER · PI KRISHNAMURTHY, PARTHA C · 2011 to 2012
$75k
NCRR NIH HHS P20 RR021940NCRR NIH HHS P20RR021940NIMH NIH HHS R03 MH093193NIMH NIH HHS R03MH093193
6 · The paper itself

Abstract

The mitochondrial ATP binding cassette transporter ABCB6 has been associated with a broad range of physiological functions, including growth and development, therapy-related drug resistance, and the new blood group system Langereis. ABCB6 has been proposed to regulate heme synthesis by shuttling coproporphyrinogen III from the cytoplasm into the mitochondria. However, direct functional information of the transport complex is not known. To understand the role of ABCB6 in mitochondrial transport, we developed an in vitro system with pure and active protein. ABCB6 overexpressed in HEK293 cells was solubilized from mitochondrial membranes and purified to homogeneity. Purified ABCB6 showed a high binding affinity for MgATP (Kd = 0.18 μM) and an ATPase activity with a Km of 0.99 mM. Reconstitution of ABCB6 into liposomes allowed biochemical characterization of the ATPase including (i) substrate-stimulated ATPase activity, (ii) transport kinetics of its proposed endogenous substrate coproporphyrinogen III, and (iii) transport kinetics of substrates identified using a high throughput screening assay. Mutagenesis of the conserved lysine to alanine (K629A) in the Walker A motif abolished ATP hydrolysis and substrate transport. These results suggest a direct interaction between mitochondrial ABCB6 and its transport substrates that is critical for the activity of the transporter. Furthermore, the simple immunoaffinity purification of ABCB6 to near homogeneity and efficient reconstitution of ABCB6 into liposomes might provide the basis for future studies on the structure/function of ABCB6.

Indexed as

Adenosine TriphosphateATP-Binding Cassette TransportersCoproporphyrinsHEK293 CellsHumansKineticsMembrane LipidsMitochondriaProtein BindingProtein ConformationProtein IsoformsABCB6 protein, humanAdenosine TriphosphateATP-Binding Cassette Transporterscoproporphyrin IIICoproporphyrinsMembrane LipidsProtein IsoformsABC TransporterLiposomesMembrane TransportProtein PurificationReconstitution of Membrane Transporters

Identifiers

PMID23792964
PMCPMC3829351
OpenAlexW1983335650

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.