Evidence map›Paper›PMID 26205815›Full record

ArticleThe Journal of biological chemistry2015

Characterization of a single b-type heme, FAD, and metal binding sites in the transmembrane domain of six-transmembrane epithelial antigen of the prostate (STEAP) family proteins.

Mark D Kleven, Mensur Dlakić, C Martin Lawrence

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 63 citations in OpenAlex.

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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

3 authors at 3 institutions in 2 countries.

Mark D KlevenFrom the Departments of Chemistry and Biochemistry and.
Mensur DlakićMicrobiology and Immunology, Montana State University, Bozeman, Montana 59717.
C Martin LawrenceFrom the Departments of Chemistry and Biochemistry and lawrence@chemistry.montana.edu.
Department of Physics, Mathematics and Informatics · BYMontana State University · USUniversity of Kansas · US

Funding

Structural and Functional Studies of Iron Transport and HomeostasisR01GM084326 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI LAWRENCE, CHARLES MARTIN · 2009 to 2012
$1.0M
NIGMS NIH HHS R01 GM084326
6 · The paper itself

Abstract

Six-transmembrane epithelial antigen of the prostate 3 (Steap3) is the major ferric reductase in developing erythrocytes. Steap family proteins are defined by a shared transmembrane domain that in Steap3 has been shown to function as a transmembrane electron shuttle, moving cytoplasmic electrons derived from NADPH across the lipid bilayer to the extracellular face where they are used to reduce Fe(3+) to Fe(2+) and potentially Cu(2+) to Cu(1+). Although the cytoplasmic N-terminal oxidoreductase domain of Steap3 and Steap4 are relatively well characterized, little work has been done to characterize the transmembrane domain of any member of the Steap family. Here we identify high affinity FAD and iron biding sites and characterize a single b-type heme binding site in the Steap3 transmembrane domain. Furthermore, we show that Steap3 is functional as a homodimer and that it utilizes an intrasubunit electron transfer pathway through the single heme moiety rather than an intersubunit electron pathway through a potential domain-swapped dimer. Importantly, the sequence motifs in the transmembrane domain that are associated with the FAD and metal binding sites are not only present in Steap2 and Steap4 but also in Steap1, which lacks the N-terminal oxidoreductase domain. This strongly suggests that Steap1 harbors latent oxidoreductase activity.

Indexed as

Antigens, NeoplasmCopperFlavin-Adenine DinucleotideHEK293 CellsHemeHumansIronNADPProtein MultimerizationProtein Structure, TertiaryAntigens, NeoplasmCopperFlavin-Adenine DinucleotideHemeIronNADPb-type cytochromecoppercopper transportcupric reductaseferric reductaseflavin adenine dinucleotide (FAD)ironiron metabolismSteap1Steap3

Identifiers

PMID26205815
PMCPMC4566230
OpenAlexW1520601156

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.