Evidence map›Paper›PMID 22357757›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility [corrected].

Keizo Tokuhiro, Masahito Ikawa, Adam M Benham, Masaru Okabe

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 98 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed, 1 pooled it
14.7field-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

98 citing papers in PubMed, 1 synthesis or guideline pooled it, 170 citations in OpenAlex.

  1. Common variants in UMOD associate with urinary uromodulin levels: a meta-analysis.Journal of the American Society of Nephrology : JASN · 2014
    Pooled it
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  20. Nature does it better: mimickingFrontiers in veterinary science · 2025
    Review

38 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Keizo TokuhiroResearch Institute for Microbial Diseases, University, Suita, Osaka 565-0871, Japan.
Masahito Ikawa
Adam M Benham
Masaru Okabe
Durham University · GBMicrobial Chemistry Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A disintegrin and metalloproteinase 3 (ADAM3) is a sperm membrane protein critical for both sperm migration from the uterus into the oviduct and sperm primary binding to the zona pellucida (ZP). Here we show that the testis-specific protein disulfide isomerase homolog (PDILT) cooperates with the testis-specific calreticulin-like chaperone, calsperin (CALR3), in the endoplasmic reticulum and plays an indispensable role in the disulfide-bond formation and folding of ADAM3. Pdilt(-/-) mice were male infertile because ADAM3 could not be folded properly and transported to the sperm surface without the PDILT/CALR3 complex. Peculiarly we find that not only Pdilt(-/-), but also Adam3(-/-), spermatozoa effectively fertilize eggs when the eggs are surrounded in cumulus oophorus. These findings reveal that ADAM3 requires testis-specific private chaperones to be folded properly and that the principle role of ADAM3 is for sperm migration into the oviduct but not for the fertilization event. Moreover, the importance of primary sperm ZP binding, which has been thought to be a critical step in mammalian fertilization, should be reconsidered.

Indexed as

ADAM ProteinsAnimalsCalcium-Binding ProteinsDisulfidesEndoplasmic ReticulumGene Expression Regulation, EnzymologicGerm CellsInfertility, MaleMaleMembrane GlycoproteinsMiceMice, KnockoutMolecular ChaperonesProtein Disulfide-IsomerasesProtein FoldingSpermatozoaAdam3 protein, mouseADAM ProteinsCalcium-Binding ProteinscalmeginDisulfidesMembrane GlycoproteinsMolecular ChaperonesPdilt protein, mouseProtein Disulfide-Isomerases

Identifiers

PMID22357757
PMCPMC3309714
OpenAlexW2076407372

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.