Evidence map›Paper›PMID 31300655›Full record

ArticleNature communications2019

Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility.

Kaoru Nishimura, Elisa Dioguardi, Shunsuke Nishio, Alessandra Villa, Ling Han, Tsukasa Matsuda, Luca Jovine

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. 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
9.1field-weighted citation impact, top 2% 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, 58 citations in OpenAlex.

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  7. Female fertility and the mammalian egg'sHistology and histopathology · 2024
    Review
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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

7 authors at 2 institutions in 2 countries.

Kaoru NishimuraDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden.ORCID http://orcid.org/0000-0002-6883-7988
Elisa DioguardiDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden.ORCID http://orcid.org/0000-0002-8734-8178
Shunsuke NishioDepartment of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan.ORCID http://orcid.org/0000-0003-3420-2578
Alessandra VillaDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden.ORCID http://orcid.org/0000-0002-9573-0326
Ling HanDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden.ORCID http://orcid.org/0000-0001-9310-4789
Tsukasa MatsudaDepartment of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya, 464-8601, Japan.ORCID http://orcid.org/0000-0002-2914-0782
Luca JovineDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden. luca.jovine@ki.se.ORCID http://orcid.org/0000-0002-2679-6946
Karolinska Institutet · SENagoya University · JP

Funding

EC | EC Seventh Framework Programm | FP7 Ideas: European Research Council (FP7-IDEAS-ERC - Specific Programme: "Ideas" Implementing the Seventh Framework Programme of the European Community for Research, Technological Development and Demonstration Activities (2007 to 2013)) 260759European Molecular Biology Organization (EMBO) YIP 2009-1931Vetenskapsrådet (Swedish Research Council) 2016-03999
6 · The paper itself

Abstract

Mammalian fertilisation begins when sperm interacts with the egg zona pellucida (ZP), whose ZP1 subunit is important for fertility by covalently cross-linking ZP filaments into a three-dimensional matrix. Like ZP4, a structurally-related component absent in the mouse, ZP1 is predicted to contain an N-terminal ZP-N domain of unknown function. Here we report a characterisation of ZP1 proteins carrying mutations from infertile patients, which suggests that, in human, filament cross-linking by ZP1 is crucial to form a stable ZP. We map the function of ZP1 to its ZP-N1 domain and determine crystal structures of ZP-N1 homodimers from a chicken homolog of ZP1. These reveal that ZP filament cross-linking is highly plastic and can be modulated by ZP1 fucosylation and, potentially, zinc sparks. Moreover, we show that ZP4 ZP-N1 forms non-covalent homodimers in chicken but not in human. Together, these data identify human ZP1 cross-links as a promising target for non-hormonal contraception.

Indexed as

AnimalsChickensCrystallography, X-RayFemaleFertilizationFrameshift MutationHumansInfertility, FemaleMolecular Dynamics SimulationProtein DomainsProtein MultimerizationRecombinant ProteinsSequence AlignmentZona PellucidaZona Pellucida GlycoproteinsRecombinant ProteinsZona Pellucida GlycoproteinsZP1 protein, humanZP4 protein, human

Identifiers

PMID31300655
PMCPMC6626044
OpenAlexW2960886004

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.