Evidence map›Paper›PMID 25217480›Full record

ArticleJournal of lipid research2014

Lrp13 is a novel vertebrate lipoprotein receptor that binds vitellogenins in teleost fishes.

Benjamin J Reading, Naoshi Hiramatsu, Justin Schilling, Katelyn T Molloy, Norm Glassbrook, Hiroko Mizuta, Wenshu Luo, David A Baltzegar, Valerie N Williams, Takashi Todo and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.4field-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

18 citing papers in PubMed, 57 citations in OpenAlex.

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  5. Direct male development in chromosomally ZZ zebrafish.Frontiers in cell and developmental biology · 2024
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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

12 authors at 3 institutions in 2 countries.

Benjamin J ReadingDepartments of Applied Ecology North Carolina State University, Raleigh, NC.
Naoshi HiramatsuGraduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, Japan.
Justin SchillingDepartments of Applied Ecology North Carolina State University, Raleigh, NC.
Katelyn T MolloyDepartments of Applied Ecology North Carolina State University, Raleigh, NC.
Norm GlassbrookGenomic Sciences Laboratory, North Carolina State University, Raleigh, NC.
Hiroko MizutaGraduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, Japan.
Wenshu LuoGraduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, Japan.
David A BaltzegarBiological Sciences, North Carolina State University, Raleigh, NC.
Valerie N WilliamsDepartments of Applied Ecology North Carolina State University, Raleigh, NC.
Takashi TodoGraduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, Japan.
Akihiko HaraGraduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, Japan.
Craig V SullivanBiological Sciences, North Carolina State University, Raleigh, NC Carolina AquaGyn, Raleigh, NC.
North Carolina State University · USHokkaido University · JPNorth Carolina Aquarium · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcripts encoding a novel member of the lipoprotein receptor superfamily, termed LDL receptor-related protein (Lrp)13, were sequenced from striped bass (Morone saxatilis) and white perch (Morone americana) ovaries. Receptor proteins were purified from perch ovary membranes by protein-affinity chromatography employing an immobilized mixture of vitellogenins Aa and Ab. RT-PCR revealed lrp13 to be predominantly expressed in striped bass ovary, and in situ hybridization detected lrp13 transcripts in the ooplasm of early secondary growth oocytes. Quantitative RT-PCR confirmed peak lrp13 expression in the ovary during early secondary growth. Quantitative mass spectrometry revealed peak Lrp13 protein levels in striped bass ovary during late-vitellogenesis, and immunohistochemistry localized Lrp13 to the oolemma and zona radiata of vitellogenic oocytes. Previously unreported orthologs of lrp13 were identified in genome sequences of fishes, chicken (Gallus gallus), mouse (Mus musculus), and dog (Canis lupus familiaris). Zebrafish (Danio rerio) and Nile tilapia (Oreochromis niloticus) lrp13 loci are discrete and share genomic synteny. The Lrp13 appears to function as a vitellogenin receptor and may be an important mediator of yolk formation in fishes and other oviparous vertebrates. The presence of lrp13 orthologs in mammals suggests that this lipoprotein receptor is widely distributed among vertebrates, where it may generally play a role in lipoprotein metabolism.

Indexed as

BassAnimalsCloning, MolecularFish ProteinsGene Expression RegulationHumansIntracellular SpaceProtein BindingProtein TransportReceptors, LipoproteinVitellogeninsFish ProteinsReceptors, LipoproteinVitellogeninsaffinity purificationeggendocytosislow density lipoprotein receptor-related protein 13oocyteoogenesisovaryvery low density lipoprotein receptorvitellogenesisyolk

Identifiers

PMID25217480
PMCPMC4617131
OpenAlexW2025226005

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.