Evidence map›Paper›PMID 23873930›Full record

ArticleThe Journal of biological chemistry2013

Cellular localization and characterization of cytosolic binding partners for Gla domain-containing proteins PRRG4 and PRRG2.

Mustafa N Yazicioglu, Luca Monaldini, Kirk Chu, Fayaz R Khazi, Samuel L Murphy, Heshu Huang, Paris Margaritis, Katherine A High

Abstract 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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  8. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
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  11. Article
  12. Review
  13. Magi-1 scaffolds NaFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  14. Article
  15. 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

8 authors.

Mustafa N YaziciogluFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Luca MonaldiniFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Kirk ChuFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Fayaz R KhaziFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Samuel L MurphyFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Heshu HuangFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Paris MargaritisFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104,; the Department of Pediatrics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104, and.
Katherine A HighFrom the Division of Hematology, The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104,; the Department of Pediatrics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104, and; the Howard Hughes Medical Institute, Chevy Chase, Maryland 20815. Electronic address: high@email.chop.edu.

Funding

Safety &Efficacy of Intravas. Del. of AAV-F.IX to Skeletal MuscleP01HL064190 · NHLBI · CHILDREN'S HOSP OF PHILADELPHIA · PI ARRUDA, VALDER R. · 2000 to 2015
$27.8M
Howard Hughes Medical InstituteNHLBI NIH HHS P01 HL064190NHLBI NIH HHS P01 HL64190
6 · The paper itself

Abstract

The genes encoding a family of proteins termed proline-rich γ-carboxyglutamic acid (PRRG) proteins were identified and characterized more than a decade ago, but their functions remain unknown. These novel membrane proteins have an extracellular γ-carboxyglutamic acid (Gla) protein domain and cytosolic WW binding motifs. We screened WW domain arrays for cytosolic binding partners for PRRG4 and identified novel protein-protein interactions for the protein. We also uncovered a new WW binding motif in PRRG4 that is essential for these newly found protein-protein interactions. Several of the PRRG-interacting proteins we identified are essential for a variety of physiologic processes. Our findings indicate possible novel and previously unidentified functions for PRRG proteins.

Indexed as

Amino Acid MotifsHEK293 CellsHumansMembrane ProteinsProtein BindingProtein Structure, TertiaryMembrane ProteinsPRRG4 protein, humanCell SignalingCytosolic Binding PartnersGla DomainMembrane ProteinsMolecular BiologyMutagenesis Site-specificProtein CarboxylationPRRG2PRRG4Vitamin K

Identifiers

PMID23873930
PMCPMC3764795

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Registered trials

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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.