Evidence map›Paper›PMID 29329397›Full record

ArticleJournal of molecular cell biology2018

MINAR1 is a Notch2-binding protein that inhibits angiogenesis and breast cancer growth.

Rachel Xi-Yeen Ho, Rosana D Meyer, Kevin B Chandler, Esma Ersoy, Michael Park, Philip A Bondzie, Nima Rahimi, Huihong Xu, Catherine E Costello, Nader Rahimi

Open access · bronzeAbstract read
In one paragraph

Article in Journal of molecular cell biology, 2018. 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
0.9field-weighted citation impact, top 27% 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, 20 citations in OpenAlex.

  1. Transcriptomic Analysis ofInternational journal of molecular sciences · 2026
    Article
  2. Transcriptomic Analysis ofbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Cortical Somatostatin Neurons Regulate Seizure Susceptibility via MINAR1/Gαs-cAMP Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. miR‑205: A dual regulator of angiogenesis in health and disease (Review).International journal of molecular medicine · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. mNature communications · 2024
    Article
  10. Article
  11. Mutations inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. TRIM28 regulates sprouting angiogenesis through VEGFR-DLL4-Notch signaling circuit.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. 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

10 authors at 1 institution in 1 country.

Rachel Xi-Yeen HoDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Rosana D MeyerDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Kevin B ChandlerDepartment of Biochemistry and Center for Biomedical Mass Spectrometry, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Esma ErsoyDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Michael ParkDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Philip A BondzieDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Nima RahimiDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Huihong XuDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Catherine E CostelloDepartment of Biochemistry and Center for Biomedical Mass Spectrometry, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Nader RahimiDepartment of Pathology, School of Medicine, Boston University Medical Campus, Boston, MA, USA.
Boston University · US

Funding

Overcoming the resistance to anti-angiogenesis therapyR21CA191970 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAHIMI, NADER · 2015 to 2016
$392k
IGPR-1 in colon cancer chemotherapyR21CA193958 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAHIMI, NADER · 2015 to 2016
$392k
NCI NIH HHS R21 CA191970NCI NIH HHS R21 CA193958
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs)/intrinsically unstructured proteins are characterized by the lack of fixed or stable tertiary structure, and are increasingly recognized as an important class of proteins with major roles in signal transduction and transcriptional regulation. In this study, we report the identification and functional characterization of a previously uncharacterized protein (UPF0258/KIAA1024), major intrinsically disordered Notch2-associated receptor 1 (MINAR1). While MINAR1 carries a single transmembrane domain and a short cytoplasmic domain, it has a large extracellular domain that shares no similarity with known protein sequences. Uncharacteristically, MINAR1 is a highly IDP with nearly 70% of its amino acids sequences unstructured. We demonstrate that MINAR1 physically interacts with Notch2 and its binding to Notch2 increases its stability and function. MINAR1 is widely expressed in various tissues including the epithelial cells of the breast and endothelial cells of blood vessels. MINAR1 plays a negative role in angiogenesis as it inhibits angiogenesis in cell culture and in mouse matrigel plug and zebrafish angiogenesis models. Furthermore, while MINAR1 is highly expressed in the normal human breast, its expression is significantly downregulated in advanced human breast cancer and its re-expression in breast cancer cells inhibited tumor growth. Our study demonstrates that MINAR1 is an IDP that negatively regulates angiogenesis and growth of breast cancer cells.

Indexed as

Amino Acid SequenceAnimalsBreast NeoplasmsCell LineCell Line, TumorCell ProliferationFemaleHEK293 CellsHumansIntrinsically Disordered ProteinsMiceNeovascularization, PathologicNeovascularization, PhysiologicProtein DomainsProtein Interaction MapsReceptor, Notch2Intrinsically Disordered ProteinsMINAR1 protein, humanNOTCH2 protein, humanReceptor, Notch2Receptors, Cell Surface

Identifiers

PMID29329397
PMCPMC6025234
OpenAlexW2782664079

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.