Evidence map›Paper›PMID 33722609›Full record

ArticleThe Journal of biological chemistry

A cross-nearest neighbor/Monte Carlo algorithm for single-molecule localization microscopy defines interactions between p53, Mdm2, and MEG3.

Nicholas C Bauer, Anli Yang, Xin Wang, Yunli Zhou, Anne Klibanski, Roy J Soberman

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Nicholas C BauerDivision of Nephrology, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts, United States.
Anli YangNeuroendocrine Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, United States.
Xin WangNeuroendocrine Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, United States.
Yunli ZhouNeuroendocrine Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, United States.
Anne KlibanskiNeuroendocrine Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, United States.
Roy J SobermanDivision of Nephrology, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts, United States. Electronic address: soberman@helix.mgh.harvard.edu.
Harvard University · US

Funding

TRAINING IN CELL STRUCTURE AND FUNCTION IN NEPHROLOGYT32DK007540 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI BROWN, DENNIS, SOBERMAN, ROY · 1986 to 2021
$7.2M
Role of B7-1 in Podocytes in Pathogenesis of ProteinuriaR01DK062472 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SOBERMAN, ROY · 2004 to 2017
$5.3M
The Role of lncRNA MEG3 in Clinically Non-functioning Pituitary AdenomasR01CA193520 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI SOBERMAN, ROY · 2016 to 2020
$1.9M
A System for FLIM MicroscopyS10RR027931 · NCRR · MASSACHUSETTS GENERAL HOSPITAL · PI SOBERMAN, ROY · 2010 to 2010
$321k
NCI NIH HHS R01 CA193520NCRR NIH HHS S10 RR027931NIDDK NIH HHS R01 DK062472NIDDK NIH HHS T32 DK007540
6 · The paper itself

Abstract

The functions of long noncoding (lnc)RNAs, such as MEG3, are defined by their interactions with other RNAs and proteins. These interactions, in turn, are shaped by their subcellular localization and temporal context. Therefore, it is important to be able to analyze the relationships of lncRNAs while preserving cellular architecture. The ability of MEG3 to suppress cell proliferation led to its recognition as a tumor suppressor. MEG3 has been proposed to activate p53 by disrupting the interaction of p53 with mouse double minute 2 homolog (Mdm2). To test this mechanism in the native cellular context, we employed two-color direct stochastic optical reconstruction microscopy, a single-molecule localization microscopy technique, to detect and quantify the localizations of p53, Mdm2, and MEG3 in U2OS cells. We developed a new cross-nearest neighbor/Monte Carlo algorithm to quantify the association of these molecules. Proof of concept for our method was obtained by examining the association between FKBP1A and mTOR, MEG3 and p53, and Mdm2 and p53. In contrast to previous models, our data support a model in which MEG3 modulates p53 independently of the interaction with Mdm2.

Indexed as

AlgorithmsMonte Carlo MethodProtein Interaction Domains and MotifsHumansImage Processing, Computer-AssistedMicroscopy, FluorescenceProto-Oncogene Proteins c-mdm2RNA, Long NoncodingSingle Molecule ImagingTumor Suppressor Protein p53MDM2 protein, humanMEG3 non-coding RNA, humanProto-Oncogene Proteins c-mdm2RNA, Long NoncodingTP53 protein, humanTumor Suppressor Protein p53computational biologyimage analysislong noncoding RNA (long ncRNA)microscopymouse double minute 2 homologp53single-molecule localization microscopystochastic optical reconstruction microscopy

Identifiers

PMID33722609
PMCPMC8038948
OpenAlexW3135474792

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.