Evidence map›Paper›PMID 32060095›Full record

ArticleThe Journal of biological chemistry2020

The Shb scaffold binds the Nck adaptor protein, p120 RasGAP, and Chimaerins and thereby facilitates heterotypic cell segregation by the receptor EphB2.

Melany J Wagner, Marilyn S Hsiung, Gerald D Gish, Rick D Bagshaw, Sasha A Doodnauth, Mohamed A Soliman, Claus Jørgensen, Monika Tucholska, Robert Rottapel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
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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

9 authors at 4 institutions in 2 countries.

Melany J WagnerPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario M5S 1A8, Canada mjdwagner@hotmail.com.
Marilyn S HsiungLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.
Gerald D GishLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.
Rick D BagshawLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.ORCID 0000-0001-5013-4291
Sasha A DoodnauthPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario M5S 1A8, Canada.
Mohamed A SolimanLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.
Claus JørgensenCancer Research UK Manchester Institute, University of Manchester, Alderley Park SK10 4TG, United Kingdom.
Monika TucholskaLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.
Robert RottapelPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario M5S 1A8, Canada rottapel@gmail.com.
Mount Sinai Hospital · CASt. Michael's Hospital · CAUniversity Health Network · CAUniversity of Manchester · GB

Funding

Cancer Research UK 19258
6 · The paper itself

Abstract

Eph receptors are a family of receptor tyrosine kinases that control directional cell movement during various biological processes, including embryogenesis, neuronal pathfinding, and tumor formation. The biochemical pathways of Eph receptors are context-dependent in part because of the varied composition of a heterotypic, oligomeric, active Eph receptor complex. Downstream of the Eph receptors, little is known about the essential phosphorylation events that define the context and instruct cell movement. Here, we define a pathway that is required for Eph receptor B2 (EphB2)-mediated cell sorting and is conserved among multiple Eph receptors. Utilizing a HEK293 model of EphB2

Indexed as

Adaptor Proteins, Signal TransducingCell SeparationChimerin ProteinsEphrin-B1HEK293 CellsHumansMass SpectrometryOncogene ProteinsPhosphorylationProtein BindingProtein SubunitsProto-Oncogene ProteinsReceptor, EphB2RNA-Binding ProteinsRNA InterferenceRNA, Small InterferingAdaptor Proteins, Signal TransducingChimerin ProteinsEFNB1 protein, humanEphrin-B1G3BP2 protein, humanNck proteinOncogene ProteinsProtein SubunitsProto-Oncogene ProteinsReceptor, EphB2RNA-Binding ProteinsRNA, Small InterferingSHB protein, humanChimaerinEphB2, Eph receptor tyrosine kinaseGTPase-activating protein (GAP)Nckp120 RasGAPphosphotyrosine signalingreceptor tyrosine kinaseShbsignal transductionSrc homology 2 domain (SH2 domain)

Identifiers

PMID32060095
PMCPMC7086039
OpenAlexW3006404123

What Socratic 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 Socratic graph.