Evidence map›Paper›PMID 28440748›Full record

ArticleeLife2017

Palmitoylated SCP1 is targeted to the plasma membrane and negatively regulates angiogenesis.

Peng Liao, Weichao Wang, Yu Li, Rui Wang, Jiali Jin, Weijuan Pang, Yunfei Chen, Mingyue Shen, Xinbo Wang, Dongyang Jiang and 6 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Akt Is S-Palmitoylated: A New Layer of Regulation for Akt.Frontiers in cell and developmental biology · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. Article
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  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 4 institutions in 2 countries.

Peng LiaoDepartment of Central Laboratory, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.
Weichao WangDepartment of Central Laboratory, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.
Yu LiInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Rui WangInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Jiali JinInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Weijuan PangInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Yunfei ChenDepartment of Central Laboratory, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.
Mingyue ShenInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Xinbo WangInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Dongyang JiangDepartment of Cardiology, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.
Jinjiang PangDepartment of Cardiology, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.
Mingyao LiuInstitute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Xia LinDepartment of Surgery, Baylor College of Medicine, Houston, United States.
Xin-Hua FengLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Zhejiang, China.
Ping WangDepartment of Central Laboratory, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.
Xin GeDepartment of Clinical Laboratory Medicine, Shanghai Tenth People's Hospital, Tongji University School of Medicine, Shanghai, China.ORCID 0000-0001-9233-2691
East China Normal University · CNTongji University · CNBaylor College of Medicine · USZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SCP1 as a nuclear transcriptional regulator acts globally to silence neuronal genes and to affect the dephosphorylation of RNA Pol ll. However, we report the first finding and description of SCP1 as a plasma membrane-localized protein in various cancer cells using EGFP- or other epitope-fused SCP1. Membrane-located SCP1 dephosphorylates AKT at serine 473, leading to the abolishment of serine 473 phosphorylation that results in suppressed angiogenesis and a decreased risk of tumorigenesis. Consistently, we observed increased AKT phosphorylation and angiogenesis followed by enhanced tumorigenesis in

Indexed as

Neovascularization, PhysiologicProtein Processing, Post-TranslationalAnimalsCell MembraneLipoylationMembrane ProteinsMice, KnockoutPhosphoprotein PhosphatasesPhosphorylationProto-Oncogene Proteins c-aktMembrane ProteinsPhosphoprotein PhosphatasesProto-Oncogene Proteins c-aktScp1 protein, mouseangiogenesiscancer biologycell biologyhuman cancer cell linesmousetumorigenesis

Identifiers

PMID28440748
PMCPMC5404917
OpenAlexW2606720673

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.