Evidence map›Paper›PMID 28924042›Full record

ArticleThe Journal of biological chemistry2017

Alternative cleavage of the bone morphogenetic protein (BMP), Gbb, produces ligands with distinct developmental functions and receptor preferences.

Edward N Anderson, Kristi A Wharton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Molecular Mechanisms of AMH Signaling.Frontiers in endocrinology · 2022
    Review
  6. BMP/TGF-β signaling as a modulator of neurodegeneration in ALS.Developmental dynamics : an official publication of the American Association of Anatomists · 2022
    Article
  7. TGF-β Pathway in Salivary Gland Fibrosis.International journal of molecular sciences · 2020
    Review
  8. Review
  9. The Role of Bone Morphogenetic Proteins in Diabetic Complications.ACS pharmacology & translational science · 2020
    Review
  10. Bio-protocol · 2019
    Article
  11. The Journal of cell biology · 2019
    Article
  12. Review
  13. Article
  14. 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

2 authors at 1 institution in 1 country.

Edward N AndersonFrom the Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912.ORCID 0000-0002-2468-0851
Kristi A WhartonFrom the Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912 kristi_wharton@brown.edu.ORCID 0000-0001-9625-4336
Brown University · US

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
DROSOPHILA GENOMICS RESOURCE CENTERP40OD010949 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Andrew Zelhof · 2012 to 2026
$9.4M
Differential regulation of BMP Signals in VivoR01GM068118 · NIGMS · BROWN UNIVERSITY · PI WHARTON, KRISTI A · 2005 to 2014
$2.5M
NIGMS NIH HHS R01 GM068118NIH HHS P40 OD010949NIH HHS P40 OD018537
6 · The paper itself

Abstract

The family of TGF-β and bone morphogenetic protein (BMP) signaling proteins has numerous developmental and physiological roles. They are made as proprotein dimers and then cleaved by proprotein convertases to release the C-terminal domain as an active ligand dimer. Multiple proteolytic processing sites in Glass bottom boat (Gbb), the

Indexed as

Gene Expression Regulation, DevelopmentalActivin Receptors, Type IIAnimalsBody PatterningCells, CulturedDrosophila melanogasterDrosophila ProteinsLigandsProprotein ConvertasesPupaReceptors, Cell SurfaceSignal TransductionTransforming Growth Factor betaWings, AnimalActivin Receptors, Type IIDrosophila Proteinsgbb protein, DrosophilaLigandsProprotein Convertasesput protein, DrosophilaReceptors, Cell SurfaceTransforming Growth Factor betawit protein, Drosophilabone morphogenetic protein (BMP)cell signalingDrosophila; O-GlcNAcylationGlass bottom boat (Gbb)prodomainproprotein convertaseprotein processingtransforming growth factor β (TGF-β)

Identifiers

PMID28924042
PMCPMC5702660
OpenAlexW2952640964

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.