Evidence map›Paper›PMID 26517884›Full record

ReviewBiochemical Society transactions2015

The role of chordin fragments generated by partial tolloid cleavage in regulating BMP activity.

Helen Troilo, Anne L Barrett, Alexander P Wohl, Thomas A Jowitt, Richard F Collins, Christopher P Bayley, Alexandra V Zuk, Gerhard Sengle, Clair Baldock

Open access · bronzeAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Crim1Mammalian genome : official journal of the International Mammalian Genome Society · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Agonists and Antagonists of TGF-β Family Ligands.Cold Spring Harbor perspectives in biology · 2016
    Review
  10. Review
  11. 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

9 authors at 1 institution in 1 country.

Helen TroiloWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, U.K.
Anne L BarrettWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, U.K.
Alexander P WohlCenter for Biochemistry, Medical Faculty, University of Cologne, D50931 Cologne, Germany.
Thomas A JowittWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, U.K.
Richard F CollinsWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, U.K.
Christopher P BayleyWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, U.K.
Alexandra V ZukCenter for Biochemistry, Medical Faculty, University of Cologne, D50931 Cologne, Germany.
Gerhard SengleCenter for Biochemistry, Medical Faculty, University of Cologne, D50931 Cologne, Germany Center for Molecular Medicine Cologne, University of Cologne, D50931 Cologne, Germany.
Clair BaldockWellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, U.K. clair.baldock@manchester.ac.uk.
University of Cologne · DE

Funding

Biotechnology and Biological Sciences Research Council BB/I019286/1Wellcome Trust 088785Wellcome Trust 106503/Z/14/Z
6 · The paper itself

Abstract

Chordin-mediated regulation of bone morphogenetic protein (BMP) family growth factors is essential in early embryogenesis and adult homoeostasis. Chordin binds to BMPs through cysteine-rich von Willebrand factor type C (vWC) homology domains and blocks them from interacting with their cell surface receptors. These domains also self-associate and enable chordin to target related proteins to fine-tune BMP regulation. The chordin-BMP inhibitory complex is strengthened by the secreted glycoprotein twisted gastrulation (Tsg); however, inhibition is relieved by cleavage of chordin at two specific sites by tolloid family metalloproteases. As Tsg enhances this cleavage process, it serves a dual role as both promoter and inhibitor of BMP signalling. Recent developments in chordin research suggest that rather than simply being by-products, the cleavage fragments of chordin continue to play a role in BMP regulation. In particular, chordin cleavage at the C-terminus potentiates its anti-BMP activity in a type-specific manner.

Indexed as

Models, BiologicalSignal TransductionAnimalsBone Morphogenetic Protein ReceptorsBone Morphogenetic ProteinsGlycoproteinsHumansIntercellular Signaling Peptides and ProteinsPeptide FragmentsProtein Interaction Domains and MotifsProteinsProtein StabilityProteolysisTolloid-Like MetalloproteinasesBone Morphogenetic Protein ReceptorsBone Morphogenetic ProteinschordinGlycoproteinsIntercellular Signaling Peptides and ProteinsPeptide FragmentsProteinsTolloid-Like MetalloproteinasesTWSG1 protein, humanbone morphogenetic protein (BMP) signallingchordintolloid cleavage

Identifiers

PMID26517884
PMCPMC4613500
OpenAlexW2254075920

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.