Evidence map›Paper›PMID 23063586›Full record

ArticleJournal of molecular biology2012

Members of the DAN family are BMP antagonists that form highly stable noncovalent dimers.

Chandramohan Kattamuri, David M Luedeke, Kristof Nolan, Scott A Rankin, Kenneth D Greis, Aaron M Zorn, Thomas B Thompson

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Genetics and Genomics ofInternational journal of molecular sciences · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Bone morphogenetic protein signaling in inflammation.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Structural Biology and Evolution of the TGF-β Family.Cold Spring Harbor perspectives in biology · 2016
    Review
  19. Article
  20. Agonists and Antagonists of TGF-β Family Ligands.Cold Spring Harbor perspectives in biology · 2016
    Review
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

7 authors at 2 institutions in 1 country.

Chandramohan KattamuriDepartment of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati Medical Sciences Building, Cincinnati, OH 45267, USA.
David M Luedeke
Kristof Nolan
Scott A Rankin
Kenneth D Greis
Aaron M Zorn
Thomas B Thompson
University of Cincinnati · USCincinnati Children's Hospital Medical Center · US

Funding

Molecular Basis of Liver Development.R01DK070858 · NIDDK · CINCINNATI CHILDRENS HOSP MED CTR · PI ZORN, AARON M · 2007 to 2017
$2.9M
Structural basis of antagonism within the TGFbeta-superfamilyR01GM084186 · NIGMS · UNIVERSITY OF CINCINNATI · PI THOMPSON, THOMAS B · 2008 to 2012
$1.6M
NIDDK NIH HHS DK070858NIDDK NIH HHS R01 DK070858NIGMS NIH HHS GM084186NIGMS NIH HHS R01 GM084186
6 · The paper itself

Abstract

Signaling of bone morphogenetic protein (BMP) ligands is antagonized by a number of extracellular proteins, including noggin, follistatin and members of the DAN (differential screening selected gene abberative in neuroblastoma) family. Structural studies on the DAN family member sclerostin (a weak BMP antagonist) have previously revealed that the protein is monomeric and consists of an eight-membered cystine knot motif with a fold similar to transforming growth factor-β ligands. In contrast to sclerostin, certain DAN family antagonists, including protein related to DAN and cerberus (PRDC), have an unpaired cysteine that is thought to function in covalent dimer assembly (analogous to transforming growth factor-β ligands). Through a combination of biophysical and biochemical studies, we determined that PRDC forms biologically active dimers that potently inhibit BMP ligands. Furthermore, we showed that PRDC dimers, surprisingly, are not covalently linked, as mutation of the unpaired cysteine does not inhibit dimer formation or biological activity. We further demonstrated that the noncovalent PRDC dimers are highly stable under both denaturing and reducing conditions. This study was extended to the founding family member DAN, which also forms noncovalent dimers that are highly stable. These results demonstrate that certain DAN family members can form both monomers and noncovalent dimers, implying that biological activity of DAN family members might be linked to their oligomeric state.

Indexed as

Protein MultimerizationAmino Acid SubstitutionAnimalsBone Morphogenetic ProteinsCysteineCytokinesMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsProteinsProtein StabilitySequence Analysis, DNABone Morphogenetic ProteinsCysteineCytokinesGrem2 protein, mouseMutant ProteinsProteins

Identifiers

PMID23063586
PMCPMC3509953
OpenAlexW2083620799

What OpenQuestion holds

Textmetadata
LicenceTDM
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.