Evidence map›Paper›PMID 9362480›Full record

ArticleThe EMBO journal1997

Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.

X Yuan, A K Downing, V Knott, P A Handford

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 121 citations in OpenAlex.

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  12. Pathophysiology and Pathogenesis of Marfan Syndrome.Advances in experimental medicine and biology · 2021
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  13. A Novel Splicing Mutation in theFrontiers in genetics · 2020
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  14. The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly.Matrix biology : journal of the International Society for Matrix Biology · 2019
    Review
  15. Article
  16. LTBPs in biology and medicine: LTBP diseases.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

X YuanDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
A K Downing
V Knott
P A Handford
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Here we describe the high resolution nuclear magnetic resonance (NMR) structure of a transforming growth factor beta (TGF-beta)-binding protein-like (TB) domain, which comes from human fibrillin-1, the protein defective in the Marfan syndrome (MFS). This domain is found in fibrillins and latent TGF-beta-binding proteins (LTBPs) which are localized to fibrillar structures in the extracellular matrix. The TB domain manifests a novel fold which is globular and comprises six antiparallel beta-strands and two alpha-helices. An unusual cysteine triplet conserved in the sequences of TB domains is localized to the hydrophobic core, at the C-terminus of an alpha-helix. The structure is stabilized by four disulfide bonds which pair in a 1-3, 2-6, 4-7, 5-8 pattern, two of which are solvent exposed. Analyses of MFS-causing mutations and the fibrillin-1 cell-binding RGD site provide the first clues to the surface specificity of TB domain interactions. Modelling of a homologous TB domain from LTBP-1 (residues 1018-1080) suggests that hydrophobic contacts may play a role in its interaction with the TGF-beta1 latency-associated peptide.

Indexed as

Extracellular MatrixTransforming Growth Factor betaAdipokinesAmino Acid SequenceCell AdhesionFibrillin-1FibrillinsHumansMarfan SyndromeMicrofilament ProteinsModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryAdipokinesFBN1 protein, humanFibrillin-1FibrillinsMicrofilament ProteinsPeptide FragmentsRecombinant ProteinsSolutionsTransforming Growth Factor beta

Identifiers

PMID9362480
PMCPMC1170270
OpenAlexW2105798249

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.