Evidence map›Paper›PMID 18789696›Full record

ReviewTrends in biochemical sciences2008

The CCN family of proteins: structure-function relationships.

Kenneth P Holbourn, K Ravi Acharya, Bernard Perbal

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 241 papers.

0numbers the graph read from it
0cells of the map it votes in
241citing papers in PubMed
–field-weighted citation impact
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

241 citing papers in PubMed.

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  18. Molecular Consequences ofInternational journal of molecular sciences · 2025
    Article
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181 more citing papers are in PubMed but not listed here.

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

3 authors.

Kenneth P HolbournDepartment of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
K Ravi Acharya
Bernard Perbal

Funding

Wellcome TrustWellcome Trust 083191
6 · The paper itself

Abstract

The CCN proteins are key signalling and regulatory molecules involved in many vital biological functions, including cell proliferation, angiogenesis, tumourigenesis and wound healing. How these proteins influence such a range of functions remains incompletely understood but is probably related to their discrete modular nature and a complex array of intra- and inter-molecular interactions with a variety of regulatory proteins and ligands. Although certain aspects of their biology can be attributed to the four individual modules that constitute the CCN proteins, recent results suggest that some of their biological functions require cooperation between modules. Indeed, the modular structure of CCN proteins provides important insight into their structure-function relationships.

Indexed as

Amino Acid SequenceAnimalsCCN Intercellular Signaling ProteinsCell DivisionHumansInsulin-Like Growth Factor Binding ProteinsModels, MolecularMolecular Sequence DataNeoplasmsNeovascularization, PhysiologicProtein ConformationSequence AlignmentSequence Homology, Amino AcidWound HealingCCN Intercellular Signaling ProteinsInsulin-Like Growth Factor Binding Proteins

Identifiers

PMID18789696
PMCPMC2683937

What Socratic 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 Socratic graph.