Evidence map›Paper›PMID 20489202›Full record

ArticleThe Journal of biological chemistry2010

Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity.

Xiaofeng Li, Rong Zhang, Haifeng Zhang, Yun He, Weidong Ji, Wang Min, Titus J Boggon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
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  9. The multifacetedGenes & diseases · 2021
    Review
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  15. Vis-à-vis: a focus on genetic features of cerebral cavernous malformations and brain arteriovenous malformations pathogenesis.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2019
    Review
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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 1 institution in 1 country.

Xiaofeng LiDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.
Rong Zhang
Haifeng Zhang
Yun He
Weidong Ji
Wang Min
Titus J Boggon
Yale University · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Thioredoxin and Endothelial Cell FunctionR01HL085789 · NHLBI · YALE UNIVERSITY · PI MIN, WANG · 2008 to 2012
$2.1M
TNF receptor-2 signaling in arteriogenesis/angiogenesisR01HL077357 · NHLBI · YALE UNIVERSITY · PI MIN, WANG · 2007 to 2010
$1.7M
NHLBI NIH HHS HL085789NHLBI NIH HHS R01 HL077357NHLBI NIH HHS R01 HL085789NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

CCM3 mutations are associated with cerebral cavernous malformation (CCM), a disease affecting 0.1-0.5% of the human population. CCM3 (PDCD10, TFAR15) is thought to form a CCM complex with CCM1 and CCM2; however, the molecular basis for these interactions is not known. We have determined the 2.5 A crystal structure of CCM3. This structure shows an all alpha-helical protein containing two domains, an N-terminal dimerization domain with a fold not previously observed, and a C-terminal focal adhesion targeting (FAT)-homology domain. We show that CCM3 binds CCM2 via this FAT-homology domain and that mutation of a highly conserved FAK-like hydrophobic pocket (HP1) abrogates CCM3-CCM2 interaction. This CCM3 FAT-homology domain also interacts with paxillin LD motifs using the same surface, and partial CCM3 co-localization with paxillin in cells is lost on HP1 mutation. Disease-related CCM3 truncations affect the FAT-homology domain suggesting a role for the FAT-homology domain in the etiology of CCM.

Indexed as

Apoptosis Regulatory ProteinsBinding, CompetitiveBrainCrystallography, X-RayDimerizationHemangioma, Cavernous, Central Nervous SystemHumansKineticsMembrane ProteinsMolecular ConformationMutationPaxillinProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryApoptosis Regulatory ProteinsMembrane ProteinsPaxillinPDCD10 protein, humanProto-Oncogene Proteins

Identifiers

PMID20489202
PMCPMC2911348
OpenAlexW2047624114

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.