Evidence map›Paper›PMID 15014436›Full record

ArticleThe EMBO journal2004

Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats.

Marc Kvansakul, Josephine C Adams, Erhard Hohenester

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
4.7field-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

87 citing papers in PubMed, 160 citations in OpenAlex.

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  10. Pathophysiological roles of thrombospondin-4 in disease development.Seminars in cell & developmental biology · 2024
    Review
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27 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 at 2 institutions in 2 countries.

Marc KvansakulDepartment of Biological Sciences, Imperial College London, South Kensington Campus, London, UK.
Josephine C Adams
Erhard Hohenester
Imperial College London · GBCleveland Clinic · US

Funding

Wellcome Trust 054334
6 · The paper itself

Abstract

Thrombospondins (TSPs) are extracellular regulators of cell-matrix interactions and cell phenotype. The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD). The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly. The T3 repeats lack secondary structure and are organised around a core of calcium ions; two DxDxDGxxDxxD motifs per repeat each encapsulate two calcium ions in a novel arrangement. The CTD forms a lectin-like beta-sandwich and contains four strictly conserved calcium-binding sites. Disruption of the hairpin structure of T3 repeats 6 and 7 decreases protein secretion and stability. The availability for cell attachment of an RGD motif in T3 repeat 7 is modulated by calcium loading. The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region. Mutations in the T3 repeats of TSP-5/COMP, which cause two human skeletal disorders, are predicted to disrupt the tertiary structure of the T3-CTD assembly.

Indexed as

Repetitive Sequences, Amino AcidAmino Acid SequenceAnimalsBinding SitesCalciumCell AdhesionCell LineCrystallography, X-RayHumansMiceModels, MolecularMolecular Sequence DataMutationOligopeptidesPeptide FragmentsProtein Structure, Tertiaryarginyl-glycyl-aspartic acidCalciumOligopeptidesPeptide FragmentsThrombospondin 1

Identifiers

PMID15014436
PMCPMC381422
OpenAlexW2006647502

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.