Evidence map›Paper›PMID 25004970›Full record

ArticleActa crystallographica. Section D, Biological crystallography2014

Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions.

Rosario Recacha, David Jiménez, Li Tian, Román Barredo, Carl G Gahmberg, José M Casasnovas

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Solution Structure of theFrontiers in cellular and infection microbiology · 2022
    Article
  2. ICAM5 as a Novel Target for Treating Cognitive Impairment in Fragile X Syndrome.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  3. Article
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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

6 authors at 1 institution in 1 country.

Rosario RecachaCentro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3,, 28049 Madrid, Spain.
David JiménezCentro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3,, 28049 Madrid, Spain.
Li TianNeuroscience Center, University of Helsinki, 00014 Helsinki, Finland.
Román BarredoCentro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3,, 28049 Madrid, Spain.
Carl G GahmbergDivision of Biochemistry and Biotechnology, University of Helsinki, 00014 Helsinki, Finland.
José M CasasnovasCentro Nacional de Biotecnología (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3,, 28049 Madrid, Spain.
University of Helsinki · FI

Funding

TIM recognition of phosphatidylserine regulates innate and adaptive immunityP01AI054456 · NIAID · STANFORD UNIVERSITY · PI FREEMAN, GORDON JAMES · 2003 to 2014
$12.8M
NIAID NIH HHS 2P01AI054456-06A1NIAID NIH HHS P01 AI054456
6 · The paper itself

Abstract

Intercellular cell adhesion molecule-5 (ICAM-5) is a member of the ICAM subfamily that is exclusively expressed in the telencephalon region of the brain. The crystal structure of the four most N-terminal glycosylated domains (D1-D4) of ICAM-5 was determined in three different space groups and the D1-D5 fragment was modelled. The structures showed a curved molecule with two pronounced interdomain bends between D2 and D3 and between D3 and D4, as well as some interdomain flexibility. In contrast to ICAM-1, ICAM-5 has patches of positive and negative electrostatic charge at D1-D2 and at D3-D5, respectively. ICAM-5 can mediate homotypic interactions. In the crystals, several charge-based intermolecular interactions between the N-terminal and C-terminal moieties of the ICAM-5 molecules were observed, which defined an interacting surface in the D1-D4 fragment. One of the crystal lattices has a molecular assembly that could represent the homophilic ICAM-5 cell adhesion complex in neurons.

Indexed as

Amino Acid SequenceCell Adhesion MoleculesCrystallography, X-RayHumansMolecular Sequence DataNerve Tissue ProteinsProtein ConformationSequence Homology, Amino AcidStatic ElectricityCell Adhesion MoleculesICAM5 protein, humanNerve Tissue Proteinscell adhesionICAM-5immunoglobulin superfamilyneuron

Identifiers

PMID25004970
PMCPMC4089487
OpenAlexW2130407567

What OpenQuestion 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 OpenQuestion graph.