Evidence map›Paper›PMID 29662311›Full record

ArticleInternational journal of nanomedicine2018

The

Filomena A Carvalho, Ana Filipa Guedes, Cedric Duval, Fraser L Macrae, Luke Swithenbank, David H Farrell, Robert As Ariëns, Nuno C Santos

Open access · goldAbstract read
In one paragraph

Article in International journal of nanomedicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 3 institutions in 3 countries.

Filomena A Carvalho *Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisbon, Portugal.
Ana Filipa Guedes *Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisbon, Portugal.
Cedric DuvalTheme Thrombosis, Division of Cardiovascular and Diabetes Research, Leeds Institute for Genetics, Health and Therapeutics, University of Leeds, Leeds, UK.
Fraser L MacraeTheme Thrombosis, Division of Cardiovascular and Diabetes Research, Leeds Institute for Genetics, Health and Therapeutics, University of Leeds, Leeds, UK.
Luke SwithenbankTheme Thrombosis, Division of Cardiovascular and Diabetes Research, Leeds Institute for Genetics, Health and Therapeutics, University of Leeds, Leeds, UK.
David H FarrellDepartment of Surgery, Oregon Health and Science University, Portland, OR, USA.
Robert As AriënsTheme Thrombosis, Division of Cardiovascular and Diabetes Research, Leeds Institute for Genetics, Health and Therapeutics, University of Leeds, Leeds, UK.
Nuno C SantosInstituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Lisbon, Portugal.
University of Leeds · GBUniversity of Lisbon · PTOregon Health & Science University · US

Funding

British Heart Foundation RG/13/3/30104
6 · The paper itself

Abstract

backgroundErythrocyte aggregation, a cardiovascular risk factor, is increased by high plasma fibrinogen levels. Here, the effect of different fibrinogen mutations on binding to its human erythrocyte receptor was assessed in order to identify the interaction sites.

methodsThree fibrinogen variants were tested, specifically mutated in their putative integrin recognition sites on the Aα chain (mutants D97E, D574E and D97E/D574E) and compared with wild-type fibrinogen.

resultsAtomic force microscopy-based force spectroscopy measurements showed a significant decrease both on the fibrinogen-erythrocyte binding force and on its frequency for fibrinogen with the D97E mutation, indicating that the corresponding arginine-glycine-aspartate sequence (residues 95-97) is involved in this interaction, and supporting that the fibrinogen receptor on erythrocytes has a β

conclusionThese findings may lead to innovative perspectives on the development of new therapeutic approaches to overcome the risks of fibrinogen-driven erythrocyte hyperaggregation.

Indexed as

Binding SitesErythrocytesFibrinFibrinogenHumansIntegrinsMicroscopy, Atomic ForceMutationProtein BindingReceptors, FibrinogenThrombosisFibrinFibrinogenfibrinogen AalphaIntegrinsReceptors, Fibrinogenatomic force microscopyerythrocyte aggregationfibrin clotfibrinogenmutant protein

Identifiers

PMID29662311
PMCPMC5892956
OpenAlexW2796459286

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.