Evidence map›Paper›PMID 27182435›Full record

ArticleRSC advances2012

NMR relaxation and structural elucidation of peptides in the presence and absence of trifluoroethanol illuminates the critical molecular nature of integrin αvβ6 ligand specificity.

Jane L Wagstaff, Michelle L Rowe, Shu-Ju Hsieh, Danielle DiCara, John F Marshall, Richard A Williamson, Mark J Howard

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC advances, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

7 authors.

Jane L WagstaffProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Michelle L RoweProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Shu-Ju HsiehProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK; Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Danielle DiCaraQueen Mary University of London, Barts and The London School of Medicine and Dentistry, Institute of Cancer and CRUK Clinical Centre, John Vane Science Centre, Charterhouse Square, London, EC1M 6BQ, UK; MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.
John F MarshallQueen Mary University of London, Barts and The London School of Medicine and Dentistry, Institute of Cancer and CRUK Clinical Centre, John Vane Science Centre, Charterhouse Square, London, EC1M 6BQ, UK.
Richard A WilliamsonProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Mark J HowardProtein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.

Funding

Wellcome Trust 091163
6 · The paper itself

Abstract

Integrin αvβ6 is an important emerging target for both imaging and therapy of cancer that requires specific ligands based on Arg-Gly-Asp (RGD) peptides. There remains little correlation between integrin-RGD ligand specificity despite studies suggesting an RGD-turn-helix ligand motif is required. Here, we describe the application of

Identifiers

PMID27182435
PMCPMC4864471

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Registered trials

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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.