Evidence map›Paper›PMID 27144715›Full record

ArticleChemMedChem2016

The Cell Surface Receptor CD44: NMR-Based Characterization of Putative Ligands.

Carlo Baggio, Elisa Barile, Gianluigi Di Sorbo, Thomas J Kipps, Maurizio Pellecchia

Abstract read
In one paragraph

Article in ChemMedChem, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
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    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

5 authors at 3 institutions in 1 country.

Carlo BaggioDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, CA, 92521, USA.
Elisa BarileDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, CA, 92521, USA.
Gianluigi Di SorboSanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Thomas J KippsDivision of Hematology/Oncology, Department of Medicine, University of California San Diego, 9500 Gilman Drive, La Jolla, CA, 92093, USA.
Maurizio PellecchiaDivision of Biomedical Sciences, School of Medicine, University of California Riverside, 900 University Avenue, Riverside, CA, 92521, USA. maurizio.pellecchia@ucr.edu.
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of California, Riverside · USUniversity of California, San Diego · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
Tissue CoreP01CA081534 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KIPPS, THOMAS J · 2000 to 2016
$59.5M
Mcl-1 in apoptosis and signal transduction: a structure/function approachR01CA168517 · NCI · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI PELLECCHIA, MAURIZIO · 2012 to 2024
$4.7M
NCI NIH HHS P01 CA081534NCI NIH HHS P30 CA030199NCI NIH HHS R01 CA168517
6 · The paper itself

Abstract

The cell surface receptor CD44 is a glycoprotein belonging to the hyaluronan-binding proteins, termed hyaladherins. CD44 is expressed in a wide variety of isoforms in many cells and, in particular, is present on the surface of malignant cells where it is involved in the onset and progression of cancer. In a first attempt to identify novel CD44-binding agents, we first characterized, with NMR spectroscopic techniques, several agents that were reported to bind to human CD44 (hCD44). To our surprise, however, none of these putative CD44-binding agents, including a peptide that is in phase 2 clinical trials (A6 peptide) and a recently reported fragment hit, were found to interact significantly with recombinant hCD44(21-178). Nonetheless, we further report that a fragment-screening campaign, with solution NMR spectroscopy as the detection method, identified a viable fragment hit that bound in a potentially functional pocket on the surface of CD44, opposite to the hyaluronic acid binding site. We hypothesize that this pocket could be indirectly associated with the cellular and in vivo activity of the A6 peptide, which would provide a novel framework for the possible development of therapeutically viable CD44 antagonists.

Indexed as

LigandsAmino Acid SequenceBinding SitesCalorimetryHumansHyaluronan ReceptorsNuclear Magnetic Resonance, BiomolecularPeptidesProtein BindingRecombinant ProteinsCD44 protein, humanHyaluronan ReceptorsLigandsPeptidesRecombinant Proteinscell recognitiondrug discoveryinhibitorspeptidesprotein-protein interactions

Identifiers

PMID27144715
PMCPMC5271563
OpenAlexW2345579719

What OpenQuestion holds

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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.