Evidence map›Paper›PMID 28296537›Full record

ArticleSLAS discovery : advancing life sciences R & D2017

Microfluidic Mobility Shift Assay for Real-Time Analysis of Peptide N-Palmitoylation.

Thomas Lanyon-Hogg, Neki V Patel, Markus Ritzefeld, Katherine J Boxall, Rosemary Burke, Julian Blagg, Anthony I Magee, Edward W Tate

Open access · hybridAbstract read
In one paragraph

Article in SLAS discovery : advancing life sciences R & D, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Thomas Lanyon-Hogg1 Department of Chemistry, Imperial College London, London, UK.
Neki V Patel1 Department of Chemistry, Imperial College London, London, UK.
Markus Ritzefeld1 Department of Chemistry, Imperial College London, London, UK.
Katherine J Boxall2 Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London, UK.
Rosemary Burke2 Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London, UK.
Julian Blagg2 Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London, UK.
Anthony I Magee3 Molecular Medicine Section, National Heart & Lung Institute, Imperial College London, London, UK.
Edward W Tate1 Department of Chemistry, Imperial College London, London, UK.
Imperial College London · GBCancer Research UK · GBInstitute of Cancer Research · GB

Funding

Cancer Research UK 11566Cancer Research UK 16402Cancer Research UK 20183Cancer Research UK C6433/A16402
6 · The paper itself

Abstract

The Hedgehog pathway is a key developmental signaling pathway but is also implicated in many types of cancer. The extracellular signaling protein Sonic hedgehog (Shh) requires dual lipidation for functional signaling, whereby N-terminal palmitoylation is performed by the enzyme Hedgehog acyltransferase (Hhat). Hhat is an attractive target for small-molecule inhibition to arrest Hedgehog signaling, and methods for assaying Hhat activity are central to understanding its function. However, all existing assays to quantify lipidation of peptides suffer limitations, such as safety hazards, high costs, extensive manual handling, restriction to stopped-assay measurements, or indirect assessment of lipidation. To address these limitations, we developed a microfluidic mobility shift assay (MSA) to analyze Shh palmitoylation. MSA allowed separation of fluorescently labeled Shh amine-substrate and palmitoylated Shh amide-product peptides based on differences in charge and hydrodynamic radius, coupled with online fluorescence intensity measurements for quantification. The MSA format was employed to study Hhat-catalyzed reactions, investigate Hhat kinetics, and determine small-molecule inhibitor IC

Indexed as

Protein Processing, Post-TranslationalAcyltransferasesAmino Acid SequenceElectrophoretic Mobility Shift AssayEnzyme AssaysEnzyme InhibitorsHedgehog ProteinsHEK293 CellsHumansKineticsLipoylationMicrofluidicsRecombinant ProteinsAcyltransferasesEnzyme InhibitorsHedgehog ProteinsHHAT protein, humanRecombinant ProteinsSHH protein, humanenzyme assays or enzyme kineticsfluorescence methodslipids or lipid metabolismmedicinal chemistry

Identifiers

PMID28296537
PMCPMC5453399
OpenAlexW2606268014

What OpenQuestion holds

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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.