Evidence map›Paper›PMID 30360356›Full record

ArticleMolecules (Basel, Switzerland)2018

NMR Structure of μ-Conotoxin GIIIC: Leucine 18 Induces Local Repacking of the N-Terminus Resulting in Reduced Na

Peta J Harvey, Nyoman D Kurniawan, Rocio K Finol-Urdaneta, Jeffrey R McArthur, Dorien Van Lysebetten, Thomas S Dash, Justine M Hill, David J Adams, Thomas Durek, David J Craik

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. 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

10 authors at 2 institutions in 1 country.

Peta J HarveyInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. peta.harvey@imb.uq.edu.au.
Nyoman D KurniawanInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. nyoman.kurniawan@cai.uq.edu.au.
Rocio K Finol-UrdanetaIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong 2522, Australia. rfinolu@uow.edu.au.
Jeffrey R McArthurIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong 2522, Australia. jeffreym@uow.edu.au.ORCID 0000-0002-2546-7913
Dorien Van LysebettenInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. Dorien.VanLysebetten@UGent.be.
Thomas S DashInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. thomas.dash@imb.uq.edu.au.
Justine M HillInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. justine.hill1@gmail.com.
David J AdamsIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong 2522, Australia. djadams@uow.edu.au.ORCID 0000-0002-7030-2288
Thomas DurekInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. t.durek@uq.edu.au.
David J CraikInstitute for Molecular Bioscience, The University of Queensland, Brisbane 4072, Australia. d.craik@imb.uq.edu.au.
The University of Queensland · AUUniversity of Wollongong · AU

Funding

Australian Research Council FL150100146National Health and Medical Research Council APP1072113
6 · The paper itself

Abstract

μ-Conotoxins are potent and highly specific peptide blockers of voltage-gated sodium channels. In this study, the solution structure of μ-conotoxin GIIIC was determined using 2D NMR spectroscopy and simulated annealing calculations. Despite high sequence similarity, GIIIC adopts a three-dimensional structure that differs from the previously observed conformation of μ-conotoxins GIIIA and GIIIB due to the presence of a bulky, non-polar leucine residue at position 18. The side chain of L18 is oriented towards the core of the molecule and consequently the N-terminus is re-modeled and located closer to L18. The functional characterization of GIIIC defines it as a canonical μ-conotoxin that displays substantial selectivity towards skeletal muscle sodium channels (Na

Indexed as

Magnetic Resonance SpectroscopyAmino Acid SequenceConotoxinsDisulfidesLeucineModels, MolecularPeptidesProtein ConformationProtein Interaction Domains and MotifsSodium Channel BlockersSodium ChannelsStructure-Activity Relationshipconotoxin GIIIConotoxinsDisulfidesLeucinePeptidesSodium Channel BlockersSodium ChannelsNMRprotein structurevoltage-gated sodium channel blockerμ-conotoxins

Identifiers

PMID30360356
PMCPMC6222493
OpenAlexW2896951540

What Socratic 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 Socratic graph.