Evidence map›Paper›PMID 28831766›Full record

ArticleBiomolecular NMR assignments2017

NMR resonance assignments of the EVH1 domain of neurofibromin's recruitment factor Spred1.

Sebastian Führer, Linda Ahammer, Angela Ausserbichler, Klaus Scheffzek, Theresia Dunzendorfer-Matt, Martin Tollinger

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

Article in Biomolecular NMR assignments, 2017. 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
0.3field-weighted citation impact, top 45% 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. The role of SPRED1 mutation in melanoma.European journal of medical research · 2025
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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

6 authors at 2 institutions in 1 country.

Sebastian FührerCenter for Molecular Biosciences Innsbruck (CMBI), Institute of Organic Chemistry, University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
Linda AhammerCenter for Molecular Biosciences Innsbruck (CMBI), Institute of Organic Chemistry, University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
Angela AusserbichlerDivision of Biological Chemistry, Biocenter, Medical University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
Klaus ScheffzekDivision of Biological Chemistry, Biocenter, Medical University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
Theresia Dunzendorfer-MattDivision of Biological Chemistry, Biocenter, Medical University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria. theresia.dunzendorfer-matt@i-med.ac.at.
Martin TollingerCenter for Molecular Biosciences Innsbruck (CMBI), Institute of Organic Chemistry, University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria. martin.tollinger@uibk.ac.at.ORCID 0000-0002-2177-983X
Innsbruck Medical University · ATUniversität Innsbruck · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurofibromin and Sprouty-related EVH1 domain-containing protein 1 (Spred1) both act as negative regulators of the mitogen-activated protein kinase pathway and are associated with the rare diseases Neurofibromatosis type 1 and Legius syndrome, respectively. Spred1 recruits the major GTPase activating protein (GAP) neurofibromin from the cytosol to the membrane in order to inactivate the small G protein Ras. These functions are dependent on the N-terminal EVH1 domain and the C-terminal Sprouty domain of Spred1 whereas the former specifically recognizes the GAP related domain of neurofibromin and the latter is responsible for membrane targeting. Within the GAP domain, Spred1 binding depends on the GAPex portion which is dispensable for Ras inactivation. In a first step towards the characterization of the Neurofibromin Spred1 interface in solution we assigned backbone and side chain

Indexed as

Nuclear Magnetic Resonance, BiomolecularAdaptor Proteins, Signal TransducingIntracellular Signaling Peptides and ProteinsMembrane ProteinsNeurofibromin 1Protein DomainsAdaptor Proteins, Signal TransducingIntracellular Signaling Peptides and ProteinsMembrane ProteinsNeurofibromin 1SPRED1 protein, humanLegius syndromeNMR resonance assignmentProtein purificationTALOS+ prediction

Identifiers

PMID28831766
PMCPMC5594049
OpenAlexW2748722825

What OpenQuestion 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 OpenQuestion graph.