Evidence map›Paper›PMID 19798736›Full record

ArticleProtein science : a publication of the Protein Society2009

Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.

Fabien Kieken, Marko Jović, Marco Tonelli, Naava Naslavsky, Steve Caplan, Paul L Sorgen

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

24 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
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  13. Review
  14. Structural insights into the activation mechanism of dynamin-like EHD ATPases.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

6 authors at 2 institutions in 1 country.

Fabien KiekenDepartment of Biochemistry and Molecular Biology and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, Nebraska 68198-5870, USA.
Marko Jović
Marco Tonelli
Naava Naslavsky
Steve Caplan
Paul L Sorgen
University of Nebraska Medical Center · USUniversity of Wisconsin–Madison · US

Funding

SUPPRESSIVE ROLE OF TGFBETA IN METASTASIS OF COLON CANCERP20RR018759 · NCRR · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2003 to 2011
$17.9M
WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
Mechanisms of Gap Junction RegulationR01GM072631 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI SORGEN, PAUL L · 2006 to 2025
$6.4M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Molecular Mechanisms Controlling Endocytic RecyclingR01GM074876 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2006 to 2015
$2.6M
Regulation of EHD protein function by molecular partner interactionsR01GM087455 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H, SORGEN, PAUL L · 2010 to 2013
$1.1M
NCRR NIH HHS P20RR018759NCRR NIH HHS P41RR02301NIGMS NIH HHS GM072631NIGMS NIH HHS GM074876NIGMS NIH HHS P41GM66326NIGMS NIH HHS R01 GM074876NIGMS NIH HHS R01 GM087455
6 · The paper itself

Abstract

Eps15 homology (EH)-domain containing proteins are regulators of endocytic membrane trafficking. EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs. We demonstrate that the three motifs interact in a similar way with the EH-domain of EHD1, with the NPF motif having the highest affinity due to the presence of an intermolecular hydrogen bond. The weaker affinity for the DPF and GPF motifs suggests that if complex formation occurs in vivo, they may require high ligand concentrations, the presence of successive motifs and/or specific flanking residues.

Indexed as

Amino Acid MotifsHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularPeptidesProtein BindingProtein Structure, TertiaryVesicular Transport ProteinsEHD1 protein, humanPeptidesVesicular Transport Proteins

Identifiers

PMID19798736
PMCPMC2821266
OpenAlexW2042897083

What OpenQuestion holds

Textmetadata
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.