Evidence map›Paper›PMID 25394204›Full record

ArticleBiochemistry and cell biology = Biochimie et biologie cellulaire2014

Discovery of novel membrane binding structures and functions.

Irina Kufareva, Marc Lenoir, Felician Dancea, Pooja Sridhar, Eugene Raush, Christin Bissig, Jean Gruenberg, Ruben Abagyan, Michael Overduin

Open access · greenAbstract read
In one paragraph

Article in Biochemistry and cell biology = Biochimie et biologie cellulaire, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

32 citing papers in PubMed, 54 citations in OpenAlex.

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  17. Multifaceted membrane binding head of the SARS-CoV-2 spike protein.Current research in structural biology · 2022
    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

9 authors at 4 institutions in 3 countries.

Irina Kufarevaa Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Marc Lenoir
Felician Dancea
Pooja Sridhar
Eugene Raush
Christin Bissig
Jean Gruenberg
Ruben Abagyan
Michael Overduin
University of Birmingham · GBUniversity of California, San Diego · USUniversity of Geneva · CHMolsoft (United States) · US

Funding

Project 3U54GM094618 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STEVENS, RAYMOND C · 2010 to 2014
$17.1M
Structure, Dynamics and Activation Mechanisms of Chemokine ReceptorsU01GM094612 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHANCE, MARK R · 2010 to 2014
$4.5M
Macromolecular DockingR01GM071872 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ABAGYAN, RUBEN · 2004 to 2017
$4.2M
Biotechnology and Biological Sciences Research Council BB/C511513/1Biotechnology and Biological Sciences Research Council BB/E013198/1Biotechnology and Biological Sciences Research Council BB/H019383/1Biotechnology and Biological Sciences Research Council BB/H024697/1Biotechnology and Biological Sciences Research Council BBS/B/10714NIGMS NIH HHS R01 GM071872NIGMS NIH HHS U01 GM094612NIGMS NIH HHS U54 GM094618Wellcome Trust
6 · The paper itself

Abstract

The function of a protein is determined by its intrinsic activity in the context of its subcellular distribution. Membranes localize proteins within cellular compartments and govern their specific activities. Discovering such membrane-protein interactions is important for understanding biological mechanisms and could uncover novel sites for therapeutic intervention. We present a method for detecting membrane interactive proteins and their exposed residues that insert into lipid bilayers. Although the development process involved analysis of how C1b, C2, ENTH, FYVE, Gla, pleckstrin homology (PH), and PX domains bind membranes, the resulting membrane optimal docking area (MODA) method yields predictions for a given protein of known three-dimensional structures without referring to canonical membrane-targeting modules. This approach was tested on the Arf1 GTPase, ATF2 acetyltransferase, von Willebrand factor A3 domain, and Neisseria gonorrhoeae MsrB protein and further refined with membrane interactive and non-interactive FAPP1 and PKD1 pleckstrin homology domains, respectively. Furthermore we demonstrate how this tool can be used to discover unprecedented membrane binding functions as illustrated by the Bro1 domain of Alix, which was revealed to recognize lysobisphosphatidic acid (LBPA). Validation of novel membrane-protein interactions relies on other techniques such as nuclear magnetic resonance spectroscopy (NMR), which was used here to map the sites of micelle interaction. Together this indicates that genome-wide identification of known and novel membrane interactive proteins and sites is now feasible and provides a new tool for functional annotation of the proteome.

Indexed as

Bacterial ProteinsCell MembraneHumansMembrane ProteinsMolecular Sequence AnnotationNeisseria gonorrhoeaeProtein Structure, TertiaryProteomeSequence Analysis, ProteinBacterial ProteinsMembrane ProteinsProteomeannotation de la structure des protéinesbilayer insertioniditification de site d’interaction lipidiqueinsertion dans la bi-couche lipidiqueinteraction phospholipidiqueinterface des interactions membranaireslipid site identificationmembrane interaction interfaceperipheral membrane proteinphospholipid interactionprotéine membranaire périphériqueprotein structure annotation

Identifiers

PMID25394204
PMCPMC4267288
OpenAlexW2021284204

What OpenQuestion holds

Textmetadata
LicenceTDM
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.