Evidence map›Paper›PMID 26512702›Full record

ArticleMembranes2015

Membrane and Protein Interactions of the Pleckstrin Homology Domain Superfamily.

Marc Lenoir, Irina Kufareva, Ruben Abagyan, Michael Overduin

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Multifaceted membrane binding head of the SARS-CoV-2 spike protein.Current research in structural biology · 2022
    Article
  13. Frontiers in cell and developmental biology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021
    Article
  19. Review
  20. Review
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

4 authors at 3 institutions in 3 countries.

Marc LenoirSchool of Cancer Sciences, Faculty of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, UK. m.lenoir@bham.ac.uk.
Irina KufarevaSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA. ikufareva@ucsd.edu.
Ruben AbagyanSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA. rabagyan@ucsd.edu.
Michael OverduinDepartment of Biochemistry, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, AB T6G 2H7, Canada. overduin@ualberta.ca.
University of California, San Diego · USUniversity of Alberta · CAUniversity of Birmingham · GB

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
NIGMS NIH HHS R01 GM071872NIGMS NIH HHS U01 GM094612NIGMS NIH HHS U54 GM094618
6 · The paper itself

Abstract

The human genome encodes about 285 proteins that contain at least one annotated pleckstrin homology (PH) domain. As the first phosphoinositide binding module domain to be discovered, the PH domain recruits diverse protein architectures to cellular membranes. PH domains constitute one of the largest protein superfamilies, and have diverged to regulate many different signaling proteins and modules such as Dbl homology (DH) and Tec homology (TH) domains. The ligands of approximately 70 PH domains have been validated by binding assays and complexed structures, allowing meaningful extrapolation across the entire superfamily. Here the Membrane Optimal Docking Area (MODA) program is used at a genome-wide level to identify all membrane docking PH structures and map their lipid-binding determinants. In addition to the linear sequence motifs which are employed for phosphoinositide recognition, the three dimensional structural features that allow peripheral membrane domains to approach and insert into the bilayer are pinpointed and can be predicted ab initio. The analysis shows that conserved structural surfaces distinguish which PH domains associate with membrane from those that do not. Moreover, the results indicate that lipid-binding PH domains can be classified into different functional subgroups based on the type of membrane insertion elements they project towards the bilayer.

Indexed as

bilayer insertionlipid bindingmembrane traffickingMODAperipheral membrane proteinPH domainphosphoinositide recognitionplasma membranepleckstrin homology domainsmall GTPase

Identifiers

PMID26512702
PMCPMC4704004
OpenAlexW1825956673

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.