Evidence map›Paper›PMID 25461777›Full record

ReviewMethods (San Diego, Calif.)2015

Membrane association of the PTEN tumor suppressor: neutron scattering and MD simulations reveal the structure of protein-membrane complexes.

Hirsh Nanda, Frank Heinrich, Mathias Lösche

Abstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural and Dynamic Effects of PTEN C-Terminal Tail Phosphorylation.Journal of chemical information and modeling · 2022
    Article
  7. Binding of CaStructure (London, England : 1993) · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structural Mechanisms of PTEN Regulation.Cold Spring Harbor perspectives in medicine · 2020
    Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

3 authors at 3 institutions in 1 country.

Hirsh NandaDepartment of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA; NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA.
Frank HeinrichDepartment of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA; NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA.
Mathias LöscheDepartment of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA; Department of Biomedical Engineering, Carnegie Mellon University, Pittsburgh, PA 15213, USA; NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA. Electronic address: quench@cmu.edu.
Carnegie Mellon University · USNational Institute of Standards and Technology · USNIST Center for Neutron Research · US

Funding

Membrane Coupling and Dynamic Reorganization of Gag in Viral BuddingR01GM101647 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LOESCHE, MATHIAS · 2012 to 2015
$1.2M
NIGMS NIH HHS 1R01 GM101647NIGMS NIH HHS R01 GM101647
6 · The paper itself

Abstract

Neutron reflection (NR) from planar interfaces is an emerging technology that provides unique and otherwise inaccessible structural information on disordered molecular systems such as membrane proteins associated with fluid bilayers, thus addressing one of the remaining challenges of structural biology. Although intrinsically a low-resolution technique, using structural information from crystallography or NMR allows the construction of NR models that describe the architecture of protein-membrane complexes at high resolution. In addition, a combination of these methods with molecular dynamics (MD) simulations has the potential to reveal the dynamics of protein interactions with the bilayer in atomistic detail. We review recent advances in this area by discussing the application of these techniques to the complex formed by the PTEN phosphatase with the plasma membrane. These studies provide insights in the cellular regulation of PTEN, its interaction with PI(4,5)P2 in the inner plasma membrane and the pathway by which its substrate, PI(3,4,5)P3, accesses the PTEN catalytic site.

Indexed as

Molecular Dynamics SimulationAnimalsCell MembraneHumansNeutron DiffractionProtein Structure, SecondaryProtein Structure, TertiaryPTEN PhosphohydrolaseTumor Suppressor ProteinsPTEN PhosphohydrolasePTEN protein, humanTumor Suppressor ProteinsMolecular dynamics simulationsNeutron reflectionPhosphatidylinositolphosphatePhosphatidylserineProtein–membrane complexPTENTethered bilayer lipid membranes

Identifiers

PMID25461777
PMCPMC4388770
OpenAlexW2148349807

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.