Evidence map›Paper›PMID 22851002›Full record

ArticleEuropean biophysics journal : EBJ2012

The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction.

Shobhna Kapoor, Katrin Weise, Mirko Erlkamp, Gemma Triola, Herbert Waldmann, Roland Winter

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
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

43 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Machine learning-driven multiscale modeling reveals lipid-dependent dynamics of RAS signaling proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Unveiling the Dynamics of KRAS4b on Lipid Model Membranes.The Journal of membrane biology · 2021
    Article
  14. The KRAS and other prenylated polybasic domain membrane anchors recognize phosphatidylserine acyl chain structure.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  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

6 authors.

Shobhna KapoorPhysical Chemistry I, Biophysical Chemistry, Faculty of Chemistry, TU Dortmund University, Otto-Hahn-Str. 6, 44227, Dortmund, Germany.
Katrin Weise
Mirko Erlkamp
Gemma Triola
Herbert Waldmann
Roland Winter

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ras proteins are proto-oncogenes that function as molecular switches linking extracellular stimuli with an overlapping but distinctive range of biological outcomes. Although modulatable interactions between the membrane and the Ras C-terminal hypervariable region (HVR) harbouring the membrane anchor motifs enable signalling specificity to be determined by their location, it is becoming clear that the spatial orientation of different Ras proteins is also crucial for their functions. To reveal the orientation of the G-domain at membranes, we conducted an extensive study on different Ras isoforms anchored to model raft membranes. The results show that the G-domain mediates the Ras-membrane interaction by inducing different sets of preferred orientations in the active and inactive states with largely parallel orientation relative to the membrane of most of the helices. The distinct locations of the different isoforms, exposing them to different effectors and regulators, coupled with different G-domain-membrane orientation, suggests synergy between this type of recognition motif and the specificity conferred by the HVR, thereby validating the concept of isoform specificity in Ras.

Indexed as

Guanosine DiphosphateGuanosine TriphosphateLipid BilayersMembrane MicrodomainsMicroscopy, Atomic ForceMolecular Dynamics SimulationProtein IsoformsProtein Structure, TertiaryProto-Oncogene Proteins p21(ras)Spectroscopy, Fourier Transform InfraredGuanosine DiphosphateGuanosine TriphosphateLipid BilayersProtein IsoformsProto-Oncogene Proteins p21(ras)

Identifiers

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.