Evidence map›Paper›PMID 29045874›Full record

ArticleBiophysical journal2017

Dynamic Scaling Analysis of Molecular Motion within the LAT:Grb2:SOS Protein Network on Membranes.

William Y C Huang, Han-Kuei Chiang, Jay T Groves

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. A unifying model of LAT condensates in reconstitution experiments.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Self-programmed dynamics of T cell receptor condensation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A two-component protein condensate of the EGFR cytoplasmic tail and Grb2 regulates Ras activation by SOS at the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Biomolecular condensates in membrane receptor signaling.Current opinion in cell biology · 2021
    Review
  14. Raf promotes dimerization of the Ras G-domain with increased allosteric connections.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

William Y C HuangDepartment of Chemistry, University of California, Berkeley, Berkeley, California.
Han-Kuei ChiangDepartment of Chemistry, University of California, Berkeley, Berkeley, California.
Jay T GrovesDepartment of Chemistry, University of California, Berkeley, Berkeley, California. Electronic address: jtgroves@lbl.gov.
University of California, Berkeley · US

Funding

ECM geometrical and mechanical properties modulate RTK signalingU01CA202241 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI GROVES, JAY T., WEAVER, VALERIE MARIE · 2015 to 2019
$3.3M
NCI NIH HHS U01 CA202241
6 · The paper itself

Abstract

Biochemical signaling pathways often involve proteins with multiple, modular interaction domains. Signaling activates binding sites, such as by tyrosine phosphorylation, which enables protein recruitment and growth of networked protein assemblies. Although widely observed, the physical properties of the assemblies, as well as the mechanisms by which they function, remain largely unknown. Here we examine molecular mobility within LAT:Grb2:SOS assemblies on supported membranes by single-molecule tracking. Trajectory analysis reveals a discrete temporal transition to subdiffusive motion below a characteristic timescale, indicating that the LAT:Grb2:SOS assembly has the dynamical structure of a loosely entangled polymer. Such dynamical analysis is also applicable in living cells, where it offers another dimension on the characteristics of cellular signaling assemblies.

Indexed as

Membranes, ArtificialAdaptor Proteins, Signal TransducingComputer SimulationDiffusionGRB2 Adaptor ProteinHumansMembrane ProteinsMonte Carlo MethodMotionPhosphotyrosinePolymersSingle Molecule ImagingSon of Sevenless Protein, DrosophilaViscoelastic SubstancesAdaptor Proteins, Signal TransducingGRB2 Adaptor ProteinGRB2 protein, humanLAT protein, humanMembrane ProteinsMembranes, ArtificialPhosphotyrosinePolymersSon of Sevenless Protein, DrosophilaViscoelastic Substances

Identifiers

PMID29045874
PMCPMC5647511
OpenAlexW2766755842

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.