Evidence map›Paper›PMID 29414700›Full record

ArticleBiophysical journal2018

Structural Impact of Phosphorylation and Dielectric Constant Variation on Synaptotagmin's IDR.

Michael E Fealey, Benjamin P Binder, Vladimir N Uversky, Anne Hinderliter, David D Thomas

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Casein kinase 1 and disordered clock proteins form functionally equivalent, phospho-based circadian modules in fungi and mammals.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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

5 authors.

Michael E FealeyDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota.
Benjamin P BinderDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota.
Vladimir N UverskyDepartment of Molecular Medicine, University of South Florida, Tampa, Florida.
Anne HinderliterDepartment of Chemistry and Biochemistry, University of Minnesota Duluth, Duluth, Minnesota.
David D ThomasDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota. Electronic address: ddt@umn.edu.

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
NIAMS NIH HHS T32 AR007612
6 · The paper itself

Abstract

We used time-resolved Förster resonance energy transfer, circular dichroism, and molecular dynamics simulation to investigate the structural dependence of synaptotagmin 1's intrinsically disordered region (IDR) on phosphorylation and dielectric constant. We found that a peptide corresponding to the full-length IDR sequence, a ∼60-residue strong polyampholyte, can sample structurally collapsed states in aqueous solution, consistent with its κ-predicted behavior, where κ is a sequence-dependent parameter that is used to predict IDR compaction. In implicit solvent simulations of this same sequence, lowering the dielectric constant to more closely mimic the environment near a lipid bilayer surface promoted further sampling of collapsed structures. We then examined the structural tendencies of central region residues of the IDR in isolation. We found that the exocytosis-modulating phosphorylation of Thr

Indexed as

Protein ConformationHumansIntrinsically Disordered ProteinsMolecular Dynamics SimulationPeptide FragmentsPhosphorylationSynaptotagminsThreonineIntrinsically Disordered ProteinsPeptide FragmentsSynaptotagminsThreonine

Identifiers

PMID29414700
PMCPMC5985037

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.