Evidence map›Paper›PMID 16949547›Full record

ArticleArchives of biochemistry and biophysics2006

Studies on titin PEVK peptides and their interaction.

Yingli Duan, Joshua G DeKeyser, Srinivasan Damodaran, Marion L Greaser

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Regulation of Poly-E Motif Flexibility by pH, CaInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Intrinsic disorder in scaffold proteins: getting more from less.Progress in biophysics and molecular biology · 2008
    Review
  12. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Yingli DuanMuscle Biology Laboratory, University of Wisconsin-Madison, Madison, WI 53706, USA.
Joshua G DeKeyser
Srinivasan Damodaran
Marion L Greaser
University of Wisconsin–Madison · US

Funding

Titin Splicing Mechanisms and Physical ImplicationsR01HL077196 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI GREASER, MARION LEWIS · 2004 to 2010
$1.9M
ACQUISITION OF MASS SPECTROMETER FOR CORE FACILITYS10RR013790 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI RAINES, RONALD T · 1999 to 1999
–
NCRR NIH HHS RR13790NCRR NIH HHS S10 RR013790NHLBI NIH HHS HL77196NHLBI NIH HHS R01 HL077196
6 · The paper itself

Abstract

Experiments were conducted on several synthetic and expressed peptides from the PEVK region of titin, the giant muscle protein. Different secondary structure prediction methods based on amino acid sequence gave estimates ranging from over 70% alpha helical to no helix (totally disordered) for the polyE peptide corresponding to human exon 115. Circular dichroism (CD) experiments demonstrated that both the positively charged PPAK modules and the negatively charged PolyE repeats had similar spectral properties with disordered secondary structure predominating. Gel permeation chromatography showed that both PPAK and polyE peptides had 2-4 times larger Stokes radii than expected from their molecular mass. Mixtures of the oppositely charged titin peptides caused no change in apparent secondary structure as observed by circular dichroism or migration properties using native gel electrophoresis. Similarly addition of calcium did not alter the CD spectra or peptide electrophoretic mobility of the individual peptides or their mixtures. The properties of both the PPAK and polyE type peptides suggest that both had most of the characteristic properties to be classified as intrinsically disordered proteins.

Indexed as

Amino Acid SequenceBinding SitesConnectinHumansMolecular Sequence DataMolecular WeightMuscle ProteinsPeptidesProtein BindingProtein ConformationProtein KinasesProtein Structure, SecondaryProtein Structure, TertiaryConnectinMuscle ProteinsPeptidesProtein KinasesTTN protein, human

Identifiers

PMID16949547
PMCPMC1635410
OpenAlexW1988223464

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.