Evidence map›Paper›PMID 23224300›Full record

ArticleEuropean biophysics journal : EBJ2013

Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium.

Michael M DuVall, Jessica L Gifford, Matthias Amrein, Walter Herzog

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In one paragraph

Article in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. CaProtein science : a publication of the Protein Society · 2022
    Article
  6. Article
  7. Regulation of Poly-E Motif Flexibility by pH, CaInternational journal of molecular sciences · 2022
    Article
  8. Review
  9. Article
  10. Titin N2A Domain and Its Interactions at the Sarcomere.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Differences in stability and calcium sensitivity of the Ig domains in titin's N2A region.Protein science : a publication of the Protein Society · 2020
    Article
  16. Article
  17. Review
  18. Review
  19. Passive force enhancement in striated muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2019
    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

4 authors at 1 institution in 1 country.

Michael M DuVallHuman Performance Laboratory, University of Calgary, 2500 University Drive NW, Calgary, AB T2N 1N4, Canada. mmduvall@ucalgary.ca
Jessica L Gifford
Matthias Amrein
Walter Herzog
University of Calgary · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Titin (connectin) based passive force regulation has been an important physiological mechanism to adjust to varying muscle stretch conditions. Upon stretch, titin behaves as a spring capable of modulating its elastic response in accordance with changes in muscle biochemistry. One such mechanism has been the calcium-dependent stiffening of titin domains that renders the spring inherently more resistant to stretch. This transient titin-calcium interaction may serve a protective function in muscle, which could preclude costly unfolding of select domains when muscles elongate to great lengths. To test this idea, fluorescence spectroscopy was performed revealing a change in the microenvironment of the investigated immunoglobulin domain 27 (I27) of titin with calcium. Additionally, an atomic force microscope was used to evaluate the calcium-dependent regulation of passive force by stretching eight linked titin I27 domains until they unfolded. When stretching in the presence of calcium, the I27 homopolymer chain became stabilized, displaying three novel properties: (1) higher stretching forces were needed to unfold the domains, (2) the stiffness, measured as a persistence length (PL), increased and (3) the peak-to-peak distance between adjacent I27 domains increased. Furthermore, a peak order dependence became apparent for both force and PL, reflecting the importance of characterizing the dynamic unfolding history of a polymer with this approach. Together, this novel titin Ig-calcium interaction may serve to stabilize the I27 domain permitting titin to tune passive force within stretched muscle in a calcium-dependent manner.

Indexed as

Mechanical PhenomenaBiomechanical PhenomenaCalciumConnectinHumansImmunoglobulinsProtein Structure, TertiaryCalciumConnectinImmunoglobulins

Identifiers

PMID23224300
OpenAlexW2015054653

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.