Evidence map›Paper›PMID 16416044›Full record

ReviewHeart failure reviews2005

Titin: physiological function and role in cardiomyopathy and failure.

Henk Granzier, Yiming Wu, Labeit Siegfried, Martin LeWinter

Abstract readReview
PubMed Publisher
In one paragraph

Review in Heart failure reviews, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 88 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
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  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Titin mutations and muscle disease.Pflugers Archiv : European journal of physiology · 2019
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Myosin light chain phosphorylation to the rescue.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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 3 institutions in 2 countries.

Henk GranzierDepartment of Veterinary and Comparative Anatomy, Washington State University, Pullman, WA 99164-6520, USA. granzier@wsunix.wsu.edu
Yiming Wu
Labeit Siegfried
Martin LeWinter
Washington State University · USAllen Hospital · USHeidelberg University · DE

Funding

Function of Giant Sarcomere Matrix Proteins in MuscleR01HL062881 · NHLBI · WASHINGTON STATE UNIVERSITY · PI GRANZIER, HENK L. · 1999 to 2018
$6.4M
NHLBI NIH HHS HL61487NHLBI NIH HHS HL62881
6 · The paper itself

Abstract

Titin is a giant protein that constitutes the third myofilament of the sarcomere. Single titin molecules anchor in the Z-disk and extend all the way to the M-line region of the sarcomere. Successive titin molecules are arranged head-to-head and tail-to-tail, providing a continuous filament along the full length of the myofibril. The majority of titin's I-band region is extensible and functions as a molecular spring that when extended develops passive force. We will discuss mechanisms for adjusting titin-based force, including alternative splicing and posttranslational modifications. Multiple biological functions can be assigned to different regions of the titin molecule. In addition to titin's role in determining passive muscle stiffness, recent evidence suggests a role in protein metabolism, compartmentalization of metabolic enzymes, binding of chaperones, and positioning of the membrane systems of the T-tubules and sarcoplasmic reticulum. We will also discuss titin-based force adjustments that occur in various muscle diseases and several disease-causing titin mutations that have been discovered. We will focus on the role of titin in heart failure patients that was recently investigated in patients with end-stage heart failure due to non-ischemic dilated cardiomyopathy. In end-stage failing hearts, compliant titin isoforms comprise a greater percentage of titin and changes in titin isoform expression in heart failure patients with DCM significantly impact diastolic filling by lowering myocardial stiffness.

Indexed as

CalciumCardiomyopathy, DilatedConnectinHeart FailureHumansMuscle ProteinsPhosphorylationProtein IsoformsProtein KinasesSarcomeresCalciumConnectinMuscle ProteinsProtein IsoformsProtein KinasesTTN protein, human

Identifiers

PMID16416044
OpenAlexW2033660111

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.