Evidence map›Paper›PMID 26041514›Full record

ArticleInternational journal of legal medicine2016

Postmortem degradation of skeletal muscle proteins: a novel approach to determine the time since death.

Stefan Pittner, Fabio C Monticelli, Alexander Pfisterer, Angela Zissler, Alexandra M Sänger, Walter Stoiber, Peter Steinbacher

Abstract read
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In one paragraph

Article in International journal of legal medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 3 pooled it
5.7field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 3 syntheses or guidelines pooled it, 90 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. "Omics" and Postmortem Interval Estimation: A Systematic Review.International journal of molecular sciences · 2025
    Pooled it
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  5. Review
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  14. RedefiningFrontiers in microbiology · 2025
    Review
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  17. Review
  18. Article
  19. Forensic Proteomics for the Discovery of NewInternational journal of molecular sciences · 2023
    Article
  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

7 authors at 1 institution in 1 country.

Stefan PittnerDepartment of Cell Biology, University of Salzburg, Hellbrunnerstr. 34, 5020, Salzburg, Austria.
Fabio C MonticelliDepartment of Forensic Medicine and Forensic Neuropsychiatry, University of Salzburg, Ignaz-Harrer-Straße 79, 5020, Salzburg, Austria.
Alexander PfistererDepartment of Cell Biology, University of Salzburg, Hellbrunnerstr. 34, 5020, Salzburg, Austria.
Angela ZisslerDepartment of Cell Biology, University of Salzburg, Hellbrunnerstr. 34, 5020, Salzburg, Austria.
Alexandra M SängerDepartment of Cell Biology, University of Salzburg, Hellbrunnerstr. 34, 5020, Salzburg, Austria.
Walter StoiberDepartment of Cell Biology, University of Salzburg, Hellbrunnerstr. 34, 5020, Salzburg, Austria.
Peter SteinbacherDepartment of Cell Biology, University of Salzburg, Hellbrunnerstr. 34, 5020, Salzburg, Austria. peter.steinbacher@sbg.ac.at.
University of Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Estimating the time since death is a very important aspect in forensic sciences which is pursued by a variety of methods. The most precise method to determine the postmortem interval (PMI) is the temperature method which is based on the decrease of the body core temperature from 37 °C. However, this method is only useful in the early postmortem phase (~0-36 h). The aim of the present work is to develop an accurate method for PMI determination beyond this present limit. For this purpose, we used sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blotting, and casein zymography to analyze the time course of degradation of selected proteins and calpain activity in porcine biceps femoris muscle until 240 h postmortem (hpm). Our results demonstrate that titin, nebulin, desmin, cardiac troponin T, and SERCA1 degraded in a regular and predictable fashion in all samples investigated. Similarly, both the native calpain 1 and calpain 2 bands disintegrate into two bands subsequently. This degradation behavior identifies muscular proteins and enzymes as promising substrates for future molecular-based PMI determination technologies.

Indexed as

Postmortem ChangesAnimalsBlotting, WesternCalpainConnectinDesminElectrophoresis, Polyacrylamide GelForensic PathologyModels, AnimalMuscle ProteinsMuscle, SkeletalSarcoplasmic Reticulum Calcium-Transporting ATPasesSwineTroponin TATP2A1 protein, humanCalpainCAPN1 protein, humanCAPN2 protein, humanConnectinDesminMuscle ProteinsnebulinSarcoplasmic Reticulum Calcium-Transporting ATPasesTroponin TDegradationPigPostmortem interval (PMI)ProteinSkeletal muscle

Identifiers

PMID26041514
OpenAlexW617901188

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.