Evidence map›Paper›PMID 21639091›Full record

ArticleBiochemistry2011

Phosphorylation, but not alternative splicing or proteolytic degradation, is conserved in human and mouse cardiac troponin T.

Jiang Zhang, Han Zhang, Serife Ayaz-Guner, Yi-Chen Chen, Xintong Dong, Qingge Xu, Ying Ge

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Proteomics of the heart.Physiological reviews · 2024
    Review
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  18. The impact of antibody selection on the detection of cardiac troponin I.Clinica chimica acta; international journal of clinical chemistry · 2013
    Article
  19. 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.

Jiang ZhangHuman Proteomics Program, School of Medicine and Public Health, University of Wisconsin, Madison, Wisconsin 53706, USA.
Han Zhang
Serife Ayaz-Guner
Yi-Chen Chen
Xintong Dong
Qingge Xu
Ying Ge
University of Wisconsin–Madison · US

Funding

Deciphering the Roles of Nebulin in Cardiac Myofibril AssemblyR01HL083146 · NHLBI · UNIVERSITY OF ARIZONA · PI GREGORIO, CAROL C · 2007 to 2011
$2.1M
Novel Protein Kinase C Isoforms in Ventricular MyocytesR01HL081386 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI GREGORIO, CAROL C · 2005 to 2009
$1.6M
NHLBI NIH HHS R01 HL081386NHLBI NIH HHS R01 HL083146
6 · The paper itself

Abstract

Cardiac troponin T (cTnT), the tropomyosin binding subunit of the troponin complex, plays a pivotal regulatory role in the Ca(2+)-mediated interaction between actin thin filament and myosin thick filament. The post-translational modifications (PTMs) and alternative splicing of cTnT may represent important regulatory mechanisms of cardiac contractility. However, a complete characterization of PTMs and alternatively spliced isoforms in cTnT present in vivo is lacking. Top-down protein mass spectrometry (MS) analyzes whole proteins, thus providing a global view of all types of modifications, including PTMs and sequence variants, simultaneously in one spectrum without a priori knowledge. In this study, we applied an integrated immunoaffinity chromatography and top-down MS approach to comprehensively characterize PTMs and alternatively spliced isoforms of cTnT purified from healthy human and wild-type mouse heart tissue. High-resolution Fourier transform MS revealed that human cTnT (hcTnT) and mouse cTnT (mcTnT) have similar phosphorylation patterns, whereas higher molecular heterogeneity was observed for mcTnT than hcTnT. Further MS/MS fragmentation of monophosphorylated hcTnT and mcTnT by electron capture dissociation and collisionally activated dissociation unambiguously identified Ser1 as the conserved in vivo phosphorylation site. In contrast, we identified a single spliced isoform for hcTnT but three alternatively spliced isoforms for mcTnT. Moreover, we observed distinct proteolytic degradation products for hcTnT and mcTnT. This study also demonstrates the advantage of top-down MS/MS with complementary fragmentation techniques for the identification of modification sites in the highly acidic N-terminal region of cTnT.

Indexed as

Alternative SplicingConserved SequenceAdultAmino Acid SequenceAnimalsHumansMiceMice, Inbred C57BLMolecular Sequence DataMyocardial ContractionMyocardiumPeptide HydrolasesPhosphorylationProtein IsoformsProtein Processing, Post-TranslationalTroponin TPeptide HydrolasesProtein IsoformsTNNT2 protein, humanTroponin T

Identifiers

PMID21639091
PMCPMC3312388
OpenAlexW2094234453

What OpenQuestion holds

Textmetadata
LicenceTDM
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.