Role of the interaction between troponin T and AMP deaminase by zinc bridge in modulating muscle contraction and ammonia production.

Open access · hybridAbstract readReview

In one paragraph

Review in Molecular and cellular biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.4field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

Role of AMP deaminase in diabetic cardiomyopathy.Molecular and cellular biochemistry · 2024
Review

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

2 authors at 1 institution in 1 country.

Francesca RoncaLaboratory of Biochemistry, Department of Pathology, University of Pisa, Via Roma 55, 56126, Pisa, Italy. francesca.ronca@med.unipi.it.ORCID http://orcid.org/0000-0003-4818-960X

Antonio RaggiLaboratory of Biochemistry, Department of Pathology, University of Pisa, Via Roma 55, 56126, Pisa, Italy.ORCID http://orcid.org/0000-0002-8727-8106

University of Pisa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N-terminal region of troponin T (TnT) does not bind any protein of the contractile machinery and the role of its hypervariability remains uncertain. In this review we report the evidence of the interaction between TnT and AMP deaminase (AMPD), a regulated zinc enzyme localized on the myofibril. In periods of intense muscular activity, a decrease in the ATP/ADP ratio, together with a decrease in the tissue pH, is the stimulus for the activation of the enzyme that deaminating AMP to IMP and NH

Indexed as

AMP DeaminaseTroponin TAdenosine TriphosphateAmmoniaAnimalsCalpainHumansMuscle ContractionMuscle, SkeletalPeptidesProteinsRabbitsZincAdenosine TriphosphateAmmoniaAMP DeaminaseCalpainPeptidesProteinsTroponin TZincAMP deaminaseCalpainFast skeletal muscleTroponin TZinc-binding motif

Identifiers

PMID37184757

DOI10.1007/s11010-023-04763-7

PMCPMC11016001

OpenAlexW4376609420

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.