Evidence map›Paper›PMID 27660393›Full record

ArticleThe Journal of biological chemistry2016

An Isozyme-specific Redox Switch in Human Brain Glycogen Phosphorylase Modulates Its Allosteric Activation by AMP.

Cécile Mathieu, Romain Duval, Angélique Cocaign, Emile Petit, Linh-Chi Bui, Iman Haddad, Joelle Vinh, Catherine Etchebest, Jean-Marie Dupret, Fernando Rodrigues-Lima

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Pooled it
  2. Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Switching the Switch: Ligand Induced Disulfide Formation in HDAC8.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  11. The regulation of glycogenolysis in the brain.The Journal of biological chemistry · 2018
    Review
  12. Article
  13. Article
  14. 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

10 authors at 2 institutions in 1 country.

Cécile MathieuFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris.
Romain DuvalFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris.
Angélique CocaignFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris.
Emile PetitFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris.
Linh-Chi BuiFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris.
Iman HaddadESPCI Paris, PSL Research University, Spectrométrie de Masse Biologique et Protéomique (SMPB), CNRS USR 3149, 10 rue Vauquelin, F75231 Paris cedex 05, France.
Joelle VinhESPCI Paris, PSL Research University, Spectrométrie de Masse Biologique et Protéomique (SMPB), CNRS USR 3149, 10 rue Vauquelin, F75231 Paris cedex 05, France.
Catherine EtchebestINSERM, UMR S1134, Université Paris Diderot, F-75015 Paris.
Jean-Marie DupretFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris.
Fernando Rodrigues-LimaFrom the Université Paris Diderot, Sorbonne Paris Cité, Unité BFA, CNRS UMR 8251, 75013 Paris, fernando.rodrigues-lima@univ-paris-diderot.fr.
Centre National de la Recherche Scientifique · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Brain glycogen and its metabolism are increasingly recognized as major players in brain functions. Moreover, alteration of glycogen metabolism in the brain contributes to neurodegenerative processes. In the brain, both muscle and brain glycogen phosphorylase isozymes regulate glycogen mobilization. However, given their distinct regulatory features, these two isozymes could confer distinct metabolic functions of glycogen in brain. Interestingly, recent proteomics studies have identified isozyme-specific reactive cysteine residues in brain glycogen phosphorylase (bGP). In this study, we show that the activity of human bGP is redox-regulated through the formation of a disulfide bond involving a highly reactive cysteine unique to the bGP isozyme. We found that this disulfide bond acts as a redox switch that precludes the allosteric activation of the enzyme by AMP without affecting its activation by phosphorylation. This unique regulatory feature of bGP sheds new light on the isoform-specific regulation of glycogen phosphorylase and glycogen metabolism.

Indexed as

Adenosine MonophosphateAllosteric RegulationAnimalsCysteineDisulfidesGlycogenGlycogen Phosphorylase, Brain FormHumansIsoenzymesOxidation-ReductionPhosphorylationRabbitsRatsAdenosine MonophosphateCysteineDisulfidesGlycogenGlycogen Phosphorylase, Brain FormIsoenzymesallosteric regulationbrain metabolismcarbohydrate metabolismdisulfideglycogenglycogen storage diseaseredox regulation

Identifiers

PMID27660393
PMCPMC5104910
OpenAlexW2521086684

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.