Evidence map›Paper›PMID 15272305›Full record

ArticleThe EMBO journal2004

Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation.

Alejandro Buschiazzo, Juan E Ugalde, Marcelo E Guerin, William Shepard, Rodolfo A Ugalde, Pedro M Alzari

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

73 citing papers in PubMed, 171 citations in OpenAlex.

  1. Protein phosphatase 2A impairs cardiac uptake of glucose in the mammalian heart.Naunyn-Schmiedeberg's archives of pharmacology · 2026
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  3. The metabolic enzyme GYS1 condenses with NONO/p54Cell death and differentiation · 2025
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  14. NovelMolecular genetics and metabolism reports · 2021
    Article
  15. Article
  16. Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  17. Co-crystal Structure ofFrontiers in microbiology · 2020
    Article
  18. TheThe Biochemical journal · 2019
    Review
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

6 authors at 4 institutions in 2 countries.

Alejandro BuschiazzoUnité de Biochimie Structurale, URA 2185 CNRS, Institut Pasteur, Paris, France.
Juan E Ugalde
Marcelo E Guerin
William Shepard
Rodolfo A Ugalde
Pedro M Alzari
Institut Pasteur · FRNational University of General San Martín · ARCentre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycogen and starch are the major readily accessible energy storage compounds in nearly all living organisms. Glycogen is a very large branched glucose homopolymer containing about 90% alpha-1,4-glucosidic linkages and 10% alpha-1,6 linkages. Its synthesis and degradation constitute central pathways in the metabolism of living cells regulating a global carbon/energy buffer compartment. Glycogen biosynthesis involves the action of several enzymes among which glycogen synthase catalyzes the synthesis of the alpha-1,4-glucose backbone. We now report the first crystal structure of glycogen synthase in the presence and absence of adenosine diphosphate. The overall fold and the active site architecture of the protein are remarkably similar to those of glycogen phosphorylase, indicating a common catalytic mechanism and comparable substrate-binding properties. In contrast to glycogen phosphorylase, glycogen synthase has a much wider catalytic cleft, which is predicted to undergo an important interdomain 'closure' movement during the catalytic cycle. The structures also provide useful hints to shed light on the allosteric regulation mechanisms of yeast/mammalian glycogen synthases.

Indexed as

Adenosine DiphosphateAgrobacterium tumefaciensAmino Acid SequenceAnimalsBinding SitesCatalysisCrystallography, X-RayGlycogenGlycogen PhosphorylaseGlycogen SynthaseModels, MolecularMolecular Sequence DataProtein Structure, TertiarySequence AlignmentStructural Homology, ProteinAdenosine DiphosphateGlycogenGlycogen PhosphorylaseGlycogen Synthase

Identifiers

PMID15272305
PMCPMC514502
OpenAlexW2099748948

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.