Evidence map›Paper›PMID 26278983›Full record

ReviewMolecular aspects of medicine2015

Getting a handle on glycogen synthase - Its interaction with glycogenin.

Elton Zeqiraj, Frank Sicheri

Open access · greenAbstract readReview
In one paragraph

Review in Molecular aspects of medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Biological roles of glycans.Glycobiology · 2017
    Review
  11. 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 2 institutions in 1 country.

Elton ZeqirajLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue, Room 1090, Toronto, ON M5G 1X5, Canada; Departments of Biochemistry and Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada. Electronic address: zeqiraj@lunenfeld.ca.
Frank SicheriLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, 600 University Avenue, Room 1090, Toronto, ON M5G 1X5, Canada; Departments of Biochemistry and Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada. Electronic address: sicheri@lunenfeld.ca.
Mount Sinai Hospital · CAUniversity of Toronto · CA

Funding

CIHR MOP-84370Wellcome Trust 092381
6 · The paper itself

Abstract

Glycogen is a polymer of glucose that serves as a major energy reserve in eukaryotes. It is synthesized through the cooperative action of glycogen synthase (GS), glycogenin (GN) and glycogen branching enzyme. GN initiates the first enzymatic step in the glycogen synthesis process by self glucosylation of a short 8-12 glucose residue primer. After interacting with GN, GS then extends this sugar primer to form glycogen particles of different sizes. We discuss recent developments in the structural biology characterization of GS and GN enzymes, which have contributed to a better understanding of how the two proteins interact and how they collaborate to synthesize glycogen particles.

Indexed as

GlucoseGlucosyltransferasesGlycogenGlycogen SynthaseGlycoproteinsGlycosylationHumansGlucoseGlucosyltransferasesGlycogenglycogeninGlycogen SynthaseGlycoproteins

Identifiers

PMID26278983
PMCPMC5839463
OpenAlexW1176178474

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.