Evidence map›Paper›PMID 27147464›Full record

ReviewCellular and molecular life sciences : CMLS2016

Starch phosphorylation: insights and perspectives.

Sebastian Mahlow, Sławomir Orzechowski, Joerg Fettke

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 75 citations in OpenAlex.

  1. A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026
    Review
  2. Article
  3. Article
  4. Article
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  6. Emerging Functions of Protein Tyrosine Phosphatases in Plants.International journal of molecular sciences · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Frontiers in plant science · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 2 institutions in 2 countries.

Sebastian MahlowBiopolymer Analytics, University of Potsdam, Karl-Liebknecht 24-25, 14476, Potsdam-Golm, Germany.
Sławomir OrzechowskiBiopolymer Analytics, University of Potsdam, Karl-Liebknecht 24-25, 14476, Potsdam-Golm, Germany.
Joerg FettkeBiopolymer Analytics, University of Potsdam, Karl-Liebknecht 24-25, 14476, Potsdam-Golm, Germany. fettke@uni-potsdam.de.
University of Potsdam · DEWarsaw University of Life Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During starch metabolism, the phosphorylation of glucosyl residues of starch, to be more precise of amylopectin, is a repeatedly observed process. This phosphorylation is mediated by dikinases, the glucan, water dikinase (GWD) and the phosphoglucan, water dikinase (PWD). The starch-related dikinases utilize ATP as dual phosphate donor transferring the terminal γ-phosphate group to water and the β-phosphate group selectively to either C6 position or C3 position of a glucosyl residue within amylopectin. By the collaborative action of both enzymes, the initiation of a transition of α-glucans from highly ordered, water-insoluble state to a less order state is realized and thus the initial process of starch degradation. Consequently, mutants lacking either GWD or PWD reveal a starch excess phenotype as well as growth retardation. In this review, we focus on the increased knowledge collected over the last years related to enzymatic properties, the precise definition of the substrates, the physiological implications, and discuss ongoing questions.

Indexed as

ArabidopsisPhenotypePhosphatesPhosphorylationStarchSubstrate SpecificityPhosphatesStarchGlucan, water dikinasePhosphoglucan, water dikinaseStarch degradationStarch metabolismStarch phosphorylation

Identifiers

PMID27147464
PMCPMC11108486
OpenAlexW2346051188

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.