Evidence map›Paper›PMID 21865170›Full record

ArticleThe Journal of biological chemistry2011

The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications.

Yi Zheng, Spencer Anderson, Yanfeng Zhang, R Michael Garavito

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
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

49 citing papers in PubMed.

  1. Article
  2. Review
  3. Structural analysis of the tetrahydrobiopterin glucosyltransferase PsBGluT from Pseudanabaena sp. Chao 1811.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  4. Review
  5. Review
  6. A Suite of Pea (International journal of molecular sciences · 2025
    Article
  7. The sucrose synthase gene family in blueberry (Frontiers in plant science · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Identification of sucrose synthase fromFrontiers in microbiology · 2023
    Article
  18. Molecular identification and expression analysis of five sucrose synthase genes inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2022
    Article
  19. Article
  20. Purification and Biochemical Characterization ofInternational journal of molecular sciences · 2021
    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

4 authors.

Yi ZhengDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824.
Spencer AndersonLife Sciences Collaborative Access Team, Northwestern University, Argonne, Illinois 60439.
Yanfeng ZhangDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824.
R Michael GaravitoDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824. Electronic address: garavito@msu.edu.

Funding

Structure and function of family 1 glycosyltransferasesR01GM065501 · NIGMS · MICHIGAN STATE UNIVERSITY · PI GARAVITO, R MICHAEL · 2003 to 2006
$1.0M
NIGMS NIH HHS GM65501NIGMS NIH HHS R01 GM065501
6 · The paper itself

Abstract

Sucrose transport is the central system for the allocation of carbon resources in vascular plants. During growth and development, plants control carbon distribution by coordinating sites of sucrose synthesis and cleavage in different plant organs and different cellular locations. Sucrose synthase, which reversibly catalyzes sucrose synthesis and cleavage, provides a direct and reversible means to regulate sucrose flux. Depending on the metabolic environment, sucrose synthase alters its cellular location to participate in cellulose, callose, and starch biosynthesis through its interactions with membranes, organelles, and cytoskeletal actin. The x-ray crystal structure of sucrose synthase isoform 1 from Arabidopsis thaliana (AtSus1) has been determined as a complex with UDP-glucose and as a complex with UDP and fructose, at 2.8- and 2.85-Å resolutions, respectively. The AtSus1 structure provides insights into sucrose catalysis and cleavage, as well as the regulation of sucrose synthase and its interactions with cellular targets.

Indexed as

ArabidopsisArabidopsis ProteinsCatalysisCrystallography, X-RayGlucosyltransferasesProtein Structure, TertiaryStructure-Activity RelationshipUridine Diphosphate GlucoseArabidopsis ProteinsGlucosyltransferasessucrose synthaseUridine Diphosphate Glucose

Identifiers

PMID21865170
PMCPMC3195635

What OpenQuestion holds

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Registered trials

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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.