Evidence map›Paper›PMID 15803415›Full record

ArticlePlant molecular biology2004

Toward a blueprint for UDP-glucose pyrophosphorylase structure/function properties: homology-modeling analyses.

Matt Geisler, Malgorzata Wilczynska, Stanislaw Karpinski, Leszek A Kleczkowski

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.9field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

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  4. Exploring Redox Modulation of Plant UDP-Glucose Pyrophosphorylase.International journal of molecular sciences · 2023
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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 at 2 institutions in 1 country.

Matt GeislerDepartment of Plant Physiology, Umeå Plant Science Centre, Umeå University, 901 87 Umeå, Sweden.
Malgorzata Wilczynska
Stanislaw Karpinski
Leszek A Kleczkowski
Umeå Plant Science Centre · SEUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UDP-glucose pyrophosphorylase (UGPase) is an important enzyme of synthesis of sucrose, cellulose, and several other polysaccharides in all plants. The protein is evolutionarily conserved among eukaryotes, but has little relation, aside from its catalytic reaction, to UGPases of prokaryotic origin. Using protein homology modeling strategy, 3D structures for barley, poplar, and Arabidopsis UGPases have been derived, based on recently published crystal structure of human UDP-N-acetylglucosamine pyrophosphorylase. The derived 3D structures correspond to a bowl-shaped protein with the active site at a central groove, and a C-terminal domain that includes a loop (I-loop) possibly involved in dimerization. Data on a plethora of earlier described UGPase mutants from a variety of eukaryotic organisms have been revisited, and we have, in most cases, verified the role of each mutation in enzyme catalysis/regulation/structural integrity. We have also found that one of two alternatively spliced forms of poplar UGPase has a very short I-loop, suggesting differences in oligomerization ability of the two isozymes. The derivation of the structural model for plant UGPase should serve as a useful blueprint for further function/structure studies on this protein.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsEukaryotic CellsGenetic VariationHumansIsoenzymesModels, MolecularMolecular Sequence DataMutationPhylogenyPlantsPopulusProkaryotic CellsProtein ConformationSequence Homology, Amino AcidIsoenzymesUTP-Glucose-1-Phosphate Uridylyltransferase

Identifiers

PMID15803415
OpenAlexW2049539843

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.