Evidence map›Paper›PMID 32896313›Full record

ArticleMethods in cell biology2020

Heterologous expression of plant glycosyltransferases for biochemistry and structural biology.

Pradeep K Prabhakar, Hsin-Tzu Wang, Peter J Smith, Jeong-Yeh Yang, William J Barnes, Maria J Peña, Kelley W Moremen, Breeanna R Urbanowicz

Open access · greenAbstract read
In one paragraph

Article in Methods in cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Frontiers in plant science · 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

8 authors at 2 institutions in 1 country.

Pradeep K PrabhakarDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States; Center for Bioenergy Innovation, Oak Ridge National Laboratory, Oakridge, TN, United States.
Hsin-Tzu WangDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States; Center for Bioenergy Innovation, Oak Ridge National Laboratory, Oakridge, TN, United States.
Peter J SmithDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States; Center for Bioenergy Innovation, Oak Ridge National Laboratory, Oakridge, TN, United States.
Jeong-Yeh YangDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States.
William J BarnesDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States.
Maria J PeñaComplex Carbohydrate Research Center, University of Georgia, Athens, GA, United States; Center for Bioenergy Innovation, Oak Ridge National Laboratory, Oakridge, TN, United States.
Kelley W MoremenDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States.
Breeanna R UrbanowiczDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, United States; Complex Carbohydrate Research Center, University of Georgia, Athens, GA, United States; Center for Bioenergy Innovation, Oak Ridge National Laboratory, Oakridge, TN, United States. Electronic address: breeanna@uga.edu.
University of Georgia · USOak Ridge National Laboratory · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI PRESTEGARD, JAMES H. · 2013 to 2017
$7.5M
Origin of N-Glycan Site-Specific HeterogeneityR01GM130915 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, MOREMEN, KELLEY W. · 2019 to 2022
$3.4M
Glycoscience Training ProgramT32GM107004 · NIGMS · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN, HALTIWANGER, ROBERT S. · 2014 to 2021
$1.3M
National Science Foundation 1817697NIGMS NIH HHS P01 GM107012NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM130915NIGMS NIH HHS T32 GM107004
6 · The paper itself

Abstract

Much of the carbon captured by photosynthesis is converted into the polysaccharides that constitute plant cell walls. These complex macrostructures are composed of cellulose, hemicellulose, and pectins, together with small amounts of structural proteins, minerals, and in many cases lignin. Wall components assemble and interact with one another to produce dynamic structures with many capabilities, including providing mechanical support to plant structures and determining plant cell shape and size. Despite their abundance, major gaps in our knowledge of the synthesis of the building blocks of these polymers remain, largely due to ineffective methods for expression and purification of active synthetic enzymes for in vitro biochemical analyses. The hemicellulosic polysaccharide, xyloglucan, comprises up to 25% of the dry weight of primary cell walls in plants. Most of the knowledge about the glycosyltransferases (GTs) involved in the xyloglucan biosynthetic pathway has been derived from the identification and carbohydrate analysis of knockout mutants, lending little information on how the catalytic biosynthesis of xyloglucan occurs in planta. In this chapter we describe methods for the heterologous expression of plant GTs using the HEK293 expression platform. As a demonstration of the utility of this platform, nine xyloglucan-relevant GTs from three different CAZy families were evaluated, and methods for expression, purification, and construct optimization are described for biochemical and structural characterization.

Indexed as

ArabidopsisBiochemistryCell WallEndopeptidasesGlucansGlycosylationGlycosyltransferasesHEK293 CellsHumansXylansEndopeptidasesGlucansGlycosyltransferasesTEV proteaseXylansxyloglucanGTsHEK293HemicelluloseProtein purificationRecombinant protein expressionXyloglucan

Identifiers

PMID32896313
PMCPMC7593805
OpenAlexW3034968647

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.