Evidence map›Paper›PMID 12913150›Full record

ArticlePlant physiology2003

Structure and properties of an engineered transketolase from maize.

Stefan Gerhardt, Stefanie Echt, Marco Busch, Jörg Freigang, Günter Auerbach, Gerd Bader, William F Martin, Adelbert Bacher, Robert Huber, Markus Fischer

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 52 citations in OpenAlex.

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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

10 authors at 3 institutions in 1 country.

Stefan GerhardtLehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Germany.
Stefanie Echt
Marco Busch
Jörg Freigang
Günter Auerbach
Gerd Bader
William F Martin
Adelbert Bacher
Robert Huber
Markus Fischer
Max Planck Institute of Biochemistry · DETechnical University of Munich · DEBayer (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.

Indexed as

Protein EngineeringAmino Acid SequenceBinding SitesCloning, MolecularCoenzymesCrystallography, X-RayModels, MolecularProtein ConformationProtein SubunitsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificityThiamine PyrophosphateTransketolaseZea maysCoenzymesProtein SubunitsThiamine PyrophosphateTransketolase

Identifiers

PMID12913150
PMCPMC181279
OpenAlexW2005513586

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.