Evidence map›Paper›PMID 16880542›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006

Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.

Tomoya Kitatani, Yoshihiro Nakamura, Kei Wada, Takayoshi Kinoshita, Masahiro Tamoi, Shigeru Shigeoka, Toshiji Tada

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact, top 90% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  3. Structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase (isoform A4) from Arabidopsis thaliana in complex with NAD.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    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

7 authors at 2 institutions in 1 country.

Tomoya KitataniDepartment of Applied Biochemistry, Graduate School of Agriculture and Life Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan.
Yoshihiro Nakamura
Kei Wada
Takayoshi Kinoshita
Masahiro Tamoi
Shigeru Shigeoka
Toshiji Tada
Osaka Prefecture University · JPKindai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of NADP-dependent apo-glyceraldehyde-3-phosphate dehydrogenase (apo-GAPDH) from Synechococcus PCC 7942 is reported. The crystal structure was solved by molecular replacement and refined to an R of 21.7% and R(free) of 27.5% at 2.9 angstroms resolution. The structural features of apo-GAPDH are as follows. The S-loop has an extremely flexible conformation and the sulfate ion is only taken into the classical P(i) site. A structural comparison with holo-GAPDHs indicated that the S-loop fixation is essential in the discrimination of NADP and NAD molecules.

Indexed as

ApoenzymesBacterial ProteinsCrystallography, X-RayGlyceraldehyde-3-Phosphate DehydrogenasesModels, MolecularNADNADPProtein Structure, SecondarySubstrate SpecificitySynechococcusApoenzymesBacterial ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesNADNADP

Identifiers

PMID16880542
PMCPMC2242934
OpenAlexW2042546680

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.