Evidence map›Paper›PMID 17705786›Full record

ArticleThe Biochemical journal2007

A stress-induced rice (Oryza sativa L.) beta-glucosidase represents a new subfamily of glycosyl hydrolase family 5 containing a fascin-like domain.

Rodjana Opassiri, Busarakum Pomthong, Takashi Akiyama, Massalin Nakphaichit, Tassanee Onkoksoong, Mariena Ketudat Cairns, James R Ketudat Cairns

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Non-Catalytic Domains of Glycoside Hydrolase Family 5 fromJournal of microbiology and biotechnology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. HvBGlu3, a GH1 β-glucosidase enzyme gene, negatively influences β-glucan content in barley grains.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2024
    Article
  10. Article
  11. microPublication biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Association Analysis of Salt Tolerance in Asiatic cotton (International journal of molecular sciences · 2019
    Article
  18. Article
  19. Article
  20. 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 2 countries.

Rodjana OpassiriSchool of Biochemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
Busarakum Pomthong
Takashi Akiyama
Massalin Nakphaichit
Tassanee Onkoksoong
Mariena Ketudat Cairns
James R Ketudat Cairns
Suranaree University of Technology · THHokkaido Agricultural Research Center · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GH5BG, the cDNA for a stress-induced GH5 (glycosyl hydrolase family 5) beta-glucosidase, was cloned from rice (Oryza sativa L.) seedlings. The GH5BG cDNA encodes a 510-amino-acid precursor protein that comprises 19 amino acids of prepeptide and 491 amino acids of mature protein. The protein was predicted to be extracellular. The mature protein is a member of a plant-specific subgroup of the GH5 exoglucanase subfamily that contains two major domains, a beta-1,3-exoglucanase-like domain and a fascin-like domain that is not commonly found in plant enzymes. The GH5BG mRNA is highly expressed in the shoot during germination and in leaf sheaths of mature plants. The GH5BG was up-regulated in response to salt stress, submergence stress, methyl jasmonate and abscisic acid in rice seedlings. A GUS (glucuronidase) reporter tagged at the C-terminus of GH5BG was found to be secreted to the apoplast when expressed in onion (Allium cepa) cells. A thioredoxin fusion protein produced from the GH5BG cDNA in Escherichia coli hydrolysed various pNP (p-nitrophenyl) glycosides, including beta-D-glucoside, alpha-L-arabinoside, beta-D-fucoside, beta-D-galactoside, beta-D-xyloside and beta-D-cellobioside, as well as beta-(1,4)-linked glucose oligosaccharides and beta-(1,3)-linked disaccharide (laminaribiose). The catalytic efficiency (kcat/K(m)) for hydrolysis of beta-(1,4)-linked oligosaccharides by the enzyme remained constant as the DP (degree of polymerization) increased from 3 to 5. This substrate specificity is significantly different from fungal GH5 exoglucanases, such as the exo-beta-(1,3)-glucanase of the yeast Candida albicans, which may correlate with a marked reduction in a loop that makes up the active-site wall in the Candida enzyme.

Indexed as

Amino Acid Sequencebeta-GlucosidaseCarrier ProteinsGlycoside HydrolasesMicrofilament ProteinsMolecular Sequence DataOryzaOxidative StressPlant ProteinsProtein Structure, Tertiarybeta-GlucosidaseCarrier ProteinsfascinGlycoside HydrolasesMicrofilament ProteinsPlant Proteins

Identifiers

PMID17705786
PMCPMC2267349
OpenAlexW2093341351

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.