ArticleBMC genomics2005
GH97 is a new family of glycoside hydrolases, which is related to the alpha-galactosidase superfamily.
Article in BMC genomics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
Who cites it
8 citing papers in PubMed.
- Exploration of Alkaliphilic Bacteria Alkalitalea saponilacus Identifies Glycoside Hydrolases With Biotechnological Potential.Microbial biotechnology · 2026Article
- The effect of barium and strontium on activity of glucoamylase QsGH97a from Qipengyuania seohaensis SW-135.Scientific reports · 2023Article
- Isolation and Identification of an α-Galactosidase-ProducingMolecules (Basel, Switzerland) · 2022Article
- Niche adaptation promoted the evolutionary diversification of tiny ocean predators.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cultivable, Host-SpecificApplied and environmental microbiology · 2020Article
- An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.Glycobiology · 2018Article
- Molecular characterization of an α-N-acetylgalactosaminidase from Clonorchis sinensis.Parasitology research · 2012Article
- Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora.Chemistry & biology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAs a rule, about 1% of genes in a given genome encode glycoside hydrolases and their homologues. On the basis of sequence similarity they have been grouped into more than ninety GH families during the last 15 years. The GH97 family has been established very recently and initially included only 18 bacterial proteins. However, the evolutionary relationship of the genes encoding proteins of this family remains unclear, as well as their distribution among main groups of the living organisms.
resultsThe extensive search of the current databases allowed us to double the number of GH97 family proteins. Five subfamilies were distinguished on the basis of pairwise sequence comparison and phylogenetic analysis. Iterative sequence analysis revealed the relationship of the GH97 family with the GH27, GH31, and GH36 families of glycosidases, which belong to the alpha-galactosidase superfamily, as well as a more distant relationship with some other glycosidase families (GH13 and GH20).
conclusionThe results of this study show an unexpected sequence similarity of GH97 family proteins with glycoside hydrolases from several other families, that have (beta/alpha)8-barrel fold of the catalytic domain and a retaining mechanism of the glycoside bond hydrolysis. These data suggest a common evolutionary origin of glycosidases representing different families and clans.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.