ArticleEnzyme research2010
In silico characterization of pectate lyase protein sequences from different source organisms.
Article in Enzyme research, 2010. 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
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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
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Genome-Wide Identification of the Pectate Lyase Gene Family in Potato and Expression Analysis under Salt Stress.Plants (Basel, Switzerland) · 2024Article
- Article
- Integrative immunoinformatics paradigm for predicting potential B-cell and T-cell epitopes as viable candidates for subunit vaccine design against COVID-19 virulence.Biomedical journal · 2021Article
- A pollen-specific calmodulin-binding protein, NPG1, interacts with putative pectate lyases.Scientific reports · 2014Article
- Cloning, Sequencing, and In Silico Analysis of β-Propeller Phytase Bacillus licheniformis Strain PB-13.Biotechnology research international · 2014Article
- Legume pectate lyase required for root infection by rhizobia.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- In silico characterization of histidine Acid phytase sequences.Enzyme research · 2012Article
- Abundance and genetic diversity of microbial polygalacturonase and pectate lyase in the sheep rumen ecosystem.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A total of 121 protein sequences of pectate lyases were subjected to homology search, multiple sequence alignment, phylogenetic tree construction, and motif analysis. The phylogenetic tree constructed revealed different clusters based on different source organisms representing bacterial, fungal, plant, and nematode pectate lyases. The multiple accessions of bacterial, fungal, nematode, and plant pectate lyase protein sequences were placed closely revealing a sequence level similarity. The multiple sequence alignment of these pectate lyase protein sequences from different source organisms showed conserved regions at different stretches with maximum homology from amino acid residues 439-467, 715-816, and 829-910 which could be used for designing degenerate primers or probes specific for pectate lyases. The motif analysis revealed a conserved Pec_Lyase_C domain uniformly observed in all pectate lyases irrespective of variable sources suggesting its possible role in structural and enzymatic functions.
Identifiers
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Registered trials
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