ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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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.
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Who cites it
5 citing papers in PubMed.
- An in silico argument for mitochondrial microRNA as a determinant of primary non function in liver transplantation.Scientific reports · 2018Article
- Large-scale detection of drug off-targets: hypotheses for drug repurposing and understanding side-effects.BMC pharmacology & toxicology · 2017Article
- Article
- Complete genome-wide screening and subtractive genomic approach revealed new virulence factors, potential drug targets against bio-war pathogen Brucella melitensis 16M.Drug design, development and therapy · 2015Article
- IsoCleft Finder - a web-based tool for the detection and analysis of protein binding-site geometric and chemical similarities.F1000Research · 2013Article
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Authors and funding
46 authors.
Funding
Abstract
The crystal structures of SPO0140 and Sbal_2486 were determined using the semiautomated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). The structures revealed a conserved core with domain duplication and a superficial similarity of the C-terminal domain to pleckstrin homology-like folds. The conservation of the domain interface indicates a potential binding site that is likely to involve a nucleotide-based ligand, with genome-context and gene-fusion analyses additionally supporting a role for this family in signal transduction, possibly during oxidative stress.
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