ArticleThe Plant cell2013
Intrinsic disorder in pathogen effectors: protein flexibility as an evolutionary hallmark in a molecular arms race.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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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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Who cites it
43 citing papers in PubMed, 94 citations in OpenAlex.
- Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness.MicrobiologyOpen · 2026Review
- How to frustrate a plant pathogen.The Plant journal : for cell and molecular biology · 2026Review
- PLM-effector: unleashing the potential of protein language models for bacterial secreted protein prediction.Briefings in bioinformatics · 2026Article
- The disordered effector RipAO of Ralstonia solanacearum destabilizes microtubule networks in Nicotiana benthamiana cells.Molecules and cells · 2025Article
- Metatranscriptome analysis to unveil the molecular signatures of transcriptionally active pathogens associated with bovine mastitis.Frontiers in veterinary science · 2025Article
- Learning the language of plant immunity: opportunities and challenges for AI-assisted modelling of fungal effector x host protein complexes.Computational and structural biotechnology journal · 2025Review
- Article
- Definition of the effector landscape across 13 phytoplasma proteomes with LEAPH and EffectorComb.NAR genomics and bioinformatics · 2024Article
- The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.PLoS pathogens · 2024Article
- Characterization ofJournal of fungi (Basel, Switzerland) · 2024Article
- The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection.Communications biology · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Evolution of Intrinsic Disorder in Protein Loops.Life (Basel, Switzerland) · 2023Article
- Characterization of Arbuscular Mycorrhizal Effector Proteins.International journal of molecular sciences · 2023Review
- Phase separation in innate immune response and inflammation-related diseases.Frontiers in immunology · 2023Review
- Prediction of effector protein structures from fungal phytopathogens enables evolutionary analyses.Nature microbiology · 2023Article
- Short Linear Motifs (SLiMs) in "Core" RxLR Effectors ofMicrobiology spectrum · 2022Article
- The emerging role of biomolecular condensates in plant immunity.The Plant cell · 2022Article
- Virus-host interaction analysis in colorectal cancer identifies core virus network signature and small molecules.Computational and structural biotechnology journal · 2022Article
- Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status.Frontiers in plant science · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effector proteins represent a refined mechanism of bacterial pathogens to overcome plants' innate immune systems. These modular proteins often manipulate host physiology by directly interfering with immune signaling of plant cells. Even if host cells have developed efficient strategies to perceive the presence of pathogenic microbes and to recognize intracellular effector activity, it remains an open question why only few effectors are recognized directly by plant resistance proteins. Based on in-silico genome-wide surveys and a reevaluation of published structural data, we estimated that bacterial effectors of phytopathogens are highly enriched in long-disordered regions (>50 residues). These structurally flexible segments have no secondary structure under physiological conditions but can fold in a stimulus-dependent manner (e.g., during protein-protein interactions). The high abundance of intrinsic disorder in effectors strongly suggests positive evolutionary selection of this structural feature and highlights the dynamic nature of these proteins. We postulate that such structural flexibility may be essential for (1) effector translocation, (2) evasion of the innate immune system, and (3) host function mimicry. The study of these dynamical regions will greatly complement current structural approaches to understand the molecular mechanisms of these proteins and may help in the prediction of new effectors.
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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.