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Comparative proteomics of osmotic signal transduction mutants in Botrytis cinerea explain loss of pathogenicity phenotypes and highlight interaction with cAMP and Ca 2+ signalling pathways

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1 of the 62 references listed on this page is in the Retraction Watch database as retracted (export 2026-11-04): 10.1042/bsr20180067 (notice 2021-04-27).

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/9783527682386.ch11openalex-snapshot
Regulation of Secondary Metabolism in the Gray Mold FungusBotrytis cinerea
inferredcites →https://doi.org/10.1002/pmic.201100120openalex-snapshot
MassChroQ: A versatile tool for mass spectrometry quantification
inferredcites →https://doi.org/10.1002/pmic.201200564openalex-snapshot
Management and dissemination of MS proteomic data with PROTICdb: Example of a quantitative comparison between methods of protein extraction
inferredcites →https://doi.org/10.1002/pmic.201400173openalex-snapshot
Comparative proteomic analyses reveal that the regulators of G‐protein signaling proteins regulate amino acid metabolism of the rice blast fungus Magnaporthe oryzae
inferredcites →https://doi.org/10.1002/ps.302openalex-snapshot
Characterization of mutations in the two‐component histidine kinase gene that confer fludioxonil resistance and osmotic sensitivity in the os‐1 mutants of Neurospora crassa
inferredcites →https://doi.org/10.1007/978-1-4020-2626-3openalex-snapshot
Botrytis: Biology, Pathology and Control
inferredcites →https://doi.org/10.1007/978-1-4020-2626-3_19openalex-snapshot
Post-Harvest Botrytis Infection: Etiology, Development and Management
inferredcites →https://doi.org/10.1007/978-3-319-23371-0openalex-snapshot
Botrytis – the Fungus, the Pathogen and its Management in Agricultural Systems
inferredcites →https://doi.org/10.1007/978-3-319-23371-0_12openalex-snapshot
Infection Process and Fungal Virulence Factors
inferredcites →https://doi.org/10.1007/978-3-319-23371-0_13openalex-snapshot
Signal Transduction Cascades Regulating Differentiation and Virulence in Botrytis cinerea
inferredcites →https://doi.org/10.1007/978-3-319-23371-0_14openalex-snapshot
Reactive Oxygen Species in the Botrytis – Host Interaction
inferredcites →https://doi.org/10.1007/978-3-319-23371-0_15openalex-snapshot
Secondary Metabolism in Botrytis cinerea: Combining Genomic and Metabolomic Approaches
inferredcites →https://doi.org/10.1007/978-3-319-23371-0_17openalex-snapshot
Overview of Plant Defence Systems: Lessons from Arabidopsis-Botrytis cinerea Systems Biology
inferredcites →https://doi.org/10.1007/978-3-319-23371-0_20openalex-snapshot
Plant Hosts of Botrytis spp.
inferredcites →https://doi.org/10.1007/bf00245214openalex-snapshot
The influence of Congo red on the cell wall and (1 → 3)-β-d-glucan microfibril biogenesis in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1007/bf00351784openalex-snapshot
Variations in ploidy among isolates of Botrytis cinerea: implications for genetic and molecular analyses
inferredcites →https://doi.org/10.1007/s00294-005-0568-2openalex-snapshot
Characterization of mutations in the two-component histidine kinase gene AbNIK1 from Alternaria brassicicola that confer high dicarboximide and phenylpyrrole resistance
inferredcites →https://doi.org/10.1016/j.fgb.2004.11.002openalex-snapshot
A two-component histidine kinase of the rice blast fungus is involved in osmotic stress response and fungicide action
inferredcites →https://doi.org/10.1016/j.fgb.2008.04.003openalex-snapshot
The HOG1-like MAP kinase Sak1 of Botrytis cinerea is negatively regulated by the upstream histidine kinase Bos1 and is not involved in dicarboximide- and phenylpyrrole-resistance
inferredcites →https://doi.org/10.1016/j.fgb.2010.12.004openalex-snapshot
The osmosensing signal transduction pathway from Botrytis cinerea regulates cell wall integrity and MAP kinase pathways control melanin biosynthesis with influence of light
inferredcites →https://doi.org/10.1016/j.postharvbio.2015.11.003openalex-snapshot
Integrated management of postharvest gray mold on fruit crops
inferredcites →https://doi.org/10.1016/s0378-1119(03)00816-3openalex-snapshot
Transcriptional regulation by the MAP kinase signaling cascades
inferredcites →https://doi.org/10.1021/acs.jproteome.5b00802openalex-snapshot
Multiplexed, Proteome-Wide Protein Expression Profiling: Yeast Deubiquitylating Enzyme Knockout Strains
inferredcites →https://doi.org/10.1021/acs.jproteome.6b00632openalex-snapshot
X!TandemPipeline: A Tool to Manage Sequence Redundancy for Protein Inference and Phosphosite Identification
inferredcites →https://doi.org/10.1021/bi990315vopenalex-snapshot
Biochemical Analysis of the Saccharomyces cerevisiae SEC18 Gene Product: Implications for the Molecular Mechanism of Membrane Fusion
inferredcites →https://doi.org/10.1038/nrm3821openalex-snapshot
The emergence of proteome-wide technologies: systematic analysis of proteins comes of age
inferredcites →https://doi.org/10.1042/bj20091813openalex-snapshot
Novel insights into mannitol metabolism in the fungal plant pathogen Botrytis cinerea
inferredcites →https://doi.org/10.1042/bsr20180067openalex-snapshot
Comparative proteomic analysis reveals the regulatory network of the veA gene during asexual and sexual spore development of Aspergillus cristatus
inferredcites →https://doi.org/10.1093/bioinformatics/bth092openalex-snapshot
TANDEM: matching proteins with tandem mass spectra
inferredcites →https://doi.org/10.1093/nar/30.1.276openalex-snapshot
The Pfam Protein Families Database
inferredcites →https://doi.org/10.1093/nar/gkn176openalex-snapshot
High-throughput functional annotation and data mining with the Blast2GO suite
inferredcites →https://doi.org/10.1093/nar/gkp985openalex-snapshot
The Pfam protein families database
inferredcites →https://doi.org/10.1094/mpmi-01-11-0007openalex-snapshot
The Botrytis cinerea Reg1 Protein, a Putative Transcriptional Regulator, Is Required for Pathogenicity, Conidiogenesis, and the Production of Secondary Metabolites
inferredcites →https://doi.org/10.1094/mpmi-10-10-0248openalex-snapshot
The Sesquiterpene Botrydial Produced by Botrytis cinerea Induces the Hypersensitive Response on Plant Tissues and Its Action Is Modulated by Salicylic Acid and Jasmonic Acid Signaling
inferredcites →https://doi.org/10.1094/mpmi-10-13-0314-ropenalex-snapshot
Knocking Out Bcsas1 in Botrytis cinerea Impacts Growth, Development, and Secretion of Extracellular Proteins, Which Decreases Virulence
inferredcites →https://doi.org/10.1094/mpmi-11-11-0299openalex-snapshot
The Mitogen-Activated Protein Kinase BcSak1 of Botrytis cinerea Is Required for Pathogenic Development and Has Broad Regulatory Functions Beyond Stress Response
inferredcites →https://doi.org/10.1094/mpmi-12-14-0411-ropenalex-snapshot
The VELVET Complex in the Gray Mold FungusBotrytis cinerea: Impact of BcLAE1 on Differentiation, Secondary Metabolism, and Virulence
inferredcites →https://doi.org/10.1094/mpmi-19-1042openalex-snapshot
A Class III Histidine Kinase Acts as a Novel Virulence Factor in Botrytis cinerea
inferredcites →https://doi.org/10.1094/mpmi.2000.13.7.724openalex-snapshot
The BMP1 Gene Is Essential for Pathogenicity in the Gray Mold Fungus Botrytis cinerea
inferredcites →https://doi.org/10.1101/gad.11.6.799openalex-snapshot
The ROOT HAIR DEFECTIVE3 gene encodes an evolutionarily conserved protein with GTP-binding motifs and is required for regulated cell enlargement in Arabidopsis.
inferredcites →https://doi.org/10.1104/pp.007716openalex-snapshot
Function of a Plant Stress-Induced Gene, HVA22. Synthetic Enhancement Screen with Its Yeast Homolog Reveals Its Role in Vesicular Traffic
inferredcites →https://doi.org/10.1105/tpc.112.096156openalex-snapshot
Mitogen-Activated Protein Kinase Signaling in Plant-Interacting Fungi: Distinct Messages from Conserved Messengers
inferredcites →https://doi.org/10.1111/j.1364-3703.2007.00383.xopenalex-snapshot
The Slt2‐type MAP kinase Bmp3 of Botrytis cinerea is required for normal saprotrophic growth, conidiation, plant surface sensing and host tissue colonization
inferredcites →https://doi.org/10.1111/j.1364-3703.2009.00579.xopenalex-snapshot
The role of mitogen‐activated protein (MAP) kinase signalling components and the Ste12 transcription factor in germination and pathogenicity of Botrytis cinerea
inferredcites →https://doi.org/10.1111/j.1364-3703.2010.00692.xopenalex-snapshot
The Botrytis cinerea phytotoxin botcinic acid requires two polyketide synthases for production and has a redundant role in virulence with botrydial
inferredcites →https://doi.org/10.1111/j.1364-3703.2011.00778.xopenalex-snapshot
BcAtf1, a global regulator, controls various differentiation processes and phytotoxin production in Botrytis cinerea
inferredcites →https://doi.org/10.1111/j.1365-2958.2005.04991.xopenalex-snapshot
Different signalling pathways involving a Gα protein, cAMP and a MAP kinase control germination of Botrytis cinerea conidia
inferredcites →https://doi.org/10.1111/j.1365-2958.2008.06105.xopenalex-snapshot
The Gα subunit BCG1, the phospholipase C (BcPLC1) and the calcineurin phosphatase co‐ordinately regulate gene expression in the grey mould fungusBotrytis cinerea
inferredcites →https://doi.org/10.1111/j.1469-8137.2006.01682.xopenalex-snapshot
Characterization of a new, nonpathogenic mutant of Botrytis cinerea with impaired plant colonization capacity
inferredcites →https://doi.org/10.1111/mmi.13262openalex-snapshot
DHN melanin biosynthesis in the plant pathogenic fungus Botrytis cinerea is based on two developmentally regulated key enzyme (PKS)‐encoding genes
inferredcites →https://doi.org/10.1111/nph.15221openalex-snapshot
Investigations on VELVET regulatory mutants confirm the role of host tissue acidification and secretion of proteins in the pathogenesis of Botrytis cinerea
inferredcites →https://doi.org/10.1126/science.1065224openalex-snapshot
Role of Erv29p in Collecting Soluble Secretory Proteins into ER-Derived Transport Vesicles
inferredcites →https://doi.org/10.1128/ec.00153-06openalex-snapshot
BcSAK1, a Stress-Activated Mitogen-Activated Protein Kinase, Is Involved in Vegetative Differentiation and Pathogenicity in Botrytis cinerea
inferredcites →https://doi.org/10.1128/ec.00193-09openalex-snapshot
Our Paths Might Cross: the Role of the Fungal Cell Wall Integrity Pathway in Stress Response and Cross Talk with Other Stress Response Pathways
inferredcites →https://doi.org/10.1128/jb.171.2.1087-1092.1989openalex-snapshot
Roles of glycerol and glycerol-3-phosphate dehydrogenase (NAD+) in acquired osmotolerance of Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1128/jb.176.18.5857-5860.1994openalex-snapshot
Nikkomycin Z is a specific inhibitor of Saccharomyces cerevisiae chitin synthase isozyme Chs3 in vitro and in vivo
inferredcites →https://doi.org/10.1128/microbiolspec.funk-0035-2016openalex-snapshot
The Fungal Cell Wall: Structure, Biosynthesis, and Function
inferredcites →https://doi.org/10.1128/mmbr.62.4.1264-1300.1998openalex-snapshot
MAP Kinase Pathways in the Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1371/journal.pgen.1002230openalex-snapshot
Genomic Analysis of the Necrotrophic Fungal Pathogens Sclerotinia sclerotiorum and Botrytis cinerea
inferredcites →https://doi.org/10.1371/journal.ppat.1005683openalex-snapshot
Major Sensing Proteins in Pathogenic Fungi: The Hybrid Histidine Kinase Family
inferredcites →https://doi.org/10.1371/journal.ppat.1007285openalex-snapshot
The MAPK kinase BcMkk1 suppresses oxalic acid biosynthesis via impeding phosphorylation of BcRim15 by BcSch9 in Botrytis cinerea
inferredcites →https://doi.org/10.3389/fmicb.2015.01019openalex-snapshot
Mannitol metabolism during pathogenic fungal–host interactions under stressed conditions

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Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2174/1389203720666190906165111openalex-snapshot
Breakpoint: Cell Wall and Glycoproteins and their Crucial Role in the Phytopathogenic Fungi Infection
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