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Polyglycine hydrolases secreted by Pleosporineae fungi that target the linker region of plant class IV chitinases
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1007/s13225-011-0139-4openalex-snapshot
Cochliobolus: an overview and current status of species
inferredcites →https://doi.org/10.1016/j.cbpa.2006.11.021openalex-snapshot
Methods for mapping protease specificity
inferredcites →https://doi.org/10.1016/j.jmb.2005.09.082openalex-snapshot
Crystal Structures of Active LytM
inferredcites →https://doi.org/10.1016/j.pmpp.2009.10.004openalex-snapshot
Maize seed chitinase is modified by a protein secreted by Bipolaris zeicola
inferredcites →https://doi.org/10.1016/j.pmpp.2012.12.001openalex-snapshot
Chitinase modifying proteins from phylogenetically distinct lineages of Brassica pathogens
inferredcites →https://doi.org/10.1016/s0021-9258(19)50474-4openalex-snapshot
Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed.
inferredcites →https://doi.org/10.1021/bi300200popenalex-snapshot
Identification of Exosite Residues of Factor Xa Involved in Recognition of PAR-2 on Endothelial Cells
inferredcites →https://doi.org/10.1021/jm400369qopenalex-snapshot
Designing Allosteric Regulators of Thrombin. Exosite 2 Features Multiple Subsites That Can Be Targeted by Sulfated Small Molecules for Inducing Inhibition
inferredcites →https://doi.org/10.1038/324365a0openalex-snapshot
Plant chitinases are potent inhibitors of fungal growth
inferredcites →https://doi.org/10.1042/0264-6021:3500563openalex-snapshot
Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
inferredcites →https://doi.org/10.1042/bj0750236openalex-snapshot
The proteins of Hevea brasiliensis latex. 4. Isolation and characterization of crystalline hevein
inferredcites →https://doi.org/10.1042/bj20081765openalex-snapshot
Design of a polypeptide FRET substrate that facilitates study of the antimicrobial protease lysostaphin
inferredcites →https://doi.org/10.1073/pnas.0508882103openalex-snapshot
Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor
inferredcites →https://doi.org/10.1073/pnas.1208031109openalex-snapshot
Structural basis for activation of the complement system by component C4 cleavage
inferredcites →https://doi.org/10.1074/jbc.272.29.17907openalex-snapshot
A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B
inferredcites →https://doi.org/10.1074/jbc.m111.279646openalex-snapshot
Identification of a Chitinase-modifying Protein from Fusarium verticillioides
inferredcites →https://doi.org/10.1074/jbc.m509691200openalex-snapshot
Cell Wall-targeting Domain of Glycylglycine Endopeptidase Distinguishes among Peptidoglycan Cross-bridges
inferredcites →https://doi.org/10.1079/9780851997438.0000openalex-snapshot
Phoma identification manual. Differentiation of specific and infra-specific taxa in culture
inferredcites →https://doi.org/10.1080/21501203.2010.519156openalex-snapshot
Highlights of the Didymellaceae: A polyphasic approach to characterize Phoma and related pleosporalean genera
inferredcites →https://doi.org/10.1093/nar/gkn663openalex-snapshot
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
inferredcites →https://doi.org/10.1094/phyto-100-7-0645openalex-snapshot
Allozyme-Specific Modification of a Maize Seed Chitinase by a Protein Secreted by the Fungal Pathogen Stenocarpella maydis
inferredcites →https://doi.org/10.1111/j.1364-3703.2010.00677.xopenalex-snapshot
Modification of recombinant maize ChitA chitinase by fungal chitinase‐modifying proteins
inferredcites →https://doi.org/10.1111/j.1364-3703.2012.00805.xopenalex-snapshot
Truncation of class IV chitinases from Arabidopsis by secreted fungal proteases
inferredcites →https://doi.org/10.1111/j.1538-7836.2004.01021.xopenalex-snapshot
Exosite-driven substrate specificity and function in coagulation
inferredcites →https://doi.org/10.1128/jb.182.9.2635-2638.2000openalex-snapshot
Site-Specific Serine Incorporation by Lif and Epr into Positions 3 and 5 of the Staphylococcal Peptidoglycan Interpeptide Bridge
inferredcites →https://doi.org/10.1371/journal.pgen.1003233openalex-snapshot
Comparative Genome Structure, Secondary Metabolite, and Effector Coding Capacity across Cochliobolus Pathogens
inferredcites →https://doi.org/10.2307/3761627openalex-snapshot
Cochliobolus Phylogenetics and the Origin of Known, Highly Virulent Pathogens, Inferred from ITS and Glyceraldehyde-3-Phosphate Dehydrogenase Gene Sequences
inferredcites →https://doi.org/10.3114/sim.2009.64.04openalex-snapshot
Multi-locus phylogeny of Pleosporales: a taxonomic, ecological and evolutionary re-evaluation
inferredcites →https://doi.org/10.3114/sim.2010.65.01openalex-snapshot
Highlights of the Didymellaceae: A polyphasic approach to characterise Phoma and related pleosporalean genera
inferredcites →https://doi.org/10.3114/sim0004openalex-snapshot
Redisposition of phoma-like anamorphs in Pleosporales
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.3897/mycokeys.105.119536zenodo-depositor-declared
Didymellaceae species associated with tea plant (Camellia sinensis) in China
inferred← citeshttps://doi.org/10.1002/pro.2705openalex-snapshot
Polyglycine hydrolases: Fungal β‐lactamase‐like endoproteases that cleave polyglycine regions within plant class IV chitinases
inferred← citeshttps://doi.org/10.1002/pro.3175openalex-snapshot
Recognition of corn defense chitinases by fungal polyglycine hydrolases
inferred← citeshttps://doi.org/10.1016/j.bbrc.2024.149746openalex-snapshot
In vitro functional analysis and in silico structural modelling of pathogen-secreted polyglycine hydrolases
inferred← citeshttps://doi.org/10.1016/j.biochi.2015.10.003openalex-snapshot
Peptidase specificity from the substrate cleavage collection in the MEROPS database and a tool to measure cleavage site conservation
inferred← citeshttps://doi.org/10.1016/j.funbio.2019.11.005openalex-snapshot
Extracellular peptidases of insect-associated fungi and their possible use in biological control programs and as pathogenicity markers
inferred← citeshttps://doi.org/10.1016/j.pbi.2024.102621openalex-snapshot
Extracellular proteases from microbial plant pathogens as virulence factors
inferred← citeshttps://doi.org/10.1016/j.pmpp.2018.12.004openalex-snapshot
Purification and in vitro activities of a chitinase-modifying protein from the corn ear rot pathogen Stenocarpella maydis
inferred← citeshttps://doi.org/10.1107/s2059798323000311openalex-snapshot
Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model
inferred← citeshttps://doi.org/10.1134/s0006297916130083openalex-snapshot
Role of proteolytic enzymes in the interaction of phytopathogenic microorganisms with plants
inferred← citeshttps://doi.org/10.3389/fpls.2015.00584openalex-snapshot
The battle in the apoplast: further insights into the roles of proteases and their inhibitors in plant–pathogen interactions
inferred← citeshttps://doi.org/10.3390/jof10120868openalex-snapshot
Comparative Genomics and Pathogenicity Analysis of Three Fungal Isolates Causing Barnyard Grass Blast
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