On the public citation graph

Recognition of corn defense chitinases by fungal polyglycine hydrolases

https://doi.org/10.1002/pro.3175
0 signed · 31 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1002/pro.2437openalex-snapshot
Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays
inferredcites →https://doi.org/10.1002/pro.2705openalex-snapshot
Polyglycine hydrolases: Fungal β‐lactamase‐like endoproteases that cleave polyglycine regions within plant class IV chitinases
inferredcites →https://doi.org/10.1006/geno.2001.6643openalex-snapshot
Identification, Genomic Organization, and mRNA Expression of LACTB, Encoding a Serine β-Lactamase-like Protein with an Amino-terminal Transmembrane Domain
inferredcites →https://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
inferredcites →https://doi.org/10.1016/j.jmb.2012.09.017openalex-snapshot
Analysis of Structure–Function Relationships in the Colibactin-Maturating Enzyme ClbP
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/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/10.1016/s0022-2836(05)80360-2openalex-snapshot
Basic Local Alignment Search Tool
inferredcites →https://doi.org/10.1016/s0969-2126(00)00188-xopenalex-snapshot
Crystal structure of a d-aminopeptidase from Ochrobactrum anthropi, a new member of the ‘penicillin-recognizing enzyme’ family
inferredcites →https://doi.org/10.1021/bi00123a016openalex-snapshot
Structural similarity of D-aminopeptidase to carboxypeptidase DD and .beta.-lactamases
inferredcites →https://doi.org/10.1021/bm060871mopenalex-snapshot
Role of Hydrophobic Clusters in the Stability of α-Helical Coiled Coils and Their Conversion to Amyloid-like β-Sheets
inferredcites →https://doi.org/10.1042/bj20140268openalex-snapshot
Polyglycine hydrolases secreted by Pleosporineae fungi that target the linker region of plant class IV chitinases
inferredcites →https://doi.org/10.1074/jbc.271.47.30256openalex-snapshot
An Alkaline D-Stereospecific Endopeptidase with β-Lactamase Activity from Bacillus cereus
inferredcites →https://doi.org/10.1080/21501203.2011.584577openalex-snapshot
Fueling the future with fungal genomics
inferredcites →https://doi.org/10.1093/nar/gks1154openalex-snapshot
ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions
inferredcites →https://doi.org/10.1093/nar/gkt1183openalex-snapshot
MycoCosm portal: gearing up for 1000 fungal genomes
inferredcites →https://doi.org/10.1110/ps.051475305openalex-snapshot
Specificity inversion of Ochrobactrum anthropi D‐aminopeptidase to a D,D‐carboxypeptidase with new penicillin binding activity by directed mutagenesis
inferredcites →https://doi.org/10.1110/ps.051641005openalex-snapshot
Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D‐Ala‐D‐Ala peptidase
inferredcites →https://doi.org/10.1110/ps.33002openalex-snapshot
EstB from Burkholderia gladioli: A novel esterase with a β‐lactamase fold reveals steric factors to discriminate between esterolytic and β‐lactam cleaving activity
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.1574-6968.2000.tb09165.xopenalex-snapshot
Identification of afmtA-like gene that has similarity to other PBPs and β-lactamases inStaphylococcus aureus
inferredcites →https://doi.org/10.1126/science.3082007openalex-snapshot
On the Origin of Bacterial Resistance to Penicillin: Comparison of a β-Lactamase and a Penicillin Target
inferredcites →https://doi.org/10.1126/science.7123246openalex-snapshot
Penicillin Target Enzyme and the Antibiotic Binding Site
inferredcites →https://doi.org/10.1128/aem.02518-08openalex-snapshot
Characterization of the Complete Zwittermicin A Biosynthesis Gene Cluster fromBacillus cereus
inferredcites →https://doi.org/10.1186/1471-2148-8-26openalex-snapshot
Evolution of a family of metazoan active-site-serine enzymes from penicillin-binding proteins: a novel facet of the bacterial legacy
inferredcites →https://doi.org/10.1371/journal.pone.0004712openalex-snapshot
Structure of the Archaeal Pab87 Peptidase Reveals a Novel Self-Compartmentalizing Protease Family

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/10.1007/s00425-018-2893-yopenalex-snapshot
Proteomic identification and purification of seed proteins from native Amazonian species displaying antifungal activity
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.ijbiomac.2020.06.123openalex-snapshot
Biochemical and antifungal characteristics of recombinant class I chitinase from Drosera rotundifolia
inferred← citeshttps://doi.org/10.1107/s2059798323000311openalex-snapshot
Crystal structure of a polyglycine hydrolase determined using a RoseTTAFold model
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.