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Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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A Modified Hot Borate Method Significantly Enhances the Yield of High-Quality RNA from Cotton (Gossypium hirsutum L.)
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Comparative Protein Modelling by Satisfaction of Spatial Restraints
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Structure and Possible Function of Aspartic Proteinases in Barley and other Plants
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Plant Aspartic Proteinases from Cynara Cardunculus Spp. Flavescens Cv. Cardoon; Nucleotide Sequence of a cDNA Encoding Cyprosin and its Organ-Specific Expression
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Cardosin A and B, Aspartic Proteases from the Flowers of Cardoon
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Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L.
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Aspartic proteinases are expressed in pitchers of the carnivorous plant Nepenthes alata Blanco
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Glycoprotein staining following electrophoresis on acrylamide gels
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Measurement of protein using bicinchoninic acid
inferredcites →https://doi.org/10.1016/0014-5793(72)80181-9openalex-snapshot
Enzymes from carnivorous plants (nepenthes). Isolation of the protease nepenthacin
inferredcites →https://doi.org/10.1016/0022-2836(90)90156-gopenalex-snapshot
X-ray analyses of aspartic proteinases
inferredcites →https://doi.org/10.1016/0076-6879(95)48009-9openalex-snapshot
[7] Families of aspartic peptidases, and those of unknown catalytic mechanism
inferredcites →https://doi.org/10.1016/0263-7855(88)80054-7openalex-snapshot
The MIDAS display system
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Handbook of Proteolytic Enzymes
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Protease activity of CND41, a chloroplast nucleoid DNA‐binding protein, isolated from cultured tobacco cells
inferredcites →https://doi.org/10.1016/s0021-9258(18)81308-4openalex-snapshot
The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated Proteins
inferredcites →https://doi.org/10.1016/s0022-2836(99)80017-5openalex-snapshot
X-ray analyses of aspartic proteinases
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Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
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A Comparative Study on the NH2-Terminal Amino Acid Sequences and Some Other Properties of Six Isozymic Forms of Human Pepsinogens and Pepsins1
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a129166openalex-snapshot
Acid Protease in Nepenthes
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a129899openalex-snapshot
Digestive Enzymes in Insectivorous Plants*
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a129956openalex-snapshot
Digestive Enzymes in Insectivorous Plants
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a130637openalex-snapshot
Specific Inhibition of Acid Proteases from Brain, Kidney, Skeletal Muscle, and Insectivorous Plants by Diazoacetyl-DL-norleucine Methyl Ester and by Pepstatin *
inferredcites →https://doi.org/10.1105/tpc.9.9.1673openalex-snapshot
A novel protein with DNA binding activity from tobacco chloroplast nucleoids.
inferredcites →https://doi.org/10.1110/ps.25801openalex-snapshot
Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes
inferredcites →https://doi.org/10.1111/j.1432-1033.1991.tb16465.xopenalex-snapshot
Primary structure of a barley‐grain aspartic proteinase
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.tb20783.xopenalex-snapshot
Rice Aspartic Proteinase, Oryzasin, Expressed During Seed Ripening and Germination, has a Gene Organization Distinct from Those of Animal and Microbial Aspartic Proteinases
inferredcites →https://doi.org/10.1159/000350087openalex-snapshot
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
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IMPROVED PURIFICATION OF SLOW MOVING PROTEASE FROM HUMAN GASTRIC MUCOSA AND ITS ACTION ON THE B CHAIN OF OXIDIZED BOVINE INSULIN
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A Novel Protein with DNA Binding Activity from Tobacco Chloroplast Nucleoids
inferredcites →https://doi.org/10.55360/cpn292.cf425openalex-snapshot
The enduring controversies concerning the process of protein digestion in Nepenthes (Nepenthaceae)
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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The liquid from carnivorous marsh pitcher plants (Heliamphora sp.) contains endogenous enzymes for prey digestion
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Novel pitcher plant–spider mutualism is dependent upon environmental resource abundance
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A dipteran larva–pitcher plant digestive mutualism is dependent on prey resource digestibility
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Protein replenishment in pitcher fluids of Nepenthes × ventrata revealed by quantitative proteomics (SWATH-MS) informed by transcriptomics
inferred← citeshttps://doi.org/10.1007/s42485-024-00172-6openalex-snapshot
Functional characterization of digestive enzymes from Nepenthes khasiana: integration of in silico and in vitro approaches
inferred← citeshttps://doi.org/10.1016/j.bbapap.2013.11.009openalex-snapshot
Secreted major Venus flytrap chitinase enables digestion of Arthropod prey
inferred← citeshttps://doi.org/10.1016/j.csbj.2016.05.003openalex-snapshot
Sequence comparison, molecular modeling, and network analysis predict structural diversity in cysteine proteases from the Cape sundew, Drosera capensis
inferred← citeshttps://doi.org/10.1016/j.fbio.2025.106159openalex-snapshot
Enzymatic properties identification of pitcher fluid proteases from Nepenthes × miranda
inferred← citeshttps://doi.org/10.1016/j.febslet.2005.09.043openalex-snapshot
An S‐like ribonuclease gene is used to generate a trap‐leaf enzyme in the carnivorous plant Drosera adelae
inferred← citeshttps://doi.org/10.1016/j.foodchem.2006.09.021openalex-snapshot
Purification and characterization of sea bream (Sparus latus Houttuyn) pepsinogens and pepsins
inferred← citeshttps://doi.org/10.1016/j.foodchem.2008.11.077openalex-snapshot
Identification of pepsinogens and pepsins from the stomach of European eel (Anguilla anguilla)
inferred← citeshttps://doi.org/10.1016/j.foodchem.2025.143714openalex-snapshot
Cleavage specificity of the pitcher fluid proteases from Nepenthes × miranda and their reduction on allergenicity of cow's milk proteins
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.12.104openalex-snapshot
Serine carboxypeptidases from the carnivorous plant Nepenthes mirabilis: Partial characterization and heterologous expression
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102355openalex-snapshot
The nepenthesin insert in the Plasmodium falciparum aspartic protease plasmepsin V is necessary for enzyme function
inferred← citeshttps://doi.org/10.1016/j.jbiotec.2017.11.014openalex-snapshot
Nepenthes: State of the art of an inspiring plant for biotechnologists
inferred← citeshttps://doi.org/10.1016/j.jcs.2013.05.007openalex-snapshot
Protein mobilization and malting-specific proteinase expression during barley germination
inferred← citeshttps://doi.org/10.1016/j.jplph.2007.03.016openalex-snapshot
Two types of aspartic proteinases from buckwheat seed – Gene structure and expression analysis
inferred← citeshttps://doi.org/10.1016/j.jprot.2012.05.048openalex-snapshot
Proteomic analysis of secreted protein induced by a component of prey in pitcher fluid of the carnivorous plant Nepenthes alata
inferred← citeshttps://doi.org/10.1016/j.jprot.2015.09.027openalex-snapshot
Quantitative proteomic analysis of Araucaria angustifolia (Bertol.) Kuntze cell lines with contrasting embryogenic potential
inferred← citeshttps://doi.org/10.1016/j.lwt.2013.07.009openalex-snapshot
Sour orange Citrus aurantium L. flowers: A new vegetable source of milk-clotting proteases
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2005.05.015openalex-snapshot
Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum
inferred← citeshttps://doi.org/10.1016/j.pep.2013.12.005openalex-snapshot
Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis
inferred← citeshttps://doi.org/10.1016/j.phytochem.2008.07.012openalex-snapshot
Expression and characterization of the recombinant aspartic proteinase A1 from Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1016/j.phytochem.2009.12.005openalex-snapshot
Structure–function characterization of the recombinant aspartic proteinase A1 from Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1016/j.phytochem.2010.11.024openalex-snapshot
Carnivorous pitcher plants: Insights in an old topic
inferred← citeshttps://doi.org/10.1016/j.phytochem.2012.05.028openalex-snapshot
Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare (Asteraceae)
inferred← citeshttps://doi.org/10.1016/j.plantsci.2025.112558openalex-snapshot
Nitric oxide stimulates digestion modifying the nutrient composition of the traps’ fluid of Nepenthes x ventrata
inferred← citeshttps://doi.org/10.1016/j.plaphy.2008.04.007openalex-snapshot
Widespread tissue expression of nepenthesin-like aspartic protease genes in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1016/j.plaphy.2016.03.008openalex-snapshot
A carnivorous sundew plant prefers protein over chitin as a source of nitrogen from its traps
inferred← citeshttps://doi.org/10.1016/j.plaphy.2021.01.049openalex-snapshot
Enzyme activities in two sister-species of carnivorous pitcher plants (Nepenthes) with contrasting nutrient sequestration strategies
inferred← citeshttps://doi.org/10.1016/j.tig.2026.01.015openalex-snapshot
Complexity and innovation in carnivorous plant genomes
inferred← citeshttps://doi.org/10.1017/s0266467410000532openalex-snapshot
The plant-ant Camponotus schmitzi helps its carnivorous host-plant Nepenthes bicalcarata to catch its prey
inferred← citeshttps://doi.org/10.1021/ac404076jopenalex-snapshot
Aspartic Protease Nepenthesin-1 as a Tool for Digestion in Hydrogen/Deuterium Exchange Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.analchem.5b00831openalex-snapshot
Recombinant Nepenthesin II for Hydrogen/Deuterium Exchange Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.analchem.6b05103openalex-snapshot
Thiol-ene Monolithic Pepsin Microreactor with a 3D-Printed Interface for Efficient UPLC-MS Peptide Mapping Analyses
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b05694openalex-snapshot
Comparative Analysis of Cleavage Specificities of Immobilized Porcine Pepsin and Nepenthesin II under Hydrogen/Deuterium Exchange Conditions
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b00224openalex-snapshot
Carnivorous Nutrition in Pitcher Plants (Nepenthes spp.) via an Unusual Complement of Endogenous Enzymes
inferred← citeshttps://doi.org/10.1021/bi9014055openalex-snapshot
The Prosegment Catalyzes Pepsin Folding to a Kinetically Trapped Native State
inferred← citeshttps://doi.org/10.1021/pr700566dopenalex-snapshot
Proteome Analysis of Pitcher Fluid of the Carnivorous Plant Nepenthes alata
inferred← citeshttps://doi.org/10.1038/nsmb.3061openalex-snapshot
Structural basis for plasmepsin V inhibition that blocks export of malaria proteins to human erythrocytes
inferred← citeshttps://doi.org/10.1038/nsmb.3077openalex-snapshot
Plasmepsin V shows its carnivorous side
inferred← citeshttps://doi.org/10.1038/s41559-016-0059openalex-snapshot
Genome of the pitcher plant Cephalotus reveals genetic changes associated with carnivory
inferred← citeshttps://doi.org/10.1038/s41598-020-61193-xopenalex-snapshot
Tropical pitcher plants (Nepenthes) act as ecological filters by altering properties of their fluid microenvironments
inferred← citeshttps://doi.org/10.1074/jbc.m115.672550openalex-snapshot
Enzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid
inferred← citeshttps://doi.org/10.1074/jbc.m702477200openalex-snapshot
Characterization of Recombinant CDR1, an Arabidopsis Aspartic Proteinase Involved in Disease Resistance
inferred← citeshttps://doi.org/10.1074/jbc.rev120.009309openalex-snapshot
Malaria parasite plasmepsins: More than just plain old degradative pepsins
inferred← citeshttps://doi.org/10.1074/mcp.m112.021006openalex-snapshot
The Protein Composition of the Digestive Fluid from the Venus Flytrap Sheds Light on Prey Digestion Mechanisms
inferred← citeshttps://doi.org/10.1074/mcp.m112.025221openalex-snapshot
Nepenthesin from Monkey Cups for Hydrogen/Deuterium Exchange Mass Spectrometry
inferred← citeshttps://doi.org/10.1074/mcp.r114.042572openalex-snapshot
Less is More: Membrane Protein Digestion Beyond Urea–Trypsin Solution for Next-level Proteomics
inferred← citeshttps://doi.org/10.1080/12538078.2005.10515467openalex-snapshot
Food web and fluid in pitchers ofNepenthes mirabilisin Zhuhai, China
inferred← citeshttps://doi.org/10.1080/17429145.2022.2123567openalex-snapshot
A semi-detritivorous pitcher plant, Nepenthes ampullaria diverges in its regulation of pitcher fluid properties
inferred← citeshttps://doi.org/10.1080/17429145.2025.2597586openalex-snapshot
Barley nepenthesin HvNEP-1 enhances the resistance to Gibberella ear rot and Fusarium ear rot in maize
inferred← citeshttps://doi.org/10.1080/23818107.2025.2545823openalex-snapshot
The acid phosphatase-containing digestive fluid secreted by Nepenthes khasiana pitchers inhibits plant growth, possibly due to the presence of heat-stable growth-inhibitory molecules
inferred← citeshttps://doi.org/10.1086/499284openalex-snapshot
Cloning and Characterization of a Ribonuclease, a Cysteine Proteinase, and an Aspartic Proteinase from Pitchers of the Carnivorous Plant Nepenthes ventricosa Blanco
inferred← citeshttps://doi.org/10.1088/1755-1315/457/1/012012openalex-snapshot
Molecular and adaptive evolution of Nep2 gene from carnivorous plant Nepenthes
inferred← citeshttps://doi.org/10.1093/aob/mcab071openalex-snapshot
Recent ecophysiological, biochemical and evolutional insights into plant carnivory
inferred← citeshttps://doi.org/10.1093/aob/mcac150openalex-snapshot
Expression and function of an S1-type nuclease in the digestive fluid of a sundew, Drosera adelae
inferred← citeshttps://doi.org/10.1093/aob/mcu266openalex-snapshot
Fluid physico-chemical properties influence capture and diet in Nepenthes pitcher plants
inferred← citeshttps://doi.org/10.1093/aob/mcw001openalex-snapshot
Proteome analysis of digestive fluids inNepenthespitchers
inferred← citeshttps://doi.org/10.1093/aob/mcw110openalex-snapshot
Slow food: insect prey and chitin induce phytohormone accumulation and gene expression in carnivorousNepenthesplants
inferred← citeshttps://doi.org/10.1093/gbe/evu110openalex-snapshot
Extensive Expansion of A1 Family Aspartic Proteinases in Fungi Revealed by Evolutionary Analyses of 107 Complete Eukaryotic Proteomes
inferred← citeshttps://doi.org/10.1093/jxb/eraa159openalex-snapshot
Jasmonate-independent regulation of digestive enzyme activity in the carnivorous butterwort Pinguicula × Tina
inferred← citeshttps://doi.org/10.1093/jxb/eraa560openalex-snapshot
Organ-specific expression and epigenetic traits of genes encoding digestive enzymes in the lance-leaf sundew (Drosera adelae)
inferred← citeshttps://doi.org/10.1093/jxb/erad359openalex-snapshot
Is the co-option of jasmonate signalling for botanical carnivory a universal trait for all carnivorous plants?
inferred← citeshttps://doi.org/10.1093/jxb/eraf147openalex-snapshot
The multifaceted roles of plant aspartic proteases
inferred← citeshttps://doi.org/10.1093/jxb/erq004openalex-snapshot
Ion fluxes across the pitcher walls of three Bornean Nepenthes pitcher plant species: flux rates and gland distribution patterns reflect nitrogen sequestration strategies
inferred← citeshttps://doi.org/10.1093/jxb/erz034openalex-snapshot
Atypical and nucellin-like aspartic proteases: emerging players in plant developmental processes and stress responses
inferred← citeshttps://doi.org/10.1093/jxb/erz188openalex-snapshot
Jasmonate signalling in carnivorous plants: copycat of plant defence mechanisms
inferred← citeshttps://doi.org/10.1093/molbev/msv020openalex-snapshot
High Gene Family Turnover Rates and Gene Space Adaptation in the Compact Genome of the Carnivorous Plant Utricularia gibba
inferred← citeshttps://doi.org/10.1093/plphys/kiac232openalex-snapshot
The digestive systems of carnivorous plants
inferred← citeshttps://doi.org/10.1093/plphys/kiag018openalex-snapshot
Jasmonate signaling and prey nutrient availability trigger distinct biochemical responses in the Drosera capensis feeding cycle
inferred← citeshttps://doi.org/10.1098/rstb.2025.0095openalex-snapshot
Variable contribution of inquilines to prey digestion in Nepenthes pitcher plants: the role of pitcher traits
inferred← citeshttps://doi.org/10.1101/2022.02.28.482356openalex-snapshot
A nepenthesin insert allosterically controls catalysis in the malaria parasite protease plasmepsin V
inferred← citeshttps://doi.org/10.1101/2023.01.07.523112openalex-snapshot
Adaptive evolution of carnivory in Nepenthes pitcher plants: a comparative transcriptomics and proteomics perspective
inferred← citeshttps://doi.org/10.1101/2025.07.18.665637openalex-snapshot
Jasmonate-induced prey response in the carnivorous plant Drosera capensis
inferred← citeshttps://doi.org/10.1107/s2053230x15022323openalex-snapshot
Crystallization of nepenthesin I using a low-pH crystallization screen
inferred← citeshttps://doi.org/10.1111/ijfs.13101openalex-snapshot
Improved extraction of disulphide‐rich bioactive proteins from soya hulls: characterisation of a novel aspartic proteinase
inferred← citeshttps://doi.org/10.1111/j.1365-3040.2011.02382.xopenalex-snapshot
Nutritional benefit from leaf litter utilization in the pitcher plant Nepenthes ampullaria
inferred← citeshttps://doi.org/10.1111/j.1439-0418.2010.01505.xopenalex-snapshot
Transcriptional analysis of molecular interactions between Pseudomonas fluorescens strain TDK1, Oryza sativa and Cnaphalocrocis medinalis
inferred← citeshttps://doi.org/10.1111/nph.14352openalex-snapshot
The role of electrical and jasmonate signalling in the recognition of captured prey in the carnivorous sundew plant Drosera capensis
inferred← citeshttps://doi.org/10.1111/nph.70229openalex-snapshot
How the diversity in digestion in carnivorous plants may have evolved
inferred← citeshttps://doi.org/10.1128/aem.00812-23openalex-snapshot
Carnivorous Nepenthes Pitchers with Less Acidic Fluid House Nitrogen-Fixing Bacteria
inferred← citeshttps://doi.org/10.11575/prism/28475openalex-snapshot
Towards a Biochemical Reconstitution of Nepenthes Pitcher Fluid for the Treatment of Celiac Disease
inferred← citeshttps://doi.org/10.1186/1471-2164-10-437openalex-snapshot
Pepsin homologues in bacteria
inferred← citeshttps://doi.org/10.1186/1471-2164-12-254openalex-snapshot
The aspartic proteinase family of three Phytophthora species
inferred← citeshttps://doi.org/10.1186/s12864-017-3979-9openalex-snapshot
Physical mapping of QTL for tuber yield, starch content and starch yield in tetraploid potato (Solanum tuberosum L.) by means of genome wide genotyping by sequencing and the 8.3 K SolCAP SNP array
inferred← citeshttps://doi.org/10.1186/s12870-016-0789-1openalex-snapshot
Transcriptome profiling of grapevine seedless segregants during berry development reveals candidate genes associated with berry weight
inferred← citeshttps://doi.org/10.1186/s12870-020-02663-2openalex-snapshot
Pitchers of Nepenthes khasiana express several digestive-enzyme encoding genes, harbor mostly fungi and probably evolved through changes in the expression of leaf polarity genes
inferred← citeshttps://doi.org/10.1186/s13104-025-07082-wopenalex-snapshot
First report of the chloroplast and mitochondrial genomes of the Indian pitcher plant, Nepenthes khasiana Hook.f.
inferred← citeshttps://doi.org/10.1186/s40709-018-0086-2openalex-snapshot
3D electron tomographic and biochemical analysis of ER, Golgi and trans Golgi network membrane systems in stimulated Venus flytrap (Dionaea muscipula) glandular cells
inferred← citeshttps://doi.org/10.1271/bbb.100234openalex-snapshot
Soybean Basic 7S Globulin: Subunit Heterogeneity and Molecular Evolution
inferred← citeshttps://doi.org/10.1371/journal.pone.0036179openalex-snapshot
A Carnivorous Plant Fed by Its Ant Symbiont: A Unique Multi-Faceted Nutritional Mutualism
inferred← citeshttps://doi.org/10.1371/journal.pone.0104424openalex-snapshot
Abundance of Cysteine Endopeptidase Dionain in Digestive Fluid of Venus Flytrap (Dionaea muscipula Ellis) Is Regulated by Different Stimuli from Prey through Jasmonates
inferred← citeshttps://doi.org/10.1371/journal.pone.0118853openalex-snapshot
Nepenthesin Protease Activity Indicates Digestive Fluid Dynamics in Carnivorous Nepenthes Plants
inferred← citeshttps://doi.org/10.2183/pjab.89.201openalex-snapshot
Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidases
inferred← citeshttps://doi.org/10.2298/abs0702119mopenalex-snapshot
Isolation and structural analysis of a gene coding for a novel type of aspartic proteinase from buckwheat seed (Fagopyrum esculentum Moench)
inferred← citeshttps://doi.org/10.2298/jsc0906607mopenalex-snapshot
Successful production of recombinant buckwheat cysteine-rich aspartic protease in Escherichia coli
inferred← citeshttps://doi.org/10.3389/fpls.2019.00793openalex-snapshot
Assessing Carnivorous Plants for the Production of Recombinant Proteins
inferred← citeshttps://doi.org/10.3389/fpls.2020.625507openalex-snapshot
Transcriptomic and Proteomic Analyses of Nepenthes ampullaria and Nepenthes rafflesiana Reveal Parental Molecular Expression in the Pitchers of Their Hybrid, Nepenthes × hookeriana
inferred← citeshttps://doi.org/10.3389/fpls.2021.702557openalex-snapshot
Barley Nepenthesin-Like Aspartic Protease HvNEP-1 Degrades Fusarium Phytase, Impairs Toxin Production, and Suppresses the Fungal Growth
inferred← citeshttps://doi.org/10.3389/fpls.2023.1072168openalex-snapshot
Phylogenetic and AlphaFold predicted structure analyses provide insights for A1 aspartic protease family classification in Arabidopsis
inferred← citeshttps://doi.org/10.3390/agronomy10020203openalex-snapshot
Overexpression of Nepenthesin HvNEP-1 in Barley Endosperm Reduces Fusarium Head Blight and Mycotoxin Accumulation
inferred← citeshttps://doi.org/10.3390/biology10020075openalex-snapshot
Defense and Offense Strategies: The Role of Aspartic Proteases in Plant–Pathogen Interactions
inferred← citeshttps://doi.org/10.3390/biology12101356openalex-snapshot
Do Reactive Oxygen and Nitrogen Species Have a Similar Effect on Digestive Processes in Carnivorous Nepenthes Plants and Humans?
inferred← citeshttps://doi.org/10.3390/catal12070726openalex-snapshot
Nepenthes mirabilis Fractionated Pitcher Fluid Use for Mixed Agro-Waste Pretreatment: Advocacy for Non-Chemical Use in Biorefineries
inferred← citeshttps://doi.org/10.3390/d16020077openalex-snapshot
A Survey of Bacteria and Fungi Associated with Leaves, Rhizophylls, and Vesicles of the Carnivorous Plant Genlisea hispidula (Lentibulariaceae)
inferred← citeshttps://doi.org/10.3390/ijms27198462openalex-snapshot
ROS Equilibrium in the Digestive Fluid of the Nepenthes × ventrata Trap at Various Developmental Stages
inferred← citeshttps://doi.org/10.3390/plants11040544openalex-snapshot
Genome-Wide Analyses of Aspartic Proteases on Potato Genome (Solanum tuberosum): Generating New Tools to Improve the Resistance of Plants to Abiotic Stress
inferred← citeshttps://doi.org/10.3390/plants12040755openalex-snapshot
Is the Phytotoxic Effect of Digestive Fluid of Nepenthes x ventrata on Tomato Related to Reactive Oxygen Species?
inferred← citeshttps://doi.org/10.3390/plants9050570openalex-snapshot
Molecular Properties and New Potentials of Plant Nepenthesins
inferred← citeshttps://doi.org/10.35537/10915/29125openalex-snapshot
Relación estructura-función de cirsina, una proteasa aspártica de Cirsium vulgare, y compuestos peptídicos derivados con actividad biológica
inferred← citeshttps://doi.org/10.3732/ajb.1300145openalex-snapshot
A simple SDS‐PAGE protein pattern from pitcher secretions as a new tool to distinguish Nepenthes species (Nepenthaceae)
inferred← citeshttps://doi.org/10.4161/psb.5.6.11238openalex-snapshot
The carnivorous syndrome in Nepenthes pitcher plants
inferred← citeshttps://doi.org/10.55360/cpn363.kt419openalex-snapshot
Variations in the content and isozymic composition of nepenthesin in the pitcher fluids among Nepenthes species
inferred← citeshttps://doi.org/10.55360/cpn383.kt848openalex-snapshot
Comparative studies on the acid proteinase activities in the digestive fluids of Nepenthes, Cephalotus, Dionaea, and Drosera
inferred← citeshttps://doi.org/10.55360/cpn414.kt962openalex-snapshot
The digestive fluid of Drosera indica contains a cysteine endopeptidase (“droserain“) similar to dionain from Dionaea muscipula
inferred← citeshttps://doi.org/10.5943/mycosphere/5/2/10openalex-snapshot
Revealing the antimicrobial and enzymatic potentials of culturable fungal endophytes from tropical pitcher plants (Nepenthes spp.)
inferred← citeshttps://doi.org/10.6084/m9.figshare.13251050openalex-snapshot
Additional file 1 of Pitchers of Nepenthes khasiana express several digestive-enzyme encoding genes, harbor mostly fungi and probably evolved through changes in the expression of leaf polarity genes
inferred← citeshttps://doi.org/10.70675/51d37987z631ez4c0dz969dz02cc2407547aopenalex-snapshot
Diversité des stratégies de nutrition chez les plantes à urnes du genre Nepenthes : le rôle du fluide digestif, de ses propriétés physicochimiques et biotiques
inferred← citeshttps://doi.org/10.70675/7de387c8zca31z4f51zbf0dz43e262157fd0openalex-snapshot
Ecology, Evolution and Development of the carnivorous pitcher-plants of the genus Nepenthes
inferred← citeshttps://doi.org/10.7717/peerj.4914openalex-snapshot
Discovery of digestive enzymes in carnivorous plants with focus on proteases
inferred← citeshttps://doi.org/10.9734/bjpr/2016/25841openalex-snapshot
Heat Stable Protease Inhibitors from Sesbania grandiflora and Terminalia catappa
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