On the public citation graph

A Novel Plant Protein-disulfide Isomerase Involved in the Oxidative Folding of Cystine Knot Defense Proteins

0 signed · 180 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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/bip.20451openalex-snapshot
The cyclotide family of circular miniproteins: Nature's combinatorial peptide template
inferredcites →https://doi.org/10.1006/jmbi.1999.3383openalex-snapshot
Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
inferredcites →https://doi.org/10.1016/0003-9861(59)90090-6openalex-snapshot
Tissue sulfhydryl groups
inferredcites →https://doi.org/10.1016/0378-1119(95)00474-kopenalex-snapshot
Cloning and sequencing of the cDNA encoding human P5
inferredcites →https://doi.org/10.1016/j.ab.2004.10.028openalex-snapshot
Studies on the membrane interactions of the cyclotides kalata B1 and kalata B6 on model membrane systems by surface plasmon resonance
inferredcites →https://doi.org/10.1016/j.bbapap.2004.02.017openalex-snapshot
Protein disulfide isomerase
inferredcites →https://doi.org/10.1016/j.bbrc.2004.05.178openalex-snapshot
Functional differences between human and yeast protein disulfide isomerase family proteins
inferredcites →https://doi.org/10.1016/j.bbrc.2005.03.147openalex-snapshot
ERp57 binds competitively to protein disulfide isomerase and calreticulin
inferredcites →https://doi.org/10.1016/j.cell.2005.10.044openalex-snapshot
The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites
inferredcites →https://doi.org/10.1016/j.febslet.2005.12.064openalex-snapshot
Fully oxidized scrambled isomers are essential and predominant folding intermediates of cardiotoxin‐III
inferredcites →https://doi.org/10.1016/j.tibs.2006.03.005openalex-snapshot
Folding of small disulfide-rich proteins: clarifying the puzzle
inferredcites →https://doi.org/10.1016/j.tibs.2006.06.001openalex-snapshot
Protein disulfide isomerase: the structure of oxidative folding
inferredcites →https://doi.org/10.1016/j.toxicon.2006.11.018openalex-snapshot
Insecticidal plant cyclotides and related cystine knot toxins
inferredcites →https://doi.org/10.1021/bi00013a002openalex-snapshot
Elucidation of the Primary and Three-Dimensional Structure of the Uterotonic Polypeptide Kalata B1
inferredcites →https://doi.org/10.1021/bi00015a019openalex-snapshot
Structural and Functional Characterization of DsbC, a Protein Involved in Disulfide Bond Formation in Escherichia coli
inferredcites →https://doi.org/10.1021/bi00077a018openalex-snapshot
Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
inferredcites →https://doi.org/10.1021/bi0354233openalex-snapshot
Propeptide Does Not Act as an Intramolecular Chaperone but Facilitates Protein Disulfide Isomerase-Assisted Folding of a Conotoxin Precursor
inferredcites →https://doi.org/10.1021/bi049711qopenalex-snapshot
Thermal, Chemical, and Enzymatic Stability of the Cyclotide Kalata B1: The Importance of the Cyclic Cystine Knot
inferredcites →https://doi.org/10.1021/bi990605bopenalex-snapshot
Chemical Synthesis and Folding Pathways of Large Cyclic Polypeptides: Studies of the Cystine Knot Polypeptide Kalata B1
inferredcites →https://doi.org/10.1021/np034068eopenalex-snapshot
Variations in Cyclotide Expression in Viola Species
inferredcites →https://doi.org/10.1038/352036a0openalex-snapshot
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
inferredcites →https://doi.org/10.1038/nrm954openalex-snapshot
Formation and transfer of disulphide bonds in living cells
inferredcites →https://doi.org/10.1038/sj.embor.7400311openalex-snapshot
The human protein disulphide isomerase family: substrate interactions and functional properties
inferredcites →https://doi.org/10.1042/0264-6021:3580681openalex-snapshot
Parameters affecting in vitro oxidation/folding of maurotoxin, a four-disulphide-bridged scorpion toxin
inferredcites →https://doi.org/10.1042/bj20040116openalex-snapshot
Functional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins
inferredcites →https://doi.org/10.1042/bj2130235openalex-snapshot
Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction
inferredcites →https://doi.org/10.1042/bj2750341openalex-snapshot
Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase
inferredcites →https://doi.org/10.1073/pnas.191366898openalex-snapshot
Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinis
inferredcites →https://doi.org/10.1074/jbc.m210492200openalex-snapshot
Disulfide Folding Pathways of Cystine Knot Proteins
inferredcites →https://doi.org/10.1074/jbc.m211147200openalex-snapshot
Twists, Knots, and Rings in Proteins
inferredcites →https://doi.org/10.1074/jbc.m308771200openalex-snapshot
Disulfide Mapping of the Cyclotide Kalata B1
inferredcites →https://doi.org/10.1074/jbc.m310922200openalex-snapshot
Different Contributions of the Three CXXC Motifs of Human Protein-disulfide Isomerase-related Protein to Isomerase Activity and Oxidative Refolding
inferredcites →https://doi.org/10.1074/jbc.m407076200openalex-snapshot
The Acidic C-terminal Domain Stabilizes the Chaperone Function of Protein Disulfide Isomerase
inferredcites →https://doi.org/10.1074/jbc.m407421200openalex-snapshot
Conserved Structural and Sequence Elements Implicated in the Processing of Gene-encoded Circular Proteins
inferredcites →https://doi.org/10.1074/jbc.m414203200openalex-snapshot
A Structural Disulfide of Yeast Protein-disulfide Isomerase Destabilizes the Active Site Disulfide of the N-terminal Thioredoxin Domain
inferredcites →https://doi.org/10.1093/emboj/18.1.65openalex-snapshot
The acidic C‐terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
inferredcites →https://doi.org/10.1093/jac/45.3.413openalex-snapshot
Using Antibodies: A Laboratory Manual
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a003242openalex-snapshot
Functional Analysis of Human P5, a Protein Disulfide Isomerase Homologue
inferredcites →https://doi.org/10.1104/pp.104.056507openalex-snapshot
Phylogenetic Analyses Identify 10 Classes of the Protein Disulfide Isomerase Family in Plants, Including Single-Domain Protein Disulfide Isomerase-Related Proteins
inferredcites →https://doi.org/10.1105/tpc.105.034678openalex-snapshot
A Continent of Plant Defense Peptide Diversity: Cyclotides in AustralianHybanthus(Violaceae)
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.04602.xopenalex-snapshot
Oxidative folding of conotoxins sharing an identical disulfide bridging framework
inferredcites →https://doi.org/10.1126/science.1125248openalex-snapshot
Seamless Proteins Tie Up Their Loose Ends

What points at this work

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

inferred← citeshttps://doi.org/10.1016/j.phytochem.2019.112215zenodo-depositor-declared
An overview of acyclotides: Past, present and future
inferred← citeshttps://doi.org/10.1016/j.phytochem.2021.112749zenodo-depositor-declared
Tropical vibes from Sri Lanka - cyclotides from Viola betonicifolia by transcriptome and mass spectrometry analysis
inferred← citeshttps://doi.org/10.1002/9780470054581.eib250openalex-snapshot
Cyclotides
inferred← citeshttps://doi.org/10.1002/9781394287888.ch14openalex-snapshot
Cyclic Peptides and Betalains
inferred← citeshttps://doi.org/10.1002/9783527631841.ch11openalex-snapshot
Role of Disulfide Bonds in Peptide and Protein Conformation
inferred← citeshttps://doi.org/10.1002/biot.200800288openalex-snapshot
Progress in kalata peptide production via plant cell bioprocessing
inferred← citeshttps://doi.org/10.1002/bip.21113openalex-snapshot
Biochemical and biophysical characterization of a novel plant protein disulfide isomerase
inferred← citeshttps://doi.org/10.1002/bip.21400openalex-snapshot
A new “era” for cyclotide sequencing
inferred← citeshttps://doi.org/10.1002/bip.21414openalex-snapshot
Global cyclotide adventure: A journey dedicated to the discovery of circular peptides from flowering plants
inferred← citeshttps://doi.org/10.1002/bip.21416openalex-snapshot
Ribosomal biosynthesis of the cyclic peptide toxins of Amanita mushrooms
inferred← citeshttps://doi.org/10.1002/bip.22328openalex-snapshot
Cyclotide discovery in Gentianales revisited—identification and characterization of cyclic cystine‐knot peptides and their phylogenetic distribution in Rubiaceae plants
inferred← citeshttps://doi.org/10.1002/bip.22741openalex-snapshot
Review seed biopharmaceutical cyclic peptides: From discovery to applications
inferred← citeshttps://doi.org/10.1002/jmr.928openalex-snapshot
Survey of the year 2007 commercial optical biosensor literature
inferred← citeshttps://doi.org/10.1007/978-0-387-73657-0_13openalex-snapshot
Enzyme Mechanism and Function of a Novel Plant PDI Involved in the Oxidative Folding of Cystine Knot Defense Peptides
inferred← citeshttps://doi.org/10.1007/978-1-4419-7273-6_3openalex-snapshot
Cystine Knot Folding in Cyclotides
inferred← citeshttps://doi.org/10.1007/978-3-0348-0541-4_2openalex-snapshot
Innate Immunity in Plants: The Role of Antimicrobial Peptides
inferred← citeshttps://doi.org/10.1007/978-3-319-91956-0_6openalex-snapshot
Molecular Chaperones: Key Players of Abiotic Stress Response in Plants
inferred← citeshttps://doi.org/10.1007/s00018-009-0159-3openalex-snapshot
Cyclotides: macrocyclic peptides with applications in drug design and agriculture
inferred← citeshttps://doi.org/10.1007/s00253-007-1159-6openalex-snapshot
Formation of cyclotides and variations in cyclotide expression in Oldenlandia affinis suspension cultures
inferred← citeshttps://doi.org/10.1007/s00425-016-2562-yopenalex-snapshot
Immunolocalization of cyclotides in plant cells, tissues and organ supports their role in host defense
inferred← citeshttps://doi.org/10.1007/s00726-012-1376-xopenalex-snapshot
Characterizing circular peptides in mixtures: sequence fragment assembly of cyclotides from a violet plant by MALDI-TOF/TOF mass spectrometry
inferred← citeshttps://doi.org/10.1007/s00726-023-03271-8openalex-snapshot
Insights into the synthesis strategies of plant-derived cyclotides
inferred← citeshttps://doi.org/10.1007/s10059-011-0150-3openalex-snapshot
Protein Disulfide Isomerase-2 of Arabidopsis Mediates Protein Folding and Localizes to Both the Secretory Pathway and Nucleus, Where It Interacts with Maternal Effect Embryo Arrest Factor
inferred← citeshttps://doi.org/10.1007/s10529-008-9704-7openalex-snapshot
Plant cell culture technology–harnessing a biological approach for competitive cyclotides production
inferred← citeshttps://doi.org/10.1007/s10930-012-9460-3openalex-snapshot
Role of the CPC Sequence in the Antioxidant Activity of GcGAST Protein in E.coli
inferred← citeshttps://doi.org/10.1007/s11101-020-09682-9openalex-snapshot
Production of bioactive cyclotides: a comprehensive overview
inferred← citeshttps://doi.org/10.1007/s11101-026-10289-9openalex-snapshot
Cyclotides as sustainable biopesticides: structure, function and agricultural potential
inferred← citeshttps://doi.org/10.1007/s11105-024-01462-5openalex-snapshot
Proximity Labelling Confirms the Involvement of Papain-Like Cysteine Proteases and Chaperones in Cyclotide Biosynthesis
inferred← citeshttps://doi.org/10.1007/s11738-017-2425-6openalex-snapshot
Induction of two cyclotide-like genes Zmcyc1 and Zmcyc5 by abiotic and biotic stresses in Zea mays
inferred← citeshttps://doi.org/10.1007/s12038-022-00283-6openalex-snapshot
LC-MS/MS identification and structural characterization of isolated cyclotides from precursor sequences of Viola odorata L. petiole tissue using computational approach
inferred← citeshttps://doi.org/10.1007/s12268-014-0511-5openalex-snapshot
Biosynthese und molekulare Wirkung von zyklischen Pflanzenpeptiden
inferred← citeshttps://doi.org/10.1007/s12892-015-0006-zopenalex-snapshot
Anti-oxidative potential of boiling soluble antioxidant enzymes inAmelioration of drought-induced oxidative stress in tolerant and sensitive cultivars of Triticum aestivum
inferred← citeshttps://doi.org/10.1007/s42535-026-01631-9openalex-snapshot
Chemical profiling of the folk medicinal plant Hippobroma longiflora as a tool for selecting ex-situ conservation site
inferred← citeshttps://doi.org/10.1016/b978-008045382-8.00115-5openalex-snapshot
Plant Peptide Toxins from Nonmarine Environments
inferred← citeshttps://doi.org/10.1016/bs.abr.2015.08.004openalex-snapshot
Primary Structural Analysis of Cyclotides
inferred← citeshttps://doi.org/10.1016/bs.abr.2015.08.005openalex-snapshot
Biosynthesis of Cyclotides
inferred← citeshttps://doi.org/10.1016/bs.abr.2015.09.002openalex-snapshot
Cyclotides in the Rubiaceae
inferred← citeshttps://doi.org/10.1016/bs.abr.2015.09.010openalex-snapshot
Cyclotides in a Biotechnological Context
inferred← citeshttps://doi.org/10.1016/j.agrcom.2026.100142openalex-snapshot
Identification of host targets for putative disulfide isomerase effector from Plasmodiophora brassicae reveals novel mechanisms of clubroot pathogenesis
inferred← citeshttps://doi.org/10.1016/j.aspen.2014.10.004openalex-snapshot
The gene expression profile of Monochamus alternatus in response to deltamethrin exposure
inferred← citeshttps://doi.org/10.1016/j.bmc.2017.08.005openalex-snapshot
Ribosomally-synthesised cyclic peptides from plants as drug leads and pharmaceutical scaffolds
inferred← citeshttps://doi.org/10.1016/j.cbpa.2013.05.033openalex-snapshot
Cyclotide biosynthesis
inferred← citeshttps://doi.org/10.1016/j.chphi.2023.100330openalex-snapshot
Induction and destruction of folding motifs in cyclotides by cyclic cystine knots
inferred← citeshttps://doi.org/10.1016/j.coph.2009.05.004openalex-snapshot
Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins
inferred← citeshttps://doi.org/10.1016/j.drudis.2013.12.002openalex-snapshot
Immunosuppressive peptides and their therapeutic applications
inferred← citeshttps://doi.org/10.1016/j.drudis.2019.09.010openalex-snapshot
Pharmaceutical applications of cyclotides
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.151840openalex-snapshot
Functional diversification of Viola arcuata protein disulfide isomerases and their roles in cyclotide oxidative folding
inferred← citeshttps://doi.org/10.1016/j.jbc.2024.107125openalex-snapshot
Nucleation of a key beta-turn promotes cyclotide oxidative folding
inferred← citeshttps://doi.org/10.1016/j.jep.2013.10.044openalex-snapshot
Immunosuppressive activity of an aqueous Viola tricolor herbal extract
inferred← citeshttps://doi.org/10.1016/j.jprot.2011.05.026openalex-snapshot
A proteomic study of in-root interactions between chickpea pathogens: The root-knot nematode Meloidogyne artiellia and the soil-borne fungus Fusarium oxysporum f. sp. ciceris race 5
inferred← citeshttps://doi.org/10.1016/j.jprot.2014.09.022openalex-snapshot
Proteomic analysis of responsive stem proteins of resistant and susceptible cashew plants after Lasiodiplodia theobromae infection
inferred← citeshttps://doi.org/10.1016/j.mocell.2025.100252openalex-snapshot
Cyclotides as novel plant-derived scaffolds for orally active cyclic peptide therapeutics
inferred← citeshttps://doi.org/10.1016/j.phytochem.2009.09.023openalex-snapshot
Cyclotide proteins and precursors from the genus Gloeospermum: Filling a blank spot in the cyclotide map of Violaceae
inferred← citeshttps://doi.org/10.1016/j.scienta.2022.111783openalex-snapshot
Are protein disulfide isomerases effectively involved in the rose senescence phenomenon?
inferred← citeshttps://doi.org/10.1016/j.tplants.2009.03.003openalex-snapshot
Circling the enemy: cyclic proteins in plant defence
inferred← citeshttps://doi.org/10.1016/j.ygeno.2010.10.001openalex-snapshot
Comparative genomic study of protein disulfide isomerases from photosynthetic organisms
inferred← citeshttps://doi.org/10.1016/s0066-4103(09)06802-1openalex-snapshot
NMR of Peptide Toxins
inferred← citeshttps://doi.org/10.1021/acs.chemrev.9b00402openalex-snapshot
Cyclotides: From Structure to Function
inferred← citeshttps://doi.org/10.1021/acs.jnatprod.2c00674openalex-snapshot
Screening for Cyclotides in Sri Lankan Medicinal Plants: Discovery, Characterization, and Bioactivity Screening of Cyclotides from Geophila repens
inferred← citeshttps://doi.org/10.1021/acs.jproteome.5b00681openalex-snapshot
Peptidomics of Circular Cysteine-Rich Plant Peptides: Analysis of the Diversity of Cyclotides from Viola tricolor by Transcriptome and Proteome Mining
inferred← citeshttps://doi.org/10.1021/acsagscitech.4c00705openalex-snapshot
In-Depth Shotgun Proteomic Characterization of Chickpea (Cicer arietinumL.): A Case Study on the Genotype Pascià Grown Using Two Water Regimes
inferred← citeshttps://doi.org/10.1021/acschembio.1c00524openalex-snapshot
Importance of the Cyclic Cystine Knot Structural Motif for Immunosuppressive Effects of Cyclotides
inferred← citeshttps://doi.org/10.1021/bi2007004openalex-snapshot
Optimal Oxidative Folding of the Novel Antimicrobial Cyclotide from Hedyotis biflora Requires High Alcohol Concentrations
inferred← citeshttps://doi.org/10.1021/cb4000585openalex-snapshot
Design of a Cyclotide Antagonist of Neuropilin-1 and -2 That Potently Inhibits Endothelial Cell Migration
inferred← citeshttps://doi.org/10.1021/jacs.6c05395openalex-snapshot
Tangled Tail of Mechanically Interlocked Peptides
inferred← citeshttps://doi.org/10.1021/jo200520vopenalex-snapshot
The Chemistry of Cyclotides
inferred← citeshttps://doi.org/10.1021/np1000413openalex-snapshot
Isolation, Sequencing, and Structure−Activity Relationships of Cyclotides
inferred← citeshttps://doi.org/10.1021/np200722wopenalex-snapshot
Do Plant Cyclotides Have Potential As Immunosuppressant Peptides?
inferred← citeshttps://doi.org/10.1021/np401055jopenalex-snapshot
Chemistry and Biology of Cyclotides: Circular Plant Peptides Outside the Box
inferred← citeshttps://doi.org/10.1038/s41598-020-69452-7openalex-snapshot
Transcriptomic profiling of the medicinal plant Clitoria ternatea: identification of potential genes in cyclotide biosynthesis
inferred← citeshttps://doi.org/10.1038/s41598-024-60246-9openalex-snapshot
Characterization and evaluation of cytotoxic and antimicrobial activities of cyclotides from Viola japonica
inferred← citeshttps://doi.org/10.1039/9781847559265-00274openalex-snapshot
Oxidative Folding of Peptides in vitro
inferred← citeshttps://doi.org/10.1039/b801667dopenalex-snapshot
Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides
inferred← citeshttps://doi.org/10.1039/c2np20085fopenalex-snapshot
Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature
inferred← citeshttps://doi.org/10.1039/d0cb00062kopenalex-snapshot
Harnessing cyclotides to design and develop novel peptide GPCR ligands
inferred← citeshttps://doi.org/10.1039/d3np00042gopenalex-snapshot
Plant peptides – redefining an area of ribosomally synthesized and post-translationally modified peptides
inferred← citeshttps://doi.org/10.1055/s-002-21673openalex-snapshot
inferred← citeshttps://doi.org/10.1055/s-0030-1250317openalex-snapshot
Uterotonic Plants and their Bioactive Constituents
inferred← citeshttps://doi.org/10.1063/5.0173548openalex-snapshot
Isolation and cloning of protein disulfide isomerase gene from soybean (Glycine max L. merrill)
inferred← citeshttps://doi.org/10.1071/ch16589openalex-snapshot
Synthesis and Protein Engineering Applications of Cyclotides
inferred← citeshttps://doi.org/10.1073/pnas.1519960113openalex-snapshot
Oral activity of a nature-derived cyclic peptide for the treatment of multiple sclerosis
inferred← citeshttps://doi.org/10.1073/pnas.1813993115openalex-snapshot
Gene-guided discovery and engineering of branched cyclic peptides in plants
inferred← citeshttps://doi.org/10.1073/pnas.1901807116openalex-snapshot
Papain-like cysteine proteases prepare plant cyclic peptide precursors for cyclization
inferred← citeshttps://doi.org/10.1074/jbc.m112.347823openalex-snapshot
Insights into Processing and Cyclization Events Associated with Biosynthesis of the Cyclic Peptide Kalata B1
inferred← citeshttps://doi.org/10.1074/jbc.m112.366781openalex-snapshot
Modulation of Conotoxin Structure and Function Is Achieved through a Multienzyme Complex in the Venom Glands of Cone Snails
inferred← citeshttps://doi.org/10.1074/jbc.m806664200openalex-snapshot
SDF2L1, a Component of the Endoplasmic Reticulum Chaperone Complex, Differentially Interacts with α-, β-, and θ-Defensin Propeptides
inferred← citeshttps://doi.org/10.1080/07388551.2024.2412780openalex-snapshot
Enhancing cyclotide bioproduction: harnessing biological synthesis methods and various expression systems for large-scale manufacturing
inferred← citeshttps://doi.org/10.1080/09168451.2019.1571900openalex-snapshot
Oxidative protein folding in the plant endoplasmic reticulum
inferred← citeshttps://doi.org/10.1080/14786419.2026.2706059openalex-snapshot
Multiomics characterization of Tilia and Actinidia arguta bee pollen
inferred← citeshttps://doi.org/10.1089/ars.2007.1849openalex-snapshot
Oxidative Folding of Cyclic Cystine Knot Proteins
inferred← citeshttps://doi.org/10.1089/ars.2012.4582openalex-snapshot
Oxidative Folding in Chloroplasts
inferred← citeshttps://doi.org/10.1093/abbs/gmr062openalex-snapshot
Various mechanisms in cyclopeptide production from precursors synthesized independently of non-ribosomal peptide synthetases
inferred← citeshttps://doi.org/10.1093/jb/mvaa058openalex-snapshot
A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6
inferred← citeshttps://doi.org/10.1093/mp/sst048openalex-snapshot
Protein Disulfide Isomerase 2 of Chlamydomonas reinhardtii Is Involved in Circadian Rhythm Regulation
inferred← citeshttps://doi.org/10.1104/pp.15.01781openalex-snapshot
Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and ERO1 in Soybean
inferred← citeshttps://doi.org/10.1105/tpc.108.062331openalex-snapshot
Distribution and Evolution of Circular Miniproteins in Flowering Plants
inferred← citeshttps://doi.org/10.1111/febs.13720openalex-snapshot
Immunostimulating and Gram‐negative‐specific antibacterial cyclotides from the butterfly pea (Clitoria ternatea)
inferred← citeshttps://doi.org/10.1111/febs.13984openalex-snapshot
Identification and characterization of GmPDIL7, a soybean ER membrane‐bound protein disulfide isomerase family protein
inferred← citeshttps://doi.org/10.1111/j.1365-313x.2007.03357.xopenalex-snapshot
Biosynthesis of circular proteins in plants
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2008.06412.xopenalex-snapshot
Molecular cloning and characterization of two soybean protein disulfide isomerases as molecular chaperones for seed storage proteins
inferred← citeshttps://doi.org/10.1111/ppl.14642openalex-snapshot
Exploring the mechanisms underlying recovery from freeze–thaw injury in Colobanthus quitensis: mechanistic insights via transcriptome profiling
inferred← citeshttps://doi.org/10.1146/annurev-arplant-042817-040413openalex-snapshot
Look Closely, the Beautiful May Be Small: Precursor-Derived Peptides in Plants
inferred← citeshttps://doi.org/10.1155/2023/5406039openalex-snapshot
A Systematic Review of Phytochemistry, Nutritional Composition, and Pharmacologic Application of Species of the Genus Viola in Noncommunicable Diseases (NCDs)
inferred← citeshttps://doi.org/10.1177/2156587211428077openalex-snapshot
Cyclotides
inferred← citeshttps://doi.org/10.1186/1471-2164-11-111openalex-snapshot
Identification of candidates for cyclotide biosynthesis and cyclisation by expressed sequence tag analysis of Oldenlandia affinis
inferred← citeshttps://doi.org/10.1186/s12870-014-0300-9openalex-snapshot
Regulatory interplay between soybean root and soybean cyst nematode during a resistant and susceptible reaction
inferred← citeshttps://doi.org/10.1186/s12870-015-0460-2openalex-snapshot
Expression and characterization of protein disulfide isomerase family proteins in bread wheat
inferred← citeshttps://doi.org/10.13021/mars/7458openalex-snapshot
Quantifying the Glycine max Proximal Cis-regulome during Pathogenesis.
inferred← citeshttps://doi.org/10.1371/journal.pone.0068016openalex-snapshot
Cyclotides Suppress Human T-Lymphocyte Proliferation by an Interleukin 2-Dependent Mechanism
inferred← citeshttps://doi.org/10.1371/journal.pone.0099970openalex-snapshot
Morphological and Proteomic Analysis Reveal the Role of Pistil under Pollination in Liriodendron chinense (Hemsl.) Sarg
inferred← citeshttps://doi.org/10.17816/rcf625482openalex-snapshot
Cyclotides. Prospects for using violet oxytocin-like substances to create a new generation of pharmacological agents
inferred← citeshttps://doi.org/10.26181/5e3a3d90e6328openalex-snapshot
Biosynthesis of cyclotides
inferred← citeshttps://doi.org/10.30848/pjb2020-5(26)openalex-snapshot
Comparative proteomics analysis reveals important drought responsive proteins in the leaves of a potato variety tolerant to drought stress
inferred← citeshttps://doi.org/10.32657/10356/146624openalex-snapshot
Discovery and characterization of hevein-like peptides in functional food and medicinal plants
inferred← citeshttps://doi.org/10.32657/10356/46476openalex-snapshot
Discovery and characterization of novel peptide biologics in herbal medicine
inferred← citeshttps://doi.org/10.32657/10356/54838openalex-snapshot
Study of molecular and functional diversity of plant cystine knot miniproteins
inferred← citeshttps://doi.org/10.32657/10356/59522openalex-snapshot
Methodological development and applications of cyclic cysteine-rich peptides for drug design
inferred← citeshttps://doi.org/10.32657/10356/62189openalex-snapshot
Design and synthesis of cysteine-rich peptides
inferred← citeshttps://doi.org/10.32657/10356/69473openalex-snapshot
Discovery and application of cysteine-rich peptides from medicinal plants in drug development
inferred← citeshttps://doi.org/10.32657/10356/73452openalex-snapshot
Discovery and characterization of novel cysteine-rich peptides in medicinal plants
inferred← citeshttps://doi.org/10.3389/fchem.2017.00073openalex-snapshot
Chemical Proteomics for Target Discovery of Head-to-Tail Cyclized Mini-Proteins
inferred← citeshttps://doi.org/10.3389/fpls.2016.01013openalex-snapshot
Shotgun Label-free Proteomic Analysis of Clubroot (Plasmodiophora brassicae) Resistance Conferred by the Gene Rcr1 in Brassica rapa
inferred← citeshttps://doi.org/10.3389/fpls.2016.01859openalex-snapshot
Proteomic Analysis Reveals the Positive Roles of the Plant-Growth-Promoting Rhizobacterium NSY50 in the Response of Cucumber Roots to Fusarium oxysporum f. sp. cucumerinum Inoculation
inferred← citeshttps://doi.org/10.3389/fpls.2018.00913openalex-snapshot
Identification and Functional Analysis of a Protein Disulfide Isomerase (AtPDI1) in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.3389/fpls.2019.00645openalex-snapshot
Butterfly Pea (Clitoria ternatea), a Cyclotide-Bearing Plant With Applications in Agriculture and Medicine
inferred← citeshttps://doi.org/10.3389/fpls.2025.1679487openalex-snapshot
Unlocking plant regeneration capacity: small signaling peptides are on aboard
inferred← citeshttps://doi.org/10.3390/biom3040848openalex-snapshot
Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase
inferred← citeshttps://doi.org/10.3390/biom9040130openalex-snapshot
Study on Differential Protein Expression in Natural Selenium-Enriched and Non-Selenium-Enriched Rice Based on iTRAQ Quantitative Proteomics
inferred← citeshttps://doi.org/10.3390/cimb47010006openalex-snapshot
Anticancer Ribosomally Synthesized and Post-Translationally Modified Peptides from Plants: Structures, Therapeutic Potential, and Future Directions
inferred← citeshttps://doi.org/10.3390/ijms23137231openalex-snapshot
Unusual Post-Translational Modifications in the Biosynthesis of Lasso Peptides
inferred← citeshttps://doi.org/10.3390/molecules26010171openalex-snapshot
PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly
inferred← citeshttps://doi.org/10.3390/molecules27196430openalex-snapshot
Using the Cyclotide Scaffold for Targeting Biomolecular Interactions in Drug Development
inferred← citeshttps://doi.org/10.3390/ph8040711openalex-snapshot
Antimicrobial Peptides from Plants
inferred← citeshttps://doi.org/10.3732/ajb.1100382openalex-snapshot
Subcellular targeting and biosynthesis of cyclotides in plant cells
inferred← citeshttps://doi.org/10.4161/psb.6.2.15490openalex-snapshot
Chaperones and foldases in endoplasmic reticulum stress signaling in plants
inferred← citeshttps://doi.org/10.4314/ahs.v17i3.26openalex-snapshot
Anti-plasmodial and anti-inflammatory activities of cyclotide-rich extract and fraction of Oldenlandia affinis (R. & S.) D.C. (Rubiaceae)
inferred← citeshttps://doi.org/10.46876/ja.846023openalex-snapshot
Soyada Protein Disülfit İzomeraz’ların İn Silico Analizi
inferred← citeshttps://doi.org/10.70675/8d12e3efz7530z4798z9984zeef7316b50afopenalex-snapshot
Les glutathion peroxydases et protéine disulfure isomérases de peuplier : potentialités du repliement thiorédoxine pour la catalyse des réactions redox
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.