On the public citation graph

Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor MCoTI-II

0 signed · 97 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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/chin.200043245openalex-snapshot
ChemInform Abstract: Preparation and Handling of Peptides Containing Methionine and Cysteine
inferredcites →https://doi.org/10.1002/ejoc.200400440openalex-snapshot
Fmoc‐Assisted Synthesis of a 29‐Residue Cystine‐Knot Trypsin Inhibitor Containing a Guaninyl Amino Acid at the P1‐Position
inferredcites →https://doi.org/10.1007/bf02443650openalex-snapshot
Nucleo amino acids as arginine mimetics in cyclic peptides
inferredcites →https://doi.org/10.1016/0005-2744(69)90420-3openalex-snapshot
Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
inferredcites →https://doi.org/10.1016/0014-5793(89)80486-7openalex-snapshot
The refined 2.0 Å X‐ray crystal structure of the complex formed between bovine β‐trypsin and CMTI‐I, a trypsin inhibitor from squash seeds (Cucurbita maxima) Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes
inferredcites →https://doi.org/10.1016/0076-6879(70)19004-5openalex-snapshot
[2] Titration of trypsin, plasmin, and thrombin with p-nitrophenyl p′-guanidinobenzoate HCl
inferredcites →https://doi.org/10.1016/b978-0-08-027379-2.50020-xopenalex-snapshot
PATHOPHYSIOLOGICAL INTERPRETATION OF KINETIC CONSTANTS OF PROTEASE INHIBITORS
inferredcites →https://doi.org/10.1016/s0006-291x(67)80055-xopenalex-snapshot
On the size of the active site in proteases. I. Papain
inferredcites →https://doi.org/10.1016/s0041-0101(01)00129-5openalex-snapshot
Plant cyclotides: circular, knotted peptide toxins
inferredcites →https://doi.org/10.1016/s0960-894x(01)00328-6openalex-snapshot
Selectivity enhancement induced by substitution of non-natural analogues of arginine and lysine in arginine-based thrombin inhibitors
inferredcites →https://doi.org/10.1016/s0968-0004(02)02057-1openalex-snapshot
Circular proteins — no end in sight
inferredcites →https://doi.org/10.1021/bi0106639openalex-snapshot
Solution Structure of the Squash Trypsin Inhibitor MCoTI-II. A New Family for Cyclic Knottins,
inferredcites →https://doi.org/10.1021/bi027323nopenalex-snapshot
Linearization of a Naturally Occurring Circular Protein Maintains Structure but Eliminates Hemolytic Activity,
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/bi9929756openalex-snapshot
Squash Trypsin Inhibitors from Momordica cochinchinensis Exhibit an Atypical Macrocyclic Structure
inferredcites →https://doi.org/10.1021/np50114a002openalex-snapshot
Cyclopsychotride A, a Biologically Active, 31-Residue Cyclic Peptide Isolated from Psychotria longipes
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/10.1073/pnas.96.16.8913openalex-snapshot
An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
inferredcites →https://doi.org/10.1074/jbc.m101666200openalex-snapshot
Circular Proteins in Plants
inferredcites →https://doi.org/10.1093/oso/9780199637256.001.0001openalex-snapshot
Fmoc Solid Phase Peptide Synthesis
inferredcites →https://doi.org/10.1107/s0907444905021207openalex-snapshot
Structure ofEcballium elateriumtrypsin inhibitor II (EETI-II): a rigid molecular scaffold
inferredcites →https://doi.org/10.1111/j.1399-3011.1989.tb00210.xopenalex-snapshot
Protease inhibitors from Ecballium elaterium seeds
inferredcites →https://doi.org/10.1111/j.1399-3011.1995.tb00585.xopenalex-snapshot
Synthesis of a mixture of cyclic peptides based on the Bowman‐Birk reactive site loop to screen for serine protease inhibitors
inferredcites →https://doi.org/10.2174/0929867013372832openalex-snapshot
Synthetic Peptide Mimics of the Bowman-Birk Inhibitor Protein
inferredcites →https://doi.org/10.2174/1389203043379468openalex-snapshot
Anti-HIV Cyclotides
inferredcites →https://doi.org/10.2174/1389203043379477openalex-snapshot
Squash Inhibitors: From Structural Motifs to Macrocyclic Knottins

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/10.1002/ange.201002906openalex-snapshot
Backbone Dynamics of Cyclotide MCoTI‐I Free and Complexed with Trypsin
inferred← citeshttps://doi.org/10.1002/ange.201008142openalex-snapshot
“Triazolbrücke”: ein Disulfidbrückenersatz durch Ruthenium‐ katalysierte Bildung von 1,5‐disubstituierten 1,2,3‐Triazolen
inferred← citeshttps://doi.org/10.1002/ange.201102607openalex-snapshot
Berichtigung: Backbone Dynamics of Cyclotide MCoTI‐I Free and Complexed with Trypsin
inferred← citeshttps://doi.org/10.1002/ange.201203857openalex-snapshot
Combination of Phage Display and Molecular Grafting Generates Highly Specific Tumor‐Targeting Miniproteins
inferred← citeshttps://doi.org/10.1002/anie.201002906openalex-snapshot
Backbone Dynamics of Cyclotide MCoTI‐I Free and Complexed with Trypsin
inferred← citeshttps://doi.org/10.1002/anie.201008142openalex-snapshot
“Triazole Bridge”: Disulfide‐Bond Replacement by Ruthenium‐Catalyzed Formation of 1,5‐Disubstituted 1,2,3‐Triazoles
inferred← citeshttps://doi.org/10.1002/anie.201102607openalex-snapshot
Corrigendum: Backbone Dynamics of Cyclotide MCoTI‐I Free and Complexed with Trypsin
inferred← citeshttps://doi.org/10.1002/anie.201203857openalex-snapshot
Combination of Phage Display and Molecular Grafting Generates Highly Specific Tumor‐Targeting Miniproteins
inferred← citeshttps://doi.org/10.1002/cbic.200700183openalex-snapshot
Biosynthesis of a Fully Functional Cyclotide inside Living Bacterial Cells
inferred← citeshttps://doi.org/10.1002/cbic.200700187openalex-snapshot
Immobilized Protease‐Assisted Synthesis of Engineered Cysteine‐Knot Microproteins
inferred← citeshttps://doi.org/10.1002/cbic.200700452openalex-snapshot
Head‐to‐Tail Cyclized Cystine‐Knot Peptides by a Combined Recombinant and Chemical Route of Synthesis
inferred← citeshttps://doi.org/10.1002/cbic.200900534openalex-snapshot
Biosynthesis and Biological Screening of a Genetically Encoded Library Based on the Cyclotide MCoTI‐I
inferred← citeshttps://doi.org/10.1002/cbic.201200604openalex-snapshot
Oxidative Folding of Peptides with Cystine‐Knot Architectures: Kinetic Studies and Optimization of Folding Conditions
inferred← citeshttps://doi.org/10.1002/cbic.202000315openalex-snapshot
Cyclotide Structures Revealed by NMR, with a Little Help from X‐ray Crystallography
inferred← citeshttps://doi.org/10.1002/cmdc.201100497openalex-snapshot
Engineering and Functionalization of the Disulfide‐Constrained Miniprotein Min‐23 as a Scaffold for Diagnostic Application
inferred← citeshttps://doi.org/10.1007/978-1-0716-0434-2_16openalex-snapshot
Recombinant Expression of Cyclotides Using Expressed Protein Ligation
inferred← citeshttps://doi.org/10.1007/978-1-4939-2020-4_10openalex-snapshot
De Novo Discovery of Bioactive Cyclic Peptides Using Bacterial Display and Flow Cytometry
inferred← citeshttps://doi.org/10.1007/978-1-59745-557-2_20openalex-snapshot
Microbodies™
inferred← citeshttps://doi.org/10.1007/978-3-319-22473-2_7openalex-snapshot
Synthetic Cystine-Knot Miniproteins – Valuable Scaffolds for Polypeptide Engineering
inferred← citeshttps://doi.org/10.1007/978-3-319-32805-8_7openalex-snapshot
Synthetic Cystine-Knot Miniproteins – Valuable Scaffolds for Polypeptide Engineering
inferred← citeshttps://doi.org/10.1007/978-94-007-1764-0_48openalex-snapshot
Momordica cochinchinensis
inferred← citeshttps://doi.org/10.1007/s00425-014-2229-5openalex-snapshot
Two Blast-independent tools, CyPerl and CyExcel, for harvesting hundreds of novel cyclotides and analogues from plant genomes and protein databases
inferred← citeshttps://doi.org/10.1007/s00425-015-2446-6openalex-snapshot
A novel cinnamyl alcohol dehydrogenase (CAD)-like reductase contributes to the structural diversity of monoterpenoid indole alkaloids in Rauvolfia
inferred← citeshttps://doi.org/10.1007/s00726-007-0569-1openalex-snapshot
Characterisation of the barrier caused by luminally secreted gastro-intestinal proteolytic enzymes for two novel cystine-knot microproteins
inferred← citeshttps://doi.org/10.1007/s11307-009-0287-zopenalex-snapshot
Sunflower Trypsin Inhibitor 1 Derivatives as Molecular Scaffolds for the Development of Novel Peptidic Radiopharmaceuticals
inferred← citeshttps://doi.org/10.1007/s12033-013-9684-2openalex-snapshot
Protein Production in Yarrowia lipolytica Via Fusion to the Secreted Lipase Lip2p
inferred← citeshttps://doi.org/10.1016/b978-0-12-396962-0.00009-4openalex-snapshot
Engineering Knottins as Novel Binding Agents
inferred← citeshttps://doi.org/10.1016/bs.abr.2015.09.003openalex-snapshot
Structural Studies of Cyclotides
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.2019.05.026openalex-snapshot
Peptide-based protease inhibitors from plants
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.10.020openalex-snapshot
Backbone cyclization of a recombinant cystine‐knot peptide by engineered Sortase A
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.jmb.2009.10.028openalex-snapshot
Engineered Cystine Knot Miniproteins as Potent Inhibitors of Human Mast Cell Tryptase β
inferred← citeshttps://doi.org/10.1016/j.jplph.2015.01.017openalex-snapshot
Transcriptomic screening for cyclotides and other cysteine-rich proteins in the metallophyte Viola baoshanensis
inferred← citeshttps://doi.org/10.1016/j.peptides.2012.09.018openalex-snapshot
A new family of cystine knot peptides from the seeds of Momordica cochinchinensis
inferred← citeshttps://doi.org/10.1021/acs.chemrev.9b00402openalex-snapshot
Cyclotides: From Structure to Function
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.2c01080openalex-snapshot
Engineering the Cyclization Loop of MCoTI-II Generates Targeted Cyclotides that Potently Inhibit Factor XIIa
inferred← citeshttps://doi.org/10.1021/acs.jnatprod.8b00716openalex-snapshot
Discovery and Characterization of Cyclic and Acyclic Trypsin Inhibitors from Momordica dioica
inferred← citeshttps://doi.org/10.1021/jacs.1c07574openalex-snapshot
An Ultrapotent and Selective Cyclic Peptide Inhibitor of Human β-Factor XIIa in a Cyclotide Scaffold
inferred← citeshttps://doi.org/10.1021/jacs.4c11589openalex-snapshot
Enhancing Sensitivity of Nuclear Magnetic Resonance in Biomolecules: Parahydrogen-Induced Hyperpolarization in Synthetic Disulfide-Rich Miniproteins
inferred← citeshttps://doi.org/10.1021/jm901233uopenalex-snapshot
Potent Inhibitors of β-Tryptase and Human Leukocyte Elastase Based on the MCoTI-II Scaffold
inferred← citeshttps://doi.org/10.1021/np1000413openalex-snapshot
Isolation, Sequencing, and Structure−Activity Relationships of Cyclotides
inferred← citeshttps://doi.org/10.1038/s41467-019-13948-yopenalex-snapshot
Targeting the tumor vasculature with engineered cystine-knot miniproteins
inferred← citeshttps://doi.org/10.1038/s41467-021-27854-9openalex-snapshot
Towards a generic prototyping approach for therapeutically-relevant peptides and proteins in a cell-free translation system
inferred← citeshttps://doi.org/10.1039/b607324gopenalex-snapshot
Total synthesis of the macrocyclic cysteine knot microprotein MCoTI-II
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/c2ob25728aopenalex-snapshot
From pico to nano: biofunctionalization of cube-octameric silsesquioxanes by peptides and miniproteins
inferred← citeshttps://doi.org/10.1071/ch25086openalex-snapshot
Rational design and selection of next-generation cyclotide drugs using the knotted cyclic peptide scaffold MCoTI-II
inferred← citeshttps://doi.org/10.1073/pnas.1107849108openalex-snapshot
Legume cyclotides shed light on the genetic origin of knotted circular proteins
inferred← citeshttps://doi.org/10.1074/jbc.m113.460030openalex-snapshot
High-affinity Cyclic Peptide Matriptase Inhibitors
inferred← citeshttps://doi.org/10.1074/jbc.m113.528240openalex-snapshot
Structural Insights into the Role of the Cyclic Backbone in a Squash Trypsin Inhibitor
inferred← citeshttps://doi.org/10.1079/9781789247329.0009openalex-snapshot
Processing Technology of Gac Seeds
inferred← citeshttps://doi.org/10.1093/molbev/msu307openalex-snapshot
The Evolution ofMomordicaCyclic Peptides
inferred← citeshttps://doi.org/10.1105/tpc.112.099085openalex-snapshot
Cyclic Peptides Arising by Evolutionary Parallelism via Asparaginyl-Endopeptidase–Mediated Biosynthesis
inferred← citeshttps://doi.org/10.1107/s0907444912043880openalex-snapshot
Structural characterization ofSpinacia oleraceatrypsin inhibitor III (SOTI-III)
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2008.06440.xopenalex-snapshot
Alternative binding proteins: Biological activity and therapeutic potential of cystine‐knot miniproteins
inferred← citeshttps://doi.org/10.11159/nddte17.117openalex-snapshot
Process Development for the Identification of Novel Microbodies against NSCLC Related Targets
inferred← citeshttps://doi.org/10.11159/nddte18.117openalex-snapshot
MAdCAM-1 Nanotargeting Uncovers Bowel Inflammation Foci in Experimental Model of Colitis
inferred← citeshttps://doi.org/10.1186/1472-6807-8-54openalex-snapshot
Knottin cyclization: impact on structure and dynamics
inferred← citeshttps://doi.org/10.1371/journal.pone.0076956openalex-snapshot
Combinatorial Optimization of Cystine-Knot Peptides towards High-Affinity Inhibitors of Human Matriptase-1
inferred← citeshttps://doi.org/10.1586/erm.10.15openalex-snapshot
Engineered cystine-knot miniproteins for diagnostic applications
inferred← citeshttps://doi.org/10.2174/138161211798999438openalex-snapshot
Cyclotides, a Novel Ultrastable Polypeptide Scaffold for Drug Discovery
inferred← citeshttps://doi.org/10.2174/1381612811319060009openalex-snapshot
Natural Proteinaceous Inhibitors of Serine Proteases
inferred← citeshttps://doi.org/10.26083/tuprints-00006908openalex-snapshot
Structure-Based Monomerization of Human Serine Protease HTRA1 towards Evolutive Engineering of Activity Modulators
inferred← citeshttps://doi.org/10.32657/10356/165731openalex-snapshot
Broaden the applications of peptidyl asparaginyl ligases
inferred← citeshttps://doi.org/10.3390/ijms241814035openalex-snapshot
Non-Canonical Amino Acids in Analyses of Protease Structure and Function
inferred← citeshttps://doi.org/10.3390/molecules171112533openalex-snapshot
Chemical Synthesis, Backbone Cyclization and Oxidative Folding of Cystine-knot Peptides — Promising Scaffolds for Applications in Drug Design
inferred← citeshttps://doi.org/10.3390/toxins10060251openalex-snapshot
Classes, Databases, and Prediction Methods of Pharmaceutically and Commercially Important Cystine-Stabilized Peptides
inferred← citeshttps://doi.org/10.54014/63a7-k596openalex-snapshot
Structural interactions and dynamics of disease related proteins by using NMR spectroscopy
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.