about
Novel inhibitor cystine knot peptides from Momordica charantiaThree-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptorDiscovery of an unusual biosynthetic origin for circular proteins in legumesIdentifying the immunomodulatory components of helminthsCarcinogenic Parasite Secretes Growth Factor That Accelerates Wound Healing and Potentially Promotes NeoplasiaSolution structure of alpha-conotoxin ImI by 1H nuclear magnetic resonanceSolution structure of BSTI: a new trypsin inhibitor from skin secretions of Bombina bombinaIsolation, structure, and activity of GID, a novel alpha 4/7-conotoxin with an extended N-terminal sequenceTwists, knots, and rings in proteins. Structural definition of the cyclotide frameworkMicrocin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backboneSolution structure of the cyclotide palicourein: implications for the development of a pharmaceutical frameworkStructure of α-conotoxin BuIA: influences of disulfide connectivity on structural dynamicsRetrocyclin-2: structural analysis of a potent anti-HIV theta-defensinStructure of the R3/I5 Chimeric Relaxin Peptide, a Selective GPCR135 and GPCR142 AgonistStructure of human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin frameworkIsolation and characterization of peptides from Momordica cochinchinensis seedsStructural and biochemical characteristics of the cyclotide kalata B5 from Oldenlandia affinisChemical synthesis and structure of the prokineticin Bv8Cyclic Peptides Arising by Evolutionary Parallelism via Asparaginyl-Endopeptidase-Mediated BiosynthesisA Synthetic mirror image of kalata B1 reveals that cyclotide activity is independent of a protein receptorThe Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial ActivityThe α-defensin salt-bridge induces backbone stability to facilitate folding and confer proteolytic resistanceOxytocic plant cyclotides as templates for peptide G protein-coupled receptor ligand designSolution Structure, Membrane Interactions, and Protein Binding Partners of the Tetraspanin Sm-TSP-2, a Vaccine Antigen from the Human Blood FlukeSchistosoma mansoniA Tarantula-Venom Peptide Antagonizes the TRPA1 Nociceptor Ion Channel by Binding to the S1–S4 Gating DomainDesign and synthesis of truncated EGF-A peptides that restore LDL-R recycling in the presence of PCSK9 in vitroSolution structure, aggregation behavior, and flexibility of human relaxin-2Transforming conotoxins into cyclotides: Backbone cyclization of P-superfamily conotoxinsThree-dimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptorSolution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activityChemical synthesis and biosynthesis of the cyclotide family of circular proteinsConserved structural and sequence elements implicated in the processing of gene-encoded circular proteinsDiscovery, structure and biological activities of the cyclotidesDiscovery and characterization of a linear cyclotide from Viola odorata: implications for the processing of circular proteinsStructural studies of conotoxinsIsolation of an orally active insecticidal toxin from the venom of an Australian tarantulaNMR and protein structure in drug design: application to cyclotides and conotoxins.Phosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions.A new family of cystine knot peptides from the seeds of Momordica cochinchinensis.Structures of muO-conotoxins from Conus marmoreus. I nhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons.
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P50
description
onderzoeker
@nl
researcher
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հետազոտող
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name
Norelle L Daly
@ast
Norelle L Daly
@en
Norelle L Daly
@es
Norelle L Daly
@nl
type
label
Norelle L Daly
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Norelle L Daly
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Norelle L Daly
@es
Norelle L Daly
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prefLabel
Norelle L Daly
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Norelle L Daly
@en
Norelle L Daly
@es
Norelle L Daly
@nl
P106
P31
P496
0000-0002-4697-6602