Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
about
Characterization of the Conus bullatus genome and its venom-duct transcriptome.Conus peptides: biodiversity-based discovery and exogenomics.Identification of Conus peptidylprolyl cis-trans isomerases (PPIases) and assessment of their role in the oxidative folding of conotoxins.Proteomic analysis provides insights on venom processing in Conus textileNatural products: a continuing source of novel drug leadsVenom evolution widespread in fishes: a phylogenetic road map for the bioprospecting of piscine venoms.Conantokin-P, an unusual conantokin with a long disulfide loopNative pyroglutamation of huwentoxin-IV: a post-translational modification that increases the trapping ability to the sodium channel.In Silico Identification of Protein Disulfide Isomerase Gene Families in the De Novo Assembled Transcriptomes of Four Different Species of the Genus Conus.Modulation of conotoxin structure and function is achieved through a multienzyme complex in the venom glands of cone snails.Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides.Follow the leader: the use of leader peptides to guide natural product biosynthesis.Optimal cleavage and oxidative folding of α-conotoxin TxIB as a therapeutic candidate peptideOn the importance of oxidative folding in the evolution of conotoxins: cysteine codon preservation through gene duplication and adaptation.Ribosomal biosynthesis of the cyclic peptide toxins of Amanita mushrooms.Incorporation of post-translational modified amino acids as an approach to increase both chemical and biological diversity of conotoxins and conopeptides.Novel alpha-conotoxins from Conus spurius and the alpha-conotoxin EI share high-affinity potentiation and low-affinity inhibition of nicotinic acetylcholine receptors.Biochemical characterization of Drosophila gamma-glutamyl carboxylase and its role in fly development.Molecular cloning, expression and characterization of protein disulfide isomerase from Conus marmoreus.Oxidative Folding of Conopeptides Modified by Conus Protein Disulfide Isomerase.The Structure-Forming Juncture in Oxidative Protein Folding: What Happens in the ER?
P2860
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P2860
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@ast
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@en
type
label
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@ast
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@en
prefLabel
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@ast
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@en
P2093
P2860
P356
P1476
Efficient oxidative folding of conotoxins and the radiation of venomous cone snails
@en
P2093
Baldomero M Olivera
Elsie C Jimenez
Grzegorz Bulaj
Ian Goodsell
Jacob S Nielsen
James E Garrett
Jessica Kranski
Olga Buczek
P2860
P304
P356
10.1073/PNAS.2335845100
P407
P433
Supplement 2
P478
100 Suppl 2
P577
2003-11-25T00:00:00Z