Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.
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Structural and Biochemical Studies Reveal Differences in the Catalytic Mechanisms of Mammalian and Drosophila melanogaster Thioredoxin Reductases †Removal of the 5-nitro-2-pyridine-sulfenyl protecting group from selenocysteine and cysteine by ascorbolysisSolid-phase synthesis of reduced selenocysteine tetrapeptides and their oxidized analogs containing selenenylsulfide eight-membered rings.Using chemical approaches to study selenoproteins-focus on thioredoxin reductasesInteractions of disulfide-deficient selenocysteine analogs of μ-conotoxin BuIIIB with the α-subunit of the voltage-gated sodium channel subtype 1.3.Specialized insulin is used for chemical warfare by fish-hunting cone snails.Expanding chemical diversity of conotoxins: peptoid-peptide chimeras of the sodium channel blocker μ-KIIIA and its selenopeptide analoguesTotal chemical synthesis of the enzyme sortase A(ΔN59) with full catalytic activity.2,2'-Dithiobis(5-nitropyridine) (DTNP) as an effective and gentle deprotectant for common cysteine protecting groups.The use of 2,2'-dithiobis(5-nitropyridine) (DTNP) for deprotection and diselenide formation in protected selenocysteine-containing peptides.Investigation of the C-terminal redox center of high-Mr thioredoxin reductase by protein engineering and semisynthesis.Synthesis of peptide substrates for mammalian thioredoxin reductaseA viable synthesis of N-methyl cysteine.Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase.Integrating the discovery pipeline for novel compounds targeting ion channels.Expressed protein ligation for metalloprotein design and engineering.Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy.Peptide ligation chemistry at selenol amino acids.A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum.Design of a selenylsulfide-bridged EGFR dimerization arm mimicSite-specific effects of diselenide bridges on the oxidative folding of a cystine knot peptide, omega-selenoconotoxin GVIA.Disulfide-Depleted Selenoconopeptides: a Minimalist Strategy to Oxidative Folding of Cysteine-Rich Peptides.Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis.Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bondsChemical synthesis and biotinylation of the thrombospondin domain TSR2.Integrated oxidative folding of cysteine/selenocysteine containing peptides: improving chemical synthesis of conotoxins.An Umpolung Approach for the Chemoselective Arylation of Selenocysteine in Unprotected Peptides.Investigation of peptide thioester formation via N→Se acyl transfer.Understanding acid lability of cysteine protecting groups.Selenopeptide analogs of EETI-II retain potent trypsin inhibitory activities.Chemical Synthesis of Human Insulin-Like Peptide-6.Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel.Cyclization of peptides by using selenolanthionine bridges.
P2860
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P2860
Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.
@en
type
label
Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.
@en
prefLabel
Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.
@en
P2093
P2860
P356
P1476
Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.
@en
P2093
Katharine M Harris
Robert J Hondal
Stevenson Flemer
P2860
P356
10.1002/PSC.795
P577
2007-02-01T00:00:00Z