Characterizing the Tick Carboxypeptidase Inhibitor

Characterizing the Tick Carboxypeptidase Inhibitor

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http://www.wikidata.org/entity/Q57956897
Insight into the sialome of the castor bean tick, Ixodes ricinus.The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathwaysMammalian metallopeptidase inhibition at the defense barrier of Ascaris parasiteTuned Escherichia coli as a host for the expression of disulfide-rich proteins.Chemical methods for producing disulfide bonds in peptides and proteins to study folding regulation.The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19.Association between foldability and aggregation propensity in small disulfide-rich proteinsScrambled isomers as key intermediates in the oxidative folding of ligand binding module 5 of the low density lipoprotein receptor.Peptidase inhibitors in tick physiology.
P2860

Characterizing the Tick Carboxypeptidase Inhibitor

Item
http://www.wikidata.org/entity/Q57956897
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Juni 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в червні 2006
@uk
name
Characterizing the Tick Carboxypeptidase Inhibitor
@en
Characterizing the Tick Carboxypeptidase Inhibitor
@nl
type
label
Characterizing the Tick Carboxypeptidase Inhibitor
@en
Characterizing the Tick Carboxypeptidase Inhibitor
@nl
prefLabel
Characterizing the Tick Carboxypeptidase Inhibitor
@en
Characterizing the Tick Carboxypeptidase Inhibitor
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Characterizing the tick carbox ...... asis for its two-domain nature
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698