Activation Mechanism of Recombinant Der p 3 Allergen Zymogen

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Systems of Zymogen Activation **

During the thirties, Northrop, Kunitz and their co-workers gave to the world a set of crystallized enzymes and zymogens.1. They also conveyed a set of corresponding ideas: that certain proteolytic enzymes are produced by the body in precursor form, that these precursors can be activated by slight proteolysis, and that this process is usually catalyzed by enzymes. Moreover, they delineated a sys...

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Correction: Cell-Penetrating Peptide Derived from Human Eosinophil Cationic Protein Inhibits Mite Allergen Der p 2 Induced Inflammasome Activation

All instances of IFN-β in the published article should be replaced by IFN-α3. article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Cell-Penetrating Peptide Derived from Human Eosinophil Cationic Protein Inhibits Mite Allergen Der p 2 Induced Inflammasome Activation

Newly discovered cell penetration peptides derived from human eosinophil cationic proteins (CPPecp) have the characteristic of cell internalization, but the effect of CPPecp on immunomodulation has not been clarified. House dust mite (HDM) major allergen, Der p 2, can induce proinflammatory cytokine production which contributes to airway inflammation and allergic asthma. However, the mechanism ...

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References 1. Yu S-J, Liao E-C, Sheu M-L, Chang D-TM, Tsai J-J (2015) Cell-Penetrating Peptide Derived from Human Eosinophil Cationic Protein Inhibits Mite Allergen Der p 2 Induced Inflammasome Activation. PLoS ONE 10(3): e0121393. doi:10.1371/journal.pone.0121393 PMID: 25807144 2. Yu S-J, Liao E-C, Sheu M-L, Margaret Chang D-T, Tsai J-J (2015) Correction: Cell-Penetrating Peptide Derived from ...

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Cys ) : Arginine Mutations That Preclude Zymogen Activation

Factor IX Chicago-2 and prothrombin Madrid were purified from patients with hemophilia B and congenital dysprothrombinemia. respectively. Each protein displays defects in zymogen activation secondary to the failure to cleave one of the sessile bonds whose cleavage is necessary for full coagulant activity. These proteins were isolated by immunoaffinity chromatography using conformation-specific ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2008

ISSN: 0021-9258

DOI: 10.1074/jbc.m803041200