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Literature DB >> 4899585

The side-chain specificity of pepsin.

G E Trout, J S Fruton.

Abstract

Mesh：

Substances：

Year: 1969 PMID： 4899585 DOI： 10.1021/bi00838a041

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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7 in total

1. The comparative specificity of acid proteinases.

Authors: I M Voynick; J S Fruton
Journal: Proc Natl Acad Sci U S A Date: 1971-02 Impact factor: 11.205

2. Inhibition of cathepsin D-type proteinase of macrophages by pepstatin, a specific pepsin inhibitor, and other substances.

Authors: M H McAdoo; A M Dannenberg; C J Hayes; S P James; J H Sanner
Journal: Infect Immun Date: 1973-04 Impact factor: 3.441

3. Nitration of the egg-allergen ovalbumin enhances protein allergenicity but reduces the risk for oral sensitization in a murine model of food allergy.

Authors: Eva Untersmayr; Susanne C Diesner; Gertie Janneke Oostingh; Kathrin Selzle; Tobias Pfaller; Cornelia Schultz; Yingyi Zhang; Durga Krishnamurthy; Philipp Starkl; Regina Knittelfelder; Elisabeth Förster-Waldl; Arnold Pollak; Otto Scheiner; Ulrich Pöschl; Erika Jensen-Jarolim; Albert Duschl
Journal: PLoS One Date: 2010-12-02 Impact factor: 3.240

Review 7. Stability of allergens.

Authors: Judith Pekar; Davide Ret; Eva Untersmayr
Journal: Mol Immunol Date: 2018-03-30 Impact factor: 4.407

7 in total

The side-chain specificity of pepsin.

1. The comparative specificity of acid proteinases.

2. Inhibition of cathepsin D-type proteinase of macrophages by pepstatin, a specific pepsin inhibitor, and other substances.

3. Nitration of the egg-allergen ovalbumin enhances protein allergenicity but reduces the risk for oral sensitization in a murine model of food allergy.

Review 4. The role of protein digestibility and antacids on food allergy outcomes.

5. Immune Effects of the Nitrated Food Allergen Beta-Lactoglobulin in an Experimental Food Allergy Model.

6. A versatile, compartmentalised gut-on-a-chip system for pharmacological and toxicological analyses.

Review 7. Stability of allergens.