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Literature summary for 3.4.22.65 extracted from

  • Deb, R.; Shakib, F.; Reid, K.; Clark, H.
    Major house dust mite allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 degrade and inactivate lung surfactant proteins A and D (2007), J. Biol. Chem., 282, 36808-36819.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
lung surfactant protein A + H2O Dermatophagoides pteronyssinus degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen ?
-
?
lung surfactant protein D + H2O Dermatophagoides pteronyssinus degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen ?
-
?

Organism

Organism UniProt Comment Textmining
Dermatophagoides pteronyssinus
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
Dermatophagoides pteronyssinus

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lung surfactant protein A + H2O
-
Dermatophagoides pteronyssinus ?
-
?
lung surfactant protein A + H2O degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen Dermatophagoides pteronyssinus ?
-
?
lung surfactant protein D + H2O
-
Dermatophagoides pteronyssinus ?
-
?
lung surfactant protein D + H2O degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen Dermatophagoides pteronyssinus ?
-
?

Synonyms

Synonyms Comment Organism
Der p 1
-
Dermatophagoides pteronyssinus