Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2 (Q27766638)

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8 December 2019

title

Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2 (English)

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8 December 2019

1

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8 December 2019

author name string

J Rautiainen

2

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8 December 2019

T Virtanen

3

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8 December 2019

T Zeiler

4

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8 December 2019

J Kauppinen

5

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8 December 2019

A Taivainen

6

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8 December 2019

R Mäntyjärvi

7

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8 December 2019

language of work or name

English

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publication date

1 January 1999

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Journal of Biological Chemistry

8 December 2019

published in

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8 December 2019

volume

274

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8 December 2019

issue

4

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8 December 2019

page(s)

2337-2343

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The lipocalin protein family: structure and function

8 December 2019

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Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin

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Molecular and crystal properties of Bos d 2, an allergenic protein of the lipocalin family.

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Cloning of cockroach allergen, Bla g 4, identifies ligand binding proteins (or calycins) as a cause of IgE antibody responses

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The major dog allergens, Can f 1 and Can f 2, are salivary lipocalin proteins: cloning and immunological characterization of the recombinant forms

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cDNA cloning and sequencing reveal the major horse allergen Equ c1 to be a glycoprotein member of the lipocalin superfamily.

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Tissue localization of bovine dander allergen Bos d 2☆☆☆★★★

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A major continuous allergenic epitope of bovine beta-lactoglobulin recognized by human IgE binding

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