Home

uns selbst Sie selbst Unschuldig ara h 1 stable trimer Küche Ernst Zersetzen

Heat-induced Conformational Changes of Ara h 1, a Major Peanut Allergen, Do  Not Affect Its Allergenic Properties - ScienceDirect
Heat-induced Conformational Changes of Ara h 1, a Major Peanut Allergen, Do Not Affect Its Allergenic Properties - ScienceDirect

The majority of the Ara h1 IgE binding epitopes are clustered in two... |  Download Scientific Diagram
The majority of the Ara h1 IgE binding epitopes are clustered in two... | Download Scientific Diagram

Cloning, Expression, and Characterization of Ara h 3, a Major Peanut  Allergen | Semantic Scholar
Cloning, Expression, and Characterization of Ara h 3, a Major Peanut Allergen | Semantic Scholar

Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an  Abundant and Highly Allergenic Peanut Protein*
Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein*

Molecular model of the Ara h 1 trimer. A space-filled, homology-based... |  Download Scientific Diagram
Molecular model of the Ara h 1 trimer. A space-filled, homology-based... | Download Scientific Diagram

RCSB PDB - 3SMH: Crystal structure of major peanut allergen Ara h 1
RCSB PDB - 3SMH: Crystal structure of major peanut allergen Ara h 1

Purification and molecular characterization of a truncated-type Ara h 1, a  major peanut allergen: oligomer structure, antigenicity, and glycoform |  SpringerLink
Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform | SpringerLink

PDF) Protein structure plays a critical role in peanut allergen Ara h 2  stability and may determine immunodominant IgE binding epitopes | Moon Sen  - Academia.edu
PDF) Protein structure plays a critical role in peanut allergen Ara h 2 stability and may determine immunodominant IgE binding epitopes | Moon Sen - Academia.edu

Electrochemical Detection of Peanut Allergen Ara h 1 Using a Sensitive DNA  Biosensor Based on Stem–Loop Probe | Journal of Agricultural and Food  Chemistry
Electrochemical Detection of Peanut Allergen Ara h 1 Using a Sensitive DNA Biosensor Based on Stem–Loop Probe | Journal of Agricultural and Food Chemistry

Ara h 1, a major allergen (vicilin) from peanut - Indoor Biotechnologies
Ara h 1, a major allergen (vicilin) from peanut - Indoor Biotechnologies

Purification and molecular characterization of a truncated-type Ara h 1, a  major peanut allergen: oligomer structure, antigenicity, and glycoform |  SpringerLink
Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform | SpringerLink

Ara h1 - Wikipedia
Ara h1 - Wikipedia

Purification and molecular characterization of a truncated-type Ara h 1, a  major peanut allergen: oligomer structure, antigenicity, and glycoform |  SpringerLink
Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform | SpringerLink

Trimer formed by rsAra h 1. Ara h 1 trimer shown in three different... |  Download Scientific Diagram
Trimer formed by rsAra h 1. Ara h 1 trimer shown in three different... | Download Scientific Diagram

Ara h 6 is involved in hetero-and homopolymeric structures after peanut...  | Download Scientific Diagram
Ara h 6 is involved in hetero-and homopolymeric structures after peanut... | Download Scientific Diagram

Cloning, Expression, and Characterization of Ara h 3, a Major Peanut  Allergen | Semantic Scholar
Cloning, Expression, and Characterization of Ara h 3, a Major Peanut Allergen | Semantic Scholar

Heat-induced Conformational Changes of Ara h 1, a Major Peanut Allergen, Do  Not Affect Its Allergenic Properties*
Heat-induced Conformational Changes of Ara h 1, a Major Peanut Allergen, Do Not Affect Its Allergenic Properties*

Structural and Immunologic Characterization of Ara h 1, a Major Peanut  Allergen - ScienceDirect
Structural and Immunologic Characterization of Ara h 1, a Major Peanut Allergen - ScienceDirect

Purification and molecular characterization of a truncated-type Ara h 1, a  major peanut allergen: oligomer structure, antigenicity, and glycoform |  SpringerLink
Purification and molecular characterization of a truncated-type Ara h 1, a major peanut allergen: oligomer structure, antigenicity, and glycoform | SpringerLink

Nutrients | Free Full-Text | Release of Major Peanut Allergens from Their  Matrix under Various pH and Simulated Saliva Conditions—Ara h2 and Ara h6  Are Readily Bio-Accessible
Nutrients | Free Full-Text | Release of Major Peanut Allergens from Their Matrix under Various pH and Simulated Saliva Conditions—Ara h2 and Ara h6 Are Readily Bio-Accessible

Structural and Immunologic Characterization of Ara h 1, a Major Peanut  Allergen - ScienceDirect
Structural and Immunologic Characterization of Ara h 1, a Major Peanut Allergen - ScienceDirect

Alignment of the primary amino acid sequences and the-carbon structural...  | Download Scientific Diagram
Alignment of the primary amino acid sequences and the-carbon structural... | Download Scientific Diagram