Build and Enhance disease object based on provided allergen and context. Here is how you sould handle analysis process:

1. Extract all allergens from documents in the context
2. Extract all food and drinks related in the context
3. Extract all symptomps referenced in the context
4. Extract all diseases referenced in the context
5. Iterate over each allergen and provide this check for allergen:
5a. Match what food or drink contains this allergen (based on context)
5b. Match each disease caused by this allergen.
5c. Match symptomps and difficulties related to this allergen and all matched diseases.
6. Iterate over all identified diseases or difficulties and based on context match related diseases with each other.
7. Create a JSON object from provided analysis with format as in this example:

Input: "gluten"

Context: ...

{
  "name": "Gluten Intolerance",
  "allergens": [ // Find all allergens related from sources to input allergen
    {
      "name": "gluten", // Name of allergen
      "source": "https://example-medical-source.com/gluten" // Source to article that references this allergen
    },
    {
      "name": "barley", // Name of allergen
      "source": "https://example-medical-source.com/gluten_intolerance" // Source to article that references this allergen
    },
    {
      "name": "spelt", // Name of allergen
      "source": "https://example-medical-source.com/gluten-intolerance" // Source to article that references this allergen
    },
    ...
  ],
  "food": [
    {
      "name": "Bread",
      "contains": ["gluten", "weat", ...],
      "source": "https://example-source.com/bread" // source referencing the food related
    }
  ],
  "symptoms": [
    {
      "name": "abdominal pain",
      "source": "https://example-medical-source.com/gluten-intolerance" // Source to article that references this symptom
    },
    {
      "name": "bloating or gas",
      "source": "https://example-medical-source.com/gluten-intolerance" // Source to article that references this symptom
    },
    ...
  ],
  "related_diseaes": [
    {
      "name": "Celiac disease",
      "related_allergens": [
        {
          "name": "wheat",
          "source": "https://example-medical-source.com/celiac-intolerance",
          "description": "Wheat cause issues as well as in Celiac Disease and forms as an allergen..."
        },
        ...
      ]
    }
  ]
}

Now, your turn:

input: ara h 1

context:

[
	{
		"distance": 0.34311825037002563,
		"document": "are located on the ends of each trimer monomer. Ara h 1 presents an overall pleat like bicupins, N- and C-terminal domains are superposed in 1.9 Å. The molecule has two modules related by an axis perpendicular to the three pleat axes of the trimer. They interact through their hydrophobic parts. The trimeric assemblies are stabilized by multiple hydrogen bonds. Influence of Ara h 1 in peanut allergies[edit] The protein Ara h 1 plays an important role in peanut allergic reactions. Several studies have demonstrated that the protein fraction of the cotyledon is the allergenic portion of the peanut.[5][8] Ara h 1 makes up 12% to 16% of the total protein in peanut extracts and is classified as a major peanut allergen because it provokes sensitization in 35% to 95% of patients with this allergy.[3] This protein is a very potent allergen and it causes a severe reaction. The symptoms can be: Skin reaction: urticarial, redness or edema. Itchy reaction: usually around the mouth and throat.",
		"id": "ara h 1_0_chunk_3",
		"metadata": {
			"accessed": 1726315490.206682,
			"term": "ara h 1",
			"url": "https://en.wikipedia.org/wiki/Ara_h1"
		}
	},
	{
		"distance": 0.3082038164138794,
		"document": "linear epitopes are described for Ara h 1, 10 for Ara h 2, and 4 for Ara h 3 [7, 47, 55, 56]. Allergens causing Class I food allergies are mainly found in sources like hen’s egg, cow’s milk, fish, crustaceans (shrimps), tree nuts, and legumes like soybean, lupine, and peanut. Class I food allergies mainly manifest in children and resolve with maturation of the gastrointestinal immune system. In only 20% of patients with peanut allergy does the disease resolve with age [43]. Class I food allergies can be associated with mild clinical symptoms (like oral allergy syndrome (OAS)) to severe clinical symptoms (systemic reactions like urticaria, asthma, gastrointestinal disorders) that can lead to anaphylactic shock. Go to: Class II food allergies Class II food allergies are mainly present in adults who have already developed a prior allergy against inhalant allergens. The immunological basis for the reactivity with allergens that can cause Class II food allergies is probably their",
		"id": "ara h 1_8_chunk_12",
		"metadata": {
			"accessed": 1726316955.246858,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881859/"
		}
	},
	{
		"distance": 0.31720107793807983,
		"document": "move to sidebar hide Actions ReadEditView history General What links hereRelated changesUpload fileSpecial pagesPermanent linkPage informationCite this pageGet shortened URLDownload QR codeWikidata item Print/export Download as PDFPrintable version In other projects Appearance move to sidebar hide From Wikipedia, the free encyclopedia Ara h 1IdentifiersOrganismArachis hypogaea (peanut)Symbolara h 1PDB3smhUniProtE5G076Search forStructuresSwiss-modelDomainsInterPro Ara h 1 is a seed storage protein from Arachis hypogaea (peanuts). It is a heat stable 7S vicilin-like globulin[1] with a stable trimeric form[2] that comprises 12-16% of the total protein in peanut extracts.[3] Ara h 1 is known because sensitization to it was found in 95% of peanut-allergic patients from North America. In spite of this high percentage, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.[4] Structure[edit] Ara h 1 is a vicilin, located in the protein fraction of the peanut",
		"id": "ara h 1_0_chunk_1",
		"metadata": {
			"accessed": 1726315490.206677,
			"term": "ara h 1",
			"url": "https://en.wikipedia.org/wiki/Ara_h1"
		}
	},
	{
		"distance": 0.31773483753204346,
		"document": "source. For the allergen source peanut, which primarily causes Class I food allergies, a birch pollen-profilin-homologous allergen (Ara h 5) and a Bet v 1-homologous allergen (Ara h 8) has also been detected. This suggests a pollen-associated cross-reactivity for Ara h 5 and Ara h 8. Vice versa, the allergen source hazelnut, which primarily triggers Class II allergic reactions, also contains allergens that can cause symptoms of a Class I food allergy (e.g., hazelnut lipid transfer protein (LTP) [7, 54]. Go to: Matrix effects [7] The current problem is finding out which allergenic potency each allergen component has. So far this can only be derived indirectly. The identification of single allergens is particularly important for the diagnostic work-up with the aim to develop a customized immunotherapy for each patient. But is the search for single allergens not being overemphasized in the context of food allergies? In contrast to pollen allergy, food allergens have to be evaluated in",
		"id": "ara h 1_8_chunk_22",
		"metadata": {
			"accessed": 1726316955.246877,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881859/"
		}
	},
	{
		"distance": 0.3439151644706726,
		"document": "form[2] that comprises 12-16% of the total protein in peanut extracts.[3] Ara h 1 is known because sensitization to it was found in 95% of peanut-allergic patients from North America. In spite of this high percentage, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.[4] Structure[edit] Ara h 1 is a vicilin, located in the protein fraction of the peanut cotyledon.[5][6] Ara h 1 forms homotrimers, and due to its highly stable structure, mediated through hydrophobic interactions, it has been established as an allergen.[7] Hydrophobic residues on α-helical bundles are located on the ends of each trimer monomer. Ara h 1 presents an overall pleat like bicupins, N- and C-terminal domains are superposed in 1.9 Å. The molecule has two modules related by an axis perpendicular to the three pleat axes of the trimer. They interact through their hydrophobic parts. The trimeric assemblies are stabilized by multiple hydrogen bonds. Influence of Ara h 1 in peanut",
		"id": "ara h 1_0_chunk_2",
		"metadata": {
			"accessed": 1726315490.206679,
			"term": "ara h 1",
			"url": "https://en.wikipedia.org/wiki/Ara_h1"
		}
	},
	{
		"distance": 0.3075460195541382,
		"document": "n 2, Jug r 2, Len c 1, Lup an 1, Pis v 3, Pis s 1, Pis s 2, Ses i 3. Other subgroups in this cluster, with no structural or known allergen representatives, include vicilin-like globulins mainly from Zea mays, Oryza sativa, and different Theobroma species. Structural Analysis of the Ara h 1 Core The Ara h 1 core (residues 170–586) crystallized in rhombohedral crystal form and in the space group R3 with two chains in the asymmetric unit, with each chain being a part of a different trimer. The trimer 3-fold axis coincides with the crystallographic 3-fold axis. While the determined crystal structures do not differ significantly in conformation of the main chains of the protein molecules, they differ slightly in the unit cell parameters (Table 1). Their Cα atoms superpose with root mean square deviation (rmsd) values of 0.5 Å. However, one of the molecules in the asymmetric unit is ordered better than the other one. In the structure reported here (PDB code: 3s7e), both chains contain",
		"id": "ara h 1_9_chunk_41",
		"metadata": {
			"accessed": 1726316955.247167,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3234756/"
		}
	},
	{
		"distance": 0.3076022267341614,
		"document": "are proteins related to prolamins. Peanut allergens (Arachis hypogaea) Ara h 2 and Ara h 6 belong to the conglutin type of 2S-albumins. Currently they are considered the most important peanut allergens [12]. The Bet v 1 superfamily Bet v 1, the birch pollen major allergen, is one of the common vegetable pathogenesis-related proteins, PR10. The detection of its molecular structure allowed for the identification of structurally related proteins in other allergen sources. In this way, a superfamily was defined and the Bet v 1 family is only one of its members [12]. The Bet v 1-homologous allergen of the peanut is Ara h 8 [44]. Profilins Profilins are present in almost all eukaryotic cells. They are conserved proteins with a molecular weight between 12 and 15 kDa. About 20% of patients affected by pollen allergy are sensitized against profilins. The corresponding IgE antibodies are highly cross-reactive between pollen and food profilins, but seem to have no clinical impact on food",
		"id": "ara h 1_8_chunk_16",
		"metadata": {
			"accessed": 1726316955.246865,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881859/"
		}
	},
	{
		"distance": 0.3483768701553345,
		"document": "peanut.[5][8] Ara h 1 makes up 12% to 16% of the total protein in peanut extracts and is classified as a major peanut allergen because it provokes sensitization in 35% to 95% of patients with this allergy.[3] This protein is a very potent allergen and it causes a severe reaction. The symptoms can be: Skin reaction: urticarial, redness or edema. Itchy reaction: usually around the mouth and throat. Digestive problems: such as diarrhea, stomach cramps, nausea or vomiting. Breath problems: it has a relation with the inflammation reaction which causes the blockage of the air passages. Heart problems: histamine can cause a coronary artery spasm. Anaphylaxis: a whole-body allergic reaction that causes low blood pressure, suffocation and can bring a person to death. As it has been shown that saliva contains up to 1110 mg/ml of Ara h 1 the exposure to peanut through saliva may cause local and systematic allergic reactions.[9] So it's important to be careful and advised in terms of sharing",
		"id": "ara h 1_0_chunk_4",
		"metadata": {
			"accessed": 1726315490.206684,
			"term": "ara h 1",
			"url": "https://en.wikipedia.org/wiki/Ara_h1"
		}
	},
	{
		"distance": 0.35530638694763184,
		"document": "severe, systemic reactions and a higher risk for anaphylaxis. Alternatively, allergies to plant derived foods may occur in pollen sensitized individuals due to pollen allergens that cross react with food allergens. Examples of pollen associated allergens are the profilins or PR10 proteins that are homologues of the major white birch pollen antigen Bet v 1. Allergy to this family of proteins is associated with symptoms that are generally limited to the oropharyngeal area (commonly referred to as the oral allergy syndrome of pollen food allergy syndrome. Component resolved diagnostics can help to:1-5 • Distinguish between allergy due to cross-reactivity and primary allergy • Improve the risk assessment using allergen components • Improve management of allergic patients Limitations Allergen-specific IgE assays do not demonstrate absolute positive and negative predictive values for allergic disease. Clinical history must be incorporated into the diagnostic determination. Although the use",
		"id": "ara h 1_2_chunk_13",
		"metadata": {
			"accessed": 1726315492.400449,
			"term": "ara h 1",
			"url": "https://www.labcorp.com/tests/603916/allergen-profile-peanut-ige-with-component-reflexes"
		}
	},
	{
		"distance": 0.35530638694763184,
		"document": "severe, systemic reactions and a higher risk for anaphylaxis. Alternatively, allergies to plant derived foods may occur in pollen sensitized individuals due to pollen allergens that cross react with food allergens. Examples of pollen associated allergens are the profilins or PR10 proteins that are homologues of the major white birch pollen antigen Bet v 1. Allergy to this family of proteins is associated with symptoms that are generally limited to the oropharyngeal area (commonly referred to as the oral allergy syndrome of pollen food allergy syndrome. Component resolved diagnostics can help to:1-5 • Distinguish between allergy due to cross-reactivity and primary allergy • Improve the risk assessment using allergen components • Improve management of allergic patients Limitations Allergen-specific IgE assays do not demonstrate absolute positive and negative predictive values for allergic disease. Clinical history must be incorporated into the diagnostic determination. Although the use",
		"id": "ara h 1_1_chunk_13",
		"metadata": {
			"accessed": 1726315490.206778,
			"term": "ara h 1",
			"url": "https://www.labcorp.com/tests/603916/allergen-profile-peanut-ige-with-component-reflexes"
		}
	},
	{
		"distance": 0.3222247362136841,
		"document": "allergen component has. So far this can only be derived indirectly. The identification of single allergens is particularly important for the diagnostic work-up with the aim to develop a customized immunotherapy for each patient. But is the search for single allergens not being overemphasized in the context of food allergies? In contrast to pollen allergy, food allergens have to be evaluated in the context of their matrix, which can vary significantly depending on the method of food preparation. Side dishes are an additional factor. In cooking, the food allergen is subject to manifold physical effects and chemical reactions, the products of which are exposed to the individual digestive process, the individual immune state, and the genetic background of each person. Antacids, for example, can trigger or increase the allergenicity of food [59]. For the major peanut allergen, Ara h 2, the reaction with sugars, the so-called Maillard reaction, has been described as increasing its",
		"id": "ara h 1_8_chunk_23",
		"metadata": {
			"accessed": 1726316955.246879,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881859/"
		}
	},
	{
		"distance": 0.3249077796936035,
		"document": "finding reveals that the residues forming the core region of the protein are sufficient for formation of Ara h 1 trimers and higher order oligomers. Natural and recombinant variants of proteins tested in in vitro gastric and duodenal digestion assays show that the natural protein is the most stable form, followed by the recombinant Ara h 1 core fragment and the full-length recombinant protein. Additionally, IgE binding studies reveal that the natural and recombinant allergens have different patterns of interaction with IgE antibodies. The molecular basis of cross-reactivity between vicilin allergens is also elucidated. Keywords: Allergen, Allergy, Protein Aggregation, Structural Biology, X-ray Crystallography, Ara h 1, IgE Binding, Food Allergen, In Vitro Digestion Go to: IntroductionSoybean, peanut, kidney bean, pea, lentil, and tree nuts are sources of a significant number of food allergens (1–3). While many types of food allergies are outgrown, the chances of outgrowing peanut and",
		"id": "ara h 1_9_chunk_11",
		"metadata": {
			"accessed": 1726316955.247106,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3234756/"
		}
	},
	{
		"distance": 0.3552941083908081,
		"document": "phenomenon of food allergy. As a paradigm we have chosen peanut allergy because it affects the highest number of patients, the triggering level of symptoms is low, and the range of clinical symptoms is wide (oral allergy syndrom to fatal anaphylactic shock). The aim of this review article is to present the structural characteristics of peanut allergens [7]. Go to: Ara h 1 Ara h 1 is a vicilin type 7S-storage protein with two conserved cupin consensus sequences and belongs to the protein superfamily of cupins. Ara h 1 is a glycoprotein with a glycosylation motif in the C-terminal area of the molecule on which a heterogeneous conglomeration of N-glycans with the structure Man5–6Glc NAc2 or Man3–4XylGlcNAc2 is conjugated through asparagine [32]. Based on the primary sequence deduced from the structural gene (accession# P43238), a molecular weight of 69 kDa without glycosylation fraction and a pI of 6.4 can be calculated. As shown by Buschmann et al. [18], Ara h 1 in peanut extract",
		"id": "ara h 1_8_chunk_26",
		"metadata": {
			"accessed": 1726316955.246884,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881859/"
		}
	},
	{
		"distance": 0.36131030321121216,
		"document": "suffer from peanut allergy, while in the USA and Europe, where peanuts are mainly eaten roasted, more people are affected by peanut allergy [9]. Another interesting observation is the fact that 11S-storage proteins tend to form aggregates, which when cooked can form gel-like structures [13]. It has to be taken into account that the digestive system is not only faced with soluble substances like antigens or allergens, but also has to interact with hardly soluble substances. In this context, it is necessary to consider the characteristics of allergens first in order to better understand the complex phenomenon of food allergy. As a paradigm we have chosen peanut allergy because it affects the highest number of patients, the triggering level of symptoms is low, and the range of clinical symptoms is wide (oral allergy syndrom to fatal anaphylactic shock). The aim of this review article is to present the structural characteristics of peanut allergens [7]. Go to: Ara h 1 Ara h 1 is a vicilin",
		"id": "ara h 1_8_chunk_25",
		"metadata": {
			"accessed": 1726316955.246882,
			"term": "ara h 1",
			"url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6881859/"
		}
	}
]