Home

Regular Products

Articles

Clearance Sale on Amazon USA

Clearance Sale on Amazon Canada

Clearance Sale on Amazon Australia

Clearance Sale on Amazon Singapore


Migraine

By Serge Kreutz, 2021
Version 2.0

This article will probably take me 6 months to write. I publish it as updated versions as I progress working on it because some information, such as the tyramine table, may be useful even when the whole thing is still a draft.


Abstract

This article advances the hypothesis that in many cases, migraine is a foodborne illness. The common causative microorganisms are a range of bacteria, including Lactobacillus strains used in the fermentation of milk and vegetables and affecting the decay of many foods. These bacteria convert amino acids into biogenic amines. All mammalian organisms use some amines as neurotransmitters and in the immune system, and can synthesize them themselves in necessary quantities. Excess amines, whether produced by an organism itself or entering the body as food, are broken down by amine oxidase enzymes present throughout any mammalian organism. The particularities of these enzymes are genetically encoded, and thus vary from person to person. Some people handle amines entering the body with food better than others. This is in line with migraine running in families. If excess biogenic amines are not broken down in a timely manner, they cause, in extreme cases, food poisoning, even fatal. On a lesser scale, so the hypothesis of this article, poorly managed excess biogenic amines cause migraine.


Foodborne disease

The US FDA, on its consumer pages, classifies 16 conditions as foodborne diseases. [What You Need to Know about Foodborne Illnesses]. Of those, 14 are caused by bacteria and 2 by viruses. Salmonella infection is the most well-known bacterial, and Hepatitis A the best-known viral foodborne disease.

The most dangerous foodborne illness on the FDA list is botulism, caused by Clostridium botulinum bacteria. An outbreak in the US was linked to potatoes baked in aluminum foil [Botulism: the hazardous baked potato]. When Otto Warmbier, sentenced to 15 years of hard labor for allegedly removing a propaganda poster from a hotel floor, was returned by North Korea on June 13, 2017, he was in a coma from a botulism infection and died 4 days later. Payment of a 2 million US dollars North Korean hospital bill was approved by Trump [Reuters].

However, the FDA definition of foodborne illnesses is too narrow. Heavy metal poisoning should also be included as it is easily avoided by not consuming contaminated food. Celiac disease, an autoimmune condition caused by the consumption of wheat, should also be on the list, and of course obesity, the mother of all foodborne diseases. Also add scombroid poisoning, caused by high levels of histamine (scombroid is a catergory of fish that includes mackerel, barracuda, and tuna). And don't forget migraine, caused by tyramine which, like histamine, is introduced into food by bacteria that decarboxylate amino acids.


What happens during migraine attacks?

The traditional view of migraine explained it as a vascular condition. During the aura phase, blood vessels around the skull were thought to be contracted (or cramped). This would reduce blood flow to the eyes, causing typical visual effects like flickering or blind spots, or other sensual deficiencies. Then the blood vessels would expand disproportionately and exert pressure on nerves around the skull, thus causing pain.

Turned out old science was wrong. When blood vessels were measured during the aura and headache phases, they weren't constricted or expanded in line with the theory. In 2009, Brain (one of the world's foremost journals of neurology, published by Oxford University Press since 1878) summarized the change of winds in the headline: "The vascular theory of migraine — a great story wrecked by the facts" [Brain, Volume 132, Issue 1, January 2009]

In the early years of the third millennium, a new theory gained traction. Migraine was considered a neurological disorder, like epilepsy, but usually not as severe. The supposed key event is called cortical spreading depression, "a slowly propagated wave of depolarization followed by suppression of brain activity" [Nature]. The Brazilian neurologist Aristides de Azevedo Pacheco Leão discovered the phenomenon in 1944. He opened the skulls of anesthetized rabbits and inserted some electrodes because he wanted to provoke epileptic seizures. What happened instead was a spreading depression of brain activity [Aristides Leão’s discovery]. Interestingly, "the cortical spreading depression (CSD) could be blocked by an incision in the cortex" [Scientific Electronic Library Online].

Remember: Frontal lobotomy (the drilling of holes into the foreheads of people) was initiated by the Portuguese neurologist António Caetano de Abreu Freire Egas Moniz in the mid-1930s in order to calm down unruly psychiatric patients. This "solution" earned him a Nobel Prize in 1949. Nowadays, surgical treatment of migraine is also being offered. It involves the severance of various branches of the trigemal nerve. Like frontal lobotomy, it is irreversible.

So, what is the link between migraine and cortical spreading depression. No interference with cortical spreading depression ever stopped a migraine, and it was never possible to induce a migraine by setting off a cortical spreading depression. All research on cortical spreading depressions was done in rabbits and cats. It wasn't even possible to prove the existence of cortical spreading depression in humans, unless a person had suffered extensive brain injury. Reason: cortical spreading depression propagates on the surface of brains. It does not jump easily over sulci (the furrows in brain folds) from brain gyri (bulged folds) to gyri; but heavily damaged brains do not have divided folds like healthy brains, thus cortical depressions spread more easily. During migraine attacks in humans, cortical spreading depression has never been measured (a fact for which neurologists came up with many excuses). [Persistent questions]

So, how was cortical spreading depression ever linked to migraine? Well, by intuition! By 1958, Peter Milner, an electrical engineer who retrained as a neuroscientist, felt that the time frame and slow intensity variations of migraine auras were similar to the time frame calculated (not measured!) for cortical spreading depressions (2 to 6 mm / minute) for the human brain. [Cortical spreading depression in neurological disorders: migraine ...] Milner based his hypothesis on the observations of a psychologist, Karl Lashley, who described his own migraine auras as slow waves overwhelming his eyesight.

Wow! Just that?

Yeap.

In 2018, the journal Neurological Research published a review by cardiologist Piet Borgdorff under the headline "Arguments against the role of cortical spreading depression in migraine". The abstract stated: "CSD is difficult to evoke in man, and electroencephalography (EEG) readings are not flattened during migraine (as opposed to EEG during CSD). Moreover, in contrast to CSD, migraine can occur bilaterally, and is not accompanied by a disrupted blood–brain barrier, increased cerebral metabolism, or cerebral cell swelling. Calcitonin gene-related peptide, which is thought to be characteristic of migraine pain, is increased in the blood from the external jugular vein during migraine in humans, but not during CSD in cats or rats." Another great story wrecked by the facts.

A less grandiose hypothesis views migraine as an often sporadic inflammation of the trigeminal nerve. This theory has the advantage that there are parameters that can actually be measured. One of them is the neuropeptide calcitonin gene-related peptide which, as indicated in the quote above, is elevated in the blood of the jugular vein during migraine headache.

As a scientific explanation for migraine, cortical spreading depression has probably undergone brain death.


Medical marketing

Cortical spreading depression, however, is still very much alive in the marketing efforts of neurologists. YouTube is full of clips that have been uploaded by headache web sites. Neurologists want you to hire their services... elaborate diagnostics, expensive consultations which they bill to your insurance comnpany. Roughly 20 percent of Americans suffer from migraine [Source: The Prevalence and Impact of Migraine and Severe Headache in the United States: Figures and Trends From Government Health Studies]. 65 million potential patients. If only half shows up for consultations with neurologists, that's going to be a bonanza.

Neurologists will prescribe neurological medications, typically expensive. Thus big pharma is on the bandwagon of the neurologists.


Nutritional triggers

The vascular, neurological, and inflammatory theories of migraine focus on what happens during migraine episodes. An entirely different perspective concentrates on what causes migraine episodes. Patients who are cured because they can avoid the causes of migraine attacks won't care much about what happens during them. Anyway, they no longer are afflicted.

Biogenic amines, mostly tyramine and histamine, have long been considered migraine triggers. In high enough dosages, tyramine and histamine in food make not just migraine sufferers sick, but any human.

Lists of prohibited and allowed foods for migraineurs are plentiful on non-academic websites. Many of these lists are dubious. It's not the specific foods that impact migraine sufferers, but the tyramine and histamine contents. And for any food, these vary from batch to batch, depending on several parameters.

As a drastic example, the histamine content of a tuna sandwich can vary by a factor of 1000 when the same tuna sandwich is bought at the same shop, but a week apart. Maybe their refrigerator broke down, you never know.

For one and the same kind of fruit, the tyramine load can vary by a factor of 100, depending on the condition under which if was harvested and how it was processed. Once the tyramine is in, you can't get it out, unless the whole lot is injected with amine oxidase enzymes that convert an amine group into ammonia, (NH3). Boiling, waving, or even deep-frying won't remove the tyramine or histamine, but can easily mask a taste that would otherwise betray spoilage.

To be meaningful at all, histamine and tyramine must be quantified. It's NOT that cheese is "prohibited" because it contains tyramine, and fruit and vegetables are "allowed".


Amino acid decarboxylation

The human body uses 20 amino acids to synthesize proteins. 9 are essential, they must come from nutrition. They are: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine. Another 11 may come from food, or are derived by the human organism from essential amino acids. They are: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, tyrosine

Human enzymes or enzymes of bacteria either within the human body or present in food we consume turn amino acids into amines by decarboxylation (the removal of carbondioxide, CO2, molecules).

The enzymatic derivates of amino acids include:

Histamine (a crucial amine in the immune system) from histidine
Tyramine from tyrosine; several important neurotransmitters, grouped as catecholamines, are also derived from tyramine: dopamine, noradrenaline, adrenaline
Agmatine from arginine
Putrescine, spermidine, spermine from arginine, glutamine, or ornithine
Cadaverine from lysine, glutamine, or ornithine
ß-phenylethylamine from phenylethylalanine
Serotonin and tryptamine from tryptophan

Most of these amines have important functions in the human body. Cadaverine, putrescine, spermidine, and spermine, and are needed in cells for protein synthesis and membranes. In human pathology, however, histamine and tyramine are the most relevant. And this article is focused on tyramine.

The following bacteria have been identified as generating tyramine:

Gram-positive: Bacillus thuringiensis. Carnobacterium divergens1, Enterococcus durans, Enterococcus hirae, Enterococcus faecalis, Enterococcus faecium, Lactobacillus brevis, Lactobacillus curvatus, Tetragenococcus halophilus
Gram-negative: Pseudomonas entomophila, Pseudomonas putida, Pseudomonas putida, Gluconacetobacter diazotrophicus, Granulibacter bethesdensis [Source: Tyramine and Phenylethylamine Biosynthesis by Food Bacteria ]


Tyramine

The most comprehensive list of tyramine measurements was compiled by Gaby Andersen, Patrick Marcinek, Nicole Sulzinger, Peter Schieberle, Dietmar Krautwurst and published in February 2019 in the journal Nutrition Reviews [Food sources and biomolecular targets of tyramine ]. Be prepared for some surprises.


Dairy (except cheese)

Buttermilk, 2.2 mg/kg, Souci et al (2016)

Cow’s milk, none detected, Novella-Rodriguez et al (2000)

Cream, 1.7 mg/kg, Souci et al (2016)

Sour cream, 1.4 mg/kg, Souci et al (2016)

Quark, 2.4 mg/kg, Souci et al (2016)

Yogurt, 1.3 mg/kg, Souci et al (2016)
None detected, Mayr & Schieberle (2012)
None detected, Novella-Rodriguez et al (2000)

Out of three tests, two were negative, and the one test that detected tyramine at all only found a very small amount. But mind you: spoiled yogurt can be loaded with tyramine up to dangerous levels. Lactobacillus varieties, responsible for yogurt fermentation, are the champions when it comes to the conversion of tyrosine to tyramine.


Cheese

A wide spectrum of measurements was reported for cheeses. For brie, it ranged from none detected to 260.0 mg/kg in tests conducted by one team, for parmesan 4.0 mg/kg to 290.0 mg/kg, for gauda 20.0 mg/kg to 670.0 mg/kg, for roquefort 27.0 mg/kg to 1100.0 mg/kg. For edam, it was 13.5 mg/kg to 310.0 mg/kg by three teams. For no food item are the measurements as confusing, and unequal, as they are for cheese. Different brands or batches of the same kind of cheese can have more than 50 times as much tyramine as other brands or batches, and you can't know why. It could be a flaw in the culture, or the aging process, or an event during transportation.

Appenzeller, 55.0 mg/kg, Souci et al (2016)

Brie, none detected to 260.0 mg/kg, Souci et al (2016)

Camembert, 37.0 mg/kg, Souci et al (2016)

Cheddar, 350.0 mg/kg, Souci et al (2016)
130.0 mg/kg, Tarjan & Janossy (1978)

Edam, 310.0 mg/kg, Souci et al (2016)
13.5 mg/kg, Lange et al (2002)
25.6 mg/kg, Tarjan & Janossy (1978)

Emmental, 42.0 mg/kg, Souci et al (2016)
128.7 mg/kg, Tarjan & Janossy (1978)

Feta, 152.0 mg/kg to 246.0 mg/kg, Valsamaki et al (2000)

Gorgonzola, 8.0 mg/kg, Lange et al (2002)

Gouda, 20.0 mg/kg to 670.0 mg/kg, Souci et al (2016)

Gruyère, 37.0 mg/kg, Souci et al (2016)

Leerdammer, none detected, Mayr & Schieberle (2012)

Parmesan, 4.0 mg/kg to 290.0 mg/kg, Souci et al (2016)
3.75 mg/kg, Mayr & Schieberle (2012)

Roquefort, 27.0 mg/kg to 1100.0 mg/kg, Souci et al (2016)
152.0 mg/kg, Lange et al (2002)

Tilsit, 32.0 mg/kg, Souci et al (2016)


Meat

Chicken liver, 100.0 mg/kg, Souci et al (2016)
50.0 mg/kg, Tarjan & Janossy (1978)

Ham, cooked, 6.0 mg/kg to 108.0 mg/kg, Saccani et al (2005)

Ham, dry cured, 7.5 mg/kg, Lange et al (2002)
4.0 mg/kg to 171.0 mg/kg, Saccani et al (2005)

Onion sausage, 32.0 mg/kg, Lange et al (2002)

Ox liver, 270.0 mg/kg, Souci et al (2016)

Pork, fresh meat, none detected to 56.0 mg/kg, Saccani et al (2005)

Salami, 77.1 mg/kg, Mayr & Schieberle (2012)
17.0 mg/kg, Lange et al (2002)


Fish

Cod, 2.0 mg/kg, Lange et al (2002)

Fermented fish sauce, 276.0 mg/L to 357.0 mg/L, Kirschbaum et al (2000)

Herring, none detected, Lange et al (2002)

Herring, cured, none detected to 3000.0 mg/kg, Souci et al (2016)

Mackerel, 25.8 mg/kg to 27.4 mg/kg, Shakila et al (2001)

Mackerel in brine, none detected, Shakila et al (2001)

Mackerel salt-dried, 398.4 mg/kg to 413.8 mg/kg, Shakila et al (2001)

Salmon, none detected, Lange et al (2002)

Sardines, 16.2 mg/kg to 11.8 mg/kg, Shakila et al (2001)

Sardines in oil, none detected, Shakila et al (2001)

Sardine, salt-dried, 169.5 mg/kg to 178.1 mg/kg, Shakila et al (2001)

Seer fish, 9.4 mg/kg to 10.7 mg/kg, Shakila et al (2001)

Seer fish, salt dried, 154.2 mg/kg to 154.1 mg/kg, Shakila et al (2001)

Shrimp, 8.8 mg/kg to 12.6 mg/kg, Shakila et al (2001)

Shrimp, salt dried, 693.2 mg/kg to 704.7 mg/kg, Shakila et al (2001)

Tuna, 0.06 mg/kg, Mayr & Schieberle (2012)

Tuna in oil, 0.72 mg/kg, Souci et al (2016)
None detected to 1.2 mg/kg, Shakila et al (2001)


Alcoholic beverages


Beer, Pilsner lager, 1.4 mg/L, Souci et al (2016)
6.85 mg/L, Kalac et al (1997)

Beer, German Vollbier, 1.8 mg/L to 12.0 mg/L, Souci et al (2016)

Beer, alcohol-free, 1.2 mg/L, Souci et al (2016)
6.16 mg/L, Kalac et al (1997)

Wine, port, 0.51 mg/L, Cunha et al (2011)

Wine, red, none detected to 20.0 mg/L, Souci et al (2016)
1.93 mg/L, Mayr & Schieberle (2012)
0.8 mg/L to 2.6 mg/L, Landete et al (2005)
38.8 mg/L, Tarjan & Janossy (1978)
1.40 mg/L, Marcobal et al (2005)
None detected to 0.292 mg/L, Anli et al (2004)
3.1 mg/L, Lüthy & Schlatter (1983)

Wine, white, none detected to 3.0, Souci et al (2016)
110.8 mg/L, Tarjan & Janossy (1978)
1.2 mg/L to 22.7 mg/L, Lüthy & Schlatter (1983)


Fruit

Apple, none detected, Tarjan & Janossy (1978)

Apple juice, 0.1 mg/L, Maxa & Brandes (1993)

Avocado, 23.0 mg/kg, Souci et al (2016)

Banana, 7.0 mg/kg, Souci et al (2016)
0.9 mg/kg, Lavizzari et al (2006)

Currants, none detected, Tarjan & Janossy (1978)

Currant juice, freshly squeezed, 3.26 mg/L, Maxa & Brandes (1993)

Grape, 691.0 mg/kg, Tarjan & Janossy (1978)

Grape juice, 0.04 mg/L, Cunha et al (2011)
0.1 mg/L, Maxa & Brandes (1993)

Grapefruit juice, freshly squeezed, 0.1 mg/L, Maxa & Brandes (1993)

Hazelnut, 1.8 mg/kg, Lavizzari et al (2006)

Orange, 10.0 mg/kg, Souci et al (2016)

Orange juice, 0.21 mg/L, Maxa & Brandes (1993)

Orange juice, freshly squeezed, 0.1 mg/L to 0.49 mg/L, Maxa & Brandes (1993)

Peach, none detected, Tarjan & Janossy (1978)

Pear, none detected, Tarjan & Janossy (1978)

Plum, none detected to 6.0 mg/kg, Souci et al (2016)
None detected, Tarjan & Janossy (1978)

Raspberry, 10.0 mg/kg to 90.0 mg/kg, Souci et al (2016)

Raspberry juice, freshly squeezed, 66.66 mg/L, Maxa & Brandes (1993)

Watermelon, 460.0 mg/kg, Tarjan & Janossy (1978)


Vegetables

Beetroot, 160.0 mg/kg, Tarjan & Janossy (1978)

Cabbage, 670.0 mg/kg, Tarjan & Janossy (1978)

Chinese cabbage, 1.26 mg/kg, Simon-Sarkadi & Holzapfel (1994)

Cabbage, sauerkraut, 20.0 mg/kg, Souci et al (2016)
60.66 mg/kg, Mayr & Schieberle (2012)
6.0 mg/kg, Lange et al (2002)

Cabbage, fermented juice, 37.1 mg/L to 73.0 mg/L, Kirschbaum et al (2000)

Kohlrabi, 930.0 mg/kg, Tarjan & Janossy (1978)

Carrot, 0.001 mg/kg, Sulzinger et al (2016)
119.0 mg/kg, Tarjan & Janossy (1978)

Carrot juice, 0.002 mg/L, Sulzinger et al. (2016)

Cauliflower, 400.0 mg/kg, Tarjan & Janossy (1978)

Cucumber, 250.0 mg/kg, Tarjan & Janossy (1978)

Endive, 1.60 mg/kg, Simon-Sarkadi & Holzapfel (1994)

Green pea, frozen, 8.7 mg/kg, Kalac et al (2002)

Haricot bean, 160.0 mg/kg, Tarjan & Janossy (1978)

Iceberg lettuce, 0.94 mg/kg, Simon-Sarkadi & Holzapfel (1994)

Miso, 24.6 mg/kg to 349.0 mg/kg, Kirschbaum et al (2000)
none detected to 49.8 mg/kg, Yen (1986)

Olives, none detected, Lange et al (2002)

Paprika, 266.0 mg/kg, Tarjan & Janossy (1978)

Potato, 1.14 mg/kg, Sulzinger et al. (2016)
840.0 mg/kg, Tarjan & Janossy (1978)
2.0 mg/kg, Lavizzari et al (2006) French fried potatoes, baked, 1.77 mg/kg, Sulzinger et al. (2016)

French fried potatoes, raw, 0.77 mg/kg, Sulzinger et al. (2016)

Radicchio, 2.73 mg/kg, Simon-Sarkadi & Holzapfel (1994)

Radish, 200.0 mg/kg, Tarjan & Janossy (1978)

Soy sauce, 17.7 mg/L to 172.0 mg/L, Kirschbaum et al (2000)
16.1 mg/L to 1699.0 mg/L, Yen (1986)

Soybeans, 9.05 mg/kg, Bartkiene et al (2015)
none detected, Gloria et al (2005)

Soybean, fermented, 27.8 mg/kg to 416.1 mg/kg, Bartkiene et al (2015)

Sufu, fermented tofu, none detected to 1125.4 mg/kg, Yen (1986)

Spinach, 3.78 mg/kg, Sulzinger et al. (2016)
286.0 mg/kg, Tarjan & Janossy (1978)
2.2 mg/kg, Lavizzari et al (2006)

Spinach purée, frozen, 10.2 mg/kg, Kalac et al (2002)

Spinach, boiled, 2.58 mg/kg, Sulzinger et al. (2016)

Tomato, 4.0 mg/kg, Souci et al (2016)
1.07 mg/kg, Sulzinger et al. (2016)
4.0 mg/kg, Lange et al (2002)
250.0 mg/kg, Tarjan & Janossy (1978)

Tomato ketchup, 33.6 mg/kg, Kalac et al (2002)

Tomato, concentrated purée, 7.23 mg/kg, Sulzinger et al. (2016)
10.4 mg/kg, Kalac et al (2002)

Turnip, none detected, Tarjan & Janossy (1978)

Zucchini, 0.06 mg/kg, Sulzinger et al. (2016)


Others

Chocolate, 3.11 mg/kg, Mayr & Schieberle (2012)
0.3 mg/kg, Lavizzari et al (2006)

Coffee, ground, 1.26 mg/kg to 16.14 mg/kg, Restuccia et al (2015)

Coffee, brewed, 0.25 mg/L to 1.89 mg/L, Restuccia et al (2015)


References:

Alkhouli, M; Mathur, M; Patil, P. (2014), Revisiting the “cheese reaction”: more than just a hypertensive crisis? Journal of Clinical Psychopharmacology:, Volume 34, Issue 5, Pages 665-667, https://pubmed.ncbi.nlm.nih.gov/25118080/

American Chemical Society New Test Could Help Consumers Avoid Surprise Headaches From Chocolate, Wine, American Chemical Society, https://www.sciencedaily.com/releases/2007/10/071001125645.htm

Andersen, G; Krautwurst, D; (2016) Trace amine-associated receptors in the cellular immune system, In: Farooqui T, Farooqui AA, eds. Trace Amines and Neurological Disorders: Potential Mechanisms and Risk Factors. San Diego, CA: Academic Press, Pages 97–106,https://scholar.google.com/scholar_lookup?title=Trace%20Amines%20and%20Neurological%20Disorders%3A%20Potential%20Mechanisms%20and%20Risk%20Factors&author=G%20Andersen&author=D.%20Krautwurst&author=T%20Farooqui&author=AA%20Farooqui&publication_year=2016&book=Trace%20Amines%20and%20Neurological%20Disorders%3A%20Potential%20Mechanisms%20and%20Risk%20Factors

Andersen, Gaby; Marcinek, Patrick; Sulzinger, Nicole; Schieberle, Peter; Krautwurst, Dietmar (2019), Food sources and biomolecular targets of tyramine Nutrition Reviews, Volume 77, Issue 2, Pages 107–115, https://doi.org/10.1093/nutrit/nuy036

Anli, RE; Vuralb, N; Yilmaza, S, (2004) The determination of biogenic amines in Turkish red wines. Journal of Food Composition and Analysis, Volume 17, Issue 1, Pages 53-62 https://doi.org/10.1016/S0889-1575(03)00104-2

Antibody Affinity, Bio-Rad, https://www.bio-rad-antibodies.com/antigen-antibody-interactions.html

Arnau, J; Guerrero, L; Sárraga, C. (1998), The effect of green ham pH and NaCl concentration on cathepsin activities and the sensory characteristics of dry-cured hams Journal Science Food Agriculture, Vol. 77: Pages 387–392, http://dx.doi.org/10.1002/(ISSN)1097-0010

Asatoor, A M; Levi, A J; Milne, M.D. (1963) Tranylcypromine and cheese, The Lancet, Volume 282, ISSUE 7310, P733-734, https://doi.org/10.1016/S0140-6736(63)90368-4

Babusyte, A; Kotthoff, M; Fiedler, J.; Krautwurst, D. (2013) Biogenic amines activate blood leukocytes via trace amine-associated receptors TAAR1 and TAAR2, Journal of Leukocyte Biology, Volume 93, Issue 3, Pages 387-394, https://doi.org/10.1189/jlb.0912433

Bartkiene, E; Krungleviciute, V; Juodeikiene, G; et al. (2015), Solid state fermentation with lactic acid bacteria to improve the nutritional quality of lupin and soya bean Journal Science Food Agriculture Vol 95(6): Pages 1336-42, https://doi.org/10.1002/jsfa.6827

Berry, MD. (2004), Mammalian central nervous system trace amines. Pharmacologic amphetamines, physiologic neuromodulators, Journal of Neurochemistry, Volume 90, Issue 2, Pages 257-271, https://doi.org/10.1111/j.1471-4159.2004.02501.x

Bieck, P.R.; Antonin, K.H. (1988) Oral tyramine pressor test and the safety of monoamine oxidase inhibitor drugs: comparison of brofaromine and tranylcypromine in healthy subjects, Journal of Clinical Psychopharmacology, Volume 8, Issue 4, Pages 237-245, https://journals.lww.com/psychopharmacology/Citation/1988/08000/Oral_Tyramine_Pressor_Test_and_the_Safety_of.2.aspx

Blackwell, B. (1963), Hypertensive crisis due to monoamine-oxidase inhibitors, Lancet, Volume 282, ISSUE 7313, P849-851, https://doi.org/10.1016/S0140-6736(63)92743-0

Borowsky, B; Adham, N; Jones, K A; Raddatz, R; Artymyshyn, R; Ogozalek, KL; Durkin, M M; Lakhlani, P P; Bonini, J A; Pathirana, S; Boyle, N; Pu, x; Kouranova, E; Lichtblau, H; Ochoa, F Y; Branchek, T A; Gerald, C (2001) Trace amines: identification of a family of mammalian G protein-coupled receptors, PNAS Vol 98 (16) Pages 8966-8971; https://doi.org/10.1073/pnas.151105198

Bonetta S, Carraro E, Coisson JD, Travaglia, F; Arlorio, M (2008), Detection of biogenic amine producer bacteria in a typical Italian goat cheese, Journal of Food Protection, Vol. 71 (1): Pages 205–209, https://doi.org/10.4315/0362-028X-71.1.205

Borgdorff, Piet (2017), Arguments against the role of cortical spreading depression in migraine, Neurological Research, Volume 40, Issue 3 , https://doi.org/10.1080/01616412.2018.1428406

Broadley, KJ. (2010), The vascular effects of trace amines and amphetamines Pharmacology & Therapeutics, Volume 125, Issue 3, Pages 363-375, https://doi.org/10.1016/j.pharmthera.2009.11.005

Broadley, KJ; Fehler, M; Ford, WR, Kidd, EJ (2013), Functional evaluation of the receptors mediating vasoconstriction of rat aorta by trace amines and amphetamines, European Journal of Pharmacology, Volume 715, Issues 1–3, Pages 370-380, https://doi.org/10.1016/j.ejphar.2013.04.034

Bover-Cid, S; Hugas, M; Izquierdo-Pulido, M; Vidal-Carou, MC (2001) Amino acid-decarboxylase activity of bacteria isolated from fermented pork sausages, International Journal of Food Microbiology Volume 66, Issue 3, Pages 185-189, https://doi.org/10.1016/S0168-1605(00)00526-2

Bueno-Solano, Carolina; López-Cervantes, Jaime, Sánchez-Machado, Dalia I.; Campas-Baypoli, Olga N. (2012), HPCL determination of histamine, tyramine and amino acids in shrimp by-products, Departamento de Biotecnología y Ciencias Alimentarias, Instituto Tecnológico de Sonora, https://doi.org/10.1590/S0103-50532012000100014

Burdychova, R; Komprda, T. (2007), Biogenic amine-forming microbial communities in cheese, FEMS, Volume 276, Issue 2, Pages: 129-215, https://doi.org/10.1111/j.1574-6968.2007.00922.x

Chander, H; Batish, VK; Babu, S, Singh, RS (1989), Factors affecting amine production by a selected strain of Lactobacillus bulgaricus, Journal of Food Science, Volume54, Issue 4, Pages 940-942, https://doi.org/10.1111/j.1365-2621.1989.tb07917.x

Chiellini, G; Frascarelli, S; Ghelardoni, S; Tobias, S C; DeBarber, A; Brogioni, S; Ronca-Testoni, S; Cerbai, E; Grandy, DV; Scanlan, TS; Zucchi, R. (2007), Cardiac effects of 3-iodothyronamine: a new aminergic system modulating cardiac function, The FASEB Journal, Volume21, Issue 7, Pages 1597-1608, https://doi.org/10.1096/fj.06-7474com

Chong, CY; Abu Bakar, F; Rahman, RA; Bakar, J; Zaman, MZ (2014), Biogenic amines, amino acids and microflora changes in Indian mackerel (Rastrellinger kanagurta) stored at ambient (25–29 °C) and ice temperature (0 °C), Journal of Food Science and Technology Volume 51, Pages 1118–1125, https://doi.org/10.1007/s13197-012-0621-3

Cid, SB; Miguelez-Arrizado, MJ; Becker, B; Holzapfel, W H.; Vidal-Caroua, M C (2008) Amino acid decarboxylation by Lactobacillus curvatus CTC273 affected by the pH and glucose availability, Food Microbiology, Volume 25, Issue 2, Pages 269-277, https://doi.org/10.1016/j.fm.2007.10.013

Cohen, G; Farooqui, R; Kesler, N. (1997), Parkinson disease: a new link between monoamine oxidase and mitochondrial electron flow, PNAS, Vol 94 (10) Pages 4890-4894,https://doi.org/10.1073/pnas.94.10.4890

Cohen, G. (2000), Oxidative stress, mitochondrial respiration, and Parkinson's disease, Annals of the New York Academy of Sciences, Volume 899, Issue 1, Pages: ix-xi, 1-424, https://nyaspubs.onlinelibrary.wiley.com/toc/17496632/2000/899/1

Coton, M; Romano, A; Spano, G; Zieglerb, K.; Vetrana, C; Desmarais, C.; Lonvaud-Fune, A.; Lucas, P.; Cotona, E. (2010), Occurrence of biogenic amine-forming lactic acid bacteria in wine and cide, Food Microbiology Volume 27, Issue 8, Pages 1078-1085, https://doi.org/10.1016/j.fm.2010.07.012

Cunha, SC; Faria, MA; Fernandes, JO (2011) Gas chromatograph–mass spectrometry assessment of amines in Port wine and grape juice after fast chloroformate extraction/derivatization Journal Agriculture Food Chemistry, Vol 59(16): Pages 8742-53, https://doi.org/10.1021/jf201379x

Dainty, R; Blom, H. (1995), Flavour chemistry of fermented sausages, Boston, MA: Springer Science+Business Media, Pages 176–193, https://scholar.google.com/scholar?cites=14094098160528838449&as_sdt=2005&sciodt=0,5&hl=en

Danchuk, Alexandra I; Komova, Nadezhda S.; Mobarez, Sarah N.; Doronin, Sergey Yu; Natalia A; Burmistrova, Markin, Alexey V.; Duerkop, Axel (2020), Optical sensors for determination of biogenic amines in food, Analytical and Bioanalytical Chemistry. https://link.springer.com/article/10.1007/s00216-020-02675-9

D’Andrea, G; D’Arrigo, A; Dalle Carbonare, M; Leon, A. (2012) Pathogenesis of migraine: role of neuromodulators, Headache, Volume 52, Issue 7 Pages: 1067-1205, https://doi.org/10.1111/j.1526-4610.2012.02168.x

D’Andrea, G; Terrazzino, S; Fortin, D; Farruggio, A; Rinaldi, L; Leon, A. (2003), HPLC electrochemical detection of trace amines in human plasma and platelets and expression of mRNA transcripts of trace amine receptors in circulating leukocytes, Neuroscience Letters, Volume 346, Issues 1–2, Pages 89-92, https://doi.org/10.1016/S0304-3940(03)00573-1

Del Rio, B; Redruello, B; Linares, D M; Linares, DM; Ladero, V; Fernandez, M; Linares, D. M.; Martin, M. C.; Ruas-Madiedo, P; Alvarez, MA (2017) The dietary biogenic amines tyramine and histamine show synergistic toxicity towards intestinal cells in culture, Food Chemistry, Volume 218, Pages 249-255, https://doi.org/10.1016/j.foodchem.2016.09.046

Dinter, J; Muhlhaus, J; Wienchol, C. L.; Yi, C X; Nürnberg, D; Morin, S; Grüters, A; Köhrle, J; Schöneberg, T; Tschöp, M; Krude, H; Kleinau, G; Bieberman, H (2015), Inverse agonistic action of 3-iodothyronamine at the human trace amine-associated receptor 5 PLoS One, https://doi.org/10.1371/journal.pone.0117774

Doeun, Dara; Davaatseren, Munkhtugs; Chung, Myung-Sub (2017), Biogenic amines in foods, Food Science Biotechnology Vol. 26(6). Pages 1463–1474, https://dx.doi.org/10.1007%2Fs10068-017-0239-3

EFSA Journal EFSA Panel on Biological Hazards (BIOHAZ). Scientific opinion on risk based control of biogenic amine formation in fermented foods, EFSA Journal, Vol 9(10): Pages 2393, https://doi.org/10.2903/j.efsa.2011.2393

Fernandez, M; Linares, DM; Rodriguez, A; Alvarez, M.A. (2007), Factors affecting tyramine production in Enterococcus durans IPLA 655, Applied Microbiology and Biotechnology, Vol 73, pages 1400–1406, https://doi.org/10.1007/s00253-006-0596-y

Espinoza, S; Gainetdinov, RR. (2017), Neuronal functions and emerging pharmacology of TAAR1. In:Krautwurst D, Taste and Smell. Cham, Germany: Springer International Publishing; 2017:175–194, https://scholar.google.com/scholar_lookup?title=Taste%20and%20Smell&author=S%20Espinoza&author=RR.%20Gainetdinov&author=D%20Krautwurst&publication_year=2017&book=Taste%20and%20Smell

Farooqui, T; Farooqui,AA (2016), Trace Amines and Neurological Disorders, Google Books,https://books.google.com/books?hl=en&lr=&id=Wj8oCwAAQBAJ&oi=fnd&pg=PP1&ots=o5BeyXT7Tr&sig=frUKOjJGDYmkf4nyURoQrA644DA

Finberg, JP; Gillman, K. (2011), Selective inhibitors of monoamine oxidase type B and the “cheese effect”, International Review of Neurobiology, Volume 100, Pages 169-190, https://doi.org/10.1016/B978-0-12-386467-3.00009-1

Fogel, WA; Lewinski, A; Jochem, J. (2007), Histamine in food: is there anything to worry about? Biochemical Society Transactions, Volume 35 (2): Pages 349–352, https://doi.org/10.1042/BST0350349

Frascarelli, S; Ghelardoni, S; Chiellini, G; Vargiu, R; Ronca-Testoni, S; Scanlan, T S; Grandy, D K; Zucchi, R (2008), Cardiac effects of trace amines: pharmacological characterization of trace amine-associated receptors, European Journal of Pharmacology, Volume 587, Issues 1–3, Pages 231-236, https://doi.org/10.1016/j.ejphar.2008.03.055

Gardini, F; Martuscelli, M; Caruso, MC, Galgano, F; Crudeleb, MA; Favati, F; Guerzonia, M A; Suzzi, G (2001), Effects of pH, temperature and NaCl concentration on the growth kinetics, proteolytic activity and biogenic amine production of Enterococcus faecalis, International Journal of Food Microbiology, Volume 64, Issues 1–2, Pages 105-117, https://doi.org/10.1016/S0168-1605(00)00445-1

Gardini, F; Ozogul, Y; Suzzi, G; Suzzi, G; Tabanelli1, G; Özogul, F (2016), Technological factors affecting biogenic amine content in foods: a review. Front Microbiology, Vol. 7: Page 1218, https://www.frontiersin.org/articles/10.3389/fmicb.2016.01218/full

Gloria, MB; Tavares-Neto, J; Labanca, RA, et al. (2005) Influence of cultivar and germination on bioactive amines in soybeans (Glycine max L. Merril) Journal Agriculture Food Chemistry, Vol 53(19): Pages 7480-5 https://doi.org/10.1021/jf0509310

Goadsby, Peter J. (2009) The vascular theory of migraine—a great story wrecked by the facts , Brain, Volume 132, Issue 1, Pages 6–7, https://doi.org/10.1093/brain/awn321

Gozal, EA; O'Neill, BE; Sawchuk, MA; Zhu, H; Halder, M; Chou CC; Hochman, S. (2014) Anatomical and functional evidence for trace amines as unique modulators of locomotor function in the mammalian spinal cord, Frontiers Neural Circuits, Vol 07, https://doi.org/10.3389/fncir.2014.00134

Granvogl, M; Bugan, S, Schieberle, P. (2006) Formation of amines and aldehydes from parent amino acids during thermal processing of cocoa and model systems: new insights into pathways of the Strecker reaction, Journal of Agricultural and Food Chemistry, Volume 54, Issue 5, Pages 1730–1739, https://doi.org/10.1021/jf0525939

Hambach, Anke; Evers, Stefan; Summ, Oliver; Husstedt, Ingo W; Frese, Achim (2013), The impact of sexual activity on idiopathic headaches: an observational study, Cephalalgia, Vol. 33(6):Pages 384-9. https://doi.org/10.1177/0333102413476374

Hanington, E. (1980), Diet and migraine, Journal of Human Nutrition, Vol 34(3): Pages 175-80, https://doi.org/10.3109/09637488009143438

Hauptmann, N; Grimsby, J; Shih, JC, Cadenas, E (1996), The metabolism of tyramine by monoamine oxidase A/B causes oxidative damage to mitochondrial DNA, Archives of Biochemistry and Biophysics, Volume 335, Issue 2, Pages 295-304, https://doi.org/10.1006/abbi.1996.0510

Innocente, N; D’Agostin, P; Formation of biogenic amines in a typical semihard Italian cheese, Journal of Food Protection, Vol. 65 (9): Pages 1498–1501, https://doi.org/10.4315/0362-028X-65.9.1498

Johansson, G; Berdague, JL; Larsson, M. Tran, N; Borcha, E (1994) Lipolysis, proteolysis and formation of volatile components during ripening of a fermented sausage with Pediococcus pentosaceus and Staphylococcus xylosus as starter cultures, Meat Science, Volume 38, Issue 2, 1994, Pages 203-218, https://doi.org/10.1016/0309-1740(94)90110-4

Kalac, P; Hlavatá, V; Krížek, M. (1997) Concentrations of five biogenic amines in Czech beers and factors affecting their formation. Food Chemistry, Volume 58, Issue 3, Pages 209-214, https://doi.org/10.1016/S0308-8146(96)00098-2

Kalac, P; Švecová, S; Pelikánová, T. (2002), Levels of biogenic amines in typical vegetable product Food Chemistry, Volume 77, Issue 3, Pages 349-351, https://doi.org/10.1016/S0308-8146(01)00360-0

Karovicová, J; Kohajdová, Z. (2005), Biogenic amines in food. Chemical Paper [formerly Chem Zvesti],Vol 59: Pages 70–79, https://www.chempap.org/file_access.php?file=591a70.pdf

Khan, MZ; Nawaz, W. (2016), The emerging roles of human trace amines and human trace amine-associated receptors (hTAARs) in central nervous system Biomedicine & Pharmacotherapy Volume 83, Pages 439-449, https://doi.org/10.1016/j.biopha.2016.07.002

Kirschbaum, J; Rebscher, K; Bruckner, H. (2000), Liquid chromatographic determination of biogenic amines in fermented foods after derivatization with 3,5-dinitrobenzoyl chloride, Journal of Chromatography Volume 881, Issues 1–2, Pages 517-53 https://doi.org/10.1016/S0021-9673(00)00257-0

KD value: a quantitative measurement of antibody affinity, AbCam, https://www.abcam.com/primary-antibodies/kd-value-a-quantitive-measurement-of-antibody-affinity

Kleinau, G; Pratzka, J; Nurnberg, D; Grüters, A; Führer-Sakel, D; Krude, H; Köhrle, H; Schöneberg, T; Biebermann, H (2011), Differential modulation of Beta-adrenergic receptor signaling by trace amine-associated receptor 1 agonists, PLoS One, https://doi.org/10.1371/journal.pone.0027073

Konczol, A; Rendes, K; Dekany, M; Müller, J; Riethmüller, E; Tibor, G (2016), Blood-brain barrier specific permeability assay reveals N-methylated tyramine derivatives in standardised leaf extracts and herbal products of Ginkgo biloba, Journal of Pharmaceutical and Biomedical Analysis, Volume 131, Issue 30, Pages 167-174, https://doi.org/10.1016/j.jpba.2016.08.032

Ladero, V; Gomez-Sordo, C; Sanchez-Llana, E; Sánchez-Llana, E; del Rio, B; Redruello, B; Fernández, M; Martín, M. C; Alvarez, MA (2016), Q69 (an E. faecalis-infecting bacteriophage) as a biocontrol agent for reducing tyramine in dairy products, Frontiers in Microbiology, Volume 7: Pages 445, https://doi.org/10.3389/fmicb.2016.00445

Landete, JM; Ferrer, S; Polo, L; et al. (2005), Biogenic amines in wines from three Spanish regions, Journal of Agricultural and Food Chemistry, Vol 53, Issue 4, Pages 1119–1124, http://dx.doi.org/10.1021/jf049340k

La Gioia, F; Rizzotti, L; Rossi F, Gardini, F; Tabanelli, G; Torriani, S. (2011), Identification of a tyrosine decarboxylase gene (tdcA) in Streptococcus thermophilus 1TT45 and analysis of its expression and tyramine production in milk, ASM Journals / Applied and Environmental Microbiology, Vol. 77, No. 3, https://doi.org/10.1128/AEM.01928-10

Lange, J; Thomas, K; Wittman, C. (2002), Comparison of a capillary electrophoresis method with high-performance liquid chromatography for the determination of biogenic amines in various food samples. Journal of Chromatography B Analytical Technology Biomed Life Sci. Vol 779: Pages 229–239. https://doi.org/10.1016/s1570-0232(02)00372-0

Lavizzari, T; Veciana-Nogués, M; Bover-Cid, S; Mariné-Font, Abel; Vidal-Carou, Maria Carmen (2006), Improved method for the determination of biogenic amines and polyamines in vegetable products by ion-pair high-performance liquid chromatography, Journal of Chromatography A, Volume 1129, Issue 1, Pages 67-72, https://doi.org/10.1016/j.chroma.2006.06.090

Ledonne, A; Federici, M; Giustizieri, M; Pessia, M; Imbrici, P; Millan, M J; Bernardi, G; Mercuri, N B (2010), Trace amines depress D2-autoreceptor-mediated responses on midbrain dopaminergic cells, British Journal of Pharmacology, Volume 160, Issue6, Pages 1509-1520, https://doi.org/10.1111/j.1476-5381.2010.00792.x

Leuschner, RG; Hammes, WP. (1998) Degradation of histamine and tyramine by Brevibacterium linens during surface ripening of Munster cheese, Journal of Food Protection, Volume 61 (7): Pages 874–878, https://doi.org/10.4315/0362-028X-61.7.874

Leuschner, RG; Kurihara, R; Hammes, W.P. (1998), Effect of enhanced proteolysis on formation of biogenic amines by lactobacilli during Gouda cheese ripening, International Journal of Food Microbiology Volume 44, Issues 1–2, Pages 15-20 https://doi.org/10.1016/S0168-1605(98)00118-4

Linares, DM; Del Rio, B; Ladero V, Martínez, N.; Fernández, M; Martín, M C; Álvarez, M A. (2012) Factors influencing biogenic amines accumulation in dairy products, Frontiers in Microbiology, https://doi.org/10.3389/fmicb.2012.00180

Lüthy, J; Schlatter, C. (1983) Biogenic amines in foods: effects of histamine, tyramine and phenylethylamine on man, Zeitschrift für Lebensmittel-Untersuchung und Forschung, Volume 177, Pages 439–443, https://doi.org/10.1007/bf01409672

Marcinek, P; Geithe, C, Krautwurst, D. (2017), Chemosensory G protein-coupled receptors (GPCR) in blood leukocytes. In:Krautwurst D , ed. Taste and Smell. Cham, Germany: Springer International Publishing, Pages 151–173.

Marcobal, A; De Las Rivas, B; Landete, J M;, Tabera, L; Muñoz, R (2011) Tyramine and phenylethylamine biosynthesis by food bacteria, Critical Reviews in Food Science and Nutrition, Volume 52, Issue 5 https://doi.org/10.1080/10408398.2010.500545

Marcobal, A; Martin-Alvarez, PJ; Moreno-Arribas, MV; Muñoz, R (2006) A multifactorial design for studying factors influencing growth and tyramine production of the lactic acid bacteria Lactobacillus brevis CECT 4669 and Enterococcus faecium BIFI-58, Research in Microbiology, Volume 157, Issue 5, Pages 417-424, https://doi.org/10.1016/j.resmic.2005.11.006

Marcobal, A; Polo, MC; Marti´n-Álvarez, PJ; Moreno-Arribas, M.V. Biogenic amine content of red Spanish wines: comparison of a direct ELISA and an HPLC method for the determination of histamine in wines, Food Research International, Volume 38, Issue 4, Pages 387-394 https://doi.org/10.1016/j.foodres.2004.10.008

Martinez-Villaluenga, C; Frias, J; Gulewicz, P; Vidal-Valverde, C (2008), Food safety evaluation of broccoli and radish sprouts, Food and Chemical Toxicology, Volume 46, Issue 5, Pages 1635-1644, https://doi.org/10.1016/j.fct.2008.01.004

Maxa, E; Brandes, W. Biogene (1993) Amine in Fruchtsäften [in German], Mitt Klosterneuburg Rebe Wein Obstb Fruchteverwert, Vol 43, Num 3, pp 101-106, https://pascal-francis.inist.fr/vibad/index.php?action=search&lang=en&terms=%220007-5922%22&index=is

Mayevsky, Avraham; Doron, Avi; Manor, Tamar; Meilin, Sigal; Zarchin, Nili. Ouaknine, George E. (1996), Cortical spreading depression recorded from the human brain using a multiparametric monitoring system, Brain Research, Volume 740, Issues 1–2, Pages 268-274, https://doi.org/10.1016/S0006-8993(96)00874-8

Mayr, CM; Schieberle, P. (2012), Development of stable isotope dilution assays for the simultaneous quantitation of biogenic amines and polyamines in foods by LC-MS/MS. Journal Agricultural Food Chem. Vol 60: Pages 3026–3032, https://doi.org/10.1021/jf204900v

Moret, Sabrina; Smela, Dana; Populin, Tiziana; Conte, Lanfranco (2005) A survey on free biogenic amine content of fresh and preserved vegetables, Food Chemistry, Vol. 89(3): Pages 355-361, http://dx.doi.org/10.1016/j.foodchem.2004.02.050

Millichap, J Gordon (1988), Oligoantigenic Diet for Epilepsy and Migraine. Pediatric Neurology Briefs, Vol. 2(12), pp.91–92. http://doi.org/10.15844/pedneurbriefs-2-12-5

Millichap, J. Gordon; MYee, Michelle (2003) The diet factor in pediatric and adolescent migraine, Pediatric Neurology Volume 28, Issue 1, Pages 9-1 https://doi.org/10.1016/S0887-8994(02)00466-6

Naila, A, Flint, S, Fletcher, G, Bremer, P; Meerdink, G (2010) Control of biogenic amines in food—existing and emerging approaches, Journal of Food Science, Volume 75: Pages R139–R150 https://doi.org/10.1111/j.1750-3841.2010.01774.x

Nguyen, TV; Juorio, AV. (1989), Binding sites for brain trace amines, Cellular Molecular Neurobiology, Vol 9(3): Pages 297-311, https://doi.org/10.1007/bf00711411

Novella-Rodriguez, S; Veciana-Nogues, MT; Vidal-Carou, MC (2000), Biogenic amines and polyamines in milks and cheeses by ion-pair high performance liquid chromatography, Journal of Agricultural and Food Chemistry, Vol 48, Issue 11, Pages 5117–5123, https://doi.org/10.1021/jf0002084

Önal A. (2007) A review: current analytical methods for the determination of biogenic amines in foods. Food Chemistry, Volume 103, Issue 4, 2007, Pages 1475-1486 https://doi.org/10.1016/j.foodchem.2006.08.028

Philips, SR; Rozdilsky, B; Boulton, AA. (1978), Evidence for the presence of m-tyramine, p-tyramine, tryptamine, and phenylethylamine in the rat brain and several areas of the human brain, Biology of Psychiatry, Vol 13(1): Pages 51-7, http://www.ncbi.nlm.nih.gov/pubmed/623853

Poeaknapo, C. (2005), Mammalian morphine: de novo formation of morphine in human cells, Medical Science Moitor, Vol 1(5): Pages MS6-17, https://pubmed.ncbi.nlm.nih.gov/15874902/

Prester, L. (2011) Biogenic amines in fish, fish products and shellfish: a review, Food Additives & Contaminants: Part A, Volume 28, 2011, Issue 11, Food Additives & Contaminants: Part A Volume 28, 2011 - Issue 11, https://doi.org/10.1080/19440049.2011.600728

Restuccia, D; Spizzirri, UG; Parisi, OI, Cirillo, G; Picci, N (2015) Brewing effect on levels of biogenic amines in different coffee samples as determined by LC-UV, Food Chemistry Volume 175, Pages 143-150 https://doi.org/10.1016/j.foodchem.2014.11.134

Roy, S; Ninkovic, J; Banerjee, S; Charboneau, R G; Das, S; Dutta, R; Kirchner, V. A; Koodie, L; Ma, J; Meng. J; Barke, RA (2011) Opioid drug abuse and modulation of immune function: consequences in the susceptibility to opportunistic infections, Journal of Neuroimmune Pharmacology, Volume 6, Article number: 442, https://link.springer.com/article/10.1007%2Fs11481-011-9292-5#citeas

Russell, F. A.; King, R.; Smillie, S.-J.; Kodji, X; Brain, S. D. (2014) Calcitonin Gene-Related Peptide: Physiology and Pathophysiology, Physiological Reviews, Vol. 94(4): Pages 1099–1142. https://dx.doi.org/10.1152%2Fphysrev.00034.2013

Saccani, G; Tanzi, E; Pastore, P; Cavallic, S; Reyd, M. (2005), Determination of biogenic amines in fresh and processed meat by suppressed ion chromatography-mass spectrometry using a cation-exchange column, Journal of Chromatography A, Volume 1082, Issue 1, Pages 43-50, https://doi.org/10.1016/j.chroma.2005.05.030

Sathyanarayana Rao, TS; Yeragani, VK. (2009) Hypertensive crisis and cheese, Indian Journal of Psychiatry, Volume : 51, Issue : 1 , Page : 65-66, https://www.indianjpsychiatry.org/text.asp?2009/51/1/65/44910

Sen, N.P. (2006) Analysis and Significance of Tyramine in Foods Journal of Food Science Vol. 34(1): Pages 22 - 26 http://dx.doi.org/10.1111/j.1365-2621.1969.tb14354.x

Shakila, RJ; Vasundhara, TS; Kumudavally, KV (2001) A comparison of the TLC-densitometry and HPLC method for the determination of biogenic amines in fish and fishery products, Food Chemistry Volume 75, Issue 2, Pages 255-259 https://doi.org/10.1016/S0308-8146(01)00173-X

Shalaby, A. R. (1996), Significance of biogenic amines to food safety and human health, Food Research International Volume 29, Issue 7, October 1996, Pages 675-690 Food Research International

Silla Santos, MH. (1996) Biogenic amines: their importance in foods. International Journal Food Microbiology Vol 29(2-3): Pages 213-31, https://doi.org/10.1016/0168-1605(95)00032-1

Simon-Sarkadi, L; Holzapfel, WH (2994), Determination of biogenic amines in leafy vegetables by amino acid analyser, Zeitschrift für Lebensmittel-Untersuchung und -Forschung Volume 198, pages 230–233, https://link.springer.com/article/10.1007%2FBF01192600#citeas

Sood, VK; Kosikowski, F.V. (1979) Accelerated cheddar cheese ripening by added microbial enzymes Journal Dairy Science, https://www.journalofdairyscience.org/article/S0022-0302(79)83516-X/pdf

Souci, SW; Fachmann, W; Kraut, H. (2016) Food Composition and Nutrition Tables, cabdirect.org, https://scholar.google.com/scholar?cites=9920400784025704931&as_sdt=2005&sciodt=0,5&hl=en

Špicka, J; Kalac, P; Bover-Cid, S; Krížek, M. (2002) Application of lactic acid bacteria starter cultures for decreasing the biogenic amine levels in sauerkraut, European Food Research and Technology, Volume 215, Pages 509–514, https://doi.org/10.1007/s00217-002-0590-2

Straub, BW; Tichaczek, PS; Kicherer, M; Hammes, WP (1994), Formation of tyramine byLactobacillus curvatus LTH 972, Zeitschrift für Lebensmittel-Untersuchung und Forschung Volume 199, pages 9–12, https://doi.org/10.1007/BF01192943

Tamang, JP; Tamang, B; Schillinger, U; Guigas, C; Holzapfel, WH (2009) Functional properties of lactic acid bacteria isolated from ethnic fermented vegetables of the Himalayas, International Journal of Food Microbiology, Volume 135, Issue 1, Pages 28-33, https://doi.org/10.1016/j.ijfoodmicro.2009.07.016

Tarjan, V; Janossy, G. (3021) The role of biogenic amines in foods, Molecular Nutrition and Food Research, Volume 65, Issue 14, https://onlinelibrary.wiley.com/doi/10.1002/mnfr.202100100

Teive, H.A.G.; Kowacs, P. A.; Filho, P. Maranhão; Piovesan, E. J.; Werneck, L. C. (2005), Leão's cortical spreading depression, HISTORICAL NEUROLOGY. https://doi.org/10.1212/01.wnl.0000183281.12779.cd

Valoti, M; Moron, JA; Benocci, A; Sgaragli, G; Unzeta, M (1998), Evidence of a coupled mechanism between monoamine oxidase and peroxidase in the metabolism of tyramine by rat intestinal mitochondria, Biochemical Pharmacology, Volume 55, Issue 1, Pages 37-43, https://doi.org/10.1016/S0006-2952(97)00379-1

Valsamaki, K; Michaelidou, A; Polychroniadou, A. (2000) Biogenic amine production in Feta cheese, Food Chemistry, Volume 71, Issue 2, November 2000, Pages 259-266, https://doi.org/10.1016/S0308-8146(00)00168-0

Vaughan, TR. (1994) The role of food in the pathogenesis of migraine headache, Clinical Reviews in Allergy Vol 12(2): Pages 167-80, https://doi.org/10.1007/bf02802353

Walker, S E; Shulman, K I; Tailor, S A; Gardner, D (1996), Tyramine content of previously restricted foods in monoamine oxidase inhibitor diets Clinical Psychopharmacololgy, Vol. 16(5):Pages 383-8, https://doi.org/10.1097/00004714-199610000-00007

Wasik, A M; Millan, M J; Scanlan, T; Barnes, N M; Gordon, J (2012), Evidence for functional trace amine associated receptor-1 in normal and malignant B cells, Leukemia Research, Volume 36, Issue 2, Pages 245-249, https://doi.org/10.1016/j.leukres.2011.10.002

Yen, GC (1986), Studies on biogenic amines in foods. I. Determination of biogenic amines in fermented soybean foods by HPLC, Journal Chinese Agricultural Chemistry Society, Volume 24: Pages 211–217, https://scholar.google.com/scholar_lookup?title=Studies%20on%20biogenic%20amines%20in%20foods.%20I.%20Determination%20of%20biogenic%20amines%20in%20fermented%20soybean%20foods%20by%20HPLC&author=GC.%20Yen&publication_year=1986&journal=J%20Chinese%20Agric%20Chem%20Soc&volume=24&pages=211-217

Zarko, Jennette (2015), Dietary and lifestyle modifications for migraine prevention, Brain Institute, https://blogs.ohsu.edu/brain/2015/06/18/dietary-and-lifestyle-modifications-for-migraine-prevention/

Ziegler, W; Hahn, M; Wallnoefer, PR. (1994) Verhalten biogener Amine bei der Zubereitung ausgewählter pflanzlicher Lebensmittel [in German], Deutsche Lebensmittel-Rundschau. Vol 90, Num 4, Pages 108-112, ISSN https://pascal-francis.inist.fr/vibad/index.php?action=search&lang=en&terms=%220012-0413%22&index=is

Zhu, W; Cadet, P; Baggerman, G; Mantione, K J; Stefano, G B (3005) Human white blood cells synthesize morphine: CYP2D6 modulation, The Journal of Immunology, Vol 175 (11) Pages 7357-7362; DOI: https://doi.org/10.4049/jimmunol.175.11.7357

Zhu, ZT; Munhall, AC; Johnson, SW. (2007), Tyramine excites rat subthalamic neurons in vitro by a dopamine-dependent mechanism, Neuropharmacology Volume 52, Issue 4, Pages 1169-1178, https://doi.org/10.1016/j.neuropharm.2006.12.005

https://epub.uni-regensburg.de/43692/1/Sarah%20Thesis%20AD%20-FINAL%20FORM_AD.pdf

https://www.reuters.com/article/us-usa-northkorea-warmbier-idUSKCN1S124E

https://core.ac.uk/download/pdf/36084456.pdf

https://pubmed.ncbi.nlm.nih.gov/7196439/

https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/amine-oxidase

https://pubmed.ncbi.nlm.nih.gov/9652437/

https://pubs.rsc.org/en/content/chapterhtml/2019/bk9781788014366-00001?isbn=978-1-78801-436-6&sercode=bk

https://www.semanticscholar.org/paper/Prophylactic-Treatment-of-Migraine-in-Children.-1.-Damen-Bruijn/fb4d952daa151add7f078046c02fa2beacb96bb0

https://www.semanticscholar.org/paper/MIGRAINE-IS-A-FOOD-ALLERGIC-DISEASE-Monro-Carini/3e4dde363c6099d73c3ae0d8cc6b1a51743d909f

https://pubmed.ncbi.nlm.nih.gov/6137694/

https://www.health.state.mn.us/diseases/scombroid/index.html

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5500297/

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3049472/

https://www.themigrainereliefcenter.com/treatments/surgery/

https://www.ncbi.nlm.nih.gov/books/NBK525950/

https://www.sciencedirect.com/science/article/abs/pii/0013469458900737#!

https://journals.physiology.org/doi/full/10.1152/classicessays.00031.2005

https://www.scielo.br/j/anp/a/jC9t9Lx5DqTKc6SnfCvkr3q/?lang=en

https://pubs.rsc.org/en/content/chapterhtml/2019/bk9781788014366-00001?isbn=978-1-78801-436-6&sercode=bk

https://www.semanticscholar.org/paper/Prophylactic-Treatment-of-Migraine-in-Children.-1.-Damen-Bruijn/fb4d952daa151add7f078046c02fa2beacb96bb0

https://www.semanticscholar.org/paper/MIGRAINE-IS-A-FOOD-ALLERGIC-DISEASE-Monro-Carini/3e4dde363c6099d73c3ae0d8cc6b1a51743d909f

https://www.health.state.mn.us/diseases/scombroid/index.html

https://pubmed.ncbi.nlm.nih.gov/7196439/

https://core.ac.uk/download/pdf/36084456.pdf

https://www.fda.gov/food/consumers/what-you-need-know-about-foodborne-illnesses

http://digital.csic.es/bitstream/10261/61424/4/food_bacteria_Marcobal.pdf

https://www.mdpi.com/2227-9040/8/4/99

https://pubmed.ncbi.nlm.nih.gov/25632438/

https://ldn.de/produkt/fc-l-3200/

https://onlinelibrary.wiley.com/doi/full/10.1111/1541-4337.12704

https://www.azurebiosystems.com/wp-content/uploads/2016/05/App-Note-Measuring-Histamine-Levels-in-Food-Samples-with-Ao-Reader_4.pdf

https://www.researchgate.net/publication/12787494_A_Test_Strip_for_Diamines_in_Tuna

https://d-nb.info/975903071/34

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7320057/

https://link.springer.com/article/10.1007/s00216-017-0696-9

https://epub.uni-regensburg.de/43692/1/Sarah%20Thesis%20AD%20-FINAL%20FORM_AD.pdf

https://www.creative-diagnostics.com/Anti-Tyramine-Antibody-3520-147.htm

https://academic.oup.com/nutritionreviews/article/77/2/107/5084469

https://www.bio-rad-antibodies.com/antigen-antibody-interactions.html

https://www.abcam.com/primary-antibodies/kd-value-a-quantitive-measurement-of-antibody-affinity#:~:text=The%20KD%20value%20relates,the%20affinity%20of%20the%20antibody.

https://www.scielo.br/j/jbchs/a/zTFXxBv7XnZ9FSqkTPRDw8p/?lang=en

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6049710/

https://www.sciencedaily.com/releases/2007/10/071001125645.htm

https://n.neurology.org/content/65/9/1455

https://www.sciencedirect.com/science/article/abs/pii/S0006899396008748

https://pubmed.ncbi.nlm.nih.gov/21438041/

https://pubmed.ncbi.nlm.nih.gov/8889911/

https://www.sciencedirect.com/science/article/abs/pii/S0887899402004666

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4187032/

https://www.tandfonline.com/doi/full/10.1080/01616412.2018.1428406

https://www.pediatricneurologybriefs.com/articles/10.15844/pedneurbriefs-2-12-5/?utm_source=TrendMD&utm_medium=cpc&utm_campaign=Pediatric_Neurology_Briefs_TrendMD_0

https://pubmed.ncbi.nlm.nih.gov/23430983/

https://www.researchgate.net/publication/13554952_Dopamine_Formation_from_Tyramine_by_CYP2D6

https://link.springer.com/chapter/10.1007/978-1-4615-1913-3_10

https://link.springer.com/article/10.1007/s00216-020-02675-9/tables/2

https://pubmed.ncbi.nlm.nih.gov/29527677/

https://www.researchgate.net/publication/223875082_A_survey_on_free_biogenic_amine_content_of_fresh_and_preserved_vegetables

https://www.efsa.europa.eu/en/efsajournal/pub/2393

https://pubmed.ncbi.nlm.nih.gov/692645/

https://www.researchgate.net/publication/229981151_Analysis_and_Significance_of_Tyramine_in_Foods


Privacy Policy

TONGKATALI.ORG - Medan - North Sumatra - Indonesia