Tuesday, 31 March 2015

Candida alters P.H. levels, causing cancer, I believe the body is trying to decompose, as Candida multiples in death

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Leafy green, allium, and cruciferous vegetables are key parts of alkaline diet.
Alkaline diet (also known as the alkaline ash diet, alkaline acid diet, acid ash diet, and the acid alkaline diet) describes a group of loosely related diets based on the belief that certain foods can affect the acidity and pH of bodily fluids, including the urine or blood, and can therefore be used to treat or prevent diseases. Due to the lack of human studies supporting any benefits of this diet, it is generally not recommended by dieticians and other health professionals.[1]
The relationship between diet and acid-base homeostasis, or the regulation of the acid-base status of the body, has been studied for decades, though the medical applications of this theory have largely focused on changing the acidity of urine. Traditionally, this diet has advocated for avoiding meat, dairy, and grains in order to make the urine more alkaline (higher pH), changing the environment of the urine to prevent recurrent urinary tract infections (UTIs) and kidney stones (nephrolithiasis). However, difficulties in effectively predicting the effects of this diet have led to medications, rather than diet modification, as the preferred method of changing urine pH. The "acid-ash" hypothesis has been considered a risk factor for osteoporosis by various scientific publications, though more recently, the available weight of scientific evidence does not support this hypothesis.
The term "alkaline diet" has also been used by alternative medicine practitioners, with the proposal that such diets treat or prevent cancer, heart disease, low energy levels as well as other illnesses. These claims are not supported by medical evidence and make incorrect assumptions about how alkaline diets function that are contrary to modern understanding of human physiology.


Medical aspects[edit]

Diet composition[edit]

According to the traditional theory underlying this diet, acid ash is produced by meat, poultry, cheese, fish, eggs, and grains. Alkaline ash is produced by fruits and vegetables, except cranberries, prunes and plums. Since the acid or alkaline ash designation is based on the residue left on combustion rather than the acidity of the food, foods such as citrus fruits that are generally considered acidic are actually considered alkaline producing in this diet.[2]

Current hypotheses[edit]

It has been suggested that diets high in "acid ash" (acid producing) elements will cause the body to try to buffer (or counteract) any additional acid load in the body by breaking down bone, leading to weaker bones and increased risk for osteoporosis. Conversely, "alkaline ash" (alkaline producing) elements will theoretically decrease the risk of osteoporosis. This theory has been advanced in a position statement of the American Dietetic Association,[2] in a publication of the U.S. National Academy of Sciences,[3] as well as other scientific publications,[4] which have stated foods high in potassium and magnesium such as fruits and vegetables may decrease the risk of osteoporosis through increased alkaline ash production. This acceptance of the acid-ash hypothesis as a major modifiable risk factor of osteoporosis by these publications, however, was largely made without significant critical review by high quality systematic analysis.[5]
Recent systematic reviews have been published which have methodically analyzed the weight of available scientific evidence, and have found no significant evidence to support the acid-ash hypothesis in regards to prevention of osteoporosis. A meta-analysis of studies on the effect of dietary phosphate intake contradicted the expected results under the acid-ash hypothesis with respect to calcium in the urine and bone metabolism. This result suggests use of this diet to prevent calcium loss from bone is not justified.[5] Other meta-analyses which have investigated the effect of total dietary acid intake have also found no evidence that acid intake increases the risk for osteoporosis as would be expected under the acid-ash hypothesis.[4][6] A review looked at the effects of dairy product intake, which have been hypothesized to increase the acid load of the body through phosphate and protein components. This review found no significant evidence suggesting dairy product intake causes acidosis or increases risk for osteoporosis.[7]
It has also been speculated that this diet may have an effect on muscle wasting, growth hormone metabolism or back pain, though there is no conclusive evidence to confirm these hypotheses.[8][9][10] Given an aging population, the effects of an alkaline diet on public health may be worth considering, though there is little scientific evidence in this area.[10]

Alternative medicine[edit]

Alternative medicine practitioners who have promoted the alkaline diet have advocated its use in the treatment of various medical conditions including cancer.[11] These claims have been mainly promoted on websites, magazines, direct mail, and books, and have been mainly directed at a lay audience.[4] While it has been proposed that this diet can help increase energy, lose weight, and treat cancer and heart disease, there is no evidence to support any of these claims.[12] This version of the diet, in addition to avoiding meats and other proteins, also advocates avoiding processed foods, white sugar, white flour, and caffeine,[9] and can involve specific exercise and nutritional supplement regimens as well.[13]

Evidence base[edit]

Advocates for alternative uses of an alkaline diet propose that since the normal pH of the blood is slightly alkaline, the goal of diet should be to mirror this by eating a diet that is alkaline producing as well. These advocates propose that diets high in acid-producing elements will generally lead the body to become acidic, which can foster disease.[9][12] This proposed mechanism, in which the diet can significantly change the acidity of the blood, goes against "everything we know about the chemistry of the human body" and has been called a "myth" in a statement by the American Institute for Cancer Research.[14] Unlike the pH level in the urine, a selectively alkaline diet has not been shown to elicit a sustained change in blood pH levels, nor to provide the clinical benefits claimed by its proponents. Because of the body's natural regulatory mechanisms, which do not require a special diet to work, eating an alkaline diet can, at most, change the blood pH minimally and transiently.[1][9][12][14]
A similar proposal by those advocating this diet suggests that cancer grows in an acidic environment, and that a proper alkaline diet can change the environment of the body to treat cancer. This proposal ignores the fact that while cancer tissue does grow in acidic environment, it is the cancer that creates the acidity. The rapid growth of cancer cells creates the acidic environment; the acidic environment does not create cancer.[11] The proposal also neglects to recognize that it is "virtually impossible" to create a less acidic environment in the body.[14] "Extreme" dietary plans such as this diet have more risks than benefits for patients with cancer.[11]
Other proposed benefits from eating an alkaline diet are likewise not supported by scientific evidence. Although it has been proposed that this diet will increase "energy" or treat cardiovascular disease, there is no evidence to support these assertions.[12] A version of this diet has also been promoted by Robert O. Young as a method of weight loss in his book The pH Miracle. According to the Academy of Nutrition and Dietetics, portions of his diet such as the emphasis on eating green leafy vegetables and exercise would likely be healthy. However, the "obscure theory" on which his diet is based and the reliance on complicated fasting regimens and nutritional supplements means that this diet "is not a healthy way to lose weight."[13] It has also been proposed that acid causes rheumatoid arthritis and osteoarthritis, and that an alkaline diet can be used to treat these conditions. There is no evidence to support this proposal.[15]
Urinary and/or saliva testing for acidity has been proposed as a way to measure the body's acidity level and therefore the level of risk for diseases.[4] However, there is no correlation between the urinary pH measured in home "test kits" and the acidity of the body.[14]

Adverse effects[edit]

Because the alkaline diet promotes excluding certain families of foods, it could result in a less-balanced diet with resulting nutrient deficiencies such as essential fatty acids and phytonutrients.[1] Many websites and books promoting this diet sell courses of supplements and foods; it should not be necessary to purchase any of these products. The level of effort needed to use this diet is considered "High" as there are many foods that need to be excluded in this diet.[9]

History[edit]

The role of the diet and its influence on the acidity of urine has been studied for decades, as physiologists have studied the kidney's role in the body's regulatory mechanisms for controlling the acidity of body fluids. The French biologist Claude Bernard provided the classical observation of this effect when he found that changing the diet of rabbits from an herbivore (mainly plant) diet to a carnivore (mainly meat) diet changed the urine from more alkaline to more acid. Spurred by these observations, subsequent investigations focused on the chemical properties and acidity of constituents of the remains of foods combusted in a bomb calorimeter, described as ash. The "dietary ash hypothesis" proposed that these foods, when metabolized, would leave a similar "acid ash" or "alkaline ash" in the body as those oxidized in combustion.[16]
Nutrition scientists began to refine this hypothesis in the early 20th century, emphasizing the role of negatively charged particles (anions) and positively charged particles (cations) in food. Diets high in chloride, phosphates and sulfates (all of which are anions) were presumed to be acid forming, while diets high in potassium, calcium and magnesium (all of which are cations) were presumed to be alkaline forming. Other investigations showed specific foods, such as cranberries, prunes and plums had unusual effects on urine pH. While these foods provided an alkaline ash in the laboratory, they contained a weak organic acid, hippuric acid, which caused the urine to become more acidic instead.[16]

Historical uses[edit]

Historically, the medical application of this diet has largely focused on preventing recurrence of kidney stones as well as the prevention of recurrent UTIs, by relying on the recognized ability of this diet to affect urinary pH. Years ago, this diet was used to adjust the acidity of the urinary environment that the stones formed in, and could theoretically help prevent stones from forming or the development of UTIs. However, the analytical methods that attempted to precisely calculate the effects of food on urinary pH were not precise except in very general terms, making effective use of this diet difficult. Therefore, medications, which can more reliably alter the urine pH, rather than diet modification, have been the treatment of choice when trying to alter the pH of the urine.[17] While there have been recent improvements in recognizing different variables that can affect acid excretion in the urine, the level of detail needed to predict the urinary pH based on diet is still daunting. Precise calculations require very detailed knowledge of the nutritional components of every meal as well as the rate of absorption of nutrients, which can vary substantially from individual to individual, making effective estimation of urine pH still not currently feasible.[18]

See also[edit]

References[edit]

  1. ^ a b c Vangsness, Stephanie (16 January 2013). "Alkaline Diets and Cancer: Fact or Fiction?". Intelihealth. Retrieved 5 February 2014. 
  2. ^ a b Cunningham E (October 2009). "What impact does pH have on food and nutrition?". J Am Diet Assoc 109 (10): 1816. doi:10.1016/j.jada.2009.08.028. PMID 19782182. 
  3. ^ Food and Nutrition Board. Dietary Reference Intakes for Water, Potassium, Sodium, Chloride, and Sulfate (2005), page 189. National Academies Press.
  4. ^ a b c d Fenton TR, Tough SC, Lyon AW, Eliasziw M, Hanley DA (2011). "Causal assessment of dietary acid load and bone disease: a systematic review & meta-analysis applying Hill's epidemiologic criteria for causality". Nutr J 10: 41. doi:10.1186/1475-2891-10-41. PMC 3114717. PMID 21529374. 
  5. ^ a b Fenton TR, Lyon AW, Eliasziw M, Tough SC, Hanley DA (2009). "Phosphate decreases urine calcium and increases calcium balance: a meta-analysis of the osteoporosis acid-ash diet hypothesis". Nutr J 8: 41. doi:10.1186/1475-2891-8-41. PMC 2761938. PMID 19754972. 
  6. ^ Fenton TR, Lyon AW, Eliasziw M, Tough SC, Hanley DA (November 2009). "Meta-analysis of the effect of the acid-ash hypothesis of osteoporosis on calcium balance". J. Bone Miner. Res. 24 (11): 1835–40. doi:10.1359/jbmr.090515. PMID 19419322. 
  7. ^ Fenton TR, Lyon AW (October 2011). "Milk and acid-base balance: proposed hypothesis versus scientific evidence". J Am Coll Nutr 30 (5 Suppl 1): 471S–5S. PMID 22081694. 
  8. ^ Pizzorno J, Frassetto LA, Katzinger J (April 2010). "Diet-induced acidosis: is it real and clinically relevant?". Br. J. Nutr. 103 (8): 1185–94. doi:10.1017/S0007114509993047. PMID 20003625. 
  9. ^ a b c d e "Alkaline Diets". WebMD. Retrieved 5 February 2014. 
  10. ^ a b Schwalfenberg GK (2012). "The alkaline diet: is there evidence that an alkaline pH diet benefits health?". J Environ Public Health (Review) 2012: 727630. doi:10.1155/2012/727630. PMC 3195546. PMID 22013455. 
  11. ^ a b c Cassileth, Carrie R. (2008). Principles and Practice of Gastrointestinal Oncology. Philadelphia, PA: Lippincott Williams & Wilkins. p. 137. ISBN 0-7817-7617-1. 
  12. ^ a b c d "An alkaline diet and cancer". Canadian Cancer Society. Retrieved 10 August 2012. 
  13. ^ a b "The pH Miracle for Weight Loss Book Review". Academy of Nutrition and Dietetics. Retrieved 10 August 2012. 
  14. ^ a b c d "Cancer and Acid-Base Balance: Busting the Myth". American Institute for Cancer Research. Retrieved 10 August 2012. 
  15. ^ Skarnulis, Leanna. "Arthritis diets and supplements: Do they work?". Retrieved 10 August 2012. 
  16. ^ a b Dwyer J, Foulkes E, Evans M, Ausman L (July 1985). "Acid/alkaline ash diets: time for assessment and change". J Am Diet Assoc 85 (7): 841–5. PMID 4008836. 
  17. ^ Williams, Sue (2001). Basic Nutrition & Diet Therapy, 11th ed. 2001: Mosby. p. 414. ISBN 0-323-00569-1. 
  18. ^ Remer T (2000). "Influence of diet on acid-base balance". Semin Dial 13 (4): 221–6. doi:10.1046/j.1525-139x.2000.00062.x. PMID 10923348. 

Further reading[edit]

Top diets rev
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Monday, 30 March 2015

Alzheimer's and antifungal drug

AsianScientist (May 14, 2014) - Eisai Co. Ltd. has exercised its option to jointly develop and commercialize its clinical candidates for Alzheimer’s disease with US biotechnology firm Biogen Idec. The option was included as part of Eisai’s collaboration agreement with Biogen Idec announced in March 2014.
Based on the agreement, Eisai and Biogen Idec will co-develop Eisai’s investigational next generation Alzheimer's disease treatment candidates E2609 and BAN2401 for major markets such as the United States, the European Union and Japan.
E2609 is believed to inhibit BACE, a key enzyme in the production of amyloid beta (Aβ). By inhibiting BACE, E2609 decreases Aβ proteins in the brain, potentially improving symptoms and slowing disease progression. BAN2401, an Aβ protofibril antibody, is believed to selectively bind to and eliminate soluble, toxic Aβ aggregates that are thought to contribute to the neurodegenerative process in Alzheimer's disease. As such, BAN2401 could potentially have an immunomodulatory effect that may suppress the progression of the disease.
A Phase II clinical trial is already underway for BAN2401, while E2609 is currently undergoing preparations for a Phase II clinical trial.
The companies will co-promote the products following marketing approval and share
overall costs, including research and development expenses incurred in Japan. Eisai will book all sales for E2609 and BAN2401 following marketing approval and launch, sharing profits with Biogen Idec. In accordance with the execution of this option, Eisai will receive from Biogen Idec an additional one-time payment as well as the right to receive additional development milestone payments.  Read more from Asian Scientist Magazine at: http://www.asianscientist.com/2014/05/pharma/alzheimers-drugs-eisai-biogen-idec-2014/
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killer yeast -Saccharomyces cerevisiae, lethal toxins- Louis Pasteur

Treat Urinary Incontinence Now No Pads, No Probes, No Worries!
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A killer yeast is a yeast, such as Saccharomyces cerevisiae, which is able to secrete one of a number of toxic proteins which are lethal to receptive cells.[1] The phenomenon was first observed by Louis Pasteur, as noted in 1877.[2] These yeast cells are immune to the toxic effects of the protein due to an intrinsic immunity.[3] Killer yeast strains can be a problem in commercial processing because they can kill desirable strains.[4] The killer yeast system was first described in 1963.[5] Study of killer toxins helped to better understand the secretion pathway of yeast, which is similar to those of higher eukaryotes. It also can be used in treatment of some diseases, mainly that caused by fungi.


Saccharomyces cerevisiae[edit]

The best characterized toxin system is from yeast (Saccharomyces cerevisiae), which was found to spoil brewing of beer. In S. cerevisiae are toxins encoded by a double-stranded RNA virus, translated to a precursor protein, cleaved and secreted outside of the cells, where they may affect susceptible yeast. There are other killer systems in S. cerevisiae, such as KHR [6] and KHS [7] genes encoded on chromosome.

RNA virus[edit]

Main article: Saccharomyces cerevisiae virus L-A
The virus, L-A, is an icosahedral virus of S. cerevisiae comprising a 4.6 kb genomic segment and several satellite double-stranded RNA sequences, called M dsRNAs. The genomic segment encodes for the viral coat protein and a protein which replicates the viral genomes.[8] The M dsRNAs encode the toxin, of which there are at least three variants in S. cerevisiae,[3][9] and many more variants across all species.[1][10]
L-A virus uses yeast Ski complex (super killer) and MAK (maintenance of killer) chromosomal genes for its preservation in the cell. The virus is not released into the environment. It spreads between cells during yeast mating.[9]

Toxins[edit]

The K1 preprotoxin, showing the α and β chains which make up the K1 toxin. The numbers count amino acid residues.
The initial protein product from translation of the M dsRNA is called the preprotoxin, which is targeted to the yeast secretory pathway. The preprotoxin is processed and cleaved to produce an α/β dimer, which is the active form of the toxin, and is released into the environment.[3][11]
The two most studied variant toxins in S. cerevisiae are K1 and K28.
K1 binds to the β-1,6-D-glucan receptor on the target cell wall, moves inside, and then binds to the plasma membrane receptor Kre1p. It forms a cation-selective ion channel in the membrane, which is lethal to the cell.[11][12]
K28 uses the α-1,6-mannoprotein receptor to enter the cell, and utilizes the secretory pathway in reverse by displaying the endoplasmic reticulum HDEL signal. From the ER, K28 moves into the cytoplasm and shuts down DNA synthesis in the nucleus, triggering apoptosis.[13][14]

Immunity[edit]

Sestia, Shiha, Nikolaevaa and Goldstein (2001) claimed that K1 inhibits the TOK1 membrane potassium channel before secretion, and although the toxin reenters through the cell wall it is unable to reactivate TOK1.[15] However Breinig, Tipper and Schmitt (2002) showed that the TOK1 channel was not the primary receptor for K1, and that TOK1 inhibition does not confer immunity.[12] Vališ, Mašek, Novotná, Pospíšek and Janderová (2006) experimented with mutants which produce K1 but do not have immunity to it, and suggested that cell membrane receptors were being degraded in the secretion pathway of immune cells, apparently due to the actions of unprocessed α chains.[16][17]
The K28 preprotoxin forms a complex with the K28 α/β dimer, neutralizing it.
Breinig, Sendzik, Eisfeld and Schmitt (2006) showed that K28 toxin is neutralized in toxin-expressing cells by the α chain in the cytosol, which has not yet been fully processed and still contains part of a γ chain attached to the C terminus. The uncleaved α chain neutralizes the K28 toxin by forming a complex with it.[3]

Kluyveromyces lactis[edit]

Killer properties of Kluyveromyces lactis are associated with linear DNA plasmids, which have on their 5'end associated proteins, which enable them to replicate themselves, in a way similar to adenoviruses. It is an example of protein priming in DNA replication. MAK genes are not known. The toxin consists of three subunits, which are matured in golgi complex by signal peptidase and glycosylated.
The mechanism of action appears to be the inhibition of adenylate cyclase in sensitive cells. Affected cells are arrested in G1 phase and lose viability.

Other yeast[edit]

Other toxin systems are found in other yeasts:

Use of toxins[edit]

The susceptibility to toxins varies greatly between yeast species and strains. Several experiments have made use of this to reliably identify strains. Morace, Archibusacci, Sestito and Polonelli (1984) used the toxins produced by 25 species of yeasts to differentiate between 112 pathogenic strains, based on their sensitivity to each toxin.[18] This was extended by Morace et al. (1989) to use toxins to differentiate between 58 bacterial cultures.[19] Vaughan-Martini, Cardinali and Martini (1996) used 24 strains of killer yeast from 13 species to find a resistance signature for each of 13 strains of S. cerevisiae which were used as starters in wine-making.[20] Buzzini and Martini (2001) showed that sensitivity to toxins could be used to discriminate between 91 strains of Candida albicans and 223 other Candida strains.[21]
Others experimented with using killer yeasts to control undesirable yeasts. Palpacelli, Ciani and Rosini (1991) found that Kluyveromyces phaffii was effective against Kloeckera apiculata, Saccharomycodes ludwigii and Zygosaccharomyces rouxii – all of which cause problems in the food industry.[22] Polonelli et al. (1994) used a killer yeast to vaccinate against C. albicans in rats.[23] Lowes et al. (2000) created a synthetic gene for the toxin HMK normally produced by Williopsis mrakii, which they inserted into Aspergillus niger and showed that the engineered strain could control aerobic spoilage in maize silage and yoghurt.[24] Ciani and Fatichenti (2001) used a toxin-producing strain of Kluyveromyces phaffii to control apiculate yeasts in wine-making.[25] Da Silvaa, Caladoa, Lucasa and Aguiar (2007) found a toxin produced by Candida nodaensis was effective at preventing spoilage of highly salted food by yeasts.[26]
Several experiments suggest that antibodies that mimic the biological activity of killer toxins have application as antifungal agents.[27]

Control methods[edit]

Young and Yagiu (1978) experimented with methods of curing killer yeasts. They found that using a cycloheximine solution at 0.05 ppm was effective in eliminating killer activity in one strain of S. cerevisiae. Incubating the yeast at 37°C eliminated activity in another strain. The methods were not effective at reducing toxin production in other yeast species.[1] Many toxins are sensitive to pH levels; for example K1 is permanently inactivated at pH levels over 6.5.[10]
The greatest potential for control of killer yeasts appears to be the addition of the L-A virus and M dsRNA, or an equivalent gene, into the industrially desirable variants of yeast, so they achieve immunity to the toxin, and also kill competing strains.[4]

See also[edit]

References[edit]

  1. ^ a b c Young, T. W.; Yagiu, M. (1978). "A comparison of the killer character in different yeasts and its classification". Antonie van Leeuwenhoek 44 (1): 59–77. doi:10.1007/BF00400077. PMID 655699. 
  2. ^ Pasteur, L., and J. F. Joubert (1877). "Charbon et septicemie". C. R. Soc. Biol. Paris 85:101–115.
  3. ^ a b c d Breinig, F.; Sendzik, T; Eisfeld, K; Schmitt, MJ (2006). "Dissecting toxin immunity in virus-infected killer yeast uncovers an intrinsic strategy of self-protection". Proceedings of the National Academy of Sciences 103 (10): 3810–5. doi:10.1073/pnas.0510070103. PMC 1533781. PMID 16505373. 
  4. ^ a b Wickner, R B (1986). "Double-Stranded RNA Replication in Yeast: The Killer System". Annual Review of Biochemistry 55: 373–95. doi:10.1146/annurev.bi.55.070186.002105. PMID 3527047. 
  5. ^ Bevan, E. A., and M. Makower. (1963). "The physiological basis of the killer character in yeast". Proc. XIth Int. Congr. Genet. 1:202–203.
  6. ^ Goto, K.; Iwatuki, Y.; Kitano, K.; Obata, T.; Hara, S. (1990). "Cloning and nucleotide sequence of the KHR killer gene of Saccharomyces cerevisiae". Agricultural and biological chemistry 54 (4): 979–984. doi:10.1271/bbb1961.54.979. PMID 1368554.  edit
  7. ^ Goto, K.; Fukuda, H.; Kichise, K.; Kitano, K.; Hara, S. (1991). "Cloning and nucleotide sequence of the KHS killer gene of Saccharomyces cerevisiae". Agricultural and biological chemistry 55 (8): 1953–1958. doi:10.1271/bbb1961.55.1953. PMID 1368726.  edit
  8. ^ Ribas, J. C.; Wickner, RB (1998). "The Gag Domain of the Gag-Pol Fusion Protein Directs Incorporation into the L-A Double-stranded RNA Viral Particles in Saccharomyces cerevisiae". Journal of Biological Chemistry 273 (15): 9306–11. doi:10.1074/jbc.273.15.9306. PMID 9535925. 
  9. ^ a b Wickner, R. B., Jinghua Tang, Gardner, N. A. & Johnson, J. E. (2008). "The Yeast dsRNA Virus L-A Resembles Mammalian dsRNA Virus Cores". In John T. Patton. Segmented Double-stranded RNA Viruses: Structure and Molecular Biology. Caister Academic Press. ISBN 978-1-904455-21-9. 
  10. ^ a b Tipper; Bostian, KA (1984). "Double-stranded ribonucleic acid killer systems in yeasts.". Microbiological reviews 48 (2): 125–56. PMC 373216. PMID 6377033. 
  11. ^ a b Bussey, H. (1991). "K1 killer toxin, a pore-forming protein from yeast". Molecular Microbiology 5 (10): 2339–43. doi:10.1111/j.1365-2958.1991.tb02079.x. PMID 1724277. 
  12. ^ a b Breinig, Frank; Tipper, Donald J.; Schmitt, Manfred J. (2002). "Kre1p, the Plasma Membrane Receptor for the Yeast K1 Viral Toxin". Cell 108 (3): 395–405. doi:10.1016/S0092-8674(02)00634-7. PMID 11853673. 
  13. ^ Reiter, J.; Herker, E; Madeo, F; Schmitt, MJ (2005). "Viral killer toxins induce caspase-mediated apoptosis in yeast". The Journal of Cell Biology 168 (3): 353–8. doi:10.1083/jcb.200408071. PMC 2171720. PMID 15668299. 
  14. ^ Eisfeld, Katrin; Riffer, Frank; Mentges, Johannes; Schmitt, Manfred J. (2000). "Endocytotic uptake and retrograde transport of a virally encoded killer toxin in yeast". Molecular Microbiology 37 (4): 926–40. doi:10.1046/j.1365-2958.2000.02063.x. PMID 10972812. 
  15. ^ Sesti, Federico; Shih, Theodore M.; Nikolaeva, Natalia; Goldstein, Steve A.N. (2001). "Immunity to K1 Killer ToxinInternal TOK1 Blockade". Cell 105 (5): 637–44. doi:10.1016/S0092-8674(01)00376-2. PMID 11389833. 
  16. ^ ValiÅ¡, K.; Masek, T.; Novotná, D.; Pospísek, M.; Janderová, B. (2006). "Immunity to killer toxin K1 is connected with the golgi-to-vacuole protein degradation pathway". Folia Microbiologica 51 (3): 196–202. doi:10.1007/BF02932122. PMID 17004650. 
  17. ^ Sturley; Elliot, Q; Levitre, J; Tipper, DJ; Bostian, KA (1986). "Mapping of functional domains within the Saccharomyces cerevisiae type 1 killer preprotoxin.". The EMBO Journal 5 (12): 3381–9. PMC 1167337. PMID 3545818. 
  18. ^ Morace, G.; Archibusacci, C.; Sestito, M.; Polonelli, L. (1984). "Strain differentiation of pathogenic yeasts by the killer system". Mycopathologia 84 (2–3): 81–5. doi:10.1007/BF00436517. PMID 6371541. 
  19. ^ Morace, G.; Manzara, S.; Dettori, G.; Fanti, F.; Conti, S.; Campani, L.; Polonelli, L.; Chezzi, C. (1989). "Biotyping of bacterial isolates using the yeast killer system". European Journal of Epidemiology 5 (3): 303–10. doi:10.1007/BF00144830. PMID 2676582. 
  20. ^ Vaughan-martini, A; Cardinali, G; Martini, A (1996). "Differential killer sensitivity as a tool for fingerprinting wine-yeast strains ofSaccharomyces cerevisiae". Journal of Industrial Microbiology 17 (2): 124–7. doi:10.1007/BF01570055. PMID 8987896. 
  21. ^ Buzzini, P.; Martini, A. (2001). "Discrimination between Candida albicans and Other Pathogenic Species of the Genus Candida by Their Differential Sensitivities to Toxins of a Panel of Killer Yeasts". Journal of Clinical Microbiology 39 (9): 3362–4. doi:10.1128/JCM.39.9.3362-3364.2001. PMC 88347. PMID 11526179. 
  22. ^ Palpacelli, Valentino; Ciani, Maurizio; Rosini, Gianfranco (1991). "Activity of different 'killer' yeasts on strains of yeast species undesirable in the food industry". FEMS Microbiology Letters 84: 75. doi:10.1111/j.1574-6968.1991.tb04572.x. 
  23. ^ Polonelli, L; De Bernardis, F; Conti, S; Boccanera, M; Gerloni, M; Morace, G; Magliani, W; Chezzi, C; Cassone, A (1994). "Idiotypic intravaginal vaccination to protect against candidal vaginitis by secretory, yeast killer toxin-like anti-idiotypic antibodies". The Journal of Immunology 152 (6): 3175–82. PMID 8144911. 
  24. ^ Lowes, K. F.; Shearman, C. A.; Payne, J.; MacKenzie, D.; Archer, D. B.; Merry, R. J.; Gasson, M. J. (2000). "Prevention of Yeast Spoilage in Feed and Food by the Yeast Mycocin HMK". Applied and Environmental Microbiology 66 (3): 1066–76. doi:10.1128/AEM.66.3.1066-1076.2000. PMC 91944. PMID 10698773. 
  25. ^ Ciani, M.; Fatichenti, F. (2001). "Killer Toxin of Kluyveromyces phaffii DBVPG 6076 as a Biopreservative Agent To Control Apiculate Wine Yeasts". Applied and Environmental Microbiology 67 (7): 3058–63. doi:10.1128/AEM.67.7.3058-3063.2001. PMC 92981. PMID 11425722. 
  26. ^ Dasilva, S; Calado, S; Lucas, C; Aguiar, C (2008). "Unusual properties of the halotolerant yeast Candida nodaensis Killer toxin, CnKT". Microbiological Research 163 (2): 243–51. doi:10.1016/j.micres.2007.04.002. PMID 17761407. 
  27. ^ Magliani, W; Conti, S; Salati, A; Vaccari, S; Ravanetti, L; Maffei, D; Polonelli, L (2004). "Therapeutic potential of yeast killer toxin-like antibodies and mimotopes". FEMS Yeast Research 5 (1): 11–8. doi:10.1016/j.femsyr.2004.06.010. PMID 15381118. 

Further reading

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