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1

Tuite, Mick F., and Brian S. Cox. "Propagation of yeast prions." Nature Reviews Molecular Cell Biology 4, no. 11 (November 2003): 878–90. http://dx.doi.org/10.1038/nrm1247.

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2

Blanco, Carlos A., Julia Rayo, and José M. Giralda. "Improving Industrial Full-Scale Production of Baker's Yeast by Optimizing Aeration Control." Journal of AOAC INTERNATIONAL 91, no. 3 (May 1, 2008): 607–13. http://dx.doi.org/10.1093/jaoac/91.3.607.

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Abstract This work analyzes the control of optimum dissolved oxygen of an industrial fed-batch procedure in which baker's yeast (Saccharomyces cerevisiae) is grown under aerobic conditions. Sugar oxidative metabolism was controlled by monitoring aeration, molasses flows, and yeast concentration in the propagator along the later stage of the propagation, and keeping pH and temperature under controlled conditions. A large number of fed-batch growth experiments were performed in the tank for a period of 16 h, for each of the 3 manufactured commercial products. For optimization and control of cultivations, the growth and metabolite formation were quantified through measurement of specific growth and ethanol concentration. Data were adjusted to a model of multiple lineal regression, and correlations representing dissolved oxygen as a function of aeration, molasses, yeast concentration in the broth, temperature, and pH were obtained. The actual influence of each variable was consistent with the mathematical model, further justified by significant levels of each variable, and optimum aeration profile during the yeast propagation was found.
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3

Gibson, Brian R., Neil S. Graham, Chris A. Boulton, Wendy G. Box, Stephen J. Lawrence, Robert S. T. Linforth, Sean T. May, and Katherine A. Smart. "Differential Yeast Gene Transcription during Brewery Propagation." Journal of the American Society of Brewing Chemists 68, no. 1 (January 2010): 21–29. http://dx.doi.org/10.1094/asbcj-2009-1123-01.

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4

Crapeau, Myriam, Laurent Maillet, and Christophe Cullin. "Ploidy controls [URE3] prion propagation in yeast." FEMS Yeast Research 14, no. 2 (November 8, 2013): 324–36. http://dx.doi.org/10.1111/1567-1364.12110.

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5

Manzano, S., S. Vargas, G. Casaubon, and Á. González. "Evaluation of an active yeast propagation system on fermentation traits and quality of C.V. Carmenère wine." BIO Web of Conferences 12 (2019): 02009. http://dx.doi.org/10.1051/bioconf/20191202009.

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Active dry yeasts (ADY, Saccharomyces cerevisiae) are widely used in oenology due to their potential benefits on the control of fermentation and quality reproducibility among other aspects. On the other hand, yeast propagation systems, so called Active Yeast Systems (AYS), can be useful to optimize the alcoholic fermentation (AF) initial lag phase and reduce production costs. The objective of this work was to determine the predominance of an ADY strain propagated by AYS and the impact of this inoculum on cv. Carmenère wine quality. Lalvin ICV D21 ADY strain was inoculate according to the protocol recommended by the manufacturer (T0), and in parallel, it was propagate by the AYS and then used as inoculum (T1). Yeast strain predominance analyzed by restriction fragment length polymorphism (RFLP) technique indicates that nine (out of 9) yeast colonies obtained from a single sample of the ADY, show the same electrophoretic pattern when compared to the ADY. The results show limited significant differences for the fermentation speed and the yeast cell counting. The result of the physicochemical analysis of the musts and resulting wines showed no significant differences between treatments. A triangular test showed no significant sensory differences between wines
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6

Kurz, T., J. Mieleitner, T. Becker, and A. Delgado. "A Model Based Simulation of Brewing Yeast Propagation." Journal of the Institute of Brewing 108, no. 2 (2002): 248–55. http://dx.doi.org/10.1002/j.2050-0416.2002.tb00548.x.

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7

Malato, Laurent, Suzana Dos Reis, Laura Benkemoun, Raimon Sabaté, and Sven J. Saupe. "Role of Hsp104 in the Propagation and Inheritance of the [Het-s] Prion." Molecular Biology of the Cell 18, no. 12 (December 2007): 4803–12. http://dx.doi.org/10.1091/mbc.e07-07-0657.

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The chaperones of the ClpB/HSP100 family play a central role in thermotolerance in bacteria, plants, and fungi by ensuring solubilization of heat-induced protein aggregates. In addition in yeast, Hsp104 was found to be required for prion propagation. Herein, we analyze the role of Podospora anserina Hsp104 (PaHsp104) in the formation and propagation of the [Het-s] prion. We show that ΔPaHsp104 strains propagate [Het-s], making [Het-s] the first native fungal prion to be propagated in the absence of Hsp104. Nevertheless, we found that [Het-s]-propagon numbers, propagation rate, and spontaneous emergence are reduced in a ΔPaHsp104 background. In addition, inactivation of PaHsp104 leads to severe meiotic instability of [Het-s] and abolishes its meiotic drive activity. Finally, we show that ΔPaHSP104 strains are less susceptible than wild type to infection by exogenous recombinant HET-s(218–289) prion amyloids. Like [URE3] and [PIN+] in yeast but unlike [PSI+], [Het-s] is not cured by constitutive PaHsp104 overexpression. The observed effects of PaHsp104 inactivation are consistent with the described role of Hsp104 in prion aggregate shearing in yeast. However, Hsp104-dependency appears less stringent in P. anserina than in yeast; presumably because in Podospora prion propagation occurs in a syncitium.
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8

Crapeau, Myriam, Christelle Marchal, Christophe Cullin, and Laurent Maillet. "The Cellular Concentration of the Yeast Ure2p Prion Protein Affects Its Propagation as a Prion." Molecular Biology of the Cell 20, no. 8 (April 15, 2009): 2286–96. http://dx.doi.org/10.1091/mbc.e08-11-1097.

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The [URE3] yeast prion is a self-propagating inactive form of the Ure2p protein. We show here that Ure2p from the species Saccharomyces paradoxus (Ure2pSp) can be efficiently converted into a prion form and propagate [URE3] when expressed in Saccharomyces cerevisiae at physiological level. We found however that Ure2pSp overexpression prevents efficient prion propagation. We have compared the aggregation rate and propagon numbers of Ure2pSp and of S. cerevisiae Ure2p (Ure2pSc) in [URE3] cells both at different expression levels. Overexpression of both Ure2p orthologues accelerates formation of large aggregates but Ure2pSp aggregates faster than Ure2pSc. Although the yeast cells that contain these large Ure2p aggregates do not transmit [URE3] to daughter cells, the corresponding crude extract retains the ability to induce [URE3] in wild-type [ure3-0] cells. At low expression level, propagon numbers are higher with Ure2pSc than with Ure2pSp. Overexpression of Ure2p decreases the number of [URE3] propagons with Ure2pSc. Together, our results demonstrate that the concentration of a prion protein is a key factor for prion propagation. We propose a model to explain how prion protein overexpression can produce a detrimental effect on prion propagation and why Ure2pSp might be more sensitive to such effects than Ure2pSc.
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9

Nielsens, Olau. "Status of the yeast propagation process and some aspects of propagation for re-fermentation." Cerevisia 35, no. 3 (October 2010): 71–74. http://dx.doi.org/10.1016/j.cervis.2010.09.003.

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10

Guinan, Emma, and Gary Jones. "Influence of Hsp70 Chaperone Machinery on Yeast Prion Propagation." Protein & Peptide Letters 16, no. 6 (June 1, 2009): 582–86. http://dx.doi.org/10.2174/092986609788490168.

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11

Chang, H. Y., J. Y. Lin, H. C. Lee, H. L. Wang, and C. Y. King. "Strain-specific sequences required for yeast [PSI+] prion propagation." Proceedings of the National Academy of Sciences 105, no. 36 (August 29, 2008): 13345–50. http://dx.doi.org/10.1073/pnas.0802215105.

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12

Alexandrov, Ilya M., Aleksandra B. Vishnevskaya, Michael D. Ter-Avanesyan, and Vitaly V. Kushnirov. "Appearance and Propagation of Polyglutamine-based Amyloids in Yeast." Journal of Biological Chemistry 283, no. 22 (April 1, 2008): 15185–92. http://dx.doi.org/10.1074/jbc.m802071200.

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13

Wickner, Reed B. "Host control of yeast dsRNA virus propagation and expression." Trends in Microbiology 1, no. 8 (November 1993): 294–99. http://dx.doi.org/10.1016/0966-842x(93)90005-c.

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14

Hardianto, Anton Muhibuddin, and Antok Wahyu Sektiono. "Optimalisasi Fosfat untuk Meningkatkan Pertumbuhan Kerapatan Populasi dan Kemampuan Antagonis Saccharomyces cerevisiae terhadap Fusarium sp." SAINTEKBU 10, no. 2 (July 23, 2018): 27–41. http://dx.doi.org/10.32764/saintekbu.v10i2.206.

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Saccharomyces cerevisiae is a common yeast used as a fermenter in the home industry. This yeast is able to grow in media like waste materials. One of the waste materials that can be used as a medium of yeast growth is waste of coconut water. The use of coconut water as a medium of yeast propagation has been widely used in some types of yeasts. The intake of nutrients such as phosphate will make the yeast cells begin to grow and work faster. The yeast cell takes phosphate as ATP. Khamir will turn it into a phosphate polymerization form that is often found within the mitochondria of these cells. S. cerevisiae has the ability not only in terms of fermentation but also can perform other functions in the biological control process. The main methods of this study include the growth test of S. cerevisiae with the addition of a phosphate (KH2PO4), S. cerevisiae growth test by aerator method, yeast antagonist test. The results showed that S. cerevisiae was able to grow higher with the addition of phosphate nutrients (0.5% KH2PO4). This yeast has the potential to control Fusarium sp. The percentage of inhibition was isolate A0 (9,67%), A1 (11%), A2 (10,67%), A3 (12%), A4 (13%), and A5 (6%). Keywords: Yeast, phosphate nutrient, biological control, Fusarium sp.
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15

Minervini, Fabio, Anna Lattanzi, Maria De Angelis, Raffaella Di Cagno, and Marco Gobbetti. "Influence of Artisan Bakery- or Laboratory-Propagated Sourdoughs on the Diversity of Lactic Acid Bacterium and Yeast Microbiotas." Applied and Environmental Microbiology 78, no. 15 (May 25, 2012): 5328–40. http://dx.doi.org/10.1128/aem.00572-12.

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ABSTRACTSeven mature type I sourdoughs were comparatively back-slopped (80 days) at artisan bakery and laboratory levels under constant technology parameters. The cell density of presumptive lactic acid bacteria and related biochemical features were not affected by the environment of propagation. On the contrary, the number of yeasts markedly decreased from artisan bakery to laboratory propagation. During late laboratory propagation, denaturing gradient gel electrophoresis (DGGE) showed that the DNA band corresponding toSaccharomyces cerevisiaewas no longer detectable in several sourdoughs. Twelve species of lactic acid bacteria were variously identified through a culture-dependent approach. All sourdoughs harbored a certain number of species and strains, which were dominant throughout time and, in several cases, varied depending on the environment of propagation. As shown by statistical permutation analysis, the lactic acid bacterium populations differed among sourdoughs propagated at artisan bakery and laboratory levels.Lactobacillus plantarum,Lactobacillus sakei, andWeissella cibariadominated in only some sourdoughs back-slopped at artisan bakeries, andLeuconostoc citreumseemed to be more persistent under laboratory conditions. Strains ofLactobacillus sanfranciscensiswere indifferently found in some sourdoughs. Together with the other stable species and strains, other lactic acid bacteria temporarily contaminated the sourdoughs and largely differed between artisan bakery and laboratory levels. The environment of propagation has an undoubted influence on the composition of sourdough yeast and lactic acid bacterium microbiotas.
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16

Rogov, Anton G., Tatiana N. Goleva, Khoren K. Epremyan, Igor I. Kireev, and Renata A. Zvyagilskaya. "Propagation of Mitochondria-Derived Reactive Oxygen Species within the Dipodascus magnusii Cells." Antioxidants 10, no. 1 (January 15, 2021): 120. http://dx.doi.org/10.3390/antiox10010120.

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Mitochondria are considered to be the main source of reactive oxygen species (ROS) in the cell. It was shown that in cardiac myocytes exposed to excessive oxidative stress, ROS-induced ROS release is triggered. However, cardiac myocytes have a network of densely packed organelles that do not move, which is not typical for the majority of eukaryotic cells. The purpose of this study was to trace the spatiotemporal development (propagation) of prooxidant-induced oxidative stress and its interplay with mitochondrial dynamics. We used Dipodascus magnusii yeast cells as a model, as they have advantages over other models, including a uniquely large size, mitochondria that are easy to visualize and freely moving, an ability to vigorously grow on well-defined low-cost substrates, and high responsibility. It was shown that prooxidant-induced oxidative stress was initiated in mitochondria, far preceding the appearance of generalized oxidative stress in the whole cell. For yeasts, these findings were obtained for the first time. Preincubation of yeast cells with SkQ1, a mitochondria-addressed antioxidant, substantially diminished production of mitochondrial ROS, while only slightly alleviating the generalized oxidative stress. This was expected, but had not yet been shown. Importantly, mitochondrial fragmentation was found to be primarily induced by mitochondrial ROS preceding the generalized oxidative stress development.
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17

Hazuchová, Miroslava, Daniela Chmelová, and Miroslav Ondrejovič. "The optimization of propagation medium for the increase of laccase production by the white-rot fungus Pleurotus ostreatus." Nova Biotechnologica et Chimica 16, no. 2 (December 1, 2017): 113–23. http://dx.doi.org/10.1515/nbec-2017-0016.

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Abstract The lignocellulolytic enzymes are routinely produced by submerged fermentation using lignocellulosic material, but for more effective production, it would be suitable to precede the production phase on the lignocellulose by propagation phase in the nutrition medium suitable for growth of the fungi. Therefore, the aim of this study was to increase the laccase production by the white-rot fungus Pleurotus ostreatus by two-step cultivation strategy. In the first step, propagation medium was optimized for the maximal biomass growth, the second step included the laccase production by produced fungal biomass in media with the selected lignocellulosic material (pine sawdust, alfalfa steam and corn straw). From our experiments, parameters such as glucose concentration, yeast extract concentration and pH of propagation medium were selected as key factors affecting growth of P. ostreatus. The optimal conditions of propagation medium for maximal fungal growth determined by response surface methodology were: glucose concentration 102.68 g/L, yeast extract concentration 43.65 g/L and pH of propagation medium 7.24. These values were experimentally verified and used statistical model of biomass production prediction was appropriate adjusted. Thus prepared fungal biomass produced in the media with lignocellulose approximately 9-16 times higher concentrations of the laccase in 3 times shorter time than the fungal biomass without propagation phase in optimized propagation medium.
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18

Masison, Daniel C., P. Aaron Kirkland, and Deepak Sharma. "Influence of Hsp70s and their regulators on yeast prion propagation." Prion 3, no. 2 (April 2009): 65–73. http://dx.doi.org/10.4161/pri.3.2.9134.

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19

Inoue, Yuji. "Life Cycle of Yeast Prions: Propagation Mediated by Amyloid Fibrils." Protein & Peptide Letters 16, no. 3 (March 1, 2009): 271–76. http://dx.doi.org/10.2174/092986609787601796.

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20

Loovers, Harriët M., Emma Guinan, and Gary W. Jones. "Importance of the Hsp70 ATPase Domain in Yeast Prion Propagation." Genetics 175, no. 2 (December 6, 2006): 621–30. http://dx.doi.org/10.1534/genetics.106.066019.

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21

Wegrzyn, Renee D., Kavita Bapat, Gary P. Newnam, Amy D. Zink, and Yury O. Chernoff. "Mechanism of Prion Loss after Hsp104 Inactivation in Yeast." Molecular and Cellular Biology 21, no. 14 (July 15, 2001): 4656–69. http://dx.doi.org/10.1128/mcb.21.14.4656-4669.2001.

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ABSTRACT In vivo propagation of [PSI +], an aggregation-prone prion isoform of the yeast release factor Sup35 (eRF3), has previously been shown to require intermediate levels of the chaperone protein Hsp104. Here we perform a detailed study on the mechanism of prion loss after Hsp104 inactivation. Complete or partial inactivation of Hsp104 was achieved by the following approaches: deleting the HSP104 gene; modifying theHSP104 promoter that results in low level of its expression; and overexpressing the dominant-negative ATPase-inactive mutant HSP104 allele. In contrast to guanidine-HCl, an agent blocking prion proliferation, Hsp104 inactivation induced relatively rapid loss of [PSI +] and another candidate yeast prion, [PIN +]. Thus, the previously hypothesized mechanism of prion dilution in cell divisions due to the blocking of prion proliferation is not sufficient to explain the effect of Hsp104 inactivation. The [PSI +] response to increased levels of another chaperone, Hsp70-Ssa, depends on whether the Hsp104 activity is increased or decreased. A decrease of Hsp104 levels or activity is accompanied by a decrease in the number of Sup35PSI+aggregates and an increase in their size. This eventually leads to accumulation of huge agglomerates, apparently possessing reduced prion forming capability and representing dead ends of the prion replication cycle. Thus, our data confirm that the primary function of Hsp104 in prion propagation is to disassemble prion aggregates and generate the small prion seeds that initiate new rounds of prion propagation (possibly assisted by Hsp70-Ssa).
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22

Reidy, Michael, Ruchika Sharma, and Daniel C. Masison. "Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation." Eukaryotic Cell 12, no. 5 (March 15, 2013): 739–45. http://dx.doi.org/10.1128/ec.00301-12.

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ABSTRACT Hsp100 chaperones protect microorganisms and plants from environmental stress by cooperating with Hsp70 and its nucleotide exchange factor (NEF) and Hsp40 cochaperones to resolubilize proteins from aggregates. The Saccharomyces cerevisiae Hsp104 (Sc-Hsp104)-based disaggregation machinery also is essential for replication of amyloid-based prions. Escherichia coli ClpB can substitute for Hsp104 to propagate [ PSI + ] prions in yeast, but only if E. coli DnaK and GrpE (Hsp70 and NEF) are coexpressed. Here, we tested if the reported inability of Schizosaccharomyces pombe Hsp104 (Sp-Hsp104) to support [ PSI + ] propagation was due to similar species-specific chaperone requirements and find that Sp-Hsp104 alone supported propagation of three different yeast prions. Sp-Hsp70 and Sp-Fes1p (NEF) likewise functioned in place of their Sa. cerevisiae counterparts. Thus, chaperones of these long-diverged species possess conserved activities that function in processes essential for both cell growth and prion propagation, suggesting Sc. pombe can propagate its own prions. We show that curing by Hsp104 overexpression and inactivation can be distinguished and confirm the observation that, unlike Sc-Hsp104, Sp-Hsp104 cannot cure yeast of [ PSI + ] when it is overexpressed. These results are consistent with a view that mechanisms underlying prion replication and elimination are distinct.
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23

Michel, Maximilian, Tim Meier-Dörnberg, Anna Kleucker, Fritz Jacob, and Mathias Hutzler. "A New Approach for Detecting Spoilage Yeast in Pure Bottom-Fermenting and Pure Torulaspora Delbrueckii Pitching Yeast, Propagation Yeast, and Finished Beer." Journal of the American Society of Brewing Chemists 74, no. 3 (June 2016): 200–205. http://dx.doi.org/10.1094/asbcj-2016-3148-01.

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24

Methner, Yvonne, Mathias Hutzler, Dagmar Matoulková, Fritz Jacob, and Maximilian Michel. "Screening for the Brewing Ability of Different Non-Saccharomyces Yeasts." Fermentation 5, no. 4 (December 12, 2019): 101. http://dx.doi.org/10.3390/fermentation5040101.

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Non-Saccharomyces yeasts have aroused interest in brewing science as an innovative and seminal way of creating new beer flavors. A screening system for potential brewing strains of non-Saccharomyces yeasts was set up to investigate the yeast’s utilization of wort sugars and to examine the effect of hop acids as well as ethanol on the growth of different yeast strains. Additionally, phenolic off-flavor (POF) and sensory odor tests of fermented wort samples were performed. The promising strains were further investigated for their propagation ability and for following fermentation trials. The produced beers were analyzed for secondary metabolites, ethanol content and judged by trained panelists. Subsequently to the screening, it was discovered that among the 110 screened yeast strains, approx. 10 strains of the species Saccharomycopsis fibuligera, Schizosaccharomyces pombe and Zygosaccharomyces rouxii generate promising fruity flavors during fermentation and were able to metabolize maltose and maltotriose as a prerequisite for the production of alcoholic beers. Consequently, the screening method described in this study makes it possible to investigate a tremendous number of different non-Saccharomyces yeasts and to test their brewing ability in a relatively short period of time.
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Cox, Brian, Frederique Ness, and Mick Tuite. "Analysis of the Generation and Segregation of Propagons: Entities That Propagate the [PSI+] Prion in Yeast." Genetics 165, no. 1 (September 1, 2003): 23–33. http://dx.doi.org/10.1093/genetics/165.1.23.

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Abstract The propagation of the prion form of the yeast Sup35p protein, the so-called [PSI+] determinant, involves the generation and partition of a small number of particulate determinants that we propose calling “propagons.” The numbers of propagons in [PSI+] cells can be inferred from the kinetics of elimination of [PSI+] during growth in the presence of a low concentration of guanidine hydrochloride (GdnHCl). Using this and an alternative method of counting the numbers of propagons, we demonstrate considerable clonal variation in the apparent numbers of propagons between different [PSI+] yeast strains, between different cultures of the same [PSI+] yeast strain, and between different cells of the same [PSI+] culture. We provide further evidence that propagon generation is blocked by growth in GdnHCl and that it is largely confined to the S phase of the cell cycle. In addition, we show that at low propagon number there is a bias toward retention of propagons in mother cells and that production of new propagons is very rapid when cells with depleted numbers of propagons are rescued into normal growth medium. The implications of our findings with respect to yeast prion propagation mechanisms are discussed.
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Kouprina, Natalay, Nana Nikolaishvili, Joan Graves, Maxim Koriabine, Michael A. Resnick, and Vladimir Larionov. "Integrity of Human YACs during Propagation in Recombination-Deficient Yeast Strains." Genomics 56, no. 3 (March 1999): 262–73. http://dx.doi.org/10.1006/geno.1998.5727.

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Gómez-Pastor, Rocío, Roberto Pérez-Torrado, Elisa Cabiscol, and Emilia Matallana. "Transcriptomic and proteomic insights of the wine yeast biomass propagation process." FEMS Yeast Research 10, no. 7 (August 25, 2010): 870–84. http://dx.doi.org/10.1111/j.1567-1364.2010.00667.x.

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Ohtake, Y., and R. B. Wickner. "Yeast virus propagation depends critically on free 60S ribosomal subunit concentration." Molecular and Cellular Biology 15, no. 5 (May 1995): 2772–81. http://dx.doi.org/10.1128/mcb.15.5.2772.

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Over 30 MAK (maintenance of killer) genes are necessary for propagation of the killer toxin-encoding M1 satellite double-stranded RNA of the L-A virus. Sequence analysis revealed that MAK7 is RPL4A, one of the two genes encoding ribosomal protein L4 of the 60S subunit. We further found that mutants with mutations in 18 MAK genes (including mak1 [top1], mak7 [rpl4A], mak8 [rpl3], mak11, and mak16) had decreased free 60S subunits. Mutants with another three mak mutations had half-mer polysomes, indicative of poor association of 60S and 40S subunits. The rest of the mak mutants, including the mak3 (N-acetyltransferase) mutant, showed a normal profile. The free 60S subunits, L-A copy number, and the amount of L-A coat protein in the mak1, mak7, mak11, and mak16 mutants were raised to the normal level by the respective normal single-copy gene. Our data suggest that most mak mutations affect M1 propagation by their effects on the supply of proteins from the L-A virus and that the translation of the non-poly(A) L-A mRNA depends critically on the amount of free 60S ribosomal subunits, probably because 60S association with the 40S subunit waiting at the initiator AUG is facilitated by the 3' poly(A).
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Zhang, Kun, Polly Wells, Yi Liang, John Love, David A. Parker, and Carolina Botella. "Effect of diluted hydrolysate as yeast propagation medium on ethanol production." Bioresource Technology 271 (January 2019): 1–8. http://dx.doi.org/10.1016/j.biortech.2018.09.080.

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30

Speransky, Vladislav V., Kimberly L. Taylor, Herman K. Edskes, Reed B. Wickner, and Alasdair C. Steven. "[URE3] Prion forms Filamentous Networks in Yeast Cytoplasm." Microscopy and Microanalysis 7, S2 (August 2001): 52–53. http://dx.doi.org/10.1017/s1431927600026337.

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The concept of prion (infectious protein) originated in studies of transmissible spongioform encephalopathies (TSE) in mammals, but more recently, two nonchromosomal genes of yeast- [PSI] and [URE3] - were identified as prions. While the agents of TSEs kill infected cells and [URE3] or [PSI+] only slow growth at most, these infections are believed to have similar mechanisms, i.e. self-propagating amyloids. TSEs are often associated with amyloid deposition in infected tissues, and both Sup35p and Ure2p have been shown to form amyloid in vitro.[URE3] is a prion of the Ure2 protein, that normally regulates nitrogen catabolism. Its ‘prion’ domain (residues 1-65) is necessary and sufficient for propagation of the prion, whereas the C-terminal portion (residues 81-354) is sufficient to carry out the nitrogen regulation function. The prion domain peptide spontaneously forms amyloid filaments in vitro. Full-length native Ure2p is a stable soluble dimer, but forms co-filaments when the prion domain peptide is added. This in vitro amyloid formation is highly specific and self-propagating, thus providing a possible explanation for the [URE3] prion. We have sought to clarify this hypothesis by examining the state of Ure2p in [URE3] cells by thin-section electron microscopy.Yeast cells with the [URE3] prion and control [ure-o] cells were thin-sectioned after fixation and embedding in an epoxy resin. We found distinctive filamentous aggregates in the cytoplasm of [URE3] cells of a strain that overexpresses Ure2p (Fig. 1). These aggregates were seen in some cell profiles represented in 50-70 nm sections, and were never seen in control sections of [ure-o] cells. in cell sections showing these structures, there was typically one such aggregate, which could be quite large - up to several μm across - and approximately globular in outline. They contain irregularly associated filaments about 25 nm in diameter.
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Mathur, Vidhu, Vibha Taneja, Yidi Sun, and Susan W. Liebman. "Analyzing the Birth and Propagation of Two Distinct Prions, [PSI+] and [Het-s]y, in Yeast." Molecular Biology of the Cell 21, no. 9 (May 2010): 1449–61. http://dx.doi.org/10.1091/mbc.e09-11-0927.

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Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin protein (with expanded polyQ), depend on a Gln or Asn (QN)-rich region for amyloid formation. Other prions, e.g., mammalian PrP and the [Het-s] prion of Podospora anserina, although still able to form infectious amyloid aggregates, do not have QN-rich regions. Furthermore, [Het-s] and yeast prions appear to differ dramatically in their amyloid conformation. Despite these differences, a fusion of the Het-s prion domain to GFP (Het-sPrD-GFP) can propagate in yeast as a prion called [Het-s]y. We analyzed the properties of two divergent prions in yeast: [Het-s]y and the native yeast prion [PSI+] (prion form of translational termination factor Sup35). Curiously, the induced appearance and transmission of [PSI+] and [Het-s]y aggregates is remarkably similar. Overexpression of tagged prion protein (Sup35-GFP or Het-sPrD-GFP) in nonprion cells gives rise to peripheral, and later internal, ring/mesh-like aggregates. The cells with these ring-like aggregates give rise to daughters with one (perivacuolar) or two (perivacuolar and juxtanuclear) dot-like aggregates per cell. These line, ring, mesh, and dot aggregates are not really the transmissible prion species and should only be regarded as phenotypic markers of the presence of the prions. Both [PSI+] and [Het-s]y first appear in daughters as numerous tiny dot-like aggregates, and both require the endocytic protein, Sla2, for ring formation, but not propagation.
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Killian, Andrea N., Sarah C. Miller, and Justin K. Hines. "Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast." Viruses 11, no. 4 (April 16, 2019): 349. http://dx.doi.org/10.3390/v11040349.

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Yeast prions are protein-based genetic elements found in the baker’s yeast Saccharomyces cerevisiae, most of which are amyloid aggregates that propagate by fragmentation and spreading of small, self-templating pieces called propagons. Fragmentation is carried out by molecular chaperones, specifically Hsp104, Hsp70, and Hsp40. Like other amyloid-forming proteins, amyloid-based yeast prions exhibit structural polymorphisms, termed “strains” in mammalian systems and “variants” in yeast, which demonstrate diverse phenotypes and chaperone requirements for propagation. Here, the known differential interactions between chaperone proteins and yeast prion variants are reviewed, specifically those of the yeast prions [PSI+], [RNQ+]/[PIN+], and [URE3]. For these prions, differences in variant-chaperone interactions (where known) with Hsp104, Hsp70s, Hsp40s, Sse1, and Hsp90 are summarized, as well as some interactions with chaperones of other species expressed in yeast. As amyloid structural differences greatly impact chaperone interactions, understanding and accounting for these variations may be crucial to the study of chaperones and both prion and non-prion amyloids.
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Pérez-Torrado, Roberto, Jose M. Bruno-Bárcena, and Emilia Matallana. "Monitoring Stress-Related Genes during the Process of Biomass Propagation of Saccharomyces cerevisiae Strains Used for Wine Making." Applied and Environmental Microbiology 71, no. 11 (November 2005): 6831–37. http://dx.doi.org/10.1128/aem.71.11.6831-6837.2005.

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ABSTRACT Physiological capabilities and fermentation performance of Saccharomyces cerevisiae strains to be employed during industrial wine fermentations are critical for the quality of the final product. During the process of biomass propagation, yeast cells are dynamically exposed to a mixed and interrelated group of known stresses such as osmotic, oxidative, thermic, and/or starvation. These stressing conditions can dramatically affect the parameters of the fermentation process and the technological abilities of the yeast, e.g., the biomass yield and its fermentative capacity. Although a good knowledge exists of the behavior of S. cerevisiae under laboratory conditions, insufficient knowledge is available about yeast stress responses under the specific media and growth conditions during industrial processes. We performed growth experiments using bench-top fermentors and employed a molecular marker approach (changes in expression levels of five stress-related genes) to investigate how the cells respond to environmental changes during the process of yeast biomass production. The data show that in addition to the general stress response pathway, using the HSP12 gene as a marker, other specific stress response pathways were induced, as indicated by the changes detected in the mRNA levels of two stress-related genes, GPD1 and TRX2. These results suggest that the cells were affected by osmotic and oxidative stresses, demonstrating that these are the major causes of the stress response throughout the process of wine yeast biomass production.
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34

Marchante, Ricardo, Michelle Rowe, Jo Zenthon, Mark J. Howard, and Mick F. Tuite. "Structural Definition Is Important for the Propagation of the Yeast [PSI+] Prion." Molecular Cell 50, no. 5 (June 2013): 675–85. http://dx.doi.org/10.1016/j.molcel.2013.05.010.

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35

Sporn, Zachary A., and Justin K. Hines. "Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity." Prion 9, no. 2 (March 4, 2015): 80–89. http://dx.doi.org/10.1080/19336896.2015.1020268.

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36

Verges, Katherine J., Melanie H. Smith, Brandon H. Toyama, and Jonathan S. Weissman. "Strain conformation, primary structure and the propagation of the yeast prion [PSI+]." Nature Structural & Molecular Biology 18, no. 4 (March 20, 2011): 493–99. http://dx.doi.org/10.1038/nsmb.2030.

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37

Trubitsina, Nina P., Olga M. Zemlyanko, Stanislav A. Bondarev, and Galina A. Zhouravleva. "Nonsense Mutations in the Yeast SUP35 Gene Affect the [PSI+] Prion Propagation." International Journal of Molecular Sciences 21, no. 5 (February 28, 2020): 1648. http://dx.doi.org/10.3390/ijms21051648.

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The essential SUP35 gene encodes yeast translation termination factor eRF3. Previously, we isolated nonsense mutations sup35-n and proposed that the viability of such mutants can be explained by readthrough of the premature stop codon. Such mutations, as well as the prion [PSI+], can appear in natural yeast populations, and their combinations may have different effects on the cells. Here, we analyze the effects of the compatibility of sup35-n mutations with the [PSI+] prion in haploid and diploid cells. We demonstrated that sup35-n mutations are incompatible with the [PSI+] prion, leading to lethality of sup35-n [PSI+] haploid cells. In diploid cells the compatibility of [PSI+] with sup35-n depends on how the corresponding diploid was obtained. Nonsense mutations sup35-21, sup35-74, and sup35-218 are compatible with the [PSI+] prion in diploid strains, but affect [PSI+] properties and lead to the formation of new prion variant. The only mutation that could replace the SUP35 wild-type allele in both haploid and diploid [PSI+] strains, sup35-240, led to the prion loss. Possibly, short Sup351–55 protein, produced from the sup35-240 allele, is included in Sup35 aggregates and destabilize them. Alternatively, single molecules of Sup351–55 can stick to aggregate ends, and thus interrupt the fibril growth. Thus, we can conclude that sup35-240 mutation prevents [PSI+] propagation and can be considered as a new pnm mutation.
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38

Paushkin, S. V. "In Vitro Propagation of the Prion-Like State of Yeast Sup35 Protein." Science 277, no. 5324 (July 18, 1997): 381–83. http://dx.doi.org/10.1126/science.277.5324.381.

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39

Jearnpipatkul, Amornrat, Rungjarat Hutacharoen, Hiroyuki Araki, and Yasuji Oshima. "A cis-acting locus for the stable propagation of yeast plasmid pSR1." Molecular and General Genetics MGG 207, no. 2-3 (May 1987): 355–60. http://dx.doi.org/10.1007/bf00331601.

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40

Lian, Hui-Yong, Kang-Wei Lin, Chuanjun Yang, and Peng Cai. "Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field." Cell Stress and Chaperones 23, no. 4 (December 6, 2017): 581–94. http://dx.doi.org/10.1007/s12192-017-0867-9.

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41

Le Vu Lan, Phuong, Sua Huynh Thi, and An Le Tri. "Establishment of a spontaneously started sourdough in Vietnam." Can Tho University Journal of Science 13, no. 1 (May 4, 2021): 12–16. http://dx.doi.org/10.22144/ctu.jen.2021.002.

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The use of sourdoughs in bread baking in Vietnam has recently been increased but little is known about microorganisms in those sourdoughs. This study was to assess changes in pH value and microbial density of a sourdough from bread flour (BF) and a sourdough from all-purpose flour (AF) during propagation. The results showed that the type of flour did not cause a significant difference in pH changes, but it could contribute to the distinct levels of lactic acid bacteria (LAB) and yeast in the two sourdoughs. The BF sourdough gained proper maturation in 15 days when it reached pH of 3.69, 1.3 x 109 CFU g-1 LAB and 7.4 x 108 CFU g-1 yeast. Meanwhile, the AF sourdough had lower levels of LAB and yeast (3.9 x 108 CFU g-1 and 1.0 x 108 CFU g-1, respectively). Sequencing analysis revealed the presence of Lactobacillus plantarum in the BF sourdough on the 10th and 15th days of the propagation process. Wickerhamomyces anomalus was found on the 10th day while Saccharomyces cerevisiae was detected on the 15th day. This sourdough can be used in further studies to assess the benefits of sourdough in bread baking.
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42

Alenkina, T. V., O. S. Zinina, M. V. Antonycheva, N. I. Vakhrushina, and A. K. Nikiforov. "Optimization of Reproduction Stage in Technology of Production of Plague Diagnostic Bacteriophage L-413C." Problems of Particularly Dangerous Infections, no. 2(108) (April 20, 2011): 79–82. http://dx.doi.org/10.21055/0370-1069-2011-2(108)-79-82.

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New nutrient media based on baker yeast autolizate were used for the first time for manufacturing of diagnostic preparation of plague bacteriophage L-413C. Experimental media provide high concentration of phage particles at the stage of propagation, and good survivability in lyophilization. Media in which yeast autolizate was a nutrient protein basis appeared to be more effective than those in which it was a stimulating additive. Phage preparations preserved stability of properties during storage at 4-8 °С, and at a higher temperature in the test of accelerated aging. Introduction of yeast nutrient media in technology of plague diagnostic bacteriophage L-413C manufacturing opens good prospects for increasing of production efficiency and decreasing of cost value of the preparation
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43

Li, Yiyong, Wanyi Luo, Baoe Wang, Tianhao Lin, Chuangxiong Li, Hui Liu, Yanhua Huang, Chong Lin, Yinglin Tong, and Zexiang Lei. "Effects of Probiotic Fermented Kitchen Waste on the Growth and Propagation of Rotifer Brachionus calyciflorus." Journal of Biobased Materials and Bioenergy 15, no. 1 (February 1, 2021): 83–89. http://dx.doi.org/10.1166/jbmb.2021.2024.

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Kitchen waste containing a large number of nutrients such as carbohydrates, proteins, lipids, and minerals can be used as fermentation substrates for producing probiotics, and then can be taken as microbial feed to cultivate rotifer. This approach not only emphasizes resource utilization of kitchen waste but also improves the growth and propagation of rotifer. In this study, kitchen wastewater and solid waste were used as fermentation substrates, respectively, while yeast, lactic acid bacteria, compound bacteria (yeast + lactic acid bacteria), and effective microorganisms (EM) bacteria were inoculated to harvest the microbial feed for the cultivation of rotifer. The population density, eggholding rate, body length, and the egg volume of rotifer were determined. These results indicate that the growth and propagation of rotifer were effectively improved by using kitchen wastewater or solid waste as fermentation substrates. When compared with the direct usage of kitchen waste for rotifer cultivation, the effect of kitchen waste fermented by probiotics on rotifer was more obvious, such as in the population density, egg-holding rate, body length, and egg volume, in the following sequence EM bacterial group > yeast group > compound bacterial group > lactic acid bacterial group ^ control group. Hence, EM bacteria can be considered as the best one for kitchen waste fermentation to prepare microbial feed for rotifer. It is thus feasible to use probiotic fermented kitchen waste to cultivate rotifer.
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44

Moriyama, Hiromitsu, Herman K. Edskes, and Reed B. Wickner. "[URE3] Prion Propagation in Saccharomyces cerevisiae: Requirement for Chaperone Hsp104 and Curing by Overexpressed Chaperone Ydj1p." Molecular and Cellular Biology 20, no. 23 (December 1, 2000): 8916–22. http://dx.doi.org/10.1128/mcb.20.23.8916-8922.2000.

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ABSTRACT The [URE3] nonchromosomal genetic element is an infectious form (prion) of the Ure2 protein, apparently a self-propagating amyloidosis. We find that an insertion mutation or deletion of HSP104results in inability to propagate the [URE3] prion. Our results indicate that Hsp104 is a common factor in the maintenance of two independent yeast prions. However, overproduction of Hsp104 does not affect the stability of [URE3], in contrast to what is found for the [PSI+] prion, which is known to be cured by either overproduction or deficiency of Hsp104. Like Hsp104, the Hsp40 class chaperone Ydj1p, with the Hsp70 class Ssa1p, can renature proteins. We find that overproduction of Ydj1p results in a gradual complete loss of [URE3]. The involvement of protein chaperones in the propagation of [URE3] indicates a role for protein conformation in inheritance.
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45

Liang, Delin, Stewart M. Gray, Igor Kaplan, and Peter Palukaitis. "Site-Directed Mutagenesis and Generation of Chimeric Viruses by Homologous Recombination in Yeast to Facilitate Analysis of Plant-Virus Interactions." Molecular Plant-Microbe Interactions® 17, no. 6 (June 2004): 571–76. http://dx.doi.org/10.1094/mpmi.2004.17.6.571.

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A yeast homologous recombination system was used to generate mutants and chimeras in the genome of Potato leafroll virus (PLRV). A yeast-bacteria shuttle vector was developed that allows mutants and chimeras generated in yeast to be transformed into Escherichia coli for confirmation of the mutations and transformed into Agrobacterium tumefaciens to facilitate agroinfection of plants by the mutant PLRV genomes. The advantages of the system include the high frequency of recovered mutants generated by yeast homologous recombination, the ability to generate over 20 mutants and chimeras using only two restriction endonuclease sites, the ability to introduce multiple additional sequences using three and four DNA fragments, and the mobilization of the same plasmid from yeast to E. coli, A. tumefaciens, and plants. The wild-type PLRV genome showed no loss of virulence after sequential propagation in yeast, E. coli, and A. tumefaciens. Moreover, many PLRV clones with mutations generated in the capsid protein and readthrough domain of the capsid protein replicated and moved throughout plants. This approach will facilitate the analysis of plant-virus interactions of in vivo-generated mutants for many plant viruses, especially those not transmissible mechanically to plants.
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46

Sulatskaya, Anna I., Stanislav A. Bondarev, Maksim I. Sulatsky, Nina P. Trubitsina, Mikhail V. Belousov, Galina A. Zhouravleva, Manuel A. Llanos, Andrey V. Kajava, Irina M. Kuznetsova, and Konstantin K. Turoverov. "Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils." Journal of Molecular Liquids 314 (September 2020): 113618. http://dx.doi.org/10.1016/j.molliq.2020.113618.

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47

Dulle, Jennifer E., Kevin C. Stein, and Heather L. True. "Regulation of the Hsp104 Middle Domain Activity Is Critical for Yeast Prion Propagation." PLoS ONE 9, no. 1 (January 23, 2014): e87521. http://dx.doi.org/10.1371/journal.pone.0087521.

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48

Masison, D. C., M. L. Maddelein, and R. B. Wickner. "The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation." Proceedings of the National Academy of Sciences 94, no. 23 (November 11, 1997): 12503–8. http://dx.doi.org/10.1073/pnas.94.23.12503.

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49

Novak, J., G. Basarova, J. A. Teixeira, and A. A. Vicente. "Monitoring of Brewing Yeast Propagation Under Aerobic and Anaerobic Conditions Employing Flow Cytometry." Journal of the Institute of Brewing 113, no. 3 (2007): 249–55. http://dx.doi.org/10.1002/j.2050-0416.2007.tb00284.x.

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50

Higurashi, T., J. K. Hines, C. Sahi, R. Aron, and E. A. Craig. "Specificity of the J-protein Sis1 in the propagation of 3 yeast prions." Proceedings of the National Academy of Sciences 105, no. 43 (October 27, 2008): 16596–601. http://dx.doi.org/10.1073/pnas.0808934105.

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