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Journal articles on the topic 'Fission yeast'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Acs-Szabo, Lajos, Laszlo Attila Papp, and Ida Miklos. "Understanding the molecular mechanisms of human diseases: the benefits of fission yeasts." Microbial Cell 11 (August 2, 2024): 288–311. http://dx.doi.org/10.15698/mic2024.08.833.

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Abstract The role of model organisms such as yeasts in life science research is crucial. Although the baker’s yeast (Saccharomyces cerevisiae) is the most popular model among yeasts, the contribution of the fission yeasts (Schizosaccharomyces) to life science is also indisputable. Since both types of yeasts share several thousands of common orthologous genes with humans, they provide a simple research platform to investigate many fundamental molecular mechanisms and functions, thereby contributing to the understanding of the background of human diseases. In this review, we would like to highli

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2

Vicente-Soler, Jero, Teresa Soto, Alejandro Franco, José Cansado, and Marisa Madrid. "The Multiple Functions of Rho GTPases in Fission Yeasts." Cells 10, no. 6 (2021): 1422. http://dx.doi.org/10.3390/cells10061422.

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The Rho family of GTPases represents highly conserved molecular switches involved in a plethora of physiological processes. Fission yeast Schizosaccharomyces pombe has become a fundamental model organism to study the functions of Rho GTPases over the past few decades. In recent years, another fission yeast species, Schizosaccharomyces japonicus, has come into focus offering insight into evolutionary changes within the genus. Both fission yeasts contain only six Rho-type GTPases that are spatiotemporally controlled by multiple guanine–nucleotide exchange factors (GEFs) and GTPase-activating pro

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3

Cortés, Juan C. G., Mariona Ramos, Masako Osumi, Pilar Pérez, and Juan Carlos Ribas. "Fission yeast septation." Communicative & Integrative Biology 9, no. 4 (2016): e1189045. http://dx.doi.org/10.1080/19420889.2016.1189045.

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4

Murray, Andrew W. "Sunburnt fission yeast." Nature 363, no. 6427 (1993): 302. http://dx.doi.org/10.1038/363302a0.

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5

Xu, Dan-Dan, and Li-Lin Du. "Fission Yeast Autophagy Machinery." Cells 11, no. 7 (2022): 1086. http://dx.doi.org/10.3390/cells11071086.

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Autophagy is a conserved process that delivers cytoplasmic components to the vacuole/lysosome. It plays important roles in maintaining cellular homeostasis and conferring stress resistance. In the fission yeast Schizosaccharomyces pombe, autophagy is important for cell survival under nutrient depletion and ER stress conditions. Experimental analyses of fission yeast autophagy machinery in the last 10 years have unveiled both similarities and differences in autophagosome biogenesis mechanisms between fission yeast and other model eukaryotes for autophagy research, in particular, the budding yea

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Johnson, Byron F., L. C. Sowden, Teena Walker, Bong Y. Yoo, and Gode B. Calleja. "Use of electron microscopy to characterize the surfaces of flocculent and nonflocculent yeast cells." Canadian Journal of Microbiology 35, no. 12 (1989): 1081–86. http://dx.doi.org/10.1139/m89-181.

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The surfaces of flocculent and nonflocculent yeast cells have been examined by electron microscopy. Nonextractive preparative procedures for scanning electron microscopy allow comparison in which sharp or softened images of surface details (scars, etc.) are the criteria for relative abundance of flocculum material. Asexually flocculent budding-yeast cells cannot be distinguished from nonflocculent budding-yeast cells in scanning electron micrographs because the scar details of both are well resolved, being hard and sharp. On the other hand, flocculent fission-yeast cells are readily distinguis

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7

Emami, Parvaneh, and Masaru Ueno. "3,3’-Diindolylmethane induces apoptosis and autophagy in fission yeast." PLOS ONE 16, no. 12 (2021): e0255758. http://dx.doi.org/10.1371/journal.pone.0255758.

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3,3’-Diindolylmethane (DIM) is a compound derived from the digestion of indole-3-carbinol, found in the broccoli family. It induces apoptosis and autophagy in some types of human cancer. DIM extends lifespan in the fission yeast Schizosaccharomyces pombe. The mechanisms by which DIM induces apoptosis and autophagy in humans and expands lifespan in fission yeasts are not fully understood. Here, we show that DIM induces apoptosis and autophagy in log-phase cells, which is dose-dependent in fission yeast. A high concentration of DIM disrupted the nuclear envelope (NE) structure and induced chromo

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8

TANG, Zhaohua, Norbert F. KÄUFER, and Ren-Jang LIN. "Interactions between two fission yeast serine/arginine-rich proteins and their modulation by phosphorylation." Biochemical Journal 368, no. 2 (2002): 527–34. http://dx.doi.org/10.1042/bj20021133.

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The unexpected low number of genes in the human genome has triggered increasing attention to alternative pre-mRNA splicing, and serine/arginine-rich (SR) proteins have been correlated with the complex alternative splicing that is a characteristic of metazoans. SR proteins interact with RNA and splicing protein factors, and they also undergo reversible phosphorylation, thereby regulating constitutive and alternative splicing in mammals and Drosophila. However, it is not clear whether the features of SR proteins and alternative splicing are present in simple and genetically tractable organisms,

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9

Chang, Fred, and Paul Nurse. "How Fission Yeast Fission in the Middle." Cell 84, no. 2 (1996): 191–94. http://dx.doi.org/10.1016/s0092-8674(00)80973-3.

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10

Lim, Hye-Won, Su-Jung Kim, Eun-Hee Park, and Chang-Jin Lim. "Overexpression of a metacaspase gene stimulates cell growth and stress response inSchizosaccharomyces pombe." Canadian Journal of Microbiology 53, no. 8 (2007): 1016–23. http://dx.doi.org/10.1139/w07-067.

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A unique gene named pca1+, encoding a metacaspase, was cloned from the fission yeast Schizosaccharomyces pombe and was used to create a recombinant plasmid, pPMC. The metacaspase mRNA level was markedly elevated in the fission yeast cells harboring the plasmid pPMC. Overexpressed Pca1+appeared to stimulate the growth of the fission yeast cells instead of arresting their growth. Its expression was enhanced by stress-inducing agents such as H2O2, sodium nitroprusside, and CdCl2, and it conferred cytoprotection, especially against CdCl2. However, such protection was not reproducible in the buddin

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11

MacKenzie, Anne M., and Soni Lacefield. "CDK Regulation of Meiosis: Lessons from S. cerevisiae and S. pombe." Genes 11, no. 7 (2020): 723. http://dx.doi.org/10.3390/genes11070723.

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Meiotic progression requires precise orchestration, such that one round of DNA replication is followed by two meiotic divisions. The order and timing of meiotic events is controlled through the modulation of the phosphorylation state of proteins. Key components of this phospho-regulatory system include cyclin-dependent kinase (CDK) and its cyclin regulatory subunits. Over the past two decades, studies in budding and fission yeast have greatly informed our understanding of the role of CDK in meiotic regulation. In this review, we provide an overview of how CDK controls meiotic events in both bu

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Houchens, Christopher R., Audrey Perreault, François Bachand, and Thomas J. Kelly. "Schizosaccharomyces pombe Noc3 Is Essential for Ribosome Biogenesis and Cell Division but Not DNA Replication." Eukaryotic Cell 7, no. 9 (2008): 1433–40. http://dx.doi.org/10.1128/ec.00119-08.

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ABSTRACT The initiation of eukaryotic DNA replication is preceded by the assembly of prereplication complexes (pre-RCs) at chromosomal origins of DNA replication. Pre-RC assembly requires the essential DNA replication proteins ORC, Cdc6, and Cdt1 to load the MCM DNA helicase onto chromatin. Saccharomyces cerevisiae Noc3 (ScNoc3), an evolutionarily conserved protein originally implicated in 60S ribosomal subunit trafficking, has been proposed to be an essential regulator of DNA replication that plays a direct role during pre-RC formation in budding yeast. We have cloned Schizosaccharomyces pomb

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13

Kim, Soo-Mi, and Joel A. Huberman. "Multiple Orientation-Dependent, Synergistically Interacting, Similar Domains in the Ribosomal DNA Replication Origin of the Fission Yeast, Schizosaccharomyces pombe." Molecular and Cellular Biology 18, no. 12 (1998): 7294–303. http://dx.doi.org/10.1128/mcb.18.12.7294.

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ABSTRACT Previous investigations have shown that the fission yeast,Schizosaccharomyces pombe, has DNA replication origins (500 to 1500 bp) that are larger than those in the budding yeast,Saccharomyces cerevisiae (100 to 150 bp). Deletion and linker substitution analyses of two fission yeast origins revealed that they contain multiple important regions with AT-rich asymmetric (abundant A residues in one strand and T residues in the complementary strand) sequence motifs. In this work we present the characterization of a third fission yeast replication origin, ars3001, which is relatively small (

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14

Golubev, W. I. "Mycocinogeny in fission yeast." Микология и фитопатология 54, no. 2 (2020): 150–52. http://dx.doi.org/10.31857/s002636482002004x.

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15

Nielsen, Olaf. "Fission yeast goes synthetic." Nature Methods 4, no. 10 (2007): 777–78. http://dx.doi.org/10.1038/nmeth1007-777.

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16

Millar, Jonathan. "Recognition for fission yeast." Trends in Cell Biology 10, no. 2 (2000): 81–82. http://dx.doi.org/10.1016/s0962-8924(99)01702-x.

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17

Solomon, Mark, Robert Booher, Marc Kirschner, and David Beach. "Cyclin in fission yeast." Cell 54, no. 6 (1988): 738–40. http://dx.doi.org/10.1016/s0092-8674(88)90933-6.

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18

Piombo, Sabrina, Gode B. Calleja, Bong Yul Yoo, and Byron F. Johnson. "Ruptured fission yeast walls." Cell Biochemistry and Biophysics 29, no. 3 (1998): 263–79. http://dx.doi.org/10.1007/bf02737898.

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19

Johnson, Byron F., Bong Yul Yoo, and Gode B. Calleja. "Smashed fission yeast walls." Cell Biophysics 26, no. 1 (1995): 57–75. http://dx.doi.org/10.1007/bf02820887.

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20

Crane, Richard, Randa Craig, Rachael Murray, Isabelle Dunand-Sauthier, Tim Humphrey, and Chris Norbury. "A Fission Yeast Homolog of Int-6, the Mammalian Oncoprotein and eIF3 Subunit, Induces Drug Resistance when Overexpressed." Molecular Biology of the Cell 11, no. 11 (2000): 3993–4003. http://dx.doi.org/10.1091/mbc.11.11.3993.

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Through a screen to identify genes that induce multi-drug resistance when overexpressed, we have identified a fission yeast homolog of Int-6, a component of the human translation initiation factor eIF3. Disruption of the murine Int-6gene by mouse mammary tumor virus (MMTV) has been implicated previously in tumorigenesis, although the underlying mechanism is not yet understood. Fission yeast Int6 was shown to interact with other presumptive components of eIF3 in vivo, and was present in size fractions consistent with its incorporation into a 43S translation preinitiation complex. Drug resistanc

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21

Fiske, Michael, Stephanie Valtierra, Keith Solvang та ін. "Contribution of Alanine-76 and Serine Phosphorylation inα-Synuclein Membrane Association and Aggregation in Yeasts". Parkinson's Disease 2011 (2011): 1–12. http://dx.doi.org/10.4061/2011/392180.

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In Parkinson's disease (PD), misfolded and aggregatedα-synuclein protein accumulates in degenerating midbrain dopaminergic neurons. The amino acid alanine-76 inα-synuclein and phosphorylation at serine-87 and serine-129 are thought to regulate its aggregation and toxicity. However, their exact contributions toα-synuclein membrane association are less clear. We found thatα-synuclein is indeed phosphorylated in fission yeast and budding yeast, the two models that we employed for assessingα-synuclein aggregation and membrane association properties, respectively. Surprisingly, blocking serine phos

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22

Zheng, Shengnan, Biyu Zheng, and Chuanhai Fu. "The Roles of Septins in Regulating Fission Yeast Cytokinesis." Journal of Fungi 10, no. 2 (2024): 115. http://dx.doi.org/10.3390/jof10020115.

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Cytokinesis is required to separate two daughter cells at the end of mitosis, and septins play crucial roles in many aspects of cytokinesis. While septins have been intensively studied in many model organisms, including the budding yeast Saccharomyces cerevisiae, septins have been relatively less characterized in the fission yeast Schizosaccharomyces pombe, which has proven to be an excellent model organism for studying fundamental cell biology. In this review, we summarize the findings of septins made in fission yeasts mainly from four aspects: the domain structure of septins, the localizatio

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23

Jang, Young Joo, Young Sook Kil, Jee Hee Ahn, et al. "Overexpression Phenotypes of Plk1 and Ndrg2 in Schizosaccharomyces Pombe: Fission Yeast System for Mammalian Gene Study." Key Engineering Materials 277-279 (January 2005): 1–6. http://dx.doi.org/10.4028/www.scientific.net/kem.277-279.1.

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The fission yeast, Schizosaccharomyces pombe is a single-celled free-living fungus that shares many features with cells of more complicated eukaryotes. Many of the genes required for the cell-cycle control, proteolysis, protein modification, and RNA splicing are highly conserved with those of higher eukaryotes. Moreover, fission yeast has the merit of genetics and its genetic system is already well characterized. As such, the current study evaluated the use of a fission yeast system as a tool for the functional study of mammalian genes and attempted to set up an assay system for novel genes. S

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24

Deng, Ruolan, Yi-Lan Li, and Ji-Long Liu. "Differential Cytoophidium Assembly between Saccharomyces cerevisiae and Schizosaccharomyces pombe." International Journal of Molecular Sciences 25, no. 18 (2024): 10092. http://dx.doi.org/10.3390/ijms251810092.

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The de novo synthesis of cytidine 5′-triphosphate (CTP) is catalyzed by the enzyme CTP synthase (CTPS), which is known to form cytoophidia across all three domains of life. In this study, we use the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe as model organisms to compare cytoophidium assembly under external environmental and intracellular CTPS alterations. We observe that under low and high temperature conditions, cytoophidia in fission yeast gradually disassemble, while cytoophidia in budding yeast remain unaffected. The effect of pH changes on cyto

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25

Chaleckis, Romanas, Masahiro Ebe, Tomáš Pluskal, Itsuo Murakami, Hiroshi Kondoh, and Mitsuhiro Yanagida. "Unexpected similarities between theSchizosaccharomycesand human blood metabolomes, and novel human metabolites." Mol. BioSyst. 10, no. 10 (2014): 2538–51. http://dx.doi.org/10.1039/c4mb00346b.

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Comparison of human blood and fission yeast metabolomes revealed that 75% of compounds found in human blood are also detected in fission yeast. Several methylated amino acids are reported as new blood components.

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26

Zhang, Jiantao, Zsigmond Benko, Chenyu Zhang, and Richard Y. Zhao. "Advanced Protocol for Molecular Characterization of Viral Genome in Fission Yeast (Schizosaccharomyces pombe)." Pathogens 13, no. 7 (2024): 566. http://dx.doi.org/10.3390/pathogens13070566.

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Fission yeast, a single-cell eukaryotic organism, shares many fundamental cellular processes with higher eukaryotes, including gene transcription and regulation, cell cycle regulation, vesicular transport and membrane trafficking, and cell death resulting from the cellular stress response. As a result, fission yeast has proven to be a versatile model organism for studying human physiology and diseases such as cell cycle dysregulation and cancer, as well as autophagy and neurodegenerative diseases like Alzheimer’s, Parkinson’s, and Huntington’s diseases. Given that viruses are obligate intracel

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27

Furuya, Kanji, and Hironori Niki. "The DNA Damage Checkpoint Regulates a Transition between Yeast and Hyphal Growth in Schizosaccharomyces japonicus." Molecular and Cellular Biology 30, no. 12 (2010): 2909–17. http://dx.doi.org/10.1128/mcb.00049-10.

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ABSTRACT Dimorphic yeasts change between unicellular growth and filamentous growth. Many dimorphic yeasts species are pathogenic for humans and plants, being infectious as invasive hypha. We have studied the determinants of the dimorphic switch in the nonpathogenic fission yeast Schizosaccharomyces japonicus, which is evolutionarily close to the well-characterized fission yeast S. pombe. We report that camptothecin, an inhibitor of topoisomerase I, reversibly induced the unicellular to hyphal transition in S. japonicus at low concentrations of camptothecin that did not induce checkpoint arrest

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28

Mukaiyama, Hiroyuki, Shiro Kajiwara, Akira Hosomi, et al. "Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial sporulation during nitrogen starvation." Microbiology 155, no. 12 (2009): 3816–26. http://dx.doi.org/10.1099/mic.0.034389-0.

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Autophagy is triggered when organisms sense radical environmental changes, including nutritional starvation. During autophagy, cytoplasmic components, including organelles, are enclosed within autophagosomes and are degraded upon lysosome–vacuole fusion. In this study, we show that processing of GFP-tagged Atg8 can serve as a marker for autophagy in the fission yeast Schizosaccharomyces pombe. Using this marker, 13 Atg homologues were also found to be required for autophagy in fission yeast. In budding yeast, autophagy-deficient mutants are known to be sterile, whereas in fission yeast we foun

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29

Nurse, Paul. "Fission yeast cell cycle mutants and the logic of eukaryotic cell cycle control." Molecular Biology of the Cell 31, no. 26 (2020): 2871–73. http://dx.doi.org/10.1091/mbc.e20-10-0623.

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Cell cycle mutants in the budding and fission yeasts have played critical roles in working out how the eukaryotic cell cycle operates and is controlled. The starting point was Lee Hartwell’s 1970s landmark papers describing the first cell division cycle (CDC) mutants in budding yeast. These mutants were blocked at different cell cycle stages and so were unable to complete the cell cycle, thus defining genes necessary for successful cell division. Inspired by Hartwell’s work, I isolated CDC mutants in the very distantly related fission yeast. This started a program of searches for mutants in fi

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30

Lu, Jia, and Thomas D. Pollard. "Profilin Binding to Poly-l-Proline and Actin Monomers along with Ability to Catalyze Actin Nucleotide Exchange Is Required for Viability of Fission Yeast." Molecular Biology of the Cell 12, no. 4 (2001): 1161–75. http://dx.doi.org/10.1091/mbc.12.4.1161.

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We tested the ability of 87 profilin point mutations to complement temperature-sensitive and null mutations of the single profilin gene of the fission yeast Schizosaccharomyces pombe. We compared the biochemical properties of 13 stable noncomplementing profilins with an equal number of complementing profilin mutants. A large quantitative database revealed the following: 1) in a profilin null background fission yeast grow normally with profilin mutations having >10% of wild-type affinity for actin or poly-l-proline, but lower affinity for either ligand is incompatible with life; 2) in thecdc

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31

Walker, Sara Imari, Hyunju Kim, and Paul C. W. Davies. "The informational architecture of the cell." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 374, no. 2063 (2016): 20150057. http://dx.doi.org/10.1098/rsta.2015.0057.

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We compare the informational architecture of biological and random networks to identify informational features that may distinguish biological networks from random. The study presented here focuses on the Boolean network model for regulation of the cell cycle of the fission yeast Schizosaccharomyces pombe . We compare calculated values of local and global information measures for the fission yeast cell cycle to the same measures as applied to two different classes of random networks: Erdös–Rényi and scale-free. We report patterns in local information processing and storage that do indeed disti

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32

Zeng, Yan, and Helen Piwnica-Worms. "DNA Damage and Replication Checkpoints in Fission Yeast Require Nuclear Exclusion of the Cdc25 Phosphatase via 14-3-3 Binding." Molecular and Cellular Biology 19, no. 11 (1999): 7410–19. http://dx.doi.org/10.1128/mcb.19.11.7410.

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ABSTRACT In fission yeast as well as in higher eukaryotic organisms, entry into mitosis is delayed in cells containing damaged or unreplicated DNA. This is accomplished in part by maintaining the Cdc25 phosphatase in a phosphorylated form that binds 14-3-3 proteins. In this study, we generated a mutant of fission yeast Cdc25 that is severely impaired in its ability to bind 14-3-3 proteins. Loss of both the DNA damage and replication checkpoints was observed in fission yeast cells expressing the 14-3-3 binding mutant. These findings indicate that 14-3-3 binding to Cdc25 is required for fission

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33

Hagan, I. M. "The fission yeast microtubule cytoskeleton." Journal of Cell Science 111, no. 12 (1998): 1603–12. http://dx.doi.org/10.1242/jcs.111.12.1603.

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The Schizosaccharomyces pombe genome sequencing project (http://www.sanger.ac.uk/Projects/S_pombe/) is nearly complete, and this is likely to generate interest in fission yeast as a model system beyond its traditional strongholds in the study of the cell cycle and sexual differentiation. In many fields S. pombe will offer a useful complement to the more widely studied Saccharomyces cerevisiae, but in some areas the impact of S. pombe may well rival or exceed that of this budding yeast in terms of relevance to higher systems. Because of the considerable differences from the S. cerevisiae microt

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34

., ,. "Centromeric chromatin in fission yeast." Frontiers in Bioscience Volume, no. 13 (2008): 3896. http://dx.doi.org/10.2741/2977.

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Rusk, Nicole. "Fission yeast defies the code." Nature Methods 7, no. 4 (2010): 255. http://dx.doi.org/10.1038/nmeth0410-254b.

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Wilson-Grady, Joshua T., Judit Villén, and Steven P. Gygi. "Phosphoproteome Analysis of Fission Yeast." Journal of Proteome Research 7, no. 3 (2008): 1088–97. http://dx.doi.org/10.1021/pr7006335.

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37

Chang, F., and S. G. Martin. "Shaping Fission Yeast with Microtubules." Cold Spring Harbor Perspectives in Biology 1, no. 1 (2009): a001347. http://dx.doi.org/10.1101/cshperspect.a001347.

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38

Pasion, Sally. "Fission yeast blooms in Kyoto." Trends in Genetics 18, no. 7 (2002): 342–43. http://dx.doi.org/10.1016/s0168-9525(02)02721-x.

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Furuya, K. "DNA checkpoints in fission yeast." Journal of Cell Science 116, no. 19 (2003): 3847–48. http://dx.doi.org/10.1242/jcs.00790.

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McIntosh, J. Richard, Mary K. Morphew, and Thomas H. Giddings. "Electron Microscopy of Fission Yeast." Cold Spring Harbor Protocols 2017, no. 1 (2017): pdb.top079822. http://dx.doi.org/10.1101/pdb.top079822.

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Pérez, Pilar, and Juan C. Ribas. "Fission Yeast Cell Wall Analysis." Cold Spring Harbor Protocols 2017, no. 11 (2017): pdb.top079897. http://dx.doi.org/10.1101/pdb.top079897.

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Khodjakov, Alexey, Sabrina La Terra, and Fred Chang. "Laser Microsurgery in Fission Yeast." Current Biology 14, no. 15 (2004): 1330–40. http://dx.doi.org/10.1016/j.cub.2004.07.028.

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43

Egel, Richard, Olaf Nielsen, and Dietmar Weilguny. "Sexual differentiation in fission yeast." Trends in Genetics 6 (1990): 369–73. http://dx.doi.org/10.1016/0168-9525(90)90279-f.

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44

Muers, Mary. "Fission yeast compared and contrasted." Nature Reviews Genetics 12, no. 6 (2011): 381. http://dx.doi.org/10.1038/nrg3006.

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Otsubo, Yoko, and Masayuki Yamamato. "TOR Signaling in Fission Yeast." Critical Reviews in Biochemistry and Molecular Biology 43, no. 4 (2008): 277–83. http://dx.doi.org/10.1080/10409230802254911.

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46

OLSON, LAURITZ W., ULLA EDÉN, MICHIKO EGEL-MITANI, and RICHARD EGEL. "Asynaptic meiosis in fission yeast?" Hereditas 89, no. 2 (2009): 189–99. http://dx.doi.org/10.1111/j.1601-5223.1978.tb01275.x.

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Morphew, Mary K., Thomas H. Giddings, and J. Richard McIntosh. "Cryoelectron Microscopy of Fission Yeast." Cold Spring Harbor Protocols 2017, no. 1 (2017): pdb.prot091330. http://dx.doi.org/10.1101/pdb.prot091330.

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Pérez, Pilar, Juan C. G. Cortés, Rebeca Martín-García, and Juan C. Ribas. "Overview of fission yeast septation." Cellular Microbiology 18, no. 9 (2016): 1201–7. http://dx.doi.org/10.1111/cmi.12611.

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49

Leupold, Urs. "Sex appeal in fission yeast." Current Genetics 12, no. 7 (1987): 543–45. http://dx.doi.org/10.1007/bf00419564.

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Davey, John. "Fusion of a fission yeast." Yeast 14, no. 16 (1998): 1529–66. http://dx.doi.org/10.1002/(sici)1097-0061(199812)14:16<1529::aid-yea357>3.0.co;2-0.

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