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Mutation Research/Reviews in Mutation Research (78)
References
150
Referenced
78
- L. Dunn, A Short History of Genetics, McGraw-Hill, New York, 1965.
- A.H. Sturtevant, A History of Genetics, Harper & Row, New York, 1965.
- R. Olby, Origins of Mendelism, Schocken Books, New York, 1966.
10.1038/171737a0
/ Nature / A structure of deoxyribose nucleic acid by Watson (1953)- A.J.F. Griffith, J.H. Miller, D.T. Suzuki, R.C. Lewontin, W.M. Gelbart, An Introduction to Genetic Analysis, 7th Edition, Freeman, New York, 2000.
10.1073/pnas.53.2.275
/ Proc. Natl. Acad. Sci. U.S.A. / Cytoplasmic inheritance of the organization of the cell cortex in Paramecium aurelia by Beisson (1965)10.1073/pnas.74.3.1115
/ Proc. Natl. Acad. Sci. U.S.A. / 180 Degrees rotation of ciliary rows and its morphogenetic implications in Tetrahymena pyriformis by Ng (1977){'key': '10.1016/S1383-5742(00)00060-0_BIB8', 'first-page': '375', 'article-title': 'Cortical memory in Paramecium: a theoretical approach to the structural heredity', 'volume': '318', 'author': 'Hyver', 'year': '1995', 'journal-title': 'C. R. Acad. Sci.'}
/ C. R. Acad. Sci. / Cortical memory in Paramecium: a theoretical approach to the structural heredity by Hyver (1995)10.1126/science.6801762
/ Science / Novel proteinaceous infectious particles cause scrapie by Prusiner (1982)10.1098/rstb.1994.0043
/ Phil. Trans. R. Soc. Lond. Ser. B: Biol. Sci. / Molecular biology and genetics of prion diseases by Prusiner (1994)10.1016/S0092-8674(00)81163-0
/ Cell / Prion protein biology by Prusiner (1998)10.1038/214764a0
/ Nature / Does the agent of scrapie replicate without nucleic acid? by Alper (1967)10.1038/2151043a0
/ Nature / Self-replication and scrapie by Griffith (1967)10.1038/nm0597-491
/ Nature Med. / Human TSE disease — viral or protein only? by Chesebro (1997)10.1126/science.7909169
/ Science / Structural clues to prion replication by Cohen (1994)10.1016/S0959-440X(97)80007-3
/ Curr. Op. Struct. Biol. / The prion folding problem by Harrison (1997)10.1016/1074-5521(95)90074-8
/ Chem. Biol. / The chemistry of scrapie reaction: the “ice 9” metaphore by Lansbury (1995)10.1016/0092-8674(83)90168-X
/ Cell / Scrapie prions aggregate to form amyloid-like birefringent rods by Prusiner (1983)10.1016/0092-8674(85)90076-5
/ Cell / Identification of prion amyloid filaments in scrapie-infected brain by DeArmond (1985)10.1038/370471a0
/ Nature / Cell-free formation of protease-resistant prion protein by Kocisko (1994)10.1126/science.7909170
/ Science / [URE3] as an altered Ure2 protein: evidence for a prion analog in Saccharomyces cerevisiae by Wickner (1994)10.1128/JB.106.2.519-522.1971
/ J. Bacteriol. / Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast by Lacroute (1971)10.1007/BF00341717
/ Mol. Gen. Genet. / Genetical aspects of [URE3], a non-mitochondrial cytoplasmically inherited mutation in yeast by Aigle (1975)10.1038/hdy.1965.65
/ Heredity / Ψ, a cytoplasmic suppressor of super-suppressor in yeast by Cox (1965)10.1002/yea.320040302
/ Yeast / The Ψ factor of yeast: a problem in inheritance by Cox (1988)10.1093/genetics/137.3.659
/ Genetics / The dominant PNM2-mutation which eliminates the Ψ factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene by Doel (1994)10.1093/genetics/137.3.671
/ Genetics / The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae by Ter-Avanesyan (1994)10.1126/science.270.5233.93
/ Science / Prion-inducing domain of yeast Ure2p and protease-resistance of Ure2p in prion-containing cells by Masison (1995)10.1073/pnas.96.4.1498
/ Proc. Natl. Acad. Sci. U.S.A. / The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments by Edskes (1999)10.1126/science.273.5275.622
/ Science / Support for the prion hypothesis for inheritance of a phenotypic trait in yeast by Patino (1996)10.1002/j.1460-2075.1996.tb00675.x
/ EMBO J. / Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor by Paushkin (1996)10.1016/S0092-8674(00)80264-0
/ Cell / Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of Saccharomyces cerevisiae by Glover (1997)10.1073/pnas.94.13.6618
/ Proc. Natl. Acad. Sci. U.S.A. / Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments by King (1997)10.1126/science.283.5406.1339
/ Science / Prion domain initiation of amyloid formation in vitro from native Ure2p by Taylor (1999)10.1074/jbc.274.19.13666
/ J. Biol. Chem. / Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2 by Thual (1999)10.1110/ps.9.3.440
/ Protein Sci. / The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein by Schlumpberger (2000)10.1126/science.289.5483.1317
/ Science / Nucleated conformational conversion and the replication of conformational information by a prion determinant by Serio (2000)10.1126/science.277.5324.381
/ Science / In vitro propagation of the prion-like state of yeast Sup35 protein by Paushkin (1999)10.1007/BF00351802
/ Curr. Genet. / Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae by Chernoff (1993)10.1093/genetics/144.4.1375
/ Genetics / Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae by Derkatch (1996)10.1126/science.289.5479.595
/ Science / Evidence for the prion hypothesis: induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein by Sparrer (2000)10.1074/jbc.274.3.1181
/ J. Biol. Chem. / The yeast [PSI+] prion: making sense of nonsense by Liebman (1999)10.1074/jbc.274.2.555
/ J. Biol. Chem. / Prions of yeast and fungi: proteins as genetic material by Wickner (1999)- R.B. Wickner, Y.O. Chernoff, Prions of yeast and fungi: [URE3], [PSI] and [Het-s] discovered as heritable traits, in: S.B. Prusiner (Ed.), Prion Biology and Diseases, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1999, pp. 229–272.
10.1016/S0962-8924(99)01711-0
/ Trends Cell Biol. / Protein-only inheritance in yeast: something to get [PSI+]-ched about by Serio (2000)10.1126/science.284.5411.159
/ Science / Phenotypic change caused by transcriptional bypass of uracil in nondividing cells by Viswanathan (1999)-
A. Viswanathan, J. Liu, P.W. Doetsch, E. coli polymerase bypass of DNA base damage: mutagenesis at the level of transcription, in: A.C. Find (Ed.), Molecular Strategies in Biological Evolution, The New York Academy of Sciences, New York, 1999; Annals 870, 386–389.
(
10.1111/j.1749-6632.1999.tb08909.x
) 10.1126/science.3310230
/ Science / The inheritance of epigenetic defects by Holliday (1987)10.1007/BF00266934
/ Mol. Gen. Genet. / Host-genotype and agent effects in scrapie incubation: change in allelic interaction with different strains of agent by Dickinson (1971)10.1038/375698a0
/ Nature / Non-genetic propagation of strain-specific properties of scrapie prion protein by Bessen (1995)10.1046/j.1365-2958.2000.01761.x
/ Mol. Microbiol. / Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein by Chernoff (2000)10.1093/emboj/19.3.324
/ EMBO J. / Prion properties of the Sup35 protein of yeast Pichia methanolica by Kushnirov (2000)10.1016/S0092-8674(00)81565-2
/ Cell / Molecular basis of a yeast prion species barrier by Santoso (2000)-
P.A. Bailleul-Winslett, G.P. Newnam, R.D. Wegrzyn, Y.O. Chernoff, An anti-prion effect of the anticytoskeletal drug latrunculin A in yeast, Gene Expression (2000), in press.
(
10.3727/000000001783992650
) 10.1093/genetics/98.4.691
/ Genetics / Agents that cause a high frequency of genetic change from [psi+] to [psi−] in Saccharomyces cerevisiae by Tuite (1981)10.1073/pnas.97.1.240
/ Proc. Natl. Acad. Sci. U.S.A. / Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI+] of Saccharomyces cerevisiae by Eaglestone (2000)10.1093/emboj/19.9.1942
/ EMBO J. / Dependence and independence of [PSI+] and [PIN+]: a two-prion system in yeast? by Derkatch (2000)10.1126/science.7754373
/ Science / Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+] by Chernoff (1995)10.1128/MCB.19.12.8103
/ Mol. Cell. Biol. / Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability, and toxicity of the [PSI] prion by Chernoff (1999)10.1007/s004120050300
/ Chromosoma / Eukaryotic DNA polymerases in DNA replication and DNA repair by Burgers (1998)10.1016/S0921-8777(98)00056-1
/ Mutat. Res. / Eukaryotic mismatch repair: an update by Jiricny (1998)10.1016/S0966-842X(98)01424-3
/ Trends Microbiol. / Escherichia coli mutator genes by Horst (1999)-
Y.O. Chernoff, B. Ono, Dosage-dependent modifiers of psi-dependent omnipotent suppression in yeast, in: A.J.P. Brown, M.F. Tuite, J.E.G. McCarthy (Eds.), Protein Synthesis and Targeting in Yeast, NATO ASI Ser. H: Cell Biology, Vol. 71, Springer, Berlin, 1993, pp. 101–110.
(
10.1007/978-3-642-84921-3_10
) 10.1038/353270a0
/ Nature / Hsp104 is a highly conserved protein with two essential nucleotide-binding sites by Parsell (1991)10.1016/0968-0004(96)10038-4
/ Trends Biochem. / HSP100/Clp proteins: a common mechanism explains diverse functions by Schirmer (1996)10.1126/science.2188365
/ Science / Hsp104 required for induced thermotolerance by Sanchez (1990)10.1002/j.1460-2075.1992.tb05295.x
/ EMBO J. / Hsp104 is required for tolerance to many forms of stress by Sanchez (1992)10.1038/372475a0
/ Nature / Protein disaggregation mediated by heat-shock protein Hsp104 by Parsell (1994)10.1016/S0092-8674(00)81223-4
/ Cell / Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins by Glover (1998)10.1128/jb.175.20.6484-6491.1993
/ J. Bacteriol. / Genetic evidence for a functional relationship between Hsp104 and Hsp70 by Sanchez (1993)10.1073/pnas.96.24.13732
/ Proc. Natl. Acad. Sci. U.S.A. / Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network by Goloubinoff (1999)10.1093/genetics/153.1.81
/ Genetics / Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae by Bailleul (1999)10.1016/S0960-9822(00)00167-6
/ Curr. Biol. / Prion-like factors in yeast by Cox (1994)10.1101/SQB.1995.060.01.050
/ Cold Spring Harbor Symp. Quant. Biol. / The role of Hsp104 in stress tolerance and [PSI+] propagation in Saccharomyces cerevisiae by Lindquist (1995)10.1016/S0966-842X(00)88979-9
/ Trends Microbiol. / Response from Chernoff et al. [Re: R.B. Wickner, Prions of yeast and heat-shock protein 104: ‘coprion’ and cure] by Chernoff (1995)10.1073/pnas.76.4.1952
/ Proc. Natl. Acad. Sci. U.S.A. / Mutation of the non-Mendelian suppressor, psi+, in yeast by hypertonic media by Singh (1979)10.1128/MCB.7.7.2568
/ Mol. Cell. Biol. / Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae by Werner-Washburne (1987)10.1128/MCB.19.2.1325
/ Mol. Cell. Biol. / Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing by Newnam (1999)10.1093/genetics/156.2.559
/ Genetics / A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress by Jung (2000)10.1242/jcs.110.13.1431
/ J. Cell Sci. / Molecular chaperones and the cytoskeleton by Liang (1997)10.1016/0092-8674(92)90269-I
/ Cell / The translation machinery and 70 kDa heat shock protein cooperate in protein synthesis by Nelson (1992)10.1093/emboj/17.14.3981
/ EMBO J. / The molecular chaperone Ssb from Saccharomyces cerevisiae is a component off the ribosome-nascent chain complex by Pfund (1998)10.1016/0014-5793(94)00873-6
/ FEBS Lett. / A 70-kDa heat shock cognate protein suppresses the defects caused by a proteasome mutation in Saccharomyces cerevisiae by Ohba (1994)10.1016/S0014-5793(97)00535-8
/ FEBS Lett. / Modulation of intracellular protein degradation by SSB1-SIS1 chaperon system in yeast Saccharomyces cerevisiae by Ohba (1997)10.1073/pnas.94.25.13938
/ Proc. Natl. Acad. Sci. U.S.A. / Chaperone supervised conversion of prion protein to its protease-resistant form by DebBurman (1997)-
H. Moriyama, H.K. Edskes, R.B. Wickner, [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p, Mol. Cell. Biol. 20 (2000) 8916–8922.
(
10.1128/MCB.20.23.8916-8922.2000
) 10.1083/jcb.122.3.635
/ J. Cell. Biol. / Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae by Holtzman (1993)10.1038/347494a0
/ Nature / Identification of an actin-binding protein from Dictyostelium as elongation factor 1α by Yang (1990)10.1002/jcb.240520204
/ J. Cell. Biochem. / ABP50: an actin-binding elongation factor 1α from Dictyostelium discoideum by Edmonds (1993)10.1046/j.1365-2443.1999.00279.x
/ Genes Cells / Overproduction of elongation factor 1alpha, an essential translational component, causes aberrant cell morphology by affecting the control of growth polarity in fission yeast by Suda (1999)10.1093/oxfordjournals.jbchem.a022583
/ J. Biochem. / Tetrahymena elongation factor-1 alpha is localized with calmodulin in the division furrow by Numata (2000)10.1016/0378-1119(88)90223-5
/ Gene / Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae by Kushnirov (1988)10.1016/0022-2836(88)90301-4
/ J. Mol. Biol. / Suf12 suppressor protein of yeast: a fusion protein related to the EF-1α family of elongation factors by Wilson (1988)10.1093/genetics/147.2.507
/ Genetics / Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae by Derkatch (1997)10.1002/j.1460-2075.1995.tb00111.x
/ EMBO J. / The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae by Stansfield (1995)10.1073/pnas.95.5.2400
/ Proc. Natl. Acad. Sci. U.S.A. / Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion by Derkatch (1998)10.1128/MCB.17.5.2798
/ Mol. Cell Biol. / Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation by Paushkin (1997)10.1017/S135583829998216X
/ RNA / C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids by Ebihara (1999)10.1002/j.1460-2075.1995.tb00078.x
/ EMBO J. / Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3 by Zhouravleva (1995)10.1073/pnas.120168697
/ Proc. Natl. Acad. Sci. U.S.A. / A protein required for prion generation: [URE3] induction requires the Ras-regulated Mks1 protein by Edskes (2000)10.1093/genetics/153.2.585
/ Genetics / Mks1p is a regulator of nitrogen catabolism upstream of Ure2p in Saccharomyces cerevisiae by Edskes (1999)10.1016/0300-9084(92)90086-T
/ Biochimie / Conservative system for dosage-dependent modulation of translational fidelity in eukaryotes by Chernoff (1992)10.1111/j.1365-2958.1993.tb01159.x
/ Mol. Microbiol. / Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein by Ter-Avanesyan (1993)10.1126/science.287.5453.661
/ Science / Creating a protein-based element of inheritance by Li (2000)10.1002/j.1460-2075.1989.tb08558.x
/ EMBO J. / A human homologue of the yeast GST1 gene codes for a GTP-binding protein and is expressed in a proliferation-dependent manner in mammalian cells by Hoshino (1989)10.1002/yea.320060603
/ Yeast / Divergence and conservation of SUP2 (SUP35) gene of yeasts Pichia pinus and Saccharomyces cerevisiae by Kushnirov (1990)- O. Jean-Jean, X. LeGoff, M. Philippe, Is there a human [psi]? C. R. Acad. Sci. Paris, Sciences de la vie/Life Sciences 319 (1996) 487–492.
10.1016/S0092-8674(00)81467-1
/ Cell / A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion by De Pace (1998){'key': '10.1016/S1383-5742(00)00060-0_BIB109', 'first-page': '427', 'article-title': 'Structural and functional similarity of Sup35p and Ure2p yeast proteins and mammalian prions', 'volume': '29', 'author': 'Kushnirov', 'year': '1995', 'journal-title': 'Mol. Biol. (Russ.)'}
/ Mol. Biol. (Russ.) / Structural and functional similarity of Sup35p and Ure2p yeast proteins and mammalian prions by Kushnirov (1995)10.1099/0022-1317-75-11-2947
/ J. Gen. Virol. / Transmissible mink encephalopathy species barrier effect between ferret and mink: PrP gene and protein analysis by Bartz (1994)10.1098/rstb.1994.0036
/ Philos. Trans. R. Soc. Lond. Ser. B: Biol. Sci. / Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier by Bruce (1994)10.1073/pnas.92.9.3923
/ Proc. Natl. Acad. Sci. U.S.A. / Species specificity in the cell free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier by Kocisco (1995)10.1016/S1097-2765(00)80412-8
/ Mol. Cell / Rnq1: an epigenetic modifier of protein function in yeast by Sondheimer (2000)10.1093/genetics/154.3.1053
/ Genetics / Trinucleotide repeats are clustered in regulatory genes in Saccharomyces cerevisiae by Young (2000)10.1073/pnas.94.18.9773
/ Proc. Natl. Acad. Sci. U.S.A. / The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog by Coustou (1997)10.1016/S0168-9525(98)01559-5
/ Trends Genet. / Protein precipitation: a common etiology in neurodegenerative disorders? by Kakizuka (1998)10.1073/pnas.96.18.9989
/ Proc. Natl. Acad. Sci. U.S.A. / Amyloid diseases: abnormal protein aggregation in neurodegeneration by Koo (1999)10.1146/annurev.med.51.1.543
/ Ann. Rev. Med. / The genetics of the amyloidoses by Buxbaum (2000)10.1007/s007020050002
/ J. Neural. Trans. / Involvement of alpha-synuclein in Parkinson’s disease and other neurodegenerative disorders by Kruger (2000)10.1146/annurev.neuro.23.1.217
/ Ann. Rev. Neurosci. / Glutamine repeats and neurodegeneration by Zoghbi (2000)10.1073/pnas.97.4.1589
/ Proc. Natl. Acad. Sci. U.S.A. / Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins by Krobitsch (2000)10.1073/pnas.140202897
/ Proc. Natl. Acad. Sci. U.S.A. / Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils by Muchowski (2000)10.1073/pnas.100107297
/ Proc. Natl. Acad. Sci. U.S.A. / Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans by Satyal (2000)10.1523/JNEUROSCI.19-23-10338.1999
/ J. Neurosci. / Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease by Chai (1999)10.1038/70532
/ Nature Genet. / Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70 by Warrick (1999)10.1126/science.287.5459.1837
/ Science / Genetic suppression of polyglutamine toxicity in Drosophila by Kazemi-Esfarjani (2000)10.1016/0165-1161(75)90046-1
/ Mutat. Res. / Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test by Ames (1975)10.1073/pnas.96.7.3590
/ Proc. Natl. Acad. Sci. U.S.A. / Designing conditions for in vitro formation of amyloid protofilaments and fibrils by Chiti (1999)10.1016/S0968-0004(99)01445-0
/ Trends Biochem. Sci. / Protein misfolding, evolution and disease by Dobson (1999)10.1006/jmbi.1995.0438
/ J. Mol. Biol. / The efficiency of translation termination is determined by a synergistic interplay between upstream and downstream sequences in Saccharomyces cerevisiae by Bonetti (1995){'key': '10.1016/S1383-5742(00)00060-0_BIB131', 'first-page': '1227', 'article-title': 'Nonsense-suppression by amplification of translation protein factor gene', 'volume': '301', 'author': 'Chernoff', 'year': '1988', 'journal-title': 'Doklady Akad. Nauk SSSR: Biol. Sci. (Russ.)'}
/ Doklady Akad. Nauk SSSR: Biol. Sci. (Russ.) / Nonsense-suppression by amplification of translation protein factor gene by Chernoff (1988)10.1002/yea.320080702
/ Yeast / Dosage-dependent translational suppression in yeast Saccharomyces cerevisiae by Chernoff (1992)10.1093/genetics/128.3.513
/ Genetics / Interactions of the yeast omnipotent suppressors SUP1 (SUP45) and SUP2 (SUP35) with non-Mendelian factors by Dagkesamanskaya (1991)10.1093/emboj/18.7.1974
/ EMBO J. / Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism by Eaglestone (1999)10.1111/j.1365-2958.1989.tb01810.x
/ Mol. Microbiol. / Mistranslation induces the heat-shock response in the yeast Saccharomyces cerevisiae by Grant (1989)10.1038/35035005
/ Nature / A yeast prion provides a mechanism for genetic variation and phenotypic diversity by True (2000)-
M.A. Jensen, H. True, Y.O. Chernoff, S. Lindquist, Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae, Genetics (2001), under revision.
(
10.1093/genetics/159.2.527
) 10.1007/s002940050379
/ Curr. Genet. / C-terminal truncation of the Sup35 protein increases the frequency of de novo generation of a prion-based [PSI+] determinant in Saccharomyces cerevisiae by Kochneva-Pervukhova (1998)10.1073/pnas.76.1.391
/ Proc. Natl. Acad. Sci. U.S.A. / Phase variation in Salmonella: genetic analysis of a recombinational switch by Silverman (1979)10.1146/annurev.bi.55.070186.003123
/ Ann. Rev. Biochem. / Biological catalysis by RNA by Cech (1986)10.1126/science.288.5463.38
/ Science / Was Lamarck just a little bit right? by Balter (2000)10.1146/annurev.ge.25.120191.000245
/ Ann. Rev. Genet. / The inheritance of acquired characteristics by Landman (1991)10.1016/S1383-5742(99)00087-3
/ Mutat. Res. / Lysenko and Stalin: commemorating the 50th anniversary of the August 1948 LAAAS Conference and the 100th anniversary of T.D. Lysenko’s birth, 29 September 1898 by Medvedev (2000)10.1074/jbc.270.38.22535
/ J. Biol. Chem. / Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP by King (1995)10.1046/j.1432-1327.1999.00078.x
/ Eur. J. Biochem. / Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms by Angelidis (1999)10.1093/emboj/18.23.6744
/ EMBO J. / Hsp26: a temperature-regulated chaperone by Haslbeck (1999)10.1126/science.289.5478.448
/ Science / One sequence, two ribozymes: implications for the emergence of new ribozyme folds by Shultes (2000)10.7124/bc.0003DD
/ Biopolym. Cells / Mobile genetics and forms of heritable changes in eukaryotes by Golubovsky (1995){'key': '10.1016/S1383-5742(00)00060-0_BIB149', 'first-page': '16', 'article-title': 'Dynamic inheritance and epigenes', 'volume': '4', 'author': 'Golubovsky', 'year': '1997', 'journal-title': 'Priroda'}
/ Priroda / Dynamic inheritance and epigenes by Golubovsky (1997)10.1038/385810a0
/ Nature / Viable offspring derived from fetal and adult mammalian cells by Wilmut (1997)
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 3:53 p.m.) |
Deposited | 4 years, 3 months ago (May 10, 2021, 8:07 p.m.) |
Indexed | 1 month, 2 weeks ago (July 16, 2025, 8:25 a.m.) |
Issued | 24 years, 6 months ago (March 1, 2001) |
Published | 24 years, 6 months ago (March 1, 2001) |
Published Print | 24 years, 6 months ago (March 1, 2001) |
@article{Chernoff_2001, title={Mutation processes at the protein level: is Lamarck back?}, volume={488}, ISSN={1383-5742}, url={http://dx.doi.org/10.1016/s1383-5742(00)00060-0}, DOI={10.1016/s1383-5742(00)00060-0}, number={1}, journal={Mutation Research/Reviews in Mutation Research}, publisher={Elsevier BV}, author={Chernoff, Yury O.}, year={2001}, month=mar, pages={39–64} }