Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (2430) 2430
Publication (539) 539
Newspaper Article (81) 81
Book Chapter (45) 45
Book Review (34) 34
Newsletter (21) 21
Book / eBook (14) 14
Conference Proceeding (14) 14
Magazine Article (11) 11
Dissertation (7) 7
Government Document (7) 7
Trade Publication Article (2) 2
Web Resource (2) 2
Data Set (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
yeast (1508) 1508
index medicus (1203) 1203
proteins (937) 937
saccharomyces-cerevisiae (881) 881
biochemistry & molecular biology (809) 809
prions (663) 663
saccharomyces cerevisiae - metabolism (591) 591
saccharomyces cerevisiae proteins - metabolism (574) 574
humans (563) 563
saccharomyces cerevisiae - genetics (543) 543
prions - metabolism (503) 503
cell biology (483) 483
research (476) 476
animals (457) 457
saccharomyces cerevisiae proteins - genetics (427) 427
mutation (365) 365
prions - chemistry (358) 358
prions - genetics (357) 357
multidisciplinary sciences (342) 342
microbiology (339) 339
protein (330) 330
prion (328) 328
protein folding (321) 321
biology (314) 314
saccharomyces cerevisiae (311) 311
genetic aspects (300) 300
propagation (298) 298
physiological aspects (296) 296
saccharomyces cerevisiae proteins - chemistry (296) 296
genetics & heredity (284) 284
yeasts (279) 279
research article (272) 272
amino acid sequence (270) 270
analysis (270) 270
amyloid (263) 263
genetics (263) 263
article (249) 249
life sciences (235) 235
gene expression (225) 225
molecular sequence data (224) 224
in-vitro (223) 223
psi (217) 217
protein conformation (212) 212
biochemistry (210) 210
psi+ prion (207) 207
molecular biology (201) 201
yeast prion (193) 193
aggregation (190) 190
peptide termination factors (188) 188
amyloid - chemistry (187) 187
protein binding (179) 179
protein structure, tertiary (178) 178
fungal proteins - genetics (176) 176
nervous system diseases (174) 174
biotechnology & applied microbiology (171) 171
models, biological (171) 171
amyloid - metabolism (170) 170
fungal proteins - metabolism (169) 169
medicine (169) 169
heat shock proteins (168) 168
hsp104 (165) 165
genes (162) 162
science (159) 159
disease (158) 158
phenotype (158) 158
heat-shock proteins - metabolism (155) 155
sup35 (154) 154
saccharomyces cerevisiae proteins (152) 152
prion protein (150) 150
biophysics (149) 149
saccharomyces (149) 149
cells (148) 148
fungi (148) 148
peptide termination factors - metabolism (147) 147
gene (144) 144
in-vivo (140) 140
fungal proteins - chemistry (136) 136
models, molecular (135) 135
neurodegenerative diseases (135) 135
amino acids (134) 134
brewer's yeast (133) 133
molecular chaperones (132) 132
gene expression regulation, fungal (130) 130
biological sciences (127) 127
protein aggregation (127) 127
yeast saccharomyces-cerevisiae (125) 125
escherichia-coli (123) 123
translation termination (123) 123
plasmids (122) 122
toxicity (116) 116
animal diseases (115) 115
binding (115) 115
chaperone (115) 115
peptides (114) 114
molecular chaperones - metabolism (113) 113
yeast fungi (110) 110
budding yeast (108) 108
expression (108) 108
mycology (107) 107
inheritance (106) 106
more...
Library Location Library Location
Library Location Library Location
X
Sort by Item Count (A-Z)
Filter by Count
Gerstein Science - Stacks (4) 4
Collection Dvlpm't (Acquisitions) - Vendor file (2) 2
Chemistry (A D Allen) - Stacks (1) 1
Earth Sciences (Noranda) - Stacks (1) 1
Engineering & Comp. Sci. - Stacks (1) 1
Online Resources - Online (1) 1
UofT at Mississauga - Stacks (1) 1
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (2581) 2581
French (10) 10
Chinese (2) 2
German (1) 1
Japanese (1) 1
Korean (1) 1
Polish (1) 1
Portuguese (1) 1
Spanish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Prions
by Stanley B. Prusiner
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/1998, Volume 95, Issue 23, pp. 13363 - 13383
Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases... 
Nervous system diseases | Neurodegenerative diseases | Prions | Creutzfeldt Jakob syndrome | Prion diseases | Viruses | Amino acids | Mice | Nucleic acids | Genetic mutation | FATAL FAMILIAL INSOMNIA | TRANSMISSIBLE MINK ENCEPHALOPATHY | CEREBELLAR PURKINJE-CELLS | BOVINE SPONGIFORM ENCEPHALOPATHY | FIBRILLARY ACIDIC PROTEIN | MULTIDISCIPLINARY SCIENCES | GERSTMANN-STRAUSSLER SYNDROME | YEAST SUP35 PROTEIN | CREUTZFELDT-JAKOB-DISEASE | SCRAPIE-ASSOCIATED PROTEIN | INCUBATION PERIOD MICE | Causes of | Nervous system | Degeneration (Pathology) | Degeneration | Research
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Growth phase‐dependent changes in the size and infectivity of SDS‐resistant Sup35p assemblies associated with the [PSI+] prion in yeast
by Wang, Kai and Melki, Ronald and Kabani, Mehdi
Molecular Microbiology, ISSN 0950-382X, 09/2019, Volume 112, Issue 3, pp. 932 - 943
Summary The translation termination factor Sup35p can form self‐replicating fibrillar aggregates responsible for the [PSI+] prion state. Sup35p aggregation... 
GENETIC-VARIATION | SUPPRESSOR | TRANSMISSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEASOME | PSI(+) | DETERMINANT | MICROBIOLOGY | CHAPERONE | INHERITANCE | SACCHAROMYCES-CEREVISIAE | PROPAGATION | Yeasts | Yeast | Gels | Fluorescence | Cytosol | Phase transitions | Lysates | Replicating | Infectious diseases | Infectivity | Prions | Translation termination | Assemblies | Prion protein | Life Sciences | Microbiology and Parasitology | Biomolecules | Subcellular Processes | Cellular Biology | Biochemistry, Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text Hsp70 Chaperones as Modulators of Prion Life Cycle: Novel Effects of Ssa and Ssb on the Saccharomyces cerevisiae Prion [PSI+]
by Allen, Kim D and Wegrzyn, Renee D and Chernova, Tatiana A and Muller, Susanne and Newnam, Gary P and Winslett, Peggy A and Wittich, Kristin B and Wilkinson, Keith D and Chernoff, Yury O
Genetics, ISSN 0016-6731, 03/2005, Volume 169, Issue 3, pp. 1227 - 1242
[PSI(+)] is a prion isoform of the yeast release factor Sup35. In some assays, the cytosolic chaperones Ssa1 and Ssb1/2 of the Hsp70 family were previously... 
Gene Expression Regulation, Fungal | Prions - metabolism | Prions - genetics | Saccharomyces cerevisiae - genetics | Adenosine Triphosphatases - metabolism | Genotype | HSP70 Heat-Shock Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | HSP70 Heat-Shock Proteins - metabolism | Escherichia coli - genetics | Plasmids | Peptide Termination Factors | Saccharomyces cerevisiae Proteins - metabolism | Proteins | Brewer's yeast | Prions
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text A bacterial global regulator forms a prion
by Yuan, Andy H and Hochschild, Ann
Science, ISSN 0036-8075, 01/2017, Volume 355, Issue 6321, pp. 198 - 198
Prions are self-propagating protein aggregates that act as protein-based elements of inheritance in fungi. Although prevalent in eukaryotes, prions have not... 
YEAST | RHO | PROTEIN | COLI | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | Amino Acid Sequence | Prions - metabolism | Rho Factor - chemistry | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Amyloid - chemistry | Saccharomyces cerevisiae Proteins - genetics | Rho Factor - metabolism | Clostridium botulinum - metabolism | Amyloid - metabolism | Escherichia coli - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Domains | Bacterial Proteins - metabolism | Rho Factor - genetics | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Physiological aspects | Prions | Proteins | Rho protein | Eukaryotes | Transcription | E coli | Bacterial proteins | Bacteria | Evolution | Genomes | Prion protein | Diseases | Fungi | Escherichia | Aggregates
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Prions in yeast
by Liebman, Susan W and Chernoff, Yury O
Genetics, ISSN 0016-6731, 08/2012, Volume 191, Issue 4, pp. 1041 - 1072
The concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that... 
TRANSMISSION ELECTRON-MICROSCOPY | SOLID-STATE NMR | CHAPERONE PROTEIN HSP104 | HET-S PRION | AMYLOID-LIKE FIBRILS | GENETICS & HEREDITY | BETA-SHEET STRUCTURE | DE-NOVO APPEARANCE | RNQ1 NONPRION DOMAIN | FUNGUS PODOSPORA-ANSERINA | RELEASE FACTOR ERF3 | Prions - physiology | Yeasts - metabolism | Physiological aspects | Genetic aspects | Research | Yeast fungi | Structure | Prions | Cell division | Genotype & phenotype | Pathology | Yeast | YeastBook
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Multiple Gln/Asn-Rich Prion Domains Confer Susceptibility to Induction of the Yeast [PSI +] Prion
by Osherovich, Lev Z and Weissman, Jonathan S
Cell, ISSN 0092-8674, 2001, Volume 106, Issue 2, pp. 183 - 194
The yeast prion [PSI ] results from self-propagating aggregates of Sup35p. De novo formation of [PSI ] requires an additional non-Mendelian trait, thought to... 
Fungal Proteins - chemistry | Molecular Chaperones - metabolism | Prions - genetics | Ataxin-3 | Machado-Joseph Disease - metabolism | Saccharomyces cerevisiae - genetics | Humans | Repressor Proteins | Peptides - genetics | Glutamine - metabolism | Molecular Sequence Data | Molecular Chaperones - chemistry | Recombinant Fusion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Nerve Tissue Proteins - chemistry | Peptides - metabolism | Glutamine - chemistry | Genes, Fungal - genetics | Asparagine - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Prions - metabolism | Gene Expression | Peptides - chemistry | Molecular Chaperones - genetics | Fungal Proteins - genetics | Prions - chemistry | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae - chemistry | Nuclear Proteins | Nerve Tissue Proteins - metabolism | Saccharomyces cerevisiae - cytology | Phenotype | Asparagine - metabolism | Glutamine - genetics | Peptide Termination Factors | Saccharomyces cerevisiae Proteins | Protein Binding | Microscopy, Fluorescence | Asparagine - chemistry | Fungal Proteins - metabolism | Physiological aspects | Protein biosynthesis | Epigenesis | Yeast | Research | Prions
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Suicidal [PSI⁺] is a lethal yeast prion
by Ryan P. McGlinchey and Dmitry Kryndushkin and Reed B. Wickner
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 3/2011, Volume 108, Issue 13, pp. 5337 - 5341
[PSI*] is a priori of the essential translation termination factor Sup35p. Although mammalian prion infections are uniformly fatal, commonly studied [PSI⁺]... 
Proteins | Yeasts | Cell growth | Plasmids | Prions | Medical genetics | Cell aggregates | Evolutionary genetics | Amyloids | Saccharomyces cerevisiae | SUPPRESSOR | SUP35 PROTEIN | IN-VITRO | DOMAIN | TRANSMISSION | MESSENGER-RNA | GENE | MULTIDISCIPLINARY SCIENCES | INCOMPATIBILITY | URE3 | SACCHAROMYCES-CEREVISIAE | Glutathione Peroxidase - metabolism | Prions - metabolism | Saccharomyces cerevisiae - physiology | Animals | Prions - genetics | Peptide Termination Factors - genetics | Saccharomyces cerevisiae - genetics | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - pathogenicity | Saccharomyces cerevisiae Proteins - genetics | Peptide Termination Factors - metabolism | Glutathione Peroxidase - genetics | Research | Yeast fungi | Properties | Health aspects | Biological Sciences
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Prions Affect the Appearance of Other Prions: The Story of [PIN +]
by Derkatch, Irina L and Bradley, Michael E and Hong, Joo Y and Liebman, Susan W
Cell, ISSN 0092-8674, 2001, Volume 106, Issue 2, pp. 171 - 182
Prions are self-propagating protein conformations. Recent research brought insight into prion propagation, but how they first appear is unknown. We previously... 
YEAST SACCHAROMYCES-CEREVISIAE | IN-VITRO | SUP35 PROTEIN | PROTEIN HSP104 | PSI+ PRION | BIOCHEMISTRY & MOLECULAR BIOLOGY | FORMING DOMAIN | PSI(+) | DE-NOVO APPEARANCE | RELEASE FACTOR | PROPAGATION | CELL BIOLOGY | Fungal Proteins - chemistry | Protein Structure, Tertiary | Prions - metabolism | Prions - genetics | Saccharomyces cerevisiae - genetics | Fungal Proteins - genetics | Prions - chemistry | Recombinant Fusion Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Saccharomyces cerevisiae - chemistry | Saccharomyces cerevisiae - metabolism | Glutathione Peroxidase | Phenotype | Models, Biological | Plasmids - genetics | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins | Protein Binding | Recombinant Fusion Proteins - genetics | Genes, Fungal - genetics | Fungal Proteins - metabolism | Physiological aspects | Prion diseases | Protein biosynthesis | Prions | Creutzfeldt-Jakob disease
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Prions
by Shkundina, I S and Ter-Avanesyan, M D
Biochemistry (Moscow), ISSN 0006-2979, 12/2007, Volume 72, Issue 13, pp. 1519 - 1536
Prions were originally defined as infectious agents of protein nature, which caused neurodegenerative diseases in animals and humans. The prion concept implies... 
Life Sciences | Biochemistry, general | conformational rearrangement | neurodegenerative disease | non-chromosomal inheritance | Microbiology | prion | Bioorganic Chemistry | Biomedicine general | PrP | Neurodegenerative disease | Prion | Conformational rearrangement | Non-chromosomal inheritance | CHAIN RELEASE FACTORS | PSI+ PRION | BIOCHEMISTRY & MOLECULAR BIOLOGY | FUNGUS PODOSPORA-ANSERINA | YEAST SACCHAROMYCES-CEREVISIAE | IN-VITRO | MESSENGER-RNA | DE-NOVO GENERATION | AMYLOID-LIKE FIBRILS | SCRAPIE PRION | TRANSLATION TERMINATION | Protein Structure, Tertiary | Molecular Chaperones - metabolism | Models, Chemical | Protein Structure, Secondary | Humans | Amyloid - chemistry | Prions - chemistry | Saccharomyces cerevisiae - metabolism | Animals | Prions - physiology | Podospora - metabolism | Models, Biological | Saccharomyces cerevisiae Proteins - metabolism | Protein Conformation | Prion Diseases - metabolism | Proteins | Genetics | Prions
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text Epigenetic control of polyamines by the prion [ PSI + ]
by Namy, Olivier and Matsufuji, Senya and Martini, Cyrielle and Rousset, Jean-Pierre and Fabret, Céline and Galopier, Aurélie
Nature Cell Biology, ISSN 1465-7392, 09/2008, Volume 10, Issue 9, pp. 1069 - 1075
Prion proteins are found in mammals and yeast, and can transmit diseases and encode heritable phenotypic traits. In Saccharomyces cerevisiae, eRF3, Rnq1, Ure2... 
YEAST | GENETIC-VARIATION | ANTIZYME | READTHROUGH | CONSERVATION | METABOLISM | ORNITHINE DECARBOXYLASE | STOP CODON | SACCHAROMYCES-CEREVISIAE | TRANSLATION TERMINATION | CELL BIOLOGY | Prions - metabolism | Saccharomyces cerevisiae - genetics | Epigenesis, Genetic | Prions - chemistry | Peptide Termination Factors - metabolism | Polyamines - metabolism | Saccharomyces cerevisiae - cytology | Saccharomyces cerevisiae - metabolism | Phenotype | Models, Biological | Intracellular Space - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Peptide Termination Factors - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Polyamines | Health aspects | Prions | Life Sciences | Microbiology and Parasitology | Biochemistry, Molecular Biology
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Full Text Hsp70/Hsp90 co‐chaperones are required for efficient Hsp104‐mediated elimination of the yeast [PSI+] prion but not for prion propagation
by Moosavi, Behrooz and Wongwigkarn, Jintana and Tuite, Mick F
Yeast, ISSN 0749-503X, 03/2010, Volume 27, Issue 3, pp. 167 - 179
The continued propagation of the yeast [PSI+] prion requires the molecular chaperone Hsp104 yet in cells engineered to overexpress Hsp104; prion propagation is... 
co‐chaperone | [PSI+] prion | chaperone | Hsp104 | Saccharomyces cerevisiae | yeast | Yeast | Co-chaperone | Chaperone | PSI | prion | TERMINAL DOMAIN | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | GUANIDINE-HYDROCHLORIDE | AGGREGATED PROTEINS | MICROBIOLOGY | SACCHAROMYCES-CEREVISIAE | PROTEIN DISAGGREGATION | DAMAGED PROTEINS | co-chaperone | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | IN-VIVO | MYCOLOGY | HSP104 INACTIVATION | CYTOSOLIC HSP70 | Prions - metabolism | Saccharomyces cerevisiae - genetics | Heat-Shock Proteins - metabolism | Mutant Proteins - genetics | HSP70 Heat-Shock Proteins - genetics | Mutant Proteins - metabolism | Cyclophilins - genetics | Cyclophilins - metabolism | Mutation, Missense | Saccharomyces cerevisiae Proteins - genetics | HSP70 Heat-Shock Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Heat-Shock Proteins - genetics | Gene Deletion | Saccharomyces cerevisiae Proteins - metabolism | HSP90 Heat-Shock Proteins - metabolism | Amino Acid Substitution - genetics | HSP90 Heat-Shock Proteins - genetics
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights