The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases.
about
Metabolic fate of the increased yeast amino Acid uptake subsequent to catabolite derepressionYeast prions [URE3] and [PSI+] are diseasesStructure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamilyMoonlighting proteins in yeastsEukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modelingPrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseThe crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2pRole of GATA factor Nil2p in nitrogen regulation of gene expression in Saccharomyces cerevisiae.The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms.Sequence of the GLN1 gene of Saccharomyces cerevisiae: role of the upstream region in regulation of glutamine synthetase expression.Role of the GATA factors Gln3p and Nil1p of Saccharomyces cerevisiae in the expression of nitrogen-regulated genes.The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant.Interaction of the GATA factor Gln3p with the nitrogen regulator Ure2p in Saccharomyces cerevisiaeRegulators of pseudohyphal differentiation in Saccharomyces cerevisiae identified through multicopy suppressor analysis in ammonium permease mutant strainsThe URE2 protein regulates nitrogen catabolic gene expression through the GATAA-containing UASNTR element in Saccharomyces cerevisiaeCross regulation of four GATA factors that control nitrogen catabolic gene expression in Saccharomyces cerevisiae.Gat1p, a GATA family protein whose production is sensitive to nitrogen catabolite repression, participates in transcriptional activation of nitrogen-catabolic genes in Saccharomyces cerevisiaeA co-activator of nitrogen-regulated transcription in Saccharomyces cerevisiae.A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae.A novel Rtg2p activity regulates nitrogen catabolism in yeast.The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae.AUA1, a gene involved in ammonia regulation of amino acid transport in Saccharomyces cerevisiae.Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathwaySequence analysis of a gene cluster involved in metabolism of 2,4,5-trichlorophenoxyacetic acid by Burkholderia cepacia AC1100A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structureRapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteinsThe TOR signaling cascade regulates gene expression in response to nutrientsPrions in Saccharomyces and Podospora spp.: protein-based inheritance.Structure of the prion Ure2p in protein fibrils assembled in vitro.Prions, amyloids, and RNA: Pieces of a puzzle.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Two prion-inducing regions of Ure2p are nonoverlapping.Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis.Improvement of nitrogen assimilation and fermentation kinetics under enological conditions by derepression of alternative nitrogen-assimilatory pathways in an industrial Saccharomyces cerevisiae strain.[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.RTG-dependent mitochondria-to-nucleus signaling is regulated by MKS1 and is linked to formation of yeast prion [URE3]Induction of distinct [URE3] yeast prion strains.Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein.The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation.The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
P2860
Q21284853-C793E38B-D37C-43AA-BC19-5B3ABD3F4B88Q24532887-C7312AE8-5E7C-4F2E-84A6-1B1470F4B558Q24533519-4A1DBB2D-0B27-4E0D-BEFD-DE7A398C41E6Q24653315-3C5A5289-CFC1-4EFC-AB8D-59BA586A9442Q24675628-856A4471-C51D-4456-B8DE-897866554242Q26753190-A16999F4-9B19-470C-8B9B-6C37FE3F6303Q27629457-8BD26F3B-61B8-4C37-BA85-FC8B7B360137Q27930651-E01AD34A-8D02-4981-94B8-966FE6DF312FQ27931000-D8BA4A8A-67A2-476D-B923-B48882539118Q27931010-FC987387-5D32-4A74-9006-C6626E69CA18Q27932214-04C8CACE-E869-4D61-BBC5-CE5B7488C6C8Q27932232-B31D6A74-C8A9-4ECB-A9DE-BA268E07280EQ27932418-4CF00380-26CE-4348-BAF5-30C5C208002EQ27932900-B2367C9A-9868-4464-BBB1-3A97927FBF0AQ27933071-505C31D2-4D2E-4351-B621-09651626F03BQ27933927-67B61310-190E-4F89-82A9-E4AFB3845D5FQ27934821-942B7EB8-6A0F-44DC-94D2-5D0F53DC1767Q27936721-99F79698-8572-4D98-8BDB-E479D76A25F7Q27937093-AF15D647-E5E6-4323-9343-259C6F5EBC90Q27937973-1EBAA7CC-8DCC-4A2C-A154-EAA5C707E4EBQ27938774-FEF4791F-10B4-422B-94FF-7A8379975D59Q27940071-50D70F68-638D-4F52-A5C2-73653B492F56Q28291202-2923A54D-24C5-463E-B11E-6AC8E744AF6EQ28367682-966793DC-B471-4DF4-AF90-4F84D7AD8472Q28395735-2F73DFF4-EA2C-4A7D-B74E-A5C835C0F739Q29617782-5C3B30E3-738B-4E6C-A7F3-68C8FB72C334Q29620801-37B0B3DB-F3DC-427F-8779-93DA86257AA8Q30323934-BDCE7841-7387-4E28-BAA0-2BD407939D5EQ33222590-5FEB100C-53A9-4A02-86F4-676B8F427521Q33363261-CBC4373F-613A-498E-920A-4257234F3863Q33575482-8685F3B3-D884-4C43-B540-D9AE45D85C03Q33652620-E51138F8-F350-4404-B0B1-00BE5FAE43A5Q33686960-E045D13E-2E48-482E-A5FE-9D62FD5CED20Q33717851-14F0DFC5-B22B-4387-9F10-CA4825027EC2Q33966712-7282EC4A-5BA0-4836-86B3-5D0EAB5E3C07Q34011717-A5339426-90BF-44A0-8692-8A9A3C93F59DQ34012527-E9B988F4-D32E-48C9-B949-97D74B3DD575Q34024232-49611B7C-E1CB-4F3D-AB0D-B4E1416FEC02Q34046537-280AFD2D-1F4C-45AA-86B3-109323742997Q34089293-26F70D29-AAD3-4C50-BE68-F50551AB56C1
P2860
The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@ast
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@en
type
label
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@ast
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@en
prefLabel
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@ast
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@en
P2860
P356
P1476
The URE2 gene product of Sacch ...... to glutathione s-transferases.
@en
P2093
B Magasanik
P W Coschigano
P2860
P304
P356
10.1128/MCB.11.2.822
P407
P577
1991-02-01T00:00:00Z