Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae.
about
Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail AnchorA Conserved Archaeal Pathway for Tail-Anchored Membrane Protein InsertionThe mechanism of membrane-associated steps in tail-anchored protein insertionTail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologueGlycerophosphocholine catabolism as a new route for choline formation for phosphatidylcholine synthesis by the Kennedy pathway.Yeast Pgc1p (YPL206c) controls the amount of phosphatidylglycerol via a phospholipase C-type degradation mechanismHph1p and Hph2p, novel components of calcineurin-mediated stress responses in Saccharomyces cerevisiae.A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum.Csm4, in collaboration with Ndj1, mediates telomere-led chromosome dynamics and recombination during yeast meiosis.Csm4-dependent telomere movement on nuclear envelope promotes meiotic recombination.The GET complex mediates insertion of tail-anchored proteins into the ER membrane.Prm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion.The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteinsKaryopherin-mediated import of integral inner nuclear membrane proteins.Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae.High confidence proteomic analysis of yeast LDs identifies additional droplet proteins and reveals connections to dolichol synthesis and sterol acetylation.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritanceBiogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum.Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.Tiered assembly of the yeast Far3-7-8-9-10-11 complex at the endoplasmic reticulumErgosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes.The yeast PUF protein Puf5 has Pop2-independent roles in response to DNA replication stress.Inheritance of cortical ER in yeast is required for normal septin organization.The essentials of protein import in the degenerate mitochondrion of Entamoeba histolyticaImporting mitochondrial proteins: machineries and mechanismsNuclear fusion and genome encounter during yeast zygote formationImmobility, inheritance and plasticity of shape of the yeast nucleus.In search of tail-anchored protein machinery in plants: reevaluating the role of arsenite transporters.Localization of the Carnation Italian ringspot virus replication protein p36 to the mitochondrial outer membrane is mediated by an internal targeting signal and the TOM complex.Hydrophobic profiles of the tail anchors in SLMAP dictate subcellular targeting.CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes.Interorganelle interactions and inheritance patterns of nuclei and vacuoles in budding yeast meiosis.Clearing tail-anchored proteins from mitochondria.Predicting the targeting of tail-anchored proteins to subcellular compartments in mammalian cells.Seamless gene tagging by endonuclease-driven homologous recombinationMembrane protein insertion at the endoplasmic reticulum.A complete set of SNAREs in yeast.Differential gradients of interaction affinities drive efficient targeting and recycling in the GET pathway
P2860
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
P248
Q27315888-0929BDD2-D953-443C-8284-5D70CBA57538Q27666278-05B39339-F4BC-45CB-BB14-ED04BD928F65Q27671975-4DCA9F1C-CA2D-4BE2-BC1E-1C19FE5AAB60Q27675864-4C6A7567-8770-458D-845B-37B116658172Q27929910-E978FE78-14D4-45FB-8240-FA6A444664EDQ27930234-DA9195D8-6155-4E3E-959E-C23339437817Q27930998-8BD18D0B-65F7-4084-B9CB-CF6E3CF0098BQ27931629-BA3F3A7D-5E11-4468-8F01-01E6827E657CQ27931634-C2A0B0D7-F7BD-4DC5-A166-83EBC476356FQ27931695-32C248A7-4A4F-47BE-8927-B21DD4C5C995Q27932687-677DB95A-A5A3-47D8-91C1-4F47BF6FE4D4Q27933142-6BB656CD-1D5B-49F2-BBBA-D37AAB29BD61Q27933340-56B2C1D2-FEA9-43BF-A2CF-A2A269FDDD77Q27933578-20A3CCA5-987F-4243-8BC1-C70BE83F677DQ27934124-5AFD7B48-E8A5-4290-B3B3-6DB951AC3ED1Q27934676-7E6544DE-90D1-454F-8AB0-46A36AB70D19Q27934755-DC2E3EDE-57CB-4F9D-A649-566ECF6DD127Q27936282-826E15A7-D465-4BC2-9D25-292987BA3157Q27937853-F12AA350-56F5-408C-A042-8BA23881D785Q27937897-B81197C3-FF2D-4B7C-A215-ECB000FBAEEFQ27938024-7D1B7C51-29BC-482C-B858-094083C6D9F5Q27939085-5F90E470-3FA0-49AF-A37E-49D9AC405AE7Q27939155-A37ABF8E-5D79-4729-8905-E331F70FDF2DQ27939702-793DF6D2-AABC-4E28-8EED-05EA3B06BEF4Q27940243-2D5DF818-59E1-4422-A444-90FBD95E2FFCQ28473253-7CEC11D7-EACE-4D1D-AE1B-4146FBB72362Q29616477-04B31B04-7B24-4D89-9EC7-3C62DF59F00FQ30438859-86A89C1C-FE5A-417D-AF4E-0601B627D0E3Q30481145-C03BBAA2-A9A0-4F19-ACFC-4CBB03E319EAQ30844370-0B9E04A5-B79F-4098-972B-1248C6A7548BQ33371376-31021DCD-1694-41C2-BA11-1CF1421E8BE0Q33470754-F99FA2C7-F961-4660-A07B-FDDCDB7C6896Q33516454-9CA752BB-54AE-488C-86B0-B35CDA228F97Q33577545-61E430E4-E7A0-422D-9802-25C744C2D1D1Q33730395-59A517E3-27AB-4940-9587-21B776637ECBQ33743186-8E9B6A88-FEC8-4D16-8AE0-F608EC8EFED0Q34018811-C85E5EBA-ED0A-4FA5-8BAE-0F44E2FDDB67Q34179638-C7A52BB5-0776-46A3-8BE5-EE29DAA8DF41Q34283635-A2333733-E7CD-4205-A123-2F1E18F52DF1Q34581057-26D1439F-962B-4125-9866-0A73EFEEB730
P2860
Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@ast
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@en
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@nl
type
label
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@ast
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@en
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@nl
prefLabel
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@ast
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@en
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@nl
P2860
P50
P3181
P356
P1476
Bipartite signals mediate subc ...... s in Saccharomyces cerevisiae.
@en
P2093
Billie Egan
Kay Hofmann
P2860
P304
P3181
P356
10.1074/JBC.M212725200
P407
P577
2003-03-07T00:00:00Z