Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.
about
An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machineProteostatic control of telomerase function through TRiC-mediated folding of TCAB1The diverse members of the mammalian HSP70 machine show distinct chaperone-like activitiesTranslational control in the stress adaptive response of cancer cells: a novel role for the heat shock protein TRAP1DNAJs: more than substrate delivery to HSPALongitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative diseaseA ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stressDissecting the ER-associated degradation of a misfolded polytopic membrane protein.Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase networkA ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesisThe Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiaeThe Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosomeA mutant plasma membrane protein is stabilized upon loss of Yvh1, a novel ribosome assembly factor.Yeast Uri1p promotes translation initiation and may provide a link to cotranslational quality control.Systematic functional prioritization of protein posttranslational modifications.Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationHsf1 activation inhibits rapamycin resistance and TOR signaling in yeast revealed by combined proteomic and genetic analysisChaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesLoss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein foldingAn atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cellA chaperome subnetwork safeguards proteostasis in aging and neurodegenerative diseaseIdentification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaKHierarchy, causation and explanation: ubiquity, locality and pluralismSelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoThe challenge of improved secretory production of active pharmaceutical ingredients in Saccharomyces cerevisiae: a case study on human insulin analogs.Biochemical and biophysical characterization of the Mg2+-induced 90-kDa heat shock protein oligomers.Hsp110 is required for spindle length control.The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.BOBBER1 is a noncanonical Arabidopsis small heat shock protein required for both development and thermotolerance.Computational analysis of the human HSPH/HSPA/DNAJ family and cloning of a human HSPH/HSPA/DNAJ expression libraryPOLAR MAPPER: a computational tool for integrated visualization of protein interaction networks and mRNA expression dataElectric pulses used in electrochemotherapy and electrogene therapy do not significantly change the expression profile of genes involved in the development of cancer in malignant melanoma cells.BAG2 structure, function and involvement in disease.The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.Modulation of phosducin-like protein 3 (PhLP3) levels promotes cytoskeletal remodelling in a MAPK and RhoA-dependent manner.Protein folding in the cytoplasm and the heat shock response.Cellular strategies of protein quality control.
P2860
2b70564f03a689343a8a4b2079cb21c6974fdcec30f1b95d5c4234be64044e12ddb53400ba5a171d67ff06b86a176ed578612de3c307dc1d5addbf27695ac8211720a4e072a664b1f6e8c342c005c05b7f33116baf2a5249b946056099a36f116a3653748d6f495b4d836feef362f70d43e841db64c4bdba90148ef15e8f1b75a2462f7e641e36475b8ca649a3ca64c9267acb603327a7765e33620a51e20e9faf5cbc31753232757d62268867f53743ced282aabb054cc85547499cbd3c983af5cecd7d8eadccbdcb8e8b0b44558fa917558b1740919c4ef900ca77f6bbda3ff62f237ad59e13387c1a29dcd97be2a0
P248
Q21134999-7600FA7F-4BFA-41CC-B9C9-5B0F3505808EQ24307986-A95425F6-B9FB-4503-8EEF-E75428E678FEQ24336905-998DFB95-BC0C-4D50-A5FE-8BD45D3475B9Q24338136-CDE68F85-3224-46A2-9803-A78CFFE7668AQ26801509-2FFEAB7D-C865-4BF3-AB15-39A805ED16F3Q26865220-1C91854B-3D8C-4829-AC10-94325E9E9A6BQ27929786-1C3A08FD-674D-4392-9B03-4DA8E34FDFD7Q27930024-353EC223-3B14-4B09-9424-A22CF812F246Q27930409-21528DD9-63ED-46EE-BE4C-AAF7ECC65BAFQ27930835-0B908DE0-66C2-475F-99C7-C4AF202815D6Q27931602-7901D957-50FA-4EC0-90F7-779F8DB75B11Q27932363-EF481CCB-43CF-4052-876B-F0C72F11C295Q27934900-F5F738B5-5F7A-4218-BE50-D8802C518B1EQ27935695-A8FA7539-C62E-4440-8ADA-C57BCFDC9E1DQ27935709-19B9826D-7E75-43C1-8EE4-06BD8C410755Q27936051-420ED59D-B1E6-4C03-BB7B-7E7EEBDF787DQ27938495-1144D7A3-A545-4AA6-8B25-0326C76105C8Q27939652-7475BD17-E42E-4602-851A-FCE58D02B641Q27940000-452C8FA7-3318-45B8-94DA-B8E53656AFABQ27967631-DFDA3942-8C33-44C0-B08F-26EDA7EAC714Q28243869-069B385E-3E4C-43DF-BE88-70CCB95E9863Q28248982-6196B714-1334-490A-B8FD-2C1820A5C1C0Q28252463-914FCA13-B183-4538-9F40-88F5932A1C6BQ28535326-28BFBC08-A71D-4934-9F04-24A1EC77E200Q28732684-FB909F92-1125-439E-9661-D7F498EB8E10Q30155411-41B573C9-8497-4C00-B5E6-5B24EC524FBAQ30429479-E7EB473D-49F5-4C87-A9E4-CC4631CCB740Q30494365-26C6732D-49EF-40D2-8F0C-9B786EC2E872Q30528920-D58D4BB3-0F08-483F-91FF-A4681C6FF308Q33285637-B5BD620E-6970-4A97-8F39-F6225FF958D9Q33347365-783C28ED-B803-4B41-9376-7EDAADC4EB09Q33358423-112DC489-492F-4268-81CB-3B4D794EFD14Q33394119-481CF3D9-D859-4A59-B6D2-E0AEC07A0E06Q33497050-66A77753-E487-4AE1-8FB7-0A2CF831EB83Q33634944-CFE6BEB0-50FE-4A67-8D37-3885E8904B65Q33693921-989BD2E2-11BD-47FE-93FA-A4B0D40DFC5BQ33963685-EAC2FE21-51A1-4450-90D3-5FAB09C17553Q34102980-BBE1A598-7625-4A1E-B60E-3BBA0554733AQ34152827-B22CD23A-108C-4E6C-B384-5547D8938F83Q34199521-0944D7FB-3E59-4706-93C1-D42BC240E8D1
P2860
Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@ast
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@en
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@nl
type
label
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@ast
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@en
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@nl
prefLabel
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@ast
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@en
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@nl
P50
P3181
P1433
P1476
Systems analyses reveal two ch ...... functions in eukaryotic cells.
@en
P2093
Alice Yen-Wen Yam
Joshua Baughman
P3181
P356
10.1016/J.CELL.2005.11.039
P407
P577
2006-01-13T00:00:00Z