about
Metazoan Hsp70-based protein disaggregases: emergence and mechanismsIts substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.Molecular chaperones and protein quality controlSelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoStructural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMRPathways of allosteric regulation in Hsp70 chaperones.ClpS is an essential component of the N-end rule pathway in Escherichia coli.Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.Getting newly synthesized proteins into shape.The heat shock response of Escherichia coli.Molecular basis for interactions of the DnaK chaperone with substrates.Structure and function of the molecular chaperone Trigger Factor.Metazoan Hsp70 machines use Hsp110 to power protein disaggregationRegulation of the Escherichia coli heat-shock response.Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.Alternative modes of client binding enable functional plasticity of Hsp70.Hsp70 chaperone machines.Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question.Monitoring protein misfolding by site-specific labeling of proteins in vivoMechanism of substrate recognition by Hsp70 chaperones.Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolismDelta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures.Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.Co-translational mechanisms of protein maturation.SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Reconstitution of maltose transport in Escherichia coli: conditions affecting import of maltose-binding protein into the periplasm of calcium-treated cells.Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators.Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux.Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32The C terminus of sigma(32) is not essential for degradation by FtsH.Global profiling of SRP interaction with nascent polypeptides.Ca2+-induced permeabilization of the Escherichia coli outer membrane: comparison of transformation and reconstitution of binding-protein-dependent transport.DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase.
P50
Q26779046-BCAD4D3D-F214-438C-B578-E2F35FE36EDDQ28354756-74F128C0-35FF-4AF0-8B1F-35B3E52988FFQ29617795-556438D7-69CF-4136-A35F-AE7E73E827EEQ30155411-6705877E-6821-4BF4-BDDA-619E9CB4ED8BQ30392115-318CA0F8-3F6F-4901-A2D4-1831E902BDE8Q30667048-67219A8A-C224-4480-A9D6-59309DA5AB4BQ33233474-89F44A90-8987-425A-8378-C257517C2493Q33575042-12A9F019-BB98-432A-A4D7-2D91C7C82547Q33901641-26F2553B-BA11-4E04-8DDE-F2D3D0F617FCQ33903993-FB087646-4E79-48E6-9219-2BCC9888198FQ34081455-FAEDB5D6-E35D-4C76-A081-E2165C5882B9Q34096951-DFE27315-3437-4049-8611-75E3265A0D2CQ34300523-4550A52C-29D2-4A20-81A0-6BD8E4D3AF0DQ34321688-D4F9207D-2ACB-43D5-9325-C8D520831A25Q34432136-F9A03F5E-B058-4320-8325-5D64429EF73CQ34543463-77DF3AEB-03BE-4F02-B08F-FA22C166ADD1Q34545594-37E99193-A805-44D8-8562-25A9E9C9F2F5Q35021869-78424910-01E2-45A2-8755-B42788C98904Q35184782-6676E9CC-A554-45C1-A90C-1C318B7E6147Q35843735-CCD32D3F-15E7-47E5-A2A9-BABB8E8F34B3Q36176422-DB3962B7-FC4C-4B9E-B3F7-8F2C8C80C09BQ36184113-B5E62169-F7E9-4337-BBCD-EAFE3F61C7BCQ36795860-D4FDDD44-78D6-477C-80DA-B47C0681E478Q37479435-F9CC6F54-7E9B-446F-8BCA-CEF4049B5507Q37639742-09B18DF5-3107-48D4-8755-AC66D879F30FQ37697966-E4C7DE7D-B021-463A-83B1-342E177E8352Q37802039-7CB226B6-8598-4BC9-973B-4F8137252162Q38203704-564A1F67-9AE8-4789-A983-5923271AA9F9Q38290386-1C3CFE4E-AFAE-47B8-9811-407BD0E6D09AQ38354638-11E7DD2E-A4A0-4B06-A2E7-777FBAE7DD73Q38574252-DBAC8BB5-04FD-4A1D-BC8F-4015854E4E3CQ38616124-FF2C424A-3724-4896-94EB-7DA5FFCFA4E9Q39496028-D1ED6754-27B0-4E05-AFBB-F3F654D23079Q39527378-B2F4A78C-34CC-4053-A8EC-BC9116996F1BQ39529450-9A08E83D-117D-4CA4-941A-08DBCB2008C2Q39980704-F01A7C78-D3AF-4956-A097-9D5569494788Q40874220-FD6EA0B9-9592-4562-A12C-99A2A28A9176Q41063873-D85FCECC-4BF0-451E-8B16-C4DA0F98F5ADQ41239669-166BA6F9-BC3A-4A99-8FC8-108B31C654B1Q41257359-9364DA31-AC1E-4C10-9D02-B2330CD36DE8