References
- Science v.286 Setting the standards: quality control in the secretory pathway Ellgaard,L.;M.Molinari;A.Helenius https://doi.org/10.1126/science.286.5446.1882
- Curr. Opin. Cell Biol. v.7 Quality control in the secretory pathway Hammond,C.;A.Helenius https://doi.org/10.1016/0955-0674(95)80009-3
- Nature v.306 Immunoglobulin heavy chain binding protein Haas,I.G.;M.WabI https://doi.org/10.1038/306387a0
- Nature v.355 Protein folding in the cell Gething,M.J.;J.Sambrook https://doi.org/10.1038/355033a0
- Cell v.92 BiP maintains the permeability barrier of the ER membrane by sealing the luminal end of the translocon pore before and early in translocation Hamman,B.D.;L.M.Hendershot;A.E.Johnson https://doi.org/10.1016/S0092-8674(00)81403-8
- J. Biol. Chem. v.274 The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct Brodsky,J.L.;E.D.Werner;M.E.Dubas;J.L.Goeckeler;K.B.Kruse;A.A.McCracken https://doi.org/10.1074/jbc.274.6.3453
- Nat. Cell Biol. v.2 Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response Bertolotti,A.;Y.Zhang;L.M.Hendershot;H.P.Harding;D.Ron https://doi.org/10.1038/35014014
- J. Mol. Evol. v.38 Molecular evolution of the Hsp70 multigene family Boorstein,W.R.;T.Ziegelhoffer;E.A.Craig
- Proc. Natl. Acad. Sci. USA v.88 Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK Liberek,K.;J.Marszalek;D.Ang;C.Georgopoulos;M.Zylicz https://doi.org/10.1073/pnas.88.7.2874
- Proc. Natl. Acad. Sci. USA v.91 The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE Szabo,A.;T.Langer;H.Schroder;J.Flanagan;B.Bukau;F.U.Hartl https://doi.org/10.1073/pnas.91.22.10345
- J. Biol. Chem. v.271 Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40 Minami,Y.;J.Hohfeld;K.Ohtsuka;F.U.Hartl https://doi.org/10.1074/jbc.271.32.19617
- EMBO J. v.17 BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release Bimston,D.;J.Song;D.Winchester;S.Takayama;J.C.Reed;R.I.Morimoto https://doi.org/10.1093/emboj/17.23.6871
- EMBO J. v.16 GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 Hohfeld,J.;S.Jentsch https://doi.org/10.1093/emboj/16.20.6209
- J. Biol. Chem. v.273 Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein Raynes,D.A.;V.Guerriero,Jr. https://doi.org/10.1074/jbc.273.49.32883
- Cell v.83 Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle Hohfeld,J.;Y.Minami;F.U.Hartl https://doi.org/10.1016/0092-8674(95)90099-3
- J. Biol. Chem. v.273 Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery Chen,S.;D.F.Smith https://doi.org/10.1074/jbc.273.52.35194
- J. Biol. Chem. v.273 Hop modulates hsp70/hsp90 interactions in protein folding Johnson,B.D.;R.J.Schumacher;E.D.Ross;D.O.Toft https://doi.org/10.1074/jbc.273.6.3679
- Mol. Cell. Biol. v.19 Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions Ballinger,C.A.;P.Connell;Y.Wu;Z.Hu;L.J.Thompson;L.Y.Yin;C.Patterson https://doi.org/10.1128/MCB.19.6.4535
- Biol. Chem. v.380 A Scj1p homolog and folding catalysts present in dog pancreas microsomes Bies,C.;S.Guth;K.Janoschek;W.J.Nastainczyk;Volkmer;R.Zimmermann https://doi.org/10.1515/BC.1999.149
- Gene v.153 Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins Brightman,S.E.;G.L.Blatch;B.R.Zetter https://doi.org/10.1016/0378-1119(94)00741-A
- J. Biol. Chem. v.277 Identification and characterization of a novel ER DnaJ homologue, which stimulates BiP's ATPase activity in vitro and is induced by ER stress Shen,Y.;L.Meunier;L.M.Hendershot https://doi.org/10.1074/jbc.M112214200
- Biol. Chem. v.380 Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog Skowronek,M.H.;M.Rotter;I.G.Haas https://doi.org/10.1515/BC.1999.142
- J. Biol. Chem. v.275 HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells Yu,M.;R.H.Haslam;D.B.Haslam https://doi.org/10.1074/jbc.M000739200
- Mol. Cell. Biol. v.20 Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum Kabani,M.;J.M.Beckerich;C.Gaillardin https://doi.org/10.1128/MCB.20.18.6923-6934.2000
- EMBO J. v.19 LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum Tyson,J.R.;C.J.Stirling https://doi.org/10.1093/emboj/19.23.6440
- J. Biol. Chem. v.269 The immunoglobulin-binding protein in vitro autophposphylation site maps to a threonine within the ATP binding cleft but is not a detectable site of in vivo phosphorylation Gaut,J.R.;L.M.Hendershot
- EMBO J. v.8 Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides Kassenbrock,C.K.;R.B.Kelly
- J. Biol. Chem. v.270 In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis Wei,J.;J.R.Gaut;L.M.Hendershot https://doi.org/10.1074/jbc.270.44.26677
- FEBS Lett. v.380 The 170 kDa glucose regulated stress protein is a large Hsp7-, Hsp110-like protein of the endoplasmic reticulum Chen,X.;D.Easton;H.J.Oh;D.S.Lee-Yoon;X.Liu;J.Subject https://doi.org/10.1016/0014-5793(96)00011-7
- Cell v.80 Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity Takayama,S.;T.Sato;S.Krajewski;K.Kochel;S.Irie;J.A.Millan;J.C.Reed https://doi.org/10.1016/0092-8674(95)90410-7
- EMBO J. v.16 BAG-1 modulates the chaperone activity of Hsp70/Hsc70 Takayama,S.;D.N.Bimston;S.Matsuzawa;B.C.Freeman;C.Aime-Sempe;Z.Xie;R.I.Morimoto;J.C.Reed https://doi.org/10.1093/emboj/16.16.4887
- Proc. Natl. Acad. Sci. USA v.89 Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation Carlino,A.;H.Toledo;D.Skaleris;R.DeLisio;H.Weissbach;N.Brot https://doi.org/10.1073/pnas.89.6.2081
- EMBO J. v.11 Interconversion of three differentially modified and assembled forms of BiP Freiden,P.J.;J.R.Gaut;L.M.Hendershot
- FEBS Lett. v.435 Mictochodrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum Brodsky,J.L.;M.Bauerle;M.Horst;A.J.McClellan https://doi.org/10.1016/S0014-5793(98)01065-5