Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
暂无分享,去创建一个
Andreas Bracher | F. Hartl | A. Bracher | Z. Dragovic | Yasuhito Shomura | Zdravko Dragovic | Sarah A. Broadley | Y. Shomura | Sarah A Broadley | F Ulrich Hartl
[1] W. Burkholder,et al. Specificity of DnaK-peptide binding. , 1994, Journal of molecular biology.
[2] S. Ackerman,et al. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP , 2005, Nature Genetics.
[3] Bernd Bukau,et al. The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.
[4] P. Parham,et al. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis , 1990, Cell.
[5] E. O’Shea,et al. Global analysis of protein expression in yeast , 2003, Nature.
[6] R. S. Muir,et al. Gene disruption with PCR products in Saccharomyces cerevisiae. , 1995, Gene.
[7] J. Reinstein,et al. The second step of ATP binding to DnaK induces peptide release. , 1996, Journal of molecular biology.
[8] Y. Kaneko,et al. A Novel hsp110-related Gene, apg-1, That Is Abundantly Expressed in the Testis Responds to a Low Temperature Heat Shock Rather than the Traditional Elevated Temperatures* , 1997, The Journal of Biological Chemistry.
[9] M Aldea,et al. A Set of Vectors with a Tetracycline‐Regulatable Promoter System for Modulated Gene Expression in Saccharomyces cerevisiae , 1997, Yeast.
[10] J. Brodsky,et al. The Function of the Yeast Molecular Chaperone Sse1 Is Mechanistically Distinct from the Closely Related Hsp70 Family* , 2004, Journal of Biological Chemistry.
[11] M. Egerton,et al. A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. , 1996, The EMBO journal.
[12] J. Tyson,et al. Coordinated Activation of Hsp70 Chaperones , 2004, Science.
[13] A. Paetau,et al. The gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone , 2005, Nature Genetics.
[14] A. Nakai,et al. Cloning and Expression of Murine High Molecular Mass Heat Shock Proteins, HSP105 (*) , 1995, The Journal of Biological Chemistry.
[15] G. Fink,et al. Methods in yeast genetics , 1979 .
[16] P. Connell,et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins , 2000, Nature Cell Biology.
[17] C. Georgopoulos,et al. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[18] N. Yamagishi,et al. Hsp105α Suppresses Hsc70 Chaperone Activity by Inhibiting Hsc70 ATPase Activity* , 2004, Journal of Biological Chemistry.
[19] J. Frydman,et al. Hsp110 Cooperates with Different Cytosolic HSP70 Systems in a Pathway for de Novo Folding* , 2005, Journal of Biological Chemistry.
[20] Andrew Emili,et al. Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone , 2005, Cell.
[21] Bernd Bukau,et al. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor , 2006, The EMBO journal.
[22] I. Harting,et al. Mutations in SIL1 cause Marinesco-Sjögren syndrome, a cerebellar ataxia with cataract and myopathy , 2005, Nature Genetics.
[23] Loss of function mutations in SIL1 cause Marinesco–Sjögren syndrome , 2006 .
[24] Lars Packschies,et al. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange , 2001, Nature Structural Biology.
[25] J. Reinstein,et al. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. , 1997, Biochemistry.
[26] M. Mayer,et al. Bag-1M Accelerates Nucleotide Release for Human Hsc70 and Hsp70 and Can Act Concentration-dependent as Positive and Negative Cofactor* , 2001, The Journal of Biological Chemistry.
[27] F. Hartl,et al. Recombination of protein domains facilitated by co-translational folding in eukaryotes , 1997, Nature.
[28] J. Brodsky,et al. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity. , 2002, Molecular biology of the cell.
[29] Xiaoguang Liu,et al. The 170 kDa glucose regulated stress protein is a large HSP70‐ HSP110‐like protein of the endoplasmic reticulum , 1996, FEBS letters.
[30] Geoffrey J. Barton,et al. JPred : a consensus secondary structure prediction server , 1999 .
[31] Andreas Bracher,et al. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. , 2005, Molecular cell.
[32] F. Hartl,et al. Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.
[33] Johannes Buchner,et al. The Yeast Hsp110 Sse1 Functionally Interacts with the Hsp70 Chaperones Ssa and Ssb* , 2005, Journal of Biological Chemistry.
[34] J. Frydman. Folding of newly translated proteins in vivo: the role of molecular chaperones. , 2001, Annual review of biochemistry.
[35] J. Frydman,et al. Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways , 2005, Cell.
[36] T. Kuno,et al. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. , 1993, Gene.
[37] C. Guy,et al. Co-immunoprecipitation of Hsp101 with cytosolic Hsc70. , 2005, Plant physiology and biochemistry : PPB.
[38] Craig M. Ogata,et al. Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK , 1996, Science.
[39] D. Cyr,et al. Protein Folding Activity of Hsp70 Is Modified Differentially by the Hsp40 Co-chaperones Sis1 and Ydj1* , 1998, The Journal of Biological Chemistry.
[40] Yoshiyuki Kaneko,et al. The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s , 2000, Cell stress & chaperones.
[41] J. Subjeck,et al. hsp110 Protects Heat-denatured Proteins and Confers Cellular Thermoresistance* , 1997, The Journal of Biological Chemistry.
[42] F. Hartl,et al. Function of Trigger Factor and DnaK in Multidomain Protein Folding Increase in Yield at the Expense of Folding Speed , 2004, Cell.
[43] D. Thiele,et al. The Yeast Hsp110 Family Member, Sse1, Is an Hsp90 Cochaperone* , 1999, The Journal of Biological Chemistry.
[44] N. Yamagishi,et al. Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity. , 2004, The Journal of biological chemistry.
[45] M. Weiner,et al. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. , 1994, Gene.
[46] F. Hartl,et al. Regulation of the Heat-shock Protein 70 Reaction Cycle by the Mammalian DnaJ Homolog, Hsp40* , 1996, The Journal of Biological Chemistry.
[47] R. Sikorski,et al. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. , 1989, Genetics.
[48] E. Repasky,et al. Characterization of native interaction of hsp110 with hsp25 and hsc70 , 2000, FEBS letters.
[49] R. Burd,et al. Identification of a Major Subfamily of Large hsp70-like Proteins through the Cloning of the Mammalian 110-kDa Heat Shock Protein (*) , 1995, The Journal of Biological Chemistry.