Crossref journal-article
Elsevier BV
Current Opinion in Microbiology (78)
Bibliography

Craig, E. A., Eisenman, H. C., & Hundley, H. A. (2003). Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding? Current Opinion in Microbiology, 6(2), 157–162.

Authors 3
  1. Elizabeth A Craig (first)
  2. Helene C Eisenman (additional)
  3. Heather A Hundley (additional)
References 47 Referenced 71
  1. 10.1016/S0959-440X(99)00045-7 / Curr. Opin. Struct. Biol. / Implications of macromolecular crowding for protein assembly by Minton (2000)
  2. 10.1021/bi00227a001 / Biochemistry / Protein folding: local structures, domains, subunits, and assemblies by Jaenicke (1991)
  3. 10.1016/S0959-440X(99)80012-8 / Curr. Opin. Struct. Biol. / The fundamentals of protein folding: bringing together theory and experiment by Dobson (1999)
  4. 10.1016/0022-2836(67)90301-4 / J. Mol. Biol. / Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding by Malkin (1967)
  5. 10.1016/S0092-8674(00)80928-9 / Cell / The Hsp70 and Hsp60 chaperone machines by Bukau (1998)
  6. 10.1146/annurev.biochem.70.1.603 / Annu. Rev. Biochem. / Folding of newly translated proteins in vivo: the role of molecular chaperones by Frydman (2001)
  7. 10.1126/science.1068408 / Science / Molecular chaperones in the cytosol: from nascent chain to folded protein by Hartl (2002)
  8. 10.1073/pnas.93.9.4437 / Proc. Natl. Acad. Sci. U.S.A. / Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains by Hesterkamp (1996)
  9. 10.1093/emboj/17.14.3981 / EMBO J. / The molecular chaperone Ssb from S. cerevisiae is a component of the ribosome-nascent chain complex by Pfund (1998)
  10. 10.1093/emboj/16.1.54 / EMBO J. / Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding by Scholz (1997)
  11. 10.1002/j.1460-2075.1995.tb00177.x / EMBO J. / A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor by Stoller (1995)
  12. 10.1073/pnas.261432298 / Proc. Natl. Acad Sci. USA / Binding specificity of Escherichia coli trigger factor by Patzelt (2001)
  13. 10.1073/pnas.062048399 / Proc. Natl. Acad. Sci. USA / The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain by Hundley (2002)
  14. 10.1073/pnas.95.26.15253 / Proc. Natl. Acad Sci. USA / The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains by Lopez-Buesa (1998)
  15. 10.1126/science.275.5298.387 / Science / Functional specificity among Hsp70 molecular chaperones by James (1997)
  16. 10.1091/mbc.12.12.3773 / Mol. Biol. Cell / Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared to other Hsp70s by Pfund (2001)
  17. 10.1515/BC.2002.182 / Biol. Chem. / Three-state equilibrium of Escherichia coli trigger factor by Patzelt (2002)
  18. 10.1093/emboj/17.16.4809 / EMBO J. / Zuotin, a ribosome-associated DnaJ molecular chaperone by Yan (1998)
  19. 10.1073/pnas.071057198 / Proc. Natl. Acad Sci. USA / RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin by Gautschi (2001)
  20. 10.1073/pnas.062048599 / Proc. Natl. Acad Sci. USA / A functional chaperone triad on the yeast ribosome by Gautschi (2002)
  21. 10.1016/S0092-8674(00)80787-4 / Cell / Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains by Teter (1999)
  22. 10.1038/23301 / Nature / Trigger factor and DnaK cooperate in folding of newly synthesized proteins by Deuerling (1999)
  23. 10.1016/S0003-9861(02)00213-8 / Arch. Biochem. Biophys. / The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor by Kramer (2002)
  24. 10.1093/emboj/16.7.1501 / EMBO J. / Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries by Rudiger (1997)
  25. 10.1074/jbc.M205950200 / J. Biol. Chem. / Trigger factor retards protein export in Escherichia coli by Lee (2002)
  26. 10.1006/jmbi.2000.5192 / J. Mol. Biol. / Dynamic association of trigger factor with protein substrates by Maier (2001)
  27. 10.1038/nsb804 / Nat. Struct. Biol. / The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase by Schiene-Fischer (2002)
  28. 10.1073/pnas.95.22.12860 / Proc. Natl. Acad Sci. USA / Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the Ssa class of cytosolic yeast Hsp70 proteins by Kim (1998)
  29. 10.1083/jcb.149.3.591 / J. Cell Biol. / The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking by McCallum (2000)
  30. 10.1083/jcb.145.2.265 / J. Cell. Biol. / Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins by Hansen (1999)
  31. 10.1093/emboj/18.1.75 / EMBO J. / Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system by Siegers (1999)
  32. 10.1016/S0092-8674(00)00165-3 / Cell / Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins by Siegert (2000)
  33. 10.1038/nature01047 / Nature / L23 protein functions as a chaperone docking site on the ribosome by Kramer (2002)
  34. 10.1128/JB.181.10.3136-3143.1999 / J. Bacteriol. / SSB, encoding a ribosome-associated chaperone, is coordinately regulated with ribosomal protein genes by Lopez (1999)
  35. 10.1016/0092-8674(92)90269-I / Cell / The translation machinery and seventy kilodalton heat shock protein cooperate in protein synthesis by Nelson (1992)
  36. 10.1126/science.1073997 / Science / Instruction of translating ribosome by nascent peptide by Gong (2002)
  37. 10.1016/S0092-8674(02)00649-9 / Cell / The ribosomal exit tunnel functions as a discriminating gate by Nakatogawa (2002)
  38. 10.1126/science.1072366 / Science / Distinct modes of signal recognition particle interaction with the ribosome by Pool (2002)
  39. 10.1016/S0092-8674(01)00539-6 / Cell / Structure of the 80S ribosome from Saccharomyces cerevisiae–tRNA–ribosome and subunit–subunit interactions by Spahn (2001)
  40. 10.1126/science.289.5481.920 / Science / The structural basis of ribosome activity in peptide bond synthesis by Nissen (2000)
  41. 10.1126/science.289.5481.905 / Science / The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution by Ban (2000)
  42. 10.1126/science.2188360 / Science / Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly by Beckmann (1990)
  43. 10.1093/emboj/18.1.85 / EMBO J. / In vivo newly translated polypeptides are sequestered in a protected folding environment by Thulasiraman (1999)
  44. 10.1006/geno.1995.9969 / Genomics / Cloning and chromosomal localization of a mouse cDNA with homology to the Saccharomyces cerevisiae gene zuotin by Hughes (1995)
  45. 10.1074/jbc.270.42.24818 / J. Biol. Chem. / MIDA1, a protein associated with Id, regulates cell growth by Shoji (1996)
  46. 10.1093/emboj/cdf315 / EMBO J. / A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes by Dudek (2002)
  47. 10.1016/S0022-2836(02)01427-4 / J. Mol. Biol. / Interaction of trigger factor with the ribosome by Maier (2003)
Dates
Type When
Created 22 years, 3 months ago (May 12, 2003, 7:10 p.m.)
Deposited 5 years, 5 months ago (March 18, 2020, 8:23 a.m.)
Indexed 1 month ago (July 25, 2025, 6:07 a.m.)
Issued 22 years, 4 months ago (April 1, 2003)
Published 22 years, 4 months ago (April 1, 2003)
Published Print 22 years, 4 months ago (April 1, 2003)
Funders 0

None

@article{Craig_2003, title={Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding?}, volume={6}, ISSN={1369-5274}, url={http://dx.doi.org/10.1016/s1369-5274(03)00030-4}, DOI={10.1016/s1369-5274(03)00030-4}, number={2}, journal={Current Opinion in Microbiology}, publisher={Elsevier BV}, author={Craig, Elizabeth A and Eisenman, Helene C and Hundley, Heather A}, year={2003}, month=apr, pages={157–162} }