Crossref journal-article
Elsevier BV
Cell (78)
Bibliography

Babbitt, S. E., Kiss, A., Deffenbaugh, A. E., Chang, Y.-H., Bailly, E., Erdjument-Bromage, H., Tempst, P., Buranda, T., Sklar, L. A., Baumler, J., Gogol, E., & Skowyra, D. (2005). RETRACTED: ATP Hydrolysis-Dependent Disassembly of the 26S Proteasome Is Part of the Catalytic Cycle. Cell, 121(4), 553–565.

Authors 12
  1. Shalon E. Babbitt (first)
  2. Alexi Kiss (additional)
  3. Andrew E. Deffenbaugh (additional)
  4. Yie-Hwa Chang (additional)
  5. Eric Bailly (additional)
  6. Hediye Erdjument-Bromage (additional)
  7. Paul Tempst (additional)
  8. Tione Buranda (additional)
  9. Larry A. Sklar (additional)
  10. Jennifer Baumler (additional)
  11. Edward Gogol (additional)
  12. Dorota Skowyra (additional)
References 52 Referenced 100
  1. 10.1021/bi981482i / Biochemistry / Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity by Adams (1998)
  2. 10.1016/S0021-9258(17)45274-4 / J. Biol. Chem. / Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity by Armon (1990)
  3. 10.1016/S1097-2765(02)00775-X / Mol. Cell / ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation by Benaroudj (2003)
  4. 10.1038/12043 / Nat. Cell Biol. / The base of the proteasome regulatory particle exhibits chaperone-like activity by Braun (1999)
  5. 10.1021/jp983842h / J. Phys. Chem. / Ligand receptor dynamics at streptavidin-coated particle surfaces: a flow cytometric and spectrofluorometric study by Buranda (1999)
  6. 10.1126/science.2538923 / Science / A multiubiuqitin chain is confined to specific lysine in a targeted short-lived protein by Chau (1989)
  7. 10.1016/S0092-8674(03)00641-X / Cell / Release of ubiquitin-charged Cdc34-S~Ub from the RING domain is essential for ubiquitination of the SCFCdc4-bound substrate Sic1 by Deffenbaugh (2003)
  8. 10.1016/S0021-9258(17)37244-7 / J. Biol. Chem. / A 26S protease subunit that binds ubiquitin conjugates by Deveraux (1994)
  9. 10.1016/S0021-9258(19)34041-4 / J. Biol. Chem. / The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex, which degrades ubiquitin-conjugated proteins by Driscoll (1990)
  10. 10.1073/pnas.86.20.7751 / Proc. Natl. Acad. Sci. USA / ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin by Eytan (1989)
  11. 10.1016/S1097-2765(04)00026-7 / Mol. Cell / Proteasomal ATPases link ubiquitination of histone H2B to methylation of histone H3 by Eshkova (2004)
  12. 10.1016/S1097-2765(01)00250-7 / Mol. Cell / The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II by Ferdous (2001)
  13. 10.1006/jsbi.1996.0030 / J. Struct. Biol. / SPIDER and WEB: processing and visualization of images in 3D electron microscopy and other fields by Frank (1996)
  14. 10.1016/S0021-9258(18)37771-8 / J. Biol. Chem. / A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation by Ganoth (1988)
  15. 10.1038/415141a / Nature / Functional organization of the yeast proteome by systematic analysis of protein complexes by Gavin (2002)
  16. 10.1101/gad.869601 / Genes Dev. / The 19S complex of the proteasome regulates nucleotide excision repair in yeast by Gillette (2001)
  17. 10.1016/S0092-8674(00)81603-7 / Cell / A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and elF3 by Glickman (1998)
  18. 10.1016/j.cell.2004.10.019 / Cell / Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-based ubiquitin ligases by Goldenberg (2004)
  19. 10.1126/science.1069490 / Science / Recruitment of a 19S proteasome subcomplex to an activated promoter by Gonzales (2002)
  20. 10.1038/80992 / Nat. Struct. Biol. / A gated channel into the proteasome core particle by Groll (2000)
  21. 10.1038/386463a0 / Nature / Structure of the 20S proteasome from yeast at 2.4A resolution by Groll (1997)
  22. 10.1006/jmbi.2001.5285 / J. Mol. Biol. / 26S proteasomes function as stable entities by Hendil (2002)
  23. 10.1023/A:1006892220996 / Mol. Biol. Rep. / Effects of nucleotides on assembly of the 26S proteasome and degradation of ubiquitin conjugates by Hoffman (1997)
  24. 10.1038/sj.emboj.7600262 / EMBO J. / Two-substrate association with the 20S proteasome at single-molecule level by Hutschenreiter (2004)
  25. 10.1101/gad.13.9.1190 / Genes Dev. / Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets by Kaiser (1999)
  26. 10.1016/S1097-2765(00)80341-X / Mol. Cell / Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown by Kisselev (1999)
  27. 10.1074/jbc.M112360200 / J. Biol. Chem. / Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of the 20S proteasomes by Kisselev (2002)
  28. 10.1074/jbc.M303725200 / J. Biol. Chem. / The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites by Kisselev (2003)
  29. 10.1016/S1097-2765(01)00274-X / Mol. Cell / The axial channel of the proteasome core particle is gated by the Rpt2 ATPases and controls both substrate entry and product release by Kohler (2001)
  30. 10.1038/416763a / Nature / A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal by Lam (2002)
  31. 10.1016/S1097-2765(01)00209-X / Mol. Cell / ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal by Lee (2001)
  32. 10.1016/S1097-2765(02)00638-X / Mol. Cell / Multiple associated proteins regulate proteasome structure and function by Leggett (2002)
  33. 10.1126/science.7725097 / Science / Crystal structure of the 20S proteasome from the Archeon T. acidophilum at 3.4 Å resolution by Lowe (1995)
  34. 10.1016/S1097-2765(01)00407-5 / Mol. Cell / Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome by Navon (2001)
  35. 10.1021/bi0159130 / Biochemistry / Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition by Osmulski (2002)
  36. 10.1038/nrm1336 / Nat. Rev. Mol. Cell Biol. / Proteasomes and their kin: proteases in the machine age by Pickart (2004)
  37. 10.1093/emboj/17.17.4909 / EMBO J. / Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome by Rubin (1998)
  38. 10.1038/nsmb914 / Nat. Struct. Mol. Biol. / The HEAT repeat protein Blom10 regulates the yeast proteasome by capping the core particle by Schmidt (2005)
  39. 10.1021/bi991615f / Biochemistry / ClpA and ClpB remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease by Sigh (1999)
  40. 10.1016/S0092-8674(00)80403-1 / Cell / F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex by Skowyra (1997)
  41. 10.1093/emboj/19.1.94 / EMBO J. / Recognition of the polyubiquitin proteolytic signal by Thrower (2000)
  42. 10.1128/MCB.16.11.6020 / Mol. Cell. Biol. / The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover by van Nocker (1996)
  43. 10.1091/mbc.11.10.3425 / Mol. Biol. Cell / Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes by Verma (2000)
  44. 10.1016/S1097-2765(01)00308-2 / Mol. Cell / Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S-phase Cyclin-Cdk by Verma (2001)
  45. 10.1126/science.1075898 / Science / Role of Rpn11 metalloprotease in deubiuqitination and degradation of the 26S proteasome by Verma (2002)
  46. 10.1016/j.cell.2004.06.014 / Cell / Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system by Verma (2004)
  47. 10.1016/S0969-2126(01)00670-0 / Structure / Nucleotide-dependent conformational changes in a protease-associated ATPase UslU by Wang (2001)
  48. 10.1038/35040607 / Nature / Structural basis for the activation of 20S proteasomes by 11S regulators by Whitby (2000)
  49. 10.1016/S1046-2023(02)00030-0 / Methods / Isolation and mass spectrometry of transcription factor complexes by Winkler (2002)
  50. 10.1073/pnas.060025497 / Proc. Natl. Acad. Sci. USA / Physical association of ubiquitin ligases and the 26S proteasome by Xie (2000)
  51. 10.1038/ncb889 / Nat. Cell Biol. / UFD4 lacking the proteasome-binding region catalyzes ubiquitination but is impaired in proteolysis by Xie (2002)
  52. 10.1038/nature01071 / Nature / A cryptic protease couples deubiquitination and degradation by the proteasome by Yao (2002)
Dates
Type When
Created 20 years, 3 months ago (May 21, 2005, 7:09 a.m.)
Deposited 1 year, 7 months ago (Jan. 26, 2024, 12:51 a.m.)
Indexed 5 months ago (April 2, 2025, 3:45 a.m.)
Issued 20 years, 4 months ago (May 1, 2005)
Published 20 years, 4 months ago (May 1, 2005)
Published Print 20 years, 4 months ago (May 1, 2005)
Funders 0

None

@article{Babbitt_2005, title={RETRACTED: ATP Hydrolysis-Dependent Disassembly of the 26S Proteasome Is Part of the Catalytic Cycle}, volume={121}, ISSN={0092-8674}, url={http://dx.doi.org/10.1016/j.cell.2005.03.028}, DOI={10.1016/j.cell.2005.03.028}, number={4}, journal={Cell}, publisher={Elsevier BV}, author={Babbitt, Shalon E. and Kiss, Alexi and Deffenbaugh, Andrew E. and Chang, Yie-Hwa and Bailly, Eric and Erdjument-Bromage, Hediye and Tempst, Paul and Buranda, Tione and Sklar, Larry A. and Baumler, Jennifer and Gogol, Edward and Skowyra, Dorota}, year={2005}, month=may, pages={553–565} }