ClpXP, an ATP-powered unfolding and protein-degradation machine.
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[1] Robert T Sauer,et al. AAA+ proteases: ATP-fueled machines of protein destruction. , 2011, Annual review of biochemistry.
[2] Carlos Bustamante,et al. ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates , 2011, Cell.
[3] Adrian O. Olivares,et al. Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine , 2011, Cell.
[4] Christian Reis,et al. ATP Binds to Proteasomal ATPases in Pairs with Distinct Functional Effects, Implying an Ordered Reaction Cycle , 2011, Cell.
[5] D. Schnappinger,et al. Protein inactivation in mycobacteria by controlled proteolysis and its application to deplete the beta subunit of RNA polymerase , 2010, Nucleic acids research.
[6] R. Ghirlando,et al. Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP. , 2010, Chemistry & biology.
[7] H. Chan,et al. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. , 2010, Structure.
[8] H. Song,et al. Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism , 2010, Nature Structural &Molecular Biology.
[9] T. Baker,et al. Control of substrate gating and translocation into ClpP by channel residues and ClpX binding. , 2010, Journal of molecular biology.
[10] Ricardo R. Brau,et al. Single-molecule denaturation and degradation of proteins by the AAA+ ClpXP protease , 2009, Proceedings of the National Academy of Sciences.
[11] R. Hengge. Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli. , 2009, Research in microbiology.
[12] S. Glynn,et al. Structures of Asymmetric ClpX Hexamers Reveal Nucleotide-Dependent Motions in a AAA+ Protein-Unfolding Machine , 2009, Cell.
[13] Joseph H. Davis,et al. Engineering Synthetic Adaptors and Substrates for Controlled ClpXP Degradation* , 2009, The Journal of Biological Chemistry.
[14] T. Baker,et al. Polypeptide translocation by the AAA+ ClpXP protease machine. , 2009, Chemistry & biology.
[15] H. Lilie,et al. The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease , 2009, EMBO molecular medicine.
[16] M. Bewley,et al. Turned on for degradation: ATPase-independent degradation by ClpP. , 2009, Journal of structural biology.
[17] T. Baker,et al. Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage , 2008, Molecular microbiology.
[18] Kevin L. Griffith,et al. Inducible protein degradation in Bacillus subtilis using heterologous peptide tags and adaptor proteins to target substrates to the protease ClpXP , 2008, Molecular microbiology.
[19] Laura D. Jennings,et al. The ClpP N-terminus coordinates substrate access with protease active site reactivity. , 2008, Biochemistry.
[20] Tania A. Baker,et al. Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding , 2008, Nature Structural &Molecular Biology.
[21] M. Maurizi,et al. Turnover of Endogenous SsrA-tagged Proteins Mediated by ATP-dependent Proteases in Escherichia coli* , 2008, Journal of Biological Chemistry.
[22] K. Kim,et al. The structural basis for the activation and peptide recognition of bacterial ClpP. , 2008, Journal of molecular biology.
[23] T. Baker,et al. Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX. , 2008, Molecular cell.
[24] Andreas Martin,et al. Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. , 2008, Molecular cell.
[25] Robert T Sauer,et al. Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes , 2008, Nature Structural &Molecular Biology.
[26] W. Houry,et al. ClpP: A distinctive family of cylindrical energy‐dependent serine proteases , 2007, FEBS letters.
[27] Andreas Martin,et al. Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease. , 2007, Molecular cell.
[28] R. Sauer,et al. The tmRNA system for translational surveillance and ribosome rescue. , 2007, Annual review of biochemistry.
[29] T. Baker,et al. Altered Tethering of the SspB Adaptor to the ClpXP Protease Causes Changes in Substrate Delivery* , 2007, Journal of Biological Chemistry.
[30] H. Song,et al. Structural basis of SspB-tail recognition by the zinc binding domain of ClpX. , 2007, Journal of molecular biology.
[31] P. Alzari,et al. Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. , 2007, Acta crystallographica. Section D, Biological crystallography.
[32] Robert T Sauer,et al. Altered specificity of a AAA+ protease. , 2007, Molecular cell.
[33] T. Baker,et al. Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction. , 2007, Genes & development.
[34] M. Maurizi,et al. Crystal structure at 1.9A of E. coli ClpP with a peptide covalently bound at the active site. , 2006, Journal of structural biology.
[35] Robert T Sauer,et al. Engineering controllable protein degradation. , 2006, Molecular cell.
[36] J. Berger,et al. Evolutionary relationships and structural mechanisms of AAA+ proteins. , 2006, Annual review of biophysics and biomolecular structure.
[37] S. Gygi,et al. Proteomic profiling of ClpXP substrates after DNA damage reveals extensive instability within SOS regulon. , 2006, Molecular cell.
[38] M. Bewley,et al. The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes. , 2006, Journal of structural biology.
[39] P. Kiley,et al. ClpXP-dependent proteolysis of FNR upon loss of its O2-sensing [4Fe-4S] cluster. , 2005, Journal of molecular biology.
[40] Walid A Houry,et al. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[41] J. Ortega,et al. Human Mitochondrial ClpP Is a Stable Heptamer That Assembles into a Tetradecamer in the Presence of ClpX* , 2005, Journal of Biological Chemistry.
[42] Tania A. Baker,et al. Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines , 2005, Nature.
[43] Robert T Sauer,et al. Ribosome rescue: tmRNA tagging activity and capacity in Escherichia coli , 2005, Molecular microbiology.
[44] H. Sahl,et al. Dysregulation of bacterial proteolytic machinery by a new class of antibiotics , 2005, Nature Medicine.
[45] Christopher M. Farrell,et al. Cytoplasmic degradation of ssrA‐tagged proteins , 2005, Molecular microbiology.
[46] Tania A. Baker,et al. Asymmetric Interactions of ATP with the AAA+ ClpX6 Unfoldase: Allosteric Control of a Protein Machine , 2005, Cell.
[47] P. Hanson,et al. AAA+ proteins: have engine, will work , 2005, Nature Reviews Molecular Cell Biology.
[48] T. Baker,et al. Versatile modes of peptide recognition by the AAA+ adaptor protein SspB , 2005, Nature Structural &Molecular Biology.
[49] K. Fiebig,et al. The ClpP Double Ring Tetradecameric Protease Exhibits Plastic Ring-Ring Interactions, and the N Termini of Its Subunits Form Flexible Loops That Are Essential for ClpXP and ClpAP Complex Formation* , 2005, Journal of Biological Chemistry.
[50] Robert T Sauer,et al. Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[51] Jon A. Kenniston,et al. Substrate denaturation and translocation by a proteolytic machine , 2005 .
[52] M. Maurizi,et al. Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP. , 2004, Journal of structural biology.
[53] T. Baker,et al. Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease. , 2004, Molecular cell.
[54] Greg L. Hersch,et al. Sculpting the Proteome with AAA+ Proteases and Disassembly Machines , 2004, Cell.
[55] T. Baker,et al. Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. , 2004, Genes & development.
[56] Robert T Sauer,et al. SspB delivery of substrates for ClpXP proteolysis probed by the design of improved degradation tags. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[57] Greg L. Hersch,et al. Communication between ClpX and ClpP during substrate processing and degradation , 2004, Nature Structural &Molecular Biology.
[58] T. Baker,et al. Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation. , 2004, Journal of structural biology.
[59] C. Gross,et al. Regulation of the Escherichia coliσE‐dependent envelope stress response , 2004, Molecular microbiology.
[60] T. Baker,et al. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. , 2004, Genes & development.
[61] Robert T Sauer,et al. Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study. , 2004, Molecular cell.
[62] Dong Young Kim,et al. Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori* , 2003, Journal of Biological Chemistry.
[63] W. Houry,et al. The N-terminal Zinc Binding Domain of ClpX Is a Dimerization Domain That Modulates the Chaperone Function* , 2003, Journal of Biological Chemistry.
[64] W. Houry,et al. Solution Structure of the Dimeric Zinc Binding Domain of the Chaperone ClpX* , 2003, Journal of Biological Chemistry.
[65] T. Baker,et al. Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate processing by the ClpXP protease , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[66] Tania A. Baker,et al. Linkage between ATP Consumption and Mechanical Unfolding during the Protein Processing Reactions of an AAA+ Degradation Machine , 2003, Cell.
[67] T. Baker,et al. Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. , 2003, Molecular cell.
[68] B. Bukau,et al. Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. , 2003, Molecular cell.
[69] T. Baker,et al. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. , 2003, Molecular cell.
[70] M. Eck,et al. Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine. , 2003, Molecular cell.
[71] T. Baker,et al. Energy‐dependent degradation: Linkage between ClpX‐catalyzed nucleotide hydrolysis and protein‐substrate processing , 2003, Protein science : a publication of the Protein Society.
[72] T. Baker,et al. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. , 2003, Molecular cell.
[73] T. Baker,et al. Characterization of a specificity factor for an AAA+ ATPase: assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. , 2002, Chemistry & biology.
[74] A. Steven,et al. Alternating translocation of protein substrates from both ends of ClpXP protease , 2002, The EMBO journal.
[75] Kiyoshi Mizuuchi,et al. ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[76] T. Baker,et al. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[77] A. Steven,et al. Functional Domains of the ClpA and ClpX Molecular Chaperones Identified by Limited Proteolysis and Deletion Analysis* , 2001, The Journal of Biological Chemistry.
[78] T. Baker,et al. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine , 2001, The EMBO journal.
[79] A. Matouschek,et al. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. , 2001, Molecular cell.
[80] T. Baker,et al. Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase , 2001, Nature Structural Biology.
[81] S. Gottesman,et al. The RssB response regulator directly targets sigma(S) for degradation by ClpXP. , 2001, Genes & development.
[82] A. Steven,et al. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. , 2000, Molecular cell.
[83] Andres F. Oberhauser,et al. Point mutations alter the mechanical stability of immunoglobulin modules , 2000, Nature Structural Biology.
[84] R. Woodgate,et al. Subunit‐specific degradation of the UmuD/D′ heterodimer by the ClpXP protease: the role of trans recognition in UmuD′ stability , 2000, The EMBO journal.
[85] T. Baker,et al. A specificity-enhancing factor for the ClpXP degradation machine. , 2000, Science.
[86] J. Hoskins,et al. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[87] T. Baker,et al. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. , 2000, Molecular cell.
[88] S. Marqusee,et al. Structural distribution of stability in a thermophilic enzyme. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[89] C. Georgopoulos,et al. Recognition, Targeting, and Hydrolysis of the λ O Replication Protein by the ClpP/ClpX Protease* , 1999, Journal of Biological Chemistry.
[90] E V Koonin,et al. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. , 1999, Genome research.
[91] C. Georgopoulos,et al. Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX protease. , 1999, The Journal of biological chemistry.
[92] A. Steven,et al. Enzymatic and Structural Similarities between theEscherichia coli ATP-dependent Proteases, ClpXP and ClpAP* , 1998, The Journal of Biological Chemistry.
[93] M. Kessel,et al. Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. , 1998, Biochemistry.
[94] R. Sauer,et al. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. , 1998, Genes & development.
[95] H. Nakai,et al. Versatile Action of Escherichia coli ClpXP as Protease or Molecular Chaperone for Bacteriophage Mu Transposition* , 1998, The Journal of Biological Chemistry.
[96] Jimin Wang,et al. The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis , 1997, Cell.
[97] T. Baker,et al. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. , 1997, Genes & development.
[98] R. Sauer,et al. Role of a Peptide Tagging System in Degradation of Proteins Synthesized from Damaged Messenger RNA , 1996, Science.
[99] H. Nakai,et al. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. , 1996, The EMBO journal.
[100] A. Toussaint,et al. Bacteriophage Mu repressor as a target for the Escherichia coli ATP‐dependent Clp Protease. , 1996, The EMBO journal.
[101] T. Baker,et al. Disassembly of the Mu transposase tetramer by the ClpX chaperone. , 1995, Genes & development.
[102] J. Wall,et al. Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore. , 1995, Biochemistry.
[103] B L Trus,et al. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. , 1995, Journal of molecular biology.
[104] M. Maurizi,et al. Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. , 1994, The Journal of biological chemistry.
[105] M. Maurizi,et al. Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis. , 1994, The Journal of biological chemistry.
[106] A. Toussaint,et al. A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein , 1994, Molecular microbiology.
[107] C. Georgopoulos,et al. Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. , 1993, The Journal of biological chemistry.
[108] S. Gottesman,et al. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. , 1993, The Journal of biological chemistry.
[109] S. Gottesman,et al. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. , 1990, The Journal of biological chemistry.
[110] S. Gottesman,et al. The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. , 1988, The Journal of biological chemistry.
[111] A. Goldberg,et al. Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits. , 1988, The Journal of biological chemistry.
[112] S. Gottesman,et al. A multiple-component, ATP-dependent protease from Escherichia coli. , 1987, The Journal of biological chemistry.
[113] J. Changeux,et al. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.