Tania A. Baker - Publications

Affiliations: 
Biology Massachusetts Institute of Technology, Cambridge, MA, United States 
Area:
macromolecular machines
Website:
https://biology.mit.edu/people/tania_baker

118 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any innacuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Amor AJ, Schmitz KR, Sello JK, Baker TA, Sauer RT. Highly dynamic interactions maintain kinetic stability of the ClpXP protease during the ATP-fueled mechanical cycle. Acs Chemical Biology. PMID 27003103 DOI: 10.1021/acschembio.6b00083  1
2016 Stein BJ, Grant RA, Sauer RT, Baker TA. Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Structure (London, England : 1993). PMID 26805523 DOI: 10.1016/j.str.2015.12.008  1
2015 Ahn BE, Baker TA. Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR. Proceedings of the National Academy of Sciences of the United States of America. PMID 26677871 DOI: 10.1073/pnas.1522687112  1
2015 Olivares AO, Baker TA, Sauer RT. Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines. Nature Reviews. Microbiology. PMID 26639779 DOI: 10.1038/nrmicro.2015.4  1
2015 Iosefson O, Olivares AO, Baker TA, Sauer RT. Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine. Cell Reports. 12: 1032-41. PMID 26235618 DOI: 10.1016/j.celrep.2015.07.007  1
2015 Kardon JR, Yien YY, Huston NC, Branco DS, Hildick-Smith GJ, Rhee KY, Paw BH, Baker TA. Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis. Cell. 161: 858-67. PMID 25957689 DOI: 10.1016/j.cell.2015.04.017  1
2015 Baytshtok V, Baker TA, Sauer RT. Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases. Proceedings of the National Academy of Sciences of the United States of America. 112: 5377-82. PMID 25870262 DOI: 10.1073/pnas.1505881112  1
2015 Stinson BM, Baytshtok V, Schmitz KR, Baker TA, Sauer RT. Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX. Nature Structural & Molecular Biology. 22: 411-6. PMID 25866879 DOI: 10.1038/nsmb.3012  1
2015 Ling L, Montaño SP, Sauer RT, Rice PA, Baker TA. Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX. Journal of Molecular Biology. 427: 2966-82. PMID 25797169 DOI: 10.1016/j.jmb.2015.03.008  1
2015 de Regt AK, Baker TA, Sauer RT. Steric clashes with bound OMP peptides activate the DegS stress-response protease. Proceedings of the National Academy of Sciences of the United States of America. 112: 3326-31. PMID 25733864 DOI: 10.1073/pnas.1502372112  1
2015 de Regt AK, Kim S, Sohn J, Grant RA, Baker TA, Sauer RT. A conserved activation cluster is required for allosteric communication in HtrA-family proteases. Structure (London, England : 1993). 23: 517-26. PMID 25703375 DOI: 10.1016/j.str.2015.01.012  1
2015 Iosefson O, Nager AR, Baker TA, Sauer RT. Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine. Nature Chemical Biology. 11: 201-6. PMID 25599533 DOI: 10.1038/nchembio.1732  1
2014 Olivares AO, Nager AR, Iosefson O, Sauer RT, Baker TA. Mechanochemical basis of protein degradation by a double-ring AAA+ machine. Nature Structural & Molecular Biology. 21: 871-5. PMID 25195048 DOI: 10.1038/nsmb.2885  1
2014 Rivera-Rivera I, Román-Hernández G, Sauer RT, Baker TA. Remodeling of a delivery complex allows ClpS-mediated degradation of N-degron substrates. Proceedings of the National Academy of Sciences of the United States of America. 111: E3853-9. PMID 25187555 DOI: 10.1073/pnas.1414933111  1
2014 Cordova JC, Olivares AO, Shin Y, Stinson BM, Calmat S, Schmitz KR, Aubin-Tam ME, Baker TA, Lang MJ, Sauer RT. Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine. Cell. 158: 647-58. PMID 25083874 DOI: 10.1016/j.cell.2014.05.043  1
2014 Al-Furoukh N, Kardon JR, Krüger M, Szibor M, Baker TA, Braun T. NOA1, a novel ClpXP substrate, takes an unexpected nuclear detour prior to mitochondrial import. Plos One. 9: e103141. PMID 25072814 DOI: 10.1371/journal.pone.0103141  1
2014 de Regt AK, Yin Y, Withers TR, Wang X, Baker TA, Sauer RT, Yu HD. Overexpression of CupB5 activates alginate overproduction in Pseudomonas aeruginosa by a novel AlgW-dependent mechanism. Molecular Microbiology. 93: 415-25. PMID 24913916 DOI: 10.1111/mmi.12665  1
2014 Barthelme D, Chen JZ, Grabenstatter J, Baker TA, Sauer RT. Architecture and assembly of the archaeal Cdc48*20S proteasome. Proceedings of the National Academy of Sciences of the United States of America. 111: E1687-94. PMID 24711419 DOI: 10.1073/pnas.1404823111  1
2014 Wohlever ML, Baker TA, Sauer RT. Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity. Molecular Microbiology. 91: 66-78. PMID 24205897 DOI: 10.1111/mmi.12444  1
2013 Wohlever ML, Baker TA, Sauer RT. A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates. Journal of Bacteriology. 195: 5622-8. PMID 24123818 DOI: 10.1128/JB.00886-13  1
2013 Vieux EF, Wohlever ML, Chen JZ, Sauer RT, Baker TA. Distinct quaternary structures of the AAA+ Lon protease control substrate degradation. Proceedings of the National Academy of Sciences of the United States of America. 110: E2002-8. PMID 23674680 DOI: 10.1073/pnas.1307066110  1
2013 Stinson BM, Nager AR, Glynn SE, Schmitz KR, Baker TA, Sauer RT. Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine. Cell. 153: 628-39. PMID 23622246 DOI: 10.1016/j.cell.2013.03.029  1
2013 Wohlever ML, Nager AR, Baker TA, Sauer RT. Engineering fluorescent protein substrates for the AAA+ Lon protease. Protein Engineering, Design & Selection : Peds. 26: 299-305. PMID 23359718 DOI: 10.1093/protein/gzs105  1
2013 Cordova JC, Shin Y, Calmat S, Schmitz KR, Aubin-Tam ME, Olivares A, Sauer RT, Baker TA, Lang MJ. Optical tweezers for monitoring unfolding by the protease ClpXP Optics Infobase Conference Papers 1
2012 Glynn SE, Nager AR, Baker TA, Sauer RT. Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine. Nature Structural & Molecular Biology. 19: 616-22. PMID 22562135 DOI: 10.1038/nsmb.2288  1
2012 Landgraf D, Okumus B, Chien P, Baker TA, Paulsson J. Segregation of molecules at cell division reveals native protein localization. Nature Methods. 9: 480-2. PMID 22484850 DOI: 10.1038/nmeth.1955  1
2012 Peterson CN, Levchenko I, Rabinowitz JD, Baker TA, Silhavy TJ. RpoS proteolysis is controlled directly by ATP levels in Escherichia coli. Genes & Development. 26: 548-53. PMID 22426532 DOI: 10.1101/gad.183517.111  1
2012 Sundar S, Baker TA, Sauer RT. The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation. Protein Science : a Publication of the Protein Society. 21: 188-98. PMID 22102327 DOI: 10.1002/pro.2001  1
2012 Baker TA, Sauer RT. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochimica Et Biophysica Acta. 1823: 15-28. PMID 21736903 DOI: 10.1016/j.bbamcr.2011.06.007  1
2011 Davis JH, Baker TA, Sauer RT. Small-molecule control of protein degradation using split adaptors. Acs Chemical Biology. 6: 1205-13. PMID 21866931 DOI: 10.1021/cb2001389  1
2011 Abel S, Chien P, Wassmann P, Schirmer T, Kaever V, Laub MT, Baker TA, Jenal U. Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks. Molecular Cell. 43: 550-60. PMID 21855795 DOI: 10.1016/j.molcel.2011.07.018  1
2011 Nager AR, Baker TA, Sauer RT. Stepwise unfolding of a β barrel protein by the AAA+ ClpXP protease. Journal of Molecular Biology. 413: 4-16. PMID 21821046 DOI: 10.1016/j.jmb.2011.07.041  1
2011 Román-Hernández G, Hou JY, Grant RA, Sauer RT, Baker TA. The ClpS adaptor mediates staged delivery of N-end rule substrates to the AAA+ ClpAP protease. Molecular Cell. 43: 217-28. PMID 21777811 DOI: 10.1016/j.molcel.2011.06.009  1
2011 Aubin-Tam ME, Olivares AO, Sauer RT, Baker TA, Lang MJ. Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Cell. 145: 257-67. PMID 21496645 DOI: 10.1016/j.cell.2011.03.036  1
2011 Sauer RT, Baker TA. AAA+ proteases: ATP-fueled machines of protein destruction. Annual Review of Biochemistry. 80: 587-612. PMID 21469952 DOI: 10.1146/annurev-biochem-060408-172623  1
2011 Meyer AS, Baker TA. Proteolysis in the Escherichia coli heat shock response: a player at many levels. Current Opinion in Microbiology. 14: 194-9. PMID 21353626 DOI: 10.1016/j.mib.2011.02.001  1
2010 Sundar S, McGinness KE, Baker TA, Sauer RT. Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV. Journal of Molecular Biology. 403: 420-9. PMID 20837023 DOI: 10.1016/j.jmb.2010.09.008  1
2010 Lee ME, Baker TA, Sauer RT. Control of substrate gating and translocation into ClpP by channel residues and ClpX binding. Journal of Molecular Biology. 399: 707-18. PMID 20416323 DOI: 10.1016/j.jmb.2010.04.027  1
2010 Bissonnette SA, Rivera-Rivera I, Sauer RT, Baker TA. The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease. Molecular Microbiology. 75: 1539-49. PMID 20158612 DOI: 10.1111/j.1365-2958.2010.07070.x  1
2010 Abdelhakim AH, Sauer RT, Baker TA. The AAA+ ClpX machine unfolds a keystone subunit to remodel the Mu transpososome. Proceedings of the National Academy of Sciences of the United States of America. 107: 2437-42. PMID 20133746 DOI: 10.1073/pnas.0910905106  1
2010 Chowdhury T, Chien P, Ebrahim S, Sauer RT, Baker TA. Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species. Protein Science : a Publication of the Protein Society. 19: 242-54. PMID 20014030 DOI: 10.1002/pro.306  1
2009 Glynn SE, Martin A, Nager AR, Baker TA, Sauer RT. Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell. 139: 744-56. PMID 19914167 DOI: 10.1016/j.cell.2009.09.034  1
2009 Shin Y, Davis JH, Brau RR, Martin A, Kenniston JA, Baker TA, Sauer RT, Lang MJ. Single-molecule denaturation and degradation of proteins by the AAA+ ClpXP protease. Proceedings of the National Academy of Sciences of the United States of America. 106: 19340-5. PMID 19892734 DOI: 10.1073/pnas.0910484106  1
2009 Pruteanu M, Baker TA. Proteolysis in the SOS response and metal homeostasis in Escherichia coli. Research in Microbiology. 160: 677-83. PMID 19747971 DOI: 10.1016/j.resmic.2009.08.012  1
2009 Davis JH, Baker TA, Sauer RT. Engineering synthetic adaptors and substrates for controlled ClpXP degradation. The Journal of Biological Chemistry. 284: 21848-55. PMID 19549779 DOI: 10.1074/jbc.M109.017624  1
2009 Barkow SR, Levchenko I, Baker TA, Sauer RT. Polypeptide translocation by the AAA+ ClpXP protease machine. Chemistry & Biology. 16: 605-12. PMID 19549599 DOI: 10.1016/j.chembiol.2009.05.007  1
2009 Román-Hernández G, Grant RA, Sauer RT, Baker TA. Molecular basis of substrate selection by the N-end rule adaptor protein ClpS. Proceedings of the National Academy of Sciences of the United States of America. 106: 8888-93. PMID 19451643 DOI: 10.1073/pnas.0903614106  1
2009 Pruteanu M, Baker TA. Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage. Molecular Microbiology. 71: 912-24. PMID 19183285 DOI: 10.1111/j.1365-2958.2008.06574.x  1
2008 Wang KH, Roman-Hernandez G, Grant RA, Sauer RT, Baker TA. The molecular basis of N-end rule recognition. Molecular Cell. 32: 406-14. PMID 18995838 DOI: 10.1016/j.molcel.2008.08.032  1
2008 Martin A, Baker TA, Sauer RT. Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding. Nature Structural & Molecular Biology. 15: 1147-51. PMID 18931677 DOI: 10.1038/nsmb.1503  1
2008 Schweidenback CT, Baker TA. Dissecting the roles of MuB in Mu transposition: ATP regulation of DNA binding is not essential for target delivery. Proceedings of the National Academy of Sciences of the United States of America. 105: 12101-7. PMID 18719126 DOI: 10.1073/pnas.0805868105  1
2008 Moore SD, Baker TA, Sauer RT. Forced extraction of targeted components from complex macromolecular assemblies. Proceedings of the National Academy of Sciences of the United States of America. 105: 11685-90. PMID 18695246 DOI: 10.1073/pnas.0805633105  1
2008 Yakamavich JA, Baker TA, Sauer RT. Asymmetric nucleotide transactions of the HslUV protease. Journal of Molecular Biology. 380: 946-57. PMID 18582897 DOI: 10.1016/j.jmb.2008.05.070  1
2008 Wang KH, Oakes ES, Sauer RT, Baker TA. Tuning the strength of a bacterial N-end rule degradation signal. The Journal of Biological Chemistry. 283: 24600-7. PMID 18550545 DOI: 10.1074/jbc.M802213200  1
2008 Abdelhakim AH, Oakes EC, Sauer RT, Baker TA. Unique contacts direct high-priority recognition of the tetrameric Mu transposase-DNA complex by the AAA+ unfoldase ClpX. Molecular Cell. 30: 39-50. PMID 18406325 DOI: 10.1016/j.molcel.2008.02.013  1
2008 Martin A, Baker TA, Sauer RT. Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. Molecular Cell. 29: 441-50. PMID 18313382 DOI: 10.1016/j.molcel.2008.02.002  1
2008 Hou JY, Sauer RT, Baker TA. Distinct structural elements of the adaptor ClpS are required for regulating degradation by ClpAP. Nature Structural & Molecular Biology. 15: 288-94. PMID 18297088 DOI: 10.1038/nsmb.1392  1
2008 Martin A, Baker TA, Sauer RT. Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes. Nature Structural & Molecular Biology. 15: 139-45. PMID 18223658 DOI: 10.1038/nsmb.1380  1
2007 Lemberg KM, Schweidenback CT, Baker TA. The dynamic Mu transpososome: MuB activation prevents disintegration. Journal of Molecular Biology. 374: 1158-71. PMID 17988683 DOI: 10.1016/j.jmb.2007.09.079  1
2007 Chien P, Grant RA, Sauer RT, Baker TA. Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors. Structure (London, England : 1993). 15: 1296-305. PMID 17937918 DOI: 10.1016/j.str.2007.08.008  1
2007 Martin A, Baker TA, Sauer RT. Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease. Molecular Cell. 27: 41-52. PMID 17612489 DOI: 10.1016/j.molcel.2007.05.024  1
2007 Chien P, Perchuk BS, Laub MT, Sauer RT, Baker TA. Direct and adaptor-mediated substrate recognition by an essential AAA+ protease. Proceedings of the National Academy of Sciences of the United States of America. 104: 6590-5. PMID 17420450 DOI: 10.1073/pnas.0701776104  1
2007 Wang KH, Sauer RT, Baker TA. ClpS modulates but is not essential for bacterial N-end rule degradation. Genes & Development. 21: 403-8. PMID 17322400 DOI: 10.1101/gad.1511907  1
2007 McGinness KE, Bolon DN, Kaganovich M, Baker TA, Sauer RT. Altered tethering of the SspB adaptor to the ClpXP protease causes changes in substrate delivery. The Journal of Biological Chemistry. 282: 11465-73. PMID 17317664 DOI: 10.1074/jbc.M610671200  1
2007 Pruteanu M, Neher SB, Baker TA. Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR. Journal of Bacteriology. 189: 3017-25. PMID 17220226 DOI: 10.1128/JB.01531-06  1
2007 Farrell CM, Baker TA, Sauer RT. Altered specificity of a AAA+ protease. Molecular Cell. 25: 161-6. PMID 17218279 DOI: 10.1016/j.molcel.2006.11.018  1
2007 Chaba R, Grigorova IL, Flynn JM, Baker TA, Gross CA. Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction. Genes & Development. 21: 124-36. PMID 17210793 DOI: 10.1101/gad.1496707  1
2006 Baker TA, Sauer RT. ATP-dependent proteases of bacteria: recognition logic and operating principles. Trends in Biochemical Sciences. 31: 647-53. PMID 17074491 DOI: 10.1016/j.tibs.2006.10.006  1
2006 McGinness KE, Baker TA, Sauer RT. Engineering controllable protein degradation. Molecular Cell. 22: 701-7. PMID 16762842 DOI: 10.1016/j.molcel.2006.04.027  1
2006 Neher SB, Villén J, Oakes EC, Bakalarski CE, Sauer RT, Gygi SP, Baker TA. Proteomic profiling of ClpXP substrates after DNA damage reveals extensive instability within SOS regulon. Molecular Cell. 22: 193-204. PMID 16630889 DOI: 10.1016/j.molcel.2006.03.007  1
2005 Martin A, Baker TA, Sauer RT. Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines. Nature. 437: 1115-20. PMID 16237435 DOI: 10.1038/nature04031  1
2005 Bolon DN, Grant RA, Baker TA, Sauer RT. Specificity versus stability in computational protein design. Proceedings of the National Academy of Sciences of the United States of America. 102: 12724-9. PMID 16129838 DOI: 10.1073/pnas.0506124102  1
2005 Burton BM, Baker TA. Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase. Protein Science : a Publication of the Protein Society. 14: 1945-54. PMID 16046622 DOI: 10.1110/ps.051417505  1
2005 Hersch GL, Burton RE, Bolon DN, Baker TA, Sauer RT. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell. 121: 1017-27. PMID 15989952 DOI: 10.1016/j.cell.2005.05.024  1
2005 Levchenko I, Grant RA, Flynn JM, Sauer RT, Baker TA. Versatile modes of peptide recognition by the AAA+ adaptor protein SspB. Nature Structural & Molecular Biology. 12: 520-5. PMID 15880122 DOI: 10.1038/nsmb934  1
2005 Burton RE, Baker TA, Sauer RT. Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nature Structural & Molecular Biology. 12: 245-51. PMID 15696175 DOI: 10.1038/nsmb898  1
2005 Kenniston JA, Baker TA, Sauer RT. Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing. Proceedings of the National Academy of Sciences of the United States of America. 102: 1390-5. PMID 15671177 DOI: 10.1073/pnas.0409634102  1
2004 Bolon DN, Grant RA, Baker TA, Sauer RT. Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease. Molecular Cell. 16: 343-50. PMID 15525508 DOI: 10.1016/j.molcel.2004.10.001  1
2004 Sauer RT, Bolon DN, Burton BM, Burton RE, Flynn JM, Grant RA, Hersch GL, Joshi SA, Kenniston JA, Levchenko I, Neher SB, Oakes ES, Siddiqui SM, Wah DA, Baker TA. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell. 119: 9-18. PMID 15454077 DOI: 10.1016/j.cell.2004.09.020  1
2004 Flynn JM, Levchenko I, Sauer RT, Baker TA. Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes & Development. 18: 2292-301. PMID 15371343 DOI: 10.1101/gad.1240104  1
2004 Hersch GL, Baker TA, Sauer RT. SspB delivery of substrates for ClpXP proteolysis probed by the design of improved degradation tags. Proceedings of the National Academy of Sciences of the United States of America. 101: 12136-41. PMID 15297609 DOI: 10.1073/pnas.0404733101  1
2004 Joshi SA, Hersch GL, Baker TA, Sauer RT. Communication between ClpX and ClpP during substrate processing and degradation. Nature Structural & Molecular Biology. 11: 404-11. PMID 15064753 DOI: 10.1038/nsmb752  1
2004 Kenniston JA, Burton RE, Siddiqui SM, Baker TA, Sauer RT. Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation. Journal of Structural Biology. 146: 130-40. PMID 15037244 DOI: 10.1016/j.jsb.2003.10.023  1
2004 Siddiqui SM, Sauer RT, Baker TA. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. Genes & Development. 18: 369-74. PMID 15004005 DOI: 10.1101/gad.1170304  1
2004 Bolon DN, Wah DA, Hersch GL, Baker TA, Sauer RT. Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study. Molecular Cell. 13: 443-9. PMID 14967151 DOI: 10.1016/S1097-2765(04)00027-9  1
2004 Williams TL, Baker TA. Reorganization of the Mu transpososome active sites during a cooperative transition between DNA cleavage and joining. The Journal of Biological Chemistry. 279: 5135-45. PMID 14585843 DOI: 10.1074/jbc.M308156200  1
2003 Spector S, Flynn JM, Tidor B, Baker TA, Sauer RT. Expression of N-formylated proteins in Escherichia coli. Protein Expression and Purification. 32: 317-22. PMID 14965779 DOI: 10.1016/j.pep.2003.08.004  1
2003 Goldhaber-Gordon I, Early MH, Baker TA. MuA transposase separates DNA sequence recognition from catalysis. Biochemistry. 42: 14633-42. PMID 14661976 DOI: 10.1021/bi035360o  1
2003 Neher SB, Sauer RT, Baker TA. Distinct peptide signals in the UmuD and UmuD' subunits of UmuD/D' mediate tethering and substrate processing by the ClpXP protease. Proceedings of the National Academy of Sciences of the United States of America. 100: 13219-24. PMID 14595014 DOI: 10.1073/pnas.2235804100  1
2003 Levchenko I, Grant RA, Wah DA, Sauer RT, Baker TA. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Molecular Cell. 12: 365-72. PMID 14536076 DOI: 10.1016/j.molcel.2003.08.014  1
2003 Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Molecular Cell. 12: 355-63. PMID 14536075 DOI: 10.1016/S1097-2765(03)00272-7  1
2003 Kenniston JA, Baker TA, Fernandez JM, Sauer RT. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell. 114: 511-20. PMID 12941278 DOI: 10.1016/S0092-8674(03)00612-3  1
2003 Goldhaber-Gordon I, Early MH, Baker TA. The terminal nucleotide of the Mu genome controls catalysis of DNA strand transfer. Proceedings of the National Academy of Sciences of the United States of America. 100: 7509-14. PMID 12796508 DOI: 10.1073/pnas.0832468100  1
2003 Coros CJ, Sekino Y, Baker TA, Chaconas G. Effect of mutations in the C-terminal domain of Mu B on DNA binding and interactions with Mu A transposase. The Journal of Biological Chemistry. 278: 31210-7. PMID 12791691 DOI: 10.1074/jbc.M303693200  1
2003 Burton BM, Baker TA. Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex. Chemistry & Biology. 10: 463-72. PMID 12770828 DOI: 10.1016/S1074-5521(03)00102-9  1
2003 Neher SB, Flynn JM, Sauer RT, Baker TA. Latent ClpX-recognition signals ensure LexA destruction after DNA damage. Genes & Development. 17: 1084-9. PMID 12730132 DOI: 10.1101/gad.1078003  1
2003 Burton RE, Baker TA, Sauer RT. Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing. Protein Science : a Publication of the Protein Society. 12: 893-902. PMID 12717012 DOI: 10.1110/ps.0237603  1
2003 Flynn JM, Neher SB, Kim YI, Sauer RT, Baker TA. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Molecular Cell. 11: 671-83. PMID 12667450 DOI: 10.1016/S1097-2765(03)00060-1  1
2003 Joshi SA, Baker TA, Sauer RT. C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding. Molecular Microbiology. 48: 67-76. PMID 12657045 DOI: 10.1046/j.1365-2958.2003.03424.x  1
2003 Sokolsky TD, Baker TA. DNA gyrase requirements distinguish the alternate pathways of Mu transposition. Molecular Microbiology. 47: 397-409. PMID 12519191 DOI: 10.1046/j.1365-2958.2003.03296.x  1
2002 Goldhaber-Gordon I, Early MH, Gray MK, Baker TA. Sequence and positional requirements for DNA sites in a mu transpososome. The Journal of Biological Chemistry. 277: 7703-12. PMID 11756424 DOI: 10.1074/jbc.M110342200  1
2002 Goldhaber-Gordon I, Williams TL, Baker TA. DNA recognition sites activate MuA transposase to perform transposition of non-Mu DNA. The Journal of Biological Chemistry. 277: 7694-702. PMID 11756423 DOI: 10.1074/jbc.M110341200  1
2001 Burton BM, Williams TL, Baker TA. ClpX-mediated remodeling of mu transpososomes: selective unfolding of subunits destabilizes the entire complex. Molecular Cell. 8: 449-54. PMID 11545746 DOI: 10.1016/S1097-2765(01)00307-0  1
2000 Kim YI, Burton RE, Burton BM, Sauer RT, Baker TA. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Molecular Cell. 5: 639-48. PMID 10882100  1
1995 Mizuuchi M, Baker TA, Mizuuchi K. Assembly of phage Mu transpososomes: cooperative transitions assisted by protein and DNA scaffolds. Cell. 83: 375-85. PMID 8521467 DOI: 10.1016/0092-8674(95)90115-9  1
1993 Baker TA, Mizuuchi M, Savilahti H, Mizuuchi K. Division of labor among monomers within the Mu transposase tetramer. Cell. 74: 723-33. PMID 8395353 DOI: 10.1016/0092-8674(93)90519-V  1
1992 Baker TA, Mizuuchi K. DNA-promoted assembly of the active tetramer of the Mu transposase. Genes & Development. 6: 2221-32. PMID 1330829  1
1992 Mizuuchi M, Baker TA, Mizuuchi K. Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition. Cell. 70: 303-11. PMID 1322248 DOI: 10.1016/0092-8674(92)90104-K  1
1991 Mizuuchi M, Baker TA, Mizuuchi K. DNase protection analysis of the stable synaptic complexes involved in Mu transposition. Proceedings of the National Academy of Sciences of the United States of America. 88: 9031-5. PMID 1656459  1
1991 Baker TA, Mizuuchi M, Mizuuchi K. MuB protein allosterically activates strand transfer by the transposase of phage Mu. Cell. 65: 1003-13. PMID 1646076 DOI: 10.1016/0092-8674(91)90552-A  1
1990 Skarstad K, Baker TA, Kornberg A. Strand separation required for initiation of replication at the chromosomal origin of E.coli is facilitated by a distant RNA--DNA hybrid. The Embo Journal. 9: 2341-8. PMID 1694129  1
1988 Baker TA, Kornberg A. Transcriptional activation of initiation of replication from the E. coli chromosomal origin: an RNA-DNA hybrid near oriC. Cell. 55: 113-23. PMID 2458841  1
1987 Funnell BE, Baker TA, Kornberg A. In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. The Journal of Biological Chemistry. 262: 10327-34. PMID 3038874  1
1987 Baker TA, Funnell BE, Kornberg A. Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro. The Journal of Biological Chemistry. 262: 6877-85. PMID 3032979  1
1986 Funnell BE, Baker TA, Kornberg A. Complete enzymatic replication of plasmids containing the origin of the Escherichia coli chromosome. The Journal of Biological Chemistry. 261: 5616-24. PMID 3514619  1
1986 Baker TA, Sekimizu K, Funnell BE, Kornberg A. Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome. Cell. 45: 53-64. PMID 3006926  1
1985 Ogawa T, Baker TA, van der Ende A, Kornberg A. Initiation of enzymatic replication at the origin of the Escherichia coli chromosome: contributions of RNA polymerase and primase. Proceedings of the National Academy of Sciences of the United States of America. 82: 3562-6. PMID 2987933  1
1985 van der Ende A, Baker TA, Ogawa T, Kornberg A. Initiation of enzymatic replication at the origin of the Escherichia coli chromosome: primase as the sole priming enzyme. Proceedings of the National Academy of Sciences of the United States of America. 82: 3954-8. PMID 2408271  1
Show low-probability matches.