| Year |
Citation |
Score |
| 2024 |
Mawla GD, Kamal SM, Cao LY, Purhonen P, Hebert H, Sauer RT, Baker TA, Römling U. The membrane-cytoplasmic linker defines activity of FtsH proteases in Pseudomonas aeruginosa clone C. The Journal of Biological Chemistry. 105622. PMID 38176647 DOI: 10.1016/j.jbc.2023.105622 |
0.546 |
|
| 2023 |
Ghanbarpour A, Sauer RT, Davis JH. A proteolytic AAA+ machine poised to unfold a protein substrate. Biorxiv : the Preprint Server For Biology. PMID 38168193 DOI: 10.1101/2023.12.14.571662 |
0.821 |
|
| 2023 |
Ghanbarpour A, Cohen SE, Fei X, Kinman LF, Bell TA, Zhang JJ, Baker TA, Davis JH, Sauer RT. A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Nature Communications. 14: 7281. PMID 37949857 DOI: 10.1038/s41467-023-43145-x |
0.793 |
|
| 2023 |
Kasal MR, Kotamarthi HC, Johnson MM, Stephens HM, Lang MJ, Sauer RT, Baker TA. Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease. Cell Reports. 42: 113061. PMID 37660294 DOI: 10.1016/j.celrep.2023.113061 |
0.815 |
|
| 2023 |
Ghanbarpour A, Fei X, Baker TA, Davis JH, Sauer RT. The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2219044120. PMID 36730206 DOI: 10.1073/pnas.2219044120 |
0.821 |
|
| 2023 |
Morehouse JP, Baker TA, Sauer RT. FtsH degrades dihydrofolate reductase by recognizing a partially folded species. Protein Science : a Publication of the Protein Society. 31: e4410. PMID 36630366 DOI: 10.1002/pro.4410 |
0.585 |
|
| 2022 |
Hari SB, Morehouse JP, Baker TA, Sauer RT. FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron. Molecular Microbiology. PMID 36456794 DOI: 10.1111/mmi.15009 |
0.818 |
|
| 2022 |
Kim S, Fei X, Sauer RT, Baker TA. AAA+ protease-adaptor structures reveal altered conformations and ring specialization. Nature Structural & Molecular Biology. 29: 1068-1079. PMID 36329286 DOI: 10.1038/s41594-022-00850-3 |
0.823 |
|
| 2021 |
Sauer RT, Fei X, Bell TA, Baker TA. Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis. Critical Reviews in Biochemistry and Molecular Biology. 1-17. PMID 34923891 DOI: 10.1080/10409238.2021.1979461 |
0.817 |
|
| 2021 |
Zuromski KL, Kim S, Sauer RT, Baker TA. Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease. The Journal of Biological Chemistry. 101407. PMID 34780718 DOI: 10.1016/j.jbc.2021.101407 |
0.542 |
|
| 2021 |
Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug. Cell Reports. 34: 108639. PMID 33472065 DOI: 10.1016/j.celrep.2020.108639 |
0.814 |
|
| 2020 |
Kim S, Zuromski KL, Bell TA, Sauer RT, Baker TA. ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP. Elife. 9. PMID 33258771 DOI: 10.7554/eLife.61451 |
0.561 |
|
| 2020 |
Mawla GD, Hall BM, Cárcamo-Oyarce G, Grant RA, Zhang JJ, Kardon JR, Ribbeck K, Sauer RT, Baker TA. ClpP1P2 peptidase activity promotes biofilm formation in P. aeruginosa. Molecular Microbiology. PMID 33231899 DOI: 10.1111/mmi.14649 |
0.495 |
|
| 2020 |
Saunders RA, Stinson BM, Baker TA, Sauer RT. Multistep substrate binding and engagement by the AAA+ ClpXP protease. Proceedings of the National Academy of Sciences of the United States of America. PMID 33106413 DOI: 10.1073/pnas.2010804117 |
0.587 |
|
| 2020 |
Fei X, Bell TA, Barkow SR, Baker TA, Sauer RT. Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Elife. 9. PMID 33089779 DOI: 10.7554/eLife.61496 |
0.836 |
|
| 2020 |
Zuromski KL, Sauer RT, Baker TA. Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease. Proceedings of the National Academy of Sciences of the United States of America. PMID 33020301 DOI: 10.1073/pnas.2014407117 |
0.481 |
|
| 2020 |
Torres-Delgado A, Kotamarthi HC, Sauer RT, Baker TA. The intrinsically disordered N-terminal extension of the ClpS adaptor reprograms its partner AAA+ ClpAP protease. Journal of Molecular Biology. PMID 32687854 DOI: 10.1016/J.Jmb.2020.07.007 |
0.825 |
|
| 2020 |
Fei X, Bell TA, Jenni S, Stinson BM, Baker TA, Harrison SC, Sauer RT. Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate. Elife. 9. PMID 32108573 DOI: 10.7554/Elife.52774 |
0.849 |
|
| 2020 |
Kotamarthi HC, Sauer RT, Baker TA. The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation. Cell Reports. 30: 2644-2654.e3. PMID 32101742 DOI: 10.1016/J.Celrep.2020.01.110 |
0.806 |
|
| 2020 |
Schmitz KR, Handy EL, Compton CL, Gupta S, Bishai WR, Sauer RT, Sello JK. Acyldepsipeptide Antibiotics and a Bioactive Fragment Thereof Differentially Perturb Mycobacterium tuberculosis ClpXP1P2 Activity in vitro. Acs Chemical Biology. PMID 32083462 DOI: 10.1021/Acschembio.9B00454 |
0.741 |
|
| 2020 |
Fei X, Bell TA, Jenni S, Stinson BM, Baker TA, Harrison SC, Sauer RT. Author response: Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate Elife. DOI: 10.7554/Elife.52774.Sa2 |
0.814 |
|
| 2019 |
Bell TA, Baker TA, Sauer RT. Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding. Elife. 8. PMID 31251172 DOI: 10.7554/Elife.46808 |
0.616 |
|
| 2019 |
Amor AJ, Schmitz KR, Baker TA, Sauer RT. Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation. Protein Science : a Publication of the Protein Society. PMID 30767302 DOI: 10.1002/Pro.3590 |
0.774 |
|
| 2019 |
Tang Y, Meister TR, Walczak M, Pulkoski-Gross MJ, Hari SB, Sauer RT, Amberg-Johnson K, Yeh E. A mutagenesis screen for essential plastid biogenesis genes in human malaria parasites. Plos Biology. 17: e3000136. PMID 30726238 DOI: 10.1371/Journal.Pbio.3000136 |
0.763 |
|
| 2019 |
Bell TA, Baker TA, Sauer RT. Author response: Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding Elife. DOI: 10.7554/Elife.46808.017 |
0.568 |
|
| 2018 |
Bell TA, Baker TA, Sauer RT. Hinge-linker elements in the AAA+ protein unfoldase ClpX mediate intersubunit communication, assembly, and mechanical activity. Biochemistry. PMID 30418765 DOI: 10.1021/Acs.Biochem.8B00907 |
0.652 |
|
| 2018 |
Hari SB, Grant RA, Sauer RT. Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase. Structure (London, England : 1993). PMID 30057024 DOI: 10.1016/J.Str.2018.06.008 |
0.771 |
|
| 2018 |
Brown BL, Kardon JR, Sauer RT, Baker TA. Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. Structure (London, England : 1993). PMID 29551290 DOI: 10.1016/J.Str.2018.02.012 |
0.607 |
|
| 2018 |
Olivares AO, Baker TA, Sauer RT. Mechanical Protein Unfolding and Degradation. Annual Review of Physiology. 80: 413-429. PMID 29433415 DOI: 10.1146/Annurev-Physiol-021317-121303 |
0.655 |
|
| 2018 |
Chandra Kotamarthi H, Sauer R, Baker T. Deciphering the Role of ATPase Domains of CLPA using Single-Molecule Optical Tweezers Biophysical Journal. 114: 170a. DOI: 10.1016/J.Bpj.2017.11.948 |
0.506 |
|
| 2017 |
Amberg-Johnson K, Hari SB, Ganesan SM, Lorenzi HA, Sauer RT, Niles JC, Yeh E. Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens. Elife. 6. PMID 28826494 DOI: 10.7554/Elife.29865 |
0.747 |
|
| 2017 |
Olivares AO, Kotamarthi HC, Stein BJ, Sauer RT, Baker TA. Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines. Proceedings of the National Academy of Sciences of the United States of America. PMID 28724722 DOI: 10.1073/Pnas.1707794114 |
0.841 |
|
| 2017 |
Baytshtok V, Chen J, Glynn SE, Nager AR, Grant RA, Baker TA, Sauer RT. Covalently Linked HslU Hexamers Support a Probabilistic Mechanism that Links ATP Hydrolysis to Protein Unfolding and Translocation. The Journal of Biological Chemistry. PMID 28223361 DOI: 10.1074/Jbc.M116.768978 |
0.642 |
|
| 2017 |
Amberg-Johnson K, Hari SB, Ganesan SM, Lorenzi HA, Sauer RT, Niles JC, Yeh E. Author response: Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens Elife. DOI: 10.7554/Elife.29865.022 |
0.722 |
|
| 2017 |
Chandra Kotamarthi H, Olivares A, Stein B, Sauer R, Baker T. Single-Molecule Dissection of the Role of Directionality in Protein Degradation by Clp Proteolytic Machines Biophysical Journal. 112: 470a. DOI: 10.1016/J.Bpj.2016.11.2524 |
0.57 |
|
| 2016 |
Hari SB, Sauer RT. The AAA+ FtsH Protease Degrades an ssrA-Tagged Model Protein in the Inner Membrane of Escherichia coli. Biochemistry. PMID 27677373 DOI: 10.1021/Acs.Biochem.6B00920 |
0.781 |
|
| 2016 |
Baytshtok V, Fei X, Grant RA, Baker TA, Sauer RT. A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure (London, England : 1993). PMID 27667691 DOI: 10.1016/J.Str.2016.08.012 |
0.837 |
|
| 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 |
0.804 |
|
| 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 |
0.613 |
|
| 2016 |
Grant RA, Sauer RT, Schmitz KR, Baytshtok V. Structure of HslU L199Q in HslUV complex Structure. DOI: 10.2210/Pdb5Ji2/Pdb |
0.685 |
|
| 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 |
0.628 |
|
| 2015 |
Barthelme D, Sauer RT. Origin and functional evolution of the Cdc48/p97/VCP AAA+ protein unfolding and remodeling machine. Journal of Molecular Biology. PMID 26608813 DOI: 10.1016/J.Jmb.2015.11.015 |
0.442 |
|
| 2015 |
Totaro KA, Barthelme D, Simpson PT, Sauer RT, Sello JK. Substrate-guided optimization of the syringolins yields potent proteasome inhibitors with activity against leukemia cell lines. Bioorganic & Medicinal Chemistry. 23: 6218-22. PMID 26296913 DOI: 10.1016/J.Bmc.2015.07.041 |
0.323 |
|
| 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 |
0.63 |
|
| 2015 |
Carney DW, Schmitz KR, Scruse AC, Sauer RT, Sello JK. Examination of a Structural Model of Peptidomimicry by Cyclic Acyldepsipeptide Antibiotics in Their Interaction with the ClpP Peptidase. Chembiochem : a European Journal of Chemical Biology. PMID 26147653 DOI: 10.1002/Cbic.201500234 |
0.72 |
|
| 2015 |
Barthelme D, Jauregui R, Sauer RT. An ALS disease mutation in Cdc48/p97 impairs 20S proteasome binding and proteolytic communication. Protein Science : a Publication of the Protein Society. PMID 26134898 DOI: 10.1002/Pro.2740 |
0.44 |
|
| 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 |
0.65 |
|
| 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 |
0.79 |
|
| 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 |
0.663 |
|
| 2015 |
Iosefson O, Nager AR, Baker TA, Sauer RT. Erratum: Coordinated gripping of substrate by subunits of an AAA+ proteolytic machine. Nature Chemical Biology. 11: 299. PMID 25785430 DOI: 10.1038/Nchembio0415-299A |
0.52 |
|
| 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 |
0.58 |
|
| 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 |
0.625 |
|
| 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 |
0.628 |
|
| 2014 |
Schmitz KR, Carney DW, Sello JK, Sauer RT. Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery. Proceedings of the National Academy of Sciences of the United States of America. 111: E4587-95. PMID 25267638 DOI: 10.1073/Pnas.1417120111 |
0.759 |
|
| 2014 |
Carney DW, Compton CL, Schmitz KR, Stevens JP, Sauer RT, Sello JK. A simple fragment of cyclic acyldepsipeptides is necessary and sufficient for ClpP activation and antibacterial activity. Chembiochem : a European Journal of Chemical Biology. 15: 2216-20. PMID 25212124 DOI: 10.1002/Cbic.201402358 |
0.706 |
|
| 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 |
0.631 |
|
| 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 |
0.602 |
|
| 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 |
0.802 |
|
| 2014 |
Schmitz KR, Sauer RT. Substrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidase. Molecular Microbiology. 93: 617-28. PMID 24976069 DOI: 10.1111/Mmi.12694 |
0.774 |
|
| 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 |
0.568 |
|
| 2014 |
Kim S, Sauer RT. Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress. Genes & Development. 28: 902-11. PMID 24736846 DOI: 10.1101/Gad.238394.114 |
0.36 |
|
| 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 |
0.651 |
|
| 2014 |
Carney DW, Schmitz KR, Truong JV, Sauer RT, Sello JK. Restriction of the conformational dynamics of the cyclic acyldepsipeptide antibiotics improves their antibacterial activity. Journal of the American Chemical Society. 136: 1922-9. PMID 24422534 DOI: 10.1021/Ja410385C |
0.722 |
|
| 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 |
0.646 |
|
| 2014 |
Sauer RT, Yosefson O, Stinson BM, Nager AR, Glynn SE, Schmitz KR, Olivares AO, Manning HW, Shin Y, Cordova JC, Lang MJ, Baker TA. ClpX, a Stochastic Protein Unfolding and Translocation Machine Biophysical Journal. 106: 444a. DOI: 10.1016/J.Bpj.2013.11.2514 |
0.817 |
|
| 2014 |
Olivares AO, Cordvoa JC, Calmat S, Lang MJ, Sauer RT, Baker TA. Mechanical Protein Unfolding and Translocation by AAA+ Proteases Biophysical Journal. 106: 246a. DOI: 10.1016/J.Bpj.2013.11.1443 |
0.642 |
|
| 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 |
0.639 |
|
| 2013 |
Compton CL, Schmitz KR, Sauer RT, Sello JK. Antibacterial activity of and resistance to small molecule inhibitors of the ClpP peptidase. Acs Chemical Biology. 8: 2669-77. PMID 24047344 DOI: 10.1021/Cb400577B |
0.703 |
|
| 2013 |
Sauer RT. Mutagenic dissection of the sequence determinants of protein folding, recognition, and machine function. Protein Science : a Publication of the Protein Society. 22: 1675-87. PMID 23963737 DOI: 10.1002/Pro.2334 |
0.503 |
|
| 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 |
0.65 |
|
| 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 |
0.796 |
|
| 2013 |
Barthelme D, Sauer RT. Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proceedings of the National Academy of Sciences of the United States of America. 110: 3327-32. PMID 23401548 DOI: 10.1073/Pnas.1300408110 |
0.458 |
|
| 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 |
0.64 |
|
| 2013 |
Mauldin RV, Sauer RT. Allosteric regulation of DegS protease subunits through a shared energy landscape. Nature Chemical Biology. 9: 90-6. PMID 23201899 DOI: 10.1038/Nchembio.1135 |
0.436 |
|
| 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. DOI: 10.1364/Fio.2013.Fth1D.4 |
0.766 |
|
| 2013 |
Nager AR, Baker TA, Sauer RT. Corrigendum to “Stepwise Unfolding of a β Barrel Protein by the AAA + ClpXP Protease” [J. Mol. Biol. 413/1 (2011) 4–16] Journal of Molecular Biology. 425: 1241-1243. DOI: 10.1016/J.Jmb.2013.02.001 |
0.528 |
|
| 2013 |
Vieux EF, Wohlever ML, Chen J, Sauer RT, Baker TA. Distinct Quaternary Structures of Lon Protease Control Substrate Degradation Biophysical Journal. 104: 554a. DOI: 10.1016/J.Bpj.2012.11.3071 |
0.645 |
|
| 2012 |
Barthelme D, Sauer RT. Identification of the Cdc48•20S proteasome as an ancient AAA+ proteolytic machine. Science (New York, N.Y.). 337: 843-6. PMID 22837385 DOI: 10.1126/Science.1224352 |
0.371 |
|
| 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 |
0.611 |
|
| 2012 |
Kim S, Sauer RT. Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival. Proceedings of the National Academy of Sciences of the United States of America. 109: 7263-8. PMID 22529381 DOI: 10.1073/Pnas.1204791109 |
0.463 |
|
| 2012 |
Gur E, Vishkautzan M, Sauer RT. Protein unfolding and degradation by the AAA+ Lon protease. Protein Science : a Publication of the Protein Society. 21: 268-78. PMID 22162032 DOI: 10.1002/Pro.2013 |
0.528 |
|
| 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 |
0.662 |
|
| 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 |
0.671 |
|
| 2012 |
Aubin-Tam M, Olivares AO, Carlos Cordova J, Calmat S, Sauer RT, Baker TA, Lang MJ. Single-Molecule Protein Unfolding and Translocation by the AAA+ Protease, ClpXP Biophysical Journal. 102: 610a. DOI: 10.1016/J.Bpj.2011.11.3328 |
0.63 |
|
| 2012 |
Stinson BM, Glynn SE, Nager AR, Baker TA, Sauer RT. Eliminating ATP Binding in Specific ClpX Subunits Yields Functional ATP-Fueled Protein-Unfolding Machines Biophysical Journal. 102: 21a. DOI: 10.1016/J.Bpj.2011.11.138 |
0.652 |
|
| 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 |
0.835 |
|
| 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 |
0.631 |
|
| 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 |
0.608 |
|
| 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 |
0.643 |
|
| 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 |
0.644 |
|
| 2011 |
Kim S, Grant RA, Sauer RT. Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell. 145: 67-78. PMID 21458668 DOI: 10.1016/J.Cell.2011.02.024 |
0.462 |
|
| 2011 |
Chaba R, Alba BM, Guo MS, Sohn J, Ahuja N, Sauer RT, Gross CA. Signal integration by DegS and RseB governs the σ E-mediated envelope stress response in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 108: 2106-11. PMID 21245315 DOI: 10.1073/Pnas.1019277108 |
0.339 |
|
| 2011 |
Davis JH, Rubin AJ, Sauer RT. Design, construction and characterization of a set of insulated bacterial promoters. Nucleic Acids Research. 39: 1131-41. PMID 20843779 DOI: 10.1093/Nar/Gkq810 |
0.78 |
|
| 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 |
0.675 |
|
| 2010 |
Sohn J, Grant RA, Sauer RT. Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. The Journal of Biological Chemistry. 285: 34039-47. PMID 20739286 DOI: 10.1074/Jbc.M110.135541 |
0.475 |
|
| 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 |
0.605 |
|
| 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 |
0.628 |
|
| 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 |
0.585 |
|
| 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 |
0.632 |
|
| 2010 |
Weiss MA, Stearman R, Jeitler-Nilsson A, Karplus M, Sauer RT. Protein-Protein Interactions in DNA Recognition: H-NMR Studies of Lambda cI Repressors Genetically Altered by Site-Directed Mutagenesis. Biophysical Journal. 49: 29-33. PMID 19431635 DOI: 10.1016/S0006-3495(86)83581-0 |
0.376 |
|
| 2010 |
Shin Y, Davis JH, Brau RR, Martin A, Baker T, Sauer RT, Lang MJ. Clpxp Degradation of Proteins Probed By Single-Molecule Fluorescence Biophysical Journal. 98: 34a. DOI: 10.1016/J.Bpj.2009.12.200 |
0.828 |
|
| 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 |
0.734 |
|
| 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 |
0.835 |
|
| 2009 |
Gur E, Sauer RT. Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine. Proceedings of the National Academy of Sciences of the United States of America. 106: 18503-8. PMID 19841274 DOI: 10.1073/Pnas.0910392106 |
0.513 |
|
| 2009 |
Sohn J, Grant RA, Sauer RT. OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure (London, England : 1993). 17: 1411-21. PMID 19836340 DOI: 10.1016/J.Str.2009.07.017 |
0.374 |
|
| 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 |
0.825 |
|
| 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 |
0.614 |
|
| 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 |
0.592 |
|
| 2009 |
Cezairliyan BO, Sauer RT. Control of Pseudomonas aeruginosa AlgW protease cleavage of MucA by peptide signals and MucB. Molecular Microbiology. 72: 368-79. PMID 19298369 DOI: 10.1111/J.1365-2958.2009.06654.X |
0.415 |
|
| 2009 |
Sohn J, Sauer RT. OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations. Molecular Cell. 33: 64-74. PMID 19150428 DOI: 10.1016/J.Molcel.2008.12.017 |
0.4 |
|
| 2009 |
Ahuja N, Korkin D, Chaba R, Cezairliyan BO, Sauer RT, Kim KK, Gross CA. Analyzing the interaction of RseA and RseB, the two negative regulators of the sigmaE envelope stress response, using a combined bioinformatic and experimental strategy. The Journal of Biological Chemistry. 284: 5403-13. PMID 19103591 DOI: 10.1074/Jbc.M806012200 |
0.425 |
|
| 2009 |
Chowdhury T, Chien P, Sauer RT, Baker TA. Elucidating The Specificity Determinants Responsible For ClpX-Adaptor Interaction Biophysical Journal. 96: 82a. DOI: 10.1016/J.Bpj.2008.12.326 |
0.647 |
|
| 2008 |
Moore SD, Sauer RT. Revisiting the mechanism of macrolide-antibiotic resistance mediated by ribosomal protein L22. Proceedings of the National Academy of Sciences of the United States of America. 105: 18261-6. PMID 19015512 DOI: 10.1073/Pnas.0810357105 |
0.658 |
|
| 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 |
0.579 |
|
| 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 |
0.742 |
|
| 2008 |
Gur E, Sauer RT. Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease. Proceedings of the National Academy of Sciences of the United States of America. 105: 16113-8. PMID 18852454 DOI: 10.1073/Pnas.0808802105 |
0.428 |
|
| 2008 |
Gur E, Sauer RT. Recognition of misfolded proteins by Lon, a AAA(+) protease. Genes & Development. 22: 2267-77. PMID 18708584 DOI: 10.1101/Gad.1670908 |
0.507 |
|
| 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 |
0.731 |
|
| 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 |
0.631 |
|
| 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 |
0.6 |
|
| 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 |
0.605 |
|
| 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 |
0.737 |
|
| 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 |
0.643 |
|
| 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 |
0.751 |
|
| 2007 |
Sohn J, Grant RA, Sauer RT. Allosteric activation of DegS, a stress sensor PDZ protease. Cell. 131: 572-83. PMID 17981123 DOI: 10.1016/J.Cell.2007.08.044 |
0.458 |
|
| 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 |
0.656 |
|
| 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 |
0.729 |
|
| 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 |
0.587 |
|
| 2007 |
Cezairliyan BO, Sauer RT. Inhibition of regulated proteolysis by RseB. Proceedings of the National Academy of Sciences of the United States of America. 104: 3771-6. PMID 17360428 DOI: 10.1073/Pnas.0611567104 |
0.419 |
|
| 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 |
0.57 |
|
| 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 |
0.795 |
|
| 2007 |
Moore SD, Sauer RT. The tmRNA system for translational surveillance and ribosome rescue. Annual Review of Biochemistry. 76: 101-24. PMID 17291191 DOI: 10.1146/Annurev.Biochem.75.103004.142733 |
0.655 |
|
| 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 |
0.667 |
|
| 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 |
0.644 |
|
| 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 |
0.605 |
|
| 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 |
0.608 |
|
| 2005 |
Anderson TA, Cordes MH, Sauer RT. Sequence determinants of a conformational switch in a protein structure. Proceedings of the National Academy of Sciences of the United States of America. 102: 18344-9. PMID 16344489 DOI: 10.1073/Pnas.0509349102 |
0.371 |
|
| 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 |
0.727 |
|
| 2005 |
Moore SD, Sauer RT. Ribosome rescue: tmRNA tagging activity and capacity in Escherichia coli. Molecular Microbiology. 58: 456-66. PMID 16194232 DOI: 10.1111/J.1365-2958.2005.04832.X |
0.688 |
|
| 2005 |
Farrell CM, Grossman AD, Sauer RT. Cytoplasmic degradation of ssrA-tagged proteins. Molecular Microbiology. 57: 1750-61. PMID 16135238 DOI: 10.1111/J.1365-2958.2005.04798.X |
0.448 |
|
| 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 |
0.751 |
|
| 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 |
0.793 |
|
| 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 |
0.583 |
|
| 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 |
0.67 |
|
| 2005 |
Tabtiang RK, Cezairliyan BO, Grant RA, Cochrane JC, Sauer RT. Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 102: 2305-9. PMID 15689399 DOI: 10.1073/Pnas.0409562102 |
0.477 |
|
| 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 |
0.659 |
|
| 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 |
0.787 |
|
| 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 |
0.774 |
|
| 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 |
0.616 |
|
| 2004 |
McGinness KE, Sauer RT. Ribosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these molecules. Proceedings of the National Academy of Sciences of the United States of America. 101: 13454-9. PMID 15340139 DOI: 10.1073/Pnas.0405521101 |
0.421 |
|
| 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 |
0.634 |
|
| 2004 |
Spector S, Sauer RT, Tidor B. Computational and experimental probes of symmetry mismatches in the Arc repressor-DNA complex. Journal of Molecular Biology. 340: 253-61. PMID 15201050 DOI: 10.1016/J.Jmb.2004.04.026 |
0.717 |
|
| 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 |
0.648 |
|
| 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 |
0.62 |
|
| 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 |
0.621 |
|
| 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 |
0.791 |
|
| 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 |
0.771 |
|
| 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 |
0.652 |
|
| 2003 |
Hayes CS, Sauer RT. Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Molecular Cell. 12: 903-11. PMID 14580341 DOI: 10.1016/S1097-2765(03)00385-X |
0.612 |
|
| 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 |
0.661 |
|
| 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 |
0.793 |
|
| 2003 |
Schreiter ER, Sintchak MD, Guo Y, Chivers PT, Sauer RT, Drennan CL. Crystal structure of the nickel-responsive transcription factor NikR. Nature Structural Biology. 10: 794-9. PMID 12970756 DOI: 10.1038/Nsb985 |
0.392 |
|
| 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 |
0.649 |
|
| 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 |
0.594 |
|
| 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 |
0.598 |
|
| 2003 |
Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT. OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell. 113: 61-71. PMID 12679035 DOI: 10.1016/S0092-8674(03)00203-4 |
0.414 |
|
| 2003 |
Moore SD, McGinness KE, Sauer RT. Structural biology. A glimpse into tmRNA-mediated ribosome rescue. Science (New York, N.Y.). 300: 72-3. PMID 12677051 DOI: 10.1126/Science.1084034 |
0.618 |
|
| 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 |
0.649 |
|
| 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 |
0.655 |
|
| 2003 |
Anderson TA, Sauer RT. Role of an N(cap) residue in determining the stability and operator-binding affinity of Arc repressor. Biophysical Chemistry. 100: 341-50. PMID 12646376 DOI: 10.1016/S0301-4622(02)00291-0 |
0.441 |
|
| 2003 |
Cordes MHJ, Walsh NP, McKnight CJ, Sauer RT. Solution structure of switch Arc, a mutant with 310 helices replacing a wild-type β-ribbon Journal of Molecular Biology. 326: 899-909. PMID 12581649 DOI: 10.1016/S0022-2836(02)01425-0 |
0.378 |
|
| 2003 |
Hayes CS, Sauer RT. Toxin-antitoxin pairs in bacteria: killers or stress regulators? Cell. 112: 2-4. PMID 12526786 DOI: 10.1016/S0092-8674(02)01282-5 |
0.569 |
|
| 2003 |
Carrington PE, Chivers PT, Al-Mjeni F, Sauer RT, Maroney MJ. Nickel coordination is regulated by the DNA-bound state of NikR. Nature Structural Biology. 10: 126-30. PMID 12524532 DOI: 10.1038/Nsb890 |
0.405 |
|
| 2002 |
Srivastava AK, Sauer RT. Mutational studies of protein stability and folding of the hyperstable MYL Arc repressor variant Biophysical Chemistry. 101: 35-42. PMID 12487987 DOI: 10.1016/S0301-4622(02)00180-1 |
0.327 |
|
| 2002 |
Wah DA, Levchenko I, Baker TA, Sauer RT. Characterization of a specificity factor for an AAA+ ATPase: assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chemistry & Biology. 9: 1237-45. PMID 12445774 DOI: 10.1016/S1074-5521(02)00268-5 |
0.666 |
|
| 2002 |
Chivers PT, Sauer RT. NikR repressor: high-affinity nickel binding to the C-terminal domain regulates binding to operator DNA. Chemistry & Biology. 9: 1141-8. PMID 12401498 DOI: 10.1016/S1074-5521(02)00241-7 |
0.379 |
|
| 2002 |
Hayes CS, Bose B, Sauer RT. Proline residues at the C terminus of nascent chains induce SsrA tagging during translation termination. The Journal of Biological Chemistry. 277: 33825-32. PMID 12105207 DOI: 10.1074/Jbc.M205405200 |
0.664 |
|
| 2002 |
Krantz BA, Srivastava AK, Nauli S, Baker D, Sauer RT, Sosnick TR. Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects. Nature Structural Biology. 9: 458-63. PMID 11979278 DOI: 10.1038/Nsb794 |
0.341 |
|
| 2002 |
Hayes CS, Bose B, Sauer RT. Stop codons preceded by rare arginine codons are efficient determinants of SsrA tagging in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 99: 3440-5. PMID 11891313 DOI: 10.1073/Pnas.052707199 |
0.644 |
|
| 2002 |
Sauer R, Burton R, Kenniston J, Joshi S, Wah D, Levchenko I, Grant R, Flynn J, Neher S, Baker T. ATP-dependent protein degradation and unfolding by ClpXP Gbm Annual Fall Meeting Halle 2002. 2002. DOI: 10.1240/sav_gbm_2002_h_000261 |
0.578 |
|
| 2002 |
Wah DA, Levchenko I, Baker TA, Sauer RT. Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer Chemistry and Biology. 9: 1237-1245. DOI: 10.1016/S1074-5521(02)00268-5 |
0.542 |
|
| 2001 |
Smith CK, Wöhnert J, Sauer RT, Schwalbe H. Assignments of the 1H,13C, and 15N resonances of the substrate-binding SSD domain from Lon protease. Journal of Biomolecular Nmr. 21: 387-8. PMID 11824761 DOI: 10.1023/A:1013386625751 |
0.354 |
|
| 2001 |
Barends S, Karzai AW, Sauer RT, Wower J, Kraal B. Simultaneous and functional binding of SmpB and EF-Tu·GTP to the alanyl acceptor arm of tmRNA Journal of Molecular Biology. 314: 9-21. PMID 11724528 DOI: 10.1006/Jmbi.2001.5114 |
0.449 |
|
| 2001 |
Flynn JM, Levchenko I, Seidel M, Wickner SH, Sauer RT, Baker TA. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis Proceedings of the National Academy of Sciences of the United States of America. 98: 10584-10589. PMID 11535833 DOI: 10.1073/Pnas.191375298 |
0.641 |
|
| 2001 |
Hendsch ZS, Nohaile MJ, Sauer RT, Tidor B. Preferential heterodimer formation via undercompensated electrostatic interactions [18] Journal of the American Chemical Society. 123: 1264-1265. PMID 11456695 DOI: 10.1021/Ja0032273 |
0.521 |
|
| 2001 |
Burton RE, Siddiqui SM, Kim YI, Baker TA, Sauer RT. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine Embo Journal. 20: 3092-3100. PMID 11406586 DOI: 10.1093/Emboj/20.12.3092 |
0.665 |
|
| 2001 |
Roche ED, Sauer RT. Identification of Endogenous SsrA-tagged Proteins Reveals Tagging at Positions Corresponding to Stop Codons Journal of Biological Chemistry. 276: 28509-28515. PMID 11373298 DOI: 10.1074/Jbc.M103864200 |
0.454 |
|
| 2001 |
Lo JH, Baker TA, Sauer RT. Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase. Protein Science : a Publication of the Protein Society. 10: 551-9. PMID 11344323 DOI: 10.1110/Ps.41401 |
0.627 |
|
| 2001 |
Nohaile MJ, Hendsch ZS, Tidor B, Sauer RT. Altering dimerization specificity by changes in surface electrostatics Proceedings of the National Academy of Sciences of the United States of America. 98: 3109-3114. PMID 11248040 DOI: 10.1073/Pnas.051624498 |
0.56 |
|
| 2001 |
Karzai AW, Sauer RT. Protein factors associated with the SsrA·SmpB tagging and ribosome rescue complex Proceedings of the National Academy of Sciences of the United States of America. 98: 3040-3044. PMID 11248028 DOI: 10.1073/Pnas.051628298 |
0.387 |
|
| 2001 |
Berggrun A, Sauer RT. Contributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor Proceedings of the National Academy of Sciences of the United States of America. 98: 2301-2305. PMID 11226234 DOI: 10.1073/Pnas.041612198 |
0.427 |
|
| 2001 |
Kim YI, Levchenko I, Fraczkowska K, Woodruff RV, Sauer RT, Baker TA. Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. Nature Structural Biology. 8: 230-3. PMID 11224567 DOI: 10.1038/84967 |
0.616 |
|
| 2000 |
Nooren IM, Folkers GE, Kaptein R, Sauer RT, Boelens R. Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex. Journal of Biomolecular Structure & Dynamics. 17: 113-22. PMID 22607414 DOI: 10.1080/07391102.2000.10506611 |
0.412 |
|
| 2000 |
Robinson CR, Sauer RT. Striking stabilization of Arc repressor by an engineered disulfide bond Biochemistry. 39: 12494-12502. PMID 11015231 DOI: 10.1021/Bi001484E |
0.337 |
|
| 2000 |
Levchenko I, Seidel M, Sauer RT, Baker TA. A specificity-enhancing factor for the clpXP degradation machine Science. 289: 2354-2356. PMID 11009422 DOI: 10.1126/Science.289.5488.2354 |
0.642 |
|
| 2000 |
Berggrun A, Sauer RT. Interactions of Arg2 in the Mnt N-terminal arm with the central and flanking regions of the mnt operator Journal of Molecular Biology. 301: 959-973. PMID 10966798 DOI: 10.1006/Jmbi.2000.4007 |
0.348 |
|
| 2000 |
Srivastava AK, Sauer RT. Evidence for partial secondary structure formation in the transition state for Arc repressor refolding and dimerization Biochemistry. 39: 8308-8314. PMID 10889040 DOI: 10.1021/Bi000423D |
0.346 |
|
| 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 DOI: 10.1016/S1097-2765(00)80243-9 |
0.633 |
|
| 2000 |
Chivers PT, Sauer RT. Regulation of high affinity nickel uptake in bacteria. Ni2+-dependent interaction of NikR with wild-type and mutant Journal of Biological Chemistry. 275: 19735-19741. PMID 10787413 DOI: 10.1074/Jbc.M002232200 |
0.404 |
|
| 2000 |
Lin H, Abida WM, Sauer RT, Cornish VW. Dexamethasone-methotrexate: An efficient chemical inducer of protein dimerization in vivo [18] Journal of the American Chemical Society. 122: 4247-4248. DOI: 10.1021/Ja9941532 |
0.715 |
|
| 1999 |
Nooren IM, George AV, Kaptein R, Sauer RT, Boelens R. NMR structure determination of the tetramerization domain of the Mnt repressor: An asymmetric alpha-helical assembly in slow exchange. Journal of Biomolecular Nmr. 15: 39-53. PMID 20703962 DOI: 10.1023/A:1008312309535 |
0.346 |
|
| 1999 |
Chivers PT, Sauer RT. NikR is a ribbon-helix-helix DNA-binding protein Protein Science. 8: 2494-2500. PMID 10595554 DOI: 10.1110/Ps.8.11.2494 |
0.399 |
|
| 1999 |
Roche ED, Sauer RT. SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity Embo Journal. 18: 4579-4589. PMID 10449423 DOI: 10.1093/Emboj/18.16.4579 |
0.364 |
|
| 1999 |
Nooren IM, Kaptein R, Sauer RT, Boelens R. The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nature Structural Biology. 6: 755-9. PMID 10426954 DOI: 10.1038/11531 |
0.4 |
|
| 1999 |
Wali Karzai A, Susskind MM, Sauer RT. SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA) Embo Journal. 18: 3793-3799. PMID 10393194 DOI: 10.1093/Emboj/18.13.3793 |
0.401 |
|
| 1999 |
Rentzeperis D, Jonsson T, Sauer RT. Acceleration of the refolding of Arc repressor by nucleic acids and other polyanions Nature Structural Biology. 6: 569-573. PMID 10360363 DOI: 10.1038/9353 |
0.323 |
|
| 1999 |
Smith CK, Baker TA, Sauer RT. Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proceedings of the National Academy of Sciences of the United States of America. 96: 6678-82. PMID 10359771 DOI: 10.1073/Pnas.96.12.6678 |
0.643 |
|
| 1999 |
Gazit E, Sauer RT. The Doc toxin and Phd antidote proteins of the bacteriophage P1 plasmid addiction system form a heterotrimeric complex. The Journal of Biological Chemistry. 274: 16813-8. PMID 10358024 DOI: 10.1074/Jbc.274.24.16813 |
0.583 |
|
| 1999 |
Nooren IM, Rietveld AW, Melacini G, Sauer RT, Kaptein R, Boelens R. The solution structure and dynamics of an Arc repressor mutant reveal premelting conformational changes related to DNA binding. Biochemistry. 38: 6035-42. PMID 10320329 DOI: 10.1021/Bi982677T |
0.414 |
|
| 1999 |
Sauer RT. Evolution of a Protein Fold in Vitro Science. 284: 325-327. PMID 10195898 DOI: 10.1126/Science.284.5412.325 |
0.418 |
|
| 1999 |
Brown BM, Sauer RT. Tolerance of arc repressor to multiple-alanine substitutions Proceedings of the National Academy of Sciences of the United States of America. 96: 1983-1988. PMID 10051581 DOI: 10.1073/Pnas.96.5.1983 |
0.427 |
|
| 1999 |
Cordes MHJ, Sauer RT. Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions Protein Science. 8: 318-325. PMID 10048325 DOI: 10.1110/Ps.8.2.318 |
0.354 |
|
| 1999 |
Schildbach JF, Karzai AW, Raumann BE, Sauer RT. Origins of DNA-binding specificity: Role of protein contacts with the DNA backbone Proceedings of the National Academy of Sciences of the United States of America. 96: 811-817. PMID 9927650 DOI: 10.1073/Pnas.96.3.811 |
0.412 |
|
| 1999 |
Gazit E, Sauer RT. Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system. The Journal of Biological Chemistry. 274: 2652-7. PMID 9915794 DOI: 10.1074/Jbc.274.5.2652 |
0.575 |
|
| 1998 |
Robinson CR, Sauer RT. Optimizing the stability of single-chain proteins by linker length and composition mutagenesis Proceedings of the National Academy of Sciences of the United States of America. 95: 5929-5934. PMID 9600894 DOI: 10.1073/Pnas.95.11.5929 |
0.423 |
|
| 1998 |
Gottesman S, Roche E, Zhou Y, Sauer RT. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes & Development. 12: 1338-47. PMID 9573050 DOI: 10.1101/Gad.12.9.1338 |
0.47 |
|
| 1998 |
Gregoret LM, Sauer RT. Tolerance of a protein helix to multiple alanine and valine substitutions. Folding & Design. 3: 119-26. PMID 9565756 DOI: 10.1016/S1359-0278(98)00017-0 |
0.437 |
|
| 1998 |
Schildbach JF, Robinson CR, Sauer RT. Biophysical characterization of the TraY protein of Escherichia coli F factor Journal of Biological Chemistry. 273: 1329-1333. PMID 9430665 DOI: 10.1074/Jbc.273.3.1329 |
0.374 |
|
| 1997 |
Levchenko I, Smith CK, Walsh NP, Sauer RT, Baker TA. PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell. 91: 939-47. PMID 9428517 DOI: 10.1016/S0092-8674(00)80485-7 |
0.633 |
|
| 1997 |
Robinson CR, Rentzeperis D, Silva JL, Sauer RT. Formation of a denatured dimer limits the thermal stability of Arc repressor Journal of Molecular Biology. 273: 692-700. PMID 9356257 DOI: 10.1006/Jmbi.1997.1342 |
0.37 |
|
| 1997 |
Tucker-Kellogg L, Rould MA, Chambers KA, Ades SE, Sauer RT, Pabo CO. Engrailed (Gln50-->Lys) homeodomain-DNA complex at 1.9 A resolution: structural basis for enhanced affinity and altered specificity. Structure (London, England : 1993). 5: 1047-54. PMID 9309220 DOI: 10.1016/S0969-2126(97)00256-6 |
0.69 |
|
| 1996 |
Sauer RT. Protein folding from a combinatorial perspective Folding and Design. 1: R27-R30. PMID 9079366 DOI: 10.1016/S1359-0278(96)00015-6 |
0.38 |
|
| 1996 |
Smith TL, Sauer RT. Role of operator subsites in arc repression Journal of Molecular Biology. 264: 233-242. PMID 8951373 DOI: 10.1006/Jmbi.1996.0637 |
0.381 |
|
| 1996 |
Robinson CR, Sauer RT. Equilibrium stability and sub-millisecond refolding of a designed single-chain Arc repressor Biochemistry. 35: 13878-13884. PMID 8909284 DOI: 10.1021/Bi961375T |
0.351 |
|
| 1996 |
Waldburger CD, Sauer RT. Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants Journal of Biological Chemistry. 271: 26630-26636. PMID 8900137 DOI: 10.1074/Jbc.271.43.26630 |
0.359 |
|
| 1996 |
Kolmar H, Waller PRH, Sauer RT. The DegP and DegQ periplasmic endoproteases of Escherichia coli: Specificity for cleavage sites and substrate conformation Journal of Bacteriology. 178: 5925-5929. PMID 8830688 DOI: 10.1128/Jb.178.20.5925-5929.1996 |
0.492 |
|
| 1996 |
Sauer RT. Lac repressor at last Structure. 4: 219-222. PMID 8805532 DOI: 10.1016/S0969-2126(96)00025-1 |
0.349 |
|
| 1996 |
Sauer R, Harrison S. Interactions of proteins with RNA and DNA. Current Opinion in Structural Biology. 6: 51-52. PMID 8805463 DOI: 10.1016/S0959-440X(96)80094-7 |
0.316 |
|
| 1996 |
Smith TL, Sauer RT. Dual regulation of open-complex formation and promoter clearance by Arc explains a novel repressor to activator switch Proceedings of the National Academy of Sciences of the United States of America. 93: 8868-8872. PMID 8799119 DOI: 10.1073/Pnas.93.17.8868 |
0.345 |
|
| 1996 |
Cordes MHJ, Davidson AR, Sauer RT. Sequence space, folding and protein design Current Opinion in Structural Biology. 6: 3-10. PMID 8696970 DOI: 10.1016/S0959-440X(96)80088-1 |
0.428 |
|
| 1996 |
Hendsch ZS, Jonsson T, Sauer RT, Tidor B. Protein stabilization by removal of unsatisfied polar groups: computational approaches and experimental tests. Biochemistry. 35: 7621-5. PMID 8672461 DOI: 10.1021/Bi9605191 |
0.602 |
|
| 1996 |
Jonsson T, Waldburger CD, Sauer RT. Nonlinear free energy relationships in arc repressor unfolding imply the existence of unstable, native-like folding intermediates Biochemistry. 35: 4795-4802. PMID 8664269 DOI: 10.1021/Bi953056S |
0.337 |
|
| 1996 |
Waldburger CD, Jonsson T, Sauer RT. Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure Proceedings of the National Academy of Sciences of the United States of America. 93: 2629-2634. PMID 8610092 DOI: 10.1073/Pnas.93.7.2629 |
0.374 |
|
| 1996 |
Keiler KC, Waller PRH, Sauer RT. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA Science. 271: 990-993. PMID 8584937 DOI: 10.1126/Science.271.5251.990 |
0.31 |
|
| 1996 |
Keiler KC, Sauer RT. Sequence determinants of C-terminal substrate recognition by the Tsp protease Journal of Biological Chemistry. 271: 2589-2593. PMID 8576225 DOI: 10.1074/Jbc.271.5.2589 |
0.428 |
|
| 1996 |
Waller PRH, Sauer RT. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease Journal of Bacteriology. 178: 1146-1153. PMID 8576051 DOI: 10.1128/Jb.178.4.1146-1153.1996 |
0.351 |
|
| 1996 |
Sauer RT, Milla ME, Waldburger CD, Brown BM, Schildbach JF. Sequence determinants of folding and stability for the P22 Arc repressor dimer Faseb Journal. 10: 42-48. PMID 8566546 DOI: 10.1096/Fasebj.10.1.8566546 |
0.381 |
|
| 1996 |
Robinson CR, Sauer RT. Covalent attachment of arc repressor subunits by a peptide linker enhances affinity for operator DNA Biochemistry. 35: 109-116. PMID 8555163 DOI: 10.1021/Bi9521194 |
0.39 |
|
| 1995 |
Raumann BE, Knight KL, Sauer RT. Dramatic changes in DNA-binding specificity caused by single residue substitutions in an Arc/Mnt hybrid repressor Nature Structural Biology. 2: 1115-1122. PMID 8846224 DOI: 10.1038/Nsb1295-1115 |
0.416 |
|
| 1995 |
Keiler KC, Silber KR, Downard KM, Papayannopoulos IA, Biemann K, Sauer RT. C-terminal specific protein degradation: activity and substrate specificity of the Tsp protease. Protein Science : a Publication of the Protein Society. 4: 1507-15. PMID 8520476 DOI: 10.1002/Pro.5560040808 |
0.477 |
|
| 1995 |
Milla ME, Sauer RT. Critical side-chain interactions at a subunit interface in the Arc repressor dimer Biochemistry. 34: 3344-3351. PMID 7880830 DOI: 10.1021/Bi00010A025 |
0.435 |
|
| 1995 |
Waldburger CD, Schildbach JF, Sauer RT. Are buried salt bridges important for protein stability and conformational specificity? Nature Structural Biology. 2: 122-128. PMID 7749916 DOI: 10.1038/Nsb0295-122 |
0.382 |
|
| 1995 |
Milla ME, Brown BM, Sauer RT. Protein stability effects of a complete set of alanine substitutions in Arc repressor. Nature Structural Biology. 1: 518-23. PMID 7664079 DOI: 10.1038/Nsb0894-518 |
0.34 |
|
| 1995 |
Brown BM, Milla ME, Smith TL, Sauer RT. Scanning mutagenesis of the Arc repressor as a functional probe of operator recognition. Nature Structural Biology. 1: 164-8. PMID 7656034 DOI: 10.1038/Nsb0394-164 |
0.425 |
|
| 1995 |
Smith TL, Sauer RT. P22 arc repressor: Role of cooperativity in repression and binding to operators with altered half-site spacing Journal of Molecular Biology. 249: 729-742. PMID 7602585 DOI: 10.1006/Jmbi.1995.0332 |
0.419 |
|
| 1995 |
Ades SE, Sauer RT. Specificity of minor-groove and major-groove interactions in a homeodomain-DNA complex Biochemistry. 34: 14601-14608. PMID 7578067 DOI: 10.1021/Bi00044A040 |
0.384 |
|
| 1995 |
Milla ME, Brown BM, Waldburger CD, Sauer RT. P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding Biochemistry. 34: 13914-13919. PMID 7577986 DOI: 10.1021/Bi00042A024 |
0.34 |
|
| 1995 |
Davidson AR, Lumb KJ, Sauer RT. Cooperatively folded proteins in random sequence libraries Nature Structural Biology. 2: 856-864. PMID 7552709 DOI: 10.1038/Nsb1095-856 |
0.441 |
|
| 1995 |
Waldburger CD, Sauer RT. Domains of Mnt repressor: Roles in tetramer formation, protein stability, and operator DNA binding Biochemistry. 34: 13109-13116. PMID 7548071 DOI: 10.1021/Bi00040A023 |
0.454 |
|
| 1995 |
Keiler KC, Sauer RT. Identification of active site residues of the Tsp protease Journal of Biological Chemistry. 270: 28864-28868. PMID 7499412 DOI: 10.1074/Jbc.270.48.28864 |
0.428 |
|
| 1994 |
Milla ME, Brown BM, Sauer RT. P22 Arc repressor: enhanced expression of unstable mutants by addition of polar C-terminal sequences. Protein Science : a Publication of the Protein Society. 2: 2198-205. PMID 8298465 DOI: 10.1002/Pro.5560021219 |
0.362 |
|
| 1994 |
Lim WA, Hodel A, Sauer RT, Richards FM. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proceedings of the National Academy of Sciences of the United States of America. 91: 423-7. PMID 8278404 DOI: 10.1073/Pnas.91.1.423 |
0.742 |
|
| 1994 |
Silber KR, Sauer RT. Deletion of the prc (tsp) gene provides evidence for additional tail-specific proteolytic activity in Escherichia coli K-12 Mgg Molecular &Amp; General Genetics. 242: 237-240. PMID 8159175 DOI: 10.1007/Bf00391018 |
0.452 |
|
| 1994 |
Davidson AR, Sauer RT. Folded proteins occur frequently in libraries of random amino acid sequences. Proceedings of the National Academy of Sciences of the United States of America. 91: 2146-50. PMID 8134363 DOI: 10.1073/Pnas.91.6.2146 |
0.44 |
|
| 1994 |
Milla ME, Sauer RT. P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. Biochemistry. 33: 1125-33. PMID 8110744 DOI: 10.1021/Bi00171A011 |
0.371 |
|
| 1994 |
Raumann BE, Rould MA, Pabo CO, Sauer RT. DNA recognition by beta-sheets in the Arc repressor-operator crystal structure. Nature. 367: 754-7. PMID 8107872 DOI: 10.1038/367754A0 |
0.658 |
|
| 1994 |
Ades SE, Sauer RT. Differential DNA-binding specificity of the engrailed homeodomain: The role of residue 50 Biochemistry. 33: 9187-9194. PMID 8049221 DOI: 10.1021/Bi00197A022 |
0.409 |
|
| 1994 |
Burgering MJ, Boelens R, Gilbert DE, Breg JN, Knight KL, Sauer RT, Kaptein R. Solution structure of dimeric Mnt repressor (1-76). Biochemistry. 33: 15036-45. PMID 7999761 DOI: 10.1021/Bi00254A012 |
0.402 |
|
| 1994 |
Marqusee S, Sauer RT. Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor. Protein Science : a Publication of the Protein Society. 3: 2217-25. PMID 7756981 DOI: 10.1002/Pro.5560031207 |
0.625 |
|
| 1994 |
Raumann BE, Brown BM, Sauer RT. Major groove DNA recognition by β-sheets: the ribbon-helix-helix family of gene regulatory proteins Current Opinion in Structural Biology. 4: 36-43. DOI: 10.1016/S0959-440X(94)90057-4 |
0.368 |
|
| 1993 |
Gregoret LM, Sauer RT. Additivity of mutant effects assessed by binomial mutagenesis Proceedings of the National Academy of Sciences of the United States of America. 90: 4246-4250. PMID 8483940 DOI: 10.1073/Pnas.90.9.4246 |
0.329 |
|
| 1993 |
Brown BM, Sauer RT. Assembly of the Arc repressor-operator complex: cooperative interactions between DNA-bound dimers. Biochemistry. 32: 1354-63. PMID 8448144 DOI: 10.1021/Bi00056A022 |
0.39 |
|
| 1993 |
Waugh DS, Sauer RT. Single amino acid substitutions uncouple the DNA binding and strand scission activities of Fok I endonuclease. Proceedings of the National Academy of Sciences of the United States of America. 90: 9596-600. PMID 8415747 DOI: 10.1073/Pnas.90.20.9596 |
0.388 |
|
| 1993 |
Beckett D, Burz DS, Ackers GK, Sauer RT. Isolation of lambda repressor mutants with defects in cooperative operator binding. Biochemistry. 32: 9073-9. PMID 8369279 DOI: 10.1021/Bi00086A012 |
0.735 |
|
| 1993 |
Hu JC, Newell NE, Tidor B, Sauer RT. Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis. Protein Science : a Publication of the Protein Society. 2: 1072-84. PMID 8102921 DOI: 10.1002/Pro.5560020701 |
0.612 |
|
| 1992 |
Silber KR, Keiler KC, Sauer RT. Tsp: A tail-specific protease that selectively degrades proteins with nonpolar C termini Proceedings of the National Academy of Sciences of the United States of America. 89: 295-299. PMID 1729701 DOI: 10.1073/Pnas.89.1.295 |
0.461 |
|
| 1992 |
Lim WA, Farruggio DC, Sauer RT. Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry. 31: 4324-33. PMID 1567879 DOI: 10.1021/Bi00132A025 |
0.641 |
|
| 1992 |
Pabo CO, Sauer RT. Transcription factors: structural families and principles of DNA recognition. Annual Review of Biochemistry. 61: 1053-95. PMID 1497306 DOI: 10.1146/Annurev.Bi.61.070192.005201 |
0.604 |
|
| 1992 |
Sauer RT, Lim WA. Mutational analysis of protein stability Current Biology. 2: 81. DOI: 10.1016/0960-9822(92)90210-2 |
0.571 |
|
| 1992 |
Sauer RT, Lim WA. Mutational analysis of protein stability. Current Opinion in Structural Biology 1992, 2:46...-51 Current Opinion in Structural Biology. 2: 46-51. DOI: 10.1016/0959-440X(92)90175-7 |
0.642 |
|
| 1992 |
Knight K, Sauer R. Biochemical and genetic analysis of operator contacts made by residues within the beta-sheet DNA binding motif of Mnt repressor. The Embo Journal. 11: 215-223. DOI: 10.1002/J.1460-2075.1992.Tb05044.X |
0.362 |
|
| 1991 |
Reidhaar-Olson JF, Parsell DA, Sauer RT. An essential proline in lambda repressor is required for resistance to intracellular proteolysis. Biochemistry. 29: 7563-71. PMID 2148681 DOI: 10.1021/Bi00485A004 |
0.426 |
|
| 1991 |
Mossing MC, Sauer RT. Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence. Science (New York, N.Y.). 250: 1712-5. PMID 2148648 DOI: 10.1126/Science.2148648 |
0.769 |
|
| 1991 |
Lim WA, Sauer RT. The role of internal packing interactions in determining the structure and stability of a protein. Journal of Molecular Biology. 219: 359-76. PMID 2038061 DOI: 10.1016/0022-2836(91)90570-V |
0.659 |
|
| 1991 |
Mossing MC, Bowie JU, Sauer RT. A streptomycin selection for DNA-binding activity. Methods in Enzymology. 208: 604-19. PMID 1838136 DOI: 10.1016/0076-6879(91)08031-C |
0.783 |
|
| 1991 |
Lim WA, Sauer RT, Lander AD. Analysis of DNA-protein interactions by affinity coelectrophoresis. Methods in Enzymology. 208: 196-210. PMID 1838134 DOI: 10.1016/0076-6879(91)08014-9 |
0.603 |
|
| 1991 |
Reidhaar-Olson JF, Bowie JU, Breyer RM, Hu JC, Knight KL, Lim WA, Mossing MC, Parsell DA, Shoemaker KR, Sauer RT. Random mutagenesis of protein sequences using oligonucleotide cassettes. Methods in Enzymology. 208: 564-86. PMID 1779849 DOI: 10.1016/0076-6879(91)08029-H |
0.798 |
|
| 1990 |
Weiss MA, Karplus M, Patel DJ, Sauer RT. Solution NMR studies of intact lambda repressor. Journal of Biomolecular Structure & Dynamics. 1: 151-7. PMID 6401108 DOI: 10.1080/07391102.1983.10507431 |
0.344 |
|
| 1990 |
Weiss MA, Karplus M, Sauer RT. Quaternary structure and function in phage lambda repressor: 1H-NMR studies of genetically altered proteins. Journal of Biomolecular Structure & Dynamics. 5: 539-56. PMID 2978735 DOI: 10.1080/07391102.1987.10506412 |
0.426 |
|
| 1990 |
Pakula AA, Sauer RT. Genetic analysis of protein stability and function. Annual Review of Genetics. 23: 289-310. PMID 2694933 DOI: 10.1146/Annurev.Ge.23.120189.001445 |
0.435 |
|
| 1990 |
Bowie JU, Reidhaar-Olson JF, Lim WA, Sauer RT. Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science (New York, N.Y.). 247: 1306-10. PMID 2315699 DOI: 10.1126/Science.2315699 |
0.714 |
|
| 1990 |
Pakula AA, Sauer RT. Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature. 344: 363-4. PMID 2314475 DOI: 10.1038/344363A0 |
0.38 |
|
| 1990 |
Bowie JU, Sauer RT. TraY proteins of F and related episomes are members of the Arc and Mnt repressor family. Journal of Molecular Biology. 211: 5-6. PMID 2299672 DOI: 10.1016/0022-2836(90)90004-6 |
0.598 |
|
| 1990 |
Brown BM, Bowie JU, Sauer RT. Arc repressor is tetrameric when bound to operator DNA. Biochemistry. 29: 11189-95. PMID 2271706 DOI: 10.1021/Bi00503A006 |
0.622 |
|
| 1990 |
Reidhaar-Olson JF, Sauer RT. Functionally acceptable substitutions in two alpha-helical regions of lambda repressor. Proteins. 7: 306-16. PMID 2199970 DOI: 10.1002/Prot.340070403 |
0.35 |
|
| 1990 |
Sauer RT, Jordan SR, Pabo CO. Lambda repressor: a model system for understanding protein-DNA interactions and protein stability. Advances in Protein Chemistry. 40: 1-61. PMID 2195849 DOI: 10.1016/S0065-3233(08)60286-7 |
0.715 |
|
| 1990 |
Parsell DA, Silber KR, Sauer RT. Carboxy-terminal determinants of intracellular protein degradation Genes and Development. 4: 277-286. PMID 2186965 DOI: 10.1101/Gad.4.2.277 |
0.465 |
|
| 1990 |
Bowie JU, Clarke ND, Pabo CO, Sauer RT. Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures. Proteins. 7: 257-64. PMID 2163535 DOI: 10.1002/Prot.340070307 |
0.751 |
|
| 1990 |
Hu JC, O'Shea EK, Kim PS, Sauer RT. Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions. Science (New York, N.Y.). 250: 1400-3. PMID 2147779 DOI: 10.1126/Science.2147779 |
0.391 |
|
| 1990 |
Doig AJ, Williams DH, Sauer RT. Surface Areas Of Unfolded Proteins Nature. 348: 397-397. PMID 2147231 DOI: 10.1038/348397B0 |
0.314 |
|
| 1989 |
Bowie JU, Sauer RT. Identifying determinants of folding and activity for a protein of unknown structure. Proceedings of the National Academy of Sciences of the United States of America. 86: 2152-6. PMID 2928323 DOI: 10.1073/Pnas.86.7.2152 |
0.648 |
|
| 1989 |
Knight KL, Bowie JU, Vershon AK, Kelley RD, Sauer RT. The Arc and Mnt repressors. A new class of sequence-specific DNA-binding protein. The Journal of Biological Chemistry. 264: 3639-42. PMID 2917965 |
0.769 |
|
| 1989 |
Vershon AK, Kelley RD, Sauer RT. Sequence-specific binding of arc repressor to DNA. Effects of operator mutations and modifications. Journal of Biological Chemistry. 264: 3267-3273. PMID 2914951 |
0.65 |
|
| 1989 |
Bowie JU, Sauer RT. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry. 28: 7139-43. PMID 2819054 DOI: 10.1021/Bi00444A001 |
0.639 |
|
| 1989 |
Pakula AA, Sauer RT. Amino acid substitutions that increase the thermal stability of the lambda Cro protein. Proteins. 5: 202-10. PMID 2780540 DOI: 10.1002/Prot.340050303 |
0.38 |
|
| 1989 |
Parsell DA, Sauer RT. Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes & Development. 3: 1226-32. PMID 2676724 DOI: 10.1101/Gad.3.8.1226 |
0.363 |
|
| 1989 |
Bowie JU, Sauer RT. Identification of C-terminal extensions that protect proteins from intracellular proteolysis. The Journal of Biological Chemistry. 264: 7596-602. PMID 2651443 |
0.627 |
|
| 1989 |
Knight KL, Sauer RT. DNA binding specificity of the Arc and Mnt repressors is determined by a short region of N-terminal residues. Proceedings of the National Academy of Sciences of the United States of America. 86: 797-801. PMID 2644643 DOI: 10.1073/Pnas.86.3.797 |
0.443 |
|
| 1989 |
Zagorski MG, Bowie JU, Vershon AK, Sauer RT, Patel DJ. NMR studies of Arc repressor mutants: proton assignments, secondary structure, and long-range contacts for the thermostable proline-8----leucine variant of Arc. Biochemistry. 28: 9813-25. PMID 2611267 DOI: 10.1021/Bi00451A041 |
0.798 |
|
| 1989 |
Lim WA, Sauer RT. Alternative packing arrangements in the hydrophobic core of lambda repressor. Nature. 339: 31-6. PMID 2524006 DOI: 10.1038/339031A0 |
0.612 |
|
| 1989 |
Gimble FS, Sauer RT. λ Repressor mutants that are better substrates for RecA-mediated cleavage Journal of Molecular Biology. 206: 29-39. PMID 2522996 DOI: 10.1016/0022-2836(89)90521-4 |
0.375 |
|
| 1988 |
Reidhaar-Olson JF, Sauer RT. Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. Science (New York, N.Y.). 241: 53-7. PMID 3388019 DOI: 10.1126/Science.3388019 |
0.396 |
|
| 1988 |
Knight KL, Sauer RT. The Mnt repressor of bacteriophage P22: role of C-terminal residues in operator binding and tetramer formation. Biochemistry. 27: 2088-94. PMID 3288281 DOI: 10.1021/Bi00406A041 |
0.456 |
|
| 1988 |
Sauer RT, Smith DL, Johnson AD. Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free Genes &Amp; Development. 2: 807-816. PMID 3061876 DOI: 10.1101/Gad.2.7.807 |
0.575 |
|
| 1987 |
Vershon AK, Liao SM, McClure WR, Sauer RT. Interaction of the bacteriophage P22 Arc repressor with operator DNA. Journal of Molecular Biology. 195: 323-31. PMID 3656415 DOI: 10.1016/0022-2836(87)90653-X |
0.709 |
|
| 1987 |
Vershon AK, Liao SM, McClure WR, Sauer RT. Bacteriophage P22 Mnt repressor. DNA binding and effects on transcription in vitro. Journal of Molecular Biology. 195: 311-22. PMID 3656414 DOI: 10.1016/0022-2836(87)90652-8 |
0.698 |
|
| 1987 |
Weiss MA, Pabo CO, Karplus M, Sauer RT. Dimerization of the operator binding domain of phage lambda repressor. Biochemistry. 26: 897-904. PMID 2952164 DOI: 10.1021/Bi00377A034 |
0.696 |
|
| 1987 |
Weiss MA, Karplus M, Sauer RT. 1H NMR aromatic spectrum of the operator binding domain of the lambda repressor: resonance assignment with application to structure and dynamics. Biochemistry. 26: 890-7. PMID 2952163 DOI: 10.1021/Bi00377A033 |
0.366 |
|
| 1987 |
Nelson HC, Sauer RT. Interaction of mutant lambda repressors with operator and non-operator DNA. Journal of Molecular Biology. 192: 27-38. PMID 2950238 DOI: 10.1016/0022-2836(86)90461-4 |
0.345 |
|
| 1987 |
Pakula AA, Young VB, Sauer RT. Bacteriophage lambda cro mutations: effects on activity and intracellular degradation. Proceedings of the National Academy of Sciences of the United States of America. 83: 8829-33. PMID 2947238 DOI: 10.1073/Pnas.83.23.8829 |
0.379 |
|
| 1986 |
Poteete AR, Hehir K, Sauer RT. Bacteriophage P22 Cro protein: sequence, purification, and properties. Biochemistry. 25: 251-6. PMID 3954988 DOI: 10.1021/Bi00349A035 |
0.422 |
|
| 1986 |
Gimble FS, Sauer RT. λ Repressor inactivation: Properties of purified ind- proteins in the autodigestion and RecA-mediated cleavage reactions Journal of Molecular Biology. 192: 39-47. PMID 3820305 DOI: 10.1016/0022-2836(86)90462-6 |
0.445 |
|
| 1986 |
Sauer RT, Hehir K, Stearman RS, Weiss MA, Jeitler-Nilsson A, Suchanek EG, Pabo CO. An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of lambda repressor. Biochemistry. 25: 5992-8. PMID 3539184 DOI: 10.1021/Bi00368A024 |
0.708 |
|
| 1986 |
Vershon AK, Bowie JU, Karplus TM, Sauer RT. Isolation and analysis of arc repressor mutants: evidence for an unusual mechanism of DNA binding. Proteins. 1: 302-11. PMID 3449859 DOI: 10.1002/Prot.340010404 |
0.792 |
|
| 1986 |
Hecht MH, Sturtevant JM, Sauer RT. Stabilization of lambda repressor against thermal denaturation by site-directed Gly----Ala changes in alpha-helix 3. Proteins. 1: 43-6. PMID 3449850 DOI: 10.1002/Prot.340010108 |
0.58 |
|
| 1985 |
Weiss MA, Sauer RT, Patel DJ, Karplus M. Amino-terminal arm of the lambda repressor: a 1H NMR study. Biochemistry. 23: 5090-5. PMID 6509013 DOI: 10.1021/Bi00317A002 |
0.368 |
|
| 1985 |
Hecht MH, Hehir KM, Nelson HC, Sturtevant JM, Sauer RT. Increasing and decreasing protein stability: effects of revertant substitutions on the thermal denaturation of phage lambda repressor. Journal of Cellular Biochemistry. 29: 217-24. PMID 4077930 DOI: 10.1002/Jcb.240290306 |
0.645 |
|
| 1985 |
Jordan SR, Pabo CO, Vershon AK, Sauer RT. Crystallization of the Arc repressor. Journal of Molecular Biology. 185: 445-6. PMID 4057251 DOI: 10.1016/0022-2836(85)90415-2 |
0.732 |
|
| 1985 |
Nelson HC, Sauer RT. Lambda repressor mutations that increase the affinity and specificity of operator binding. Cell. 42: 549-58. PMID 3161621 DOI: 10.1016/0092-8674(85)90112-6 |
0.344 |
|
| 1985 |
Vershon AK, Youderian P, Susskind MM, Sauer RT. The bacteriophage P22 Arc and Mnt repressors. Overproduction, purification, and properties Journal of Biological Chemistry. 260: 12124-12129. PMID 2995361 |
0.694 |
|
| 1985 |
Hecht MH, Sauer RT. Phage lambda repressor revertants. Amino acid substitutions that restore activity to mutant proteins. Journal of Molecular Biology. 186: 53-63. PMID 2934554 DOI: 10.1016/0022-2836(85)90256-6 |
0.624 |
|
| 1984 |
Hopper P, Harrison SC, Sauer RT. Structure of tomato bushy stunt virus. V. Coat protein sequence determination and its structural implications. Journal of Molecular Biology. 177: 701-13. PMID 6481803 DOI: 10.1016/0022-2836(84)90045-7 |
0.37 |
|
| 1984 |
Hecht MH, Sturtevant JM, Sauer RT. Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor. Proceedings of the National Academy of Sciences of the United States of America. 81: 5685-9. PMID 6237363 DOI: 10.1073/Pnas.81.18.5685 |
0.569 |
|
| 1984 |
Pabo CO, Sauer RT. Protein-DNA recognition. Annual Review of Biochemistry. 53: 293-321. PMID 6236744 DOI: 10.1146/Annurev.Bi.53.070184.001453 |
0.685 |
|
| 1983 |
Youderian P, Vershon A, Bouvier S, Sauer RT, Susskind MM. Changing the DNA-binding specificity of a repressor. Cell. 35: 777-83. PMID 6652685 DOI: 10.1016/0092-8674(83)90110-1 |
0.7 |
|
| 1983 |
Poteete AR, Sauer RT, Hendrix RW. Domain structure and quaternary organization of the bacteriophage P22 Erf protein Journal of Molecular Biology. 171: 401-418. PMID 6607360 DOI: 10.1016/0022-2836(83)90037-2 |
0.432 |
|
| 1983 |
Sauer RT, Krovatin W, DeAnda J, Youderian P, Susskind MM. Primary structure of the immI immunity region of bacteriophage P22. Journal of Molecular Biology. 168: 699-713. PMID 6350606 DOI: 10.1016/S0022-2836(83)80070-9 |
0.393 |
|
| 1983 |
Berget PB, Poteete AR, Sauer RT. Control of phage P22 tail protein expression by transcription termination. Journal of Molecular Biology. 164: 561-72. PMID 6341605 DOI: 10.1016/0022-2836(83)90050-5 |
0.306 |
|
| 1983 |
Sauer RT, Nelson HC, Hehir K, Hecht MH, Gimble FS, DeAnda J, Poteete AR. The lambda and P22 phage repressors. Journal of Biomolecular Structure & Dynamics. 1: 1011-22. PMID 6242868 DOI: 10.1080/07391102.1983.10507499 |
0.621 |
|
| 1983 |
Nelson HC, Hecht MH, Sauer RT. Mutations defining the operator-binding sites of bacteriophage lambda repressor. Cold Spring Harbor Symposia On Quantitative Biology. 47: 441-9. PMID 6222865 DOI: 10.1101/Sqb.1983.047.01.052 |
0.594 |
|
| 1983 |
Hecht MH, Nelson HC, Sauer RT. Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding. Proceedings of the National Academy of Sciences of the United States of America. 80: 2676-80. PMID 6221342 DOI: 10.1073/Pnas.80.9.2676 |
0.629 |
|
| 1983 |
Gussin GN, Johnson AD, Pabo CO, Sauer RT. Repressor and Cro Protein: Structure, Function, and Role in Lysogenization Cold Spring Harbor Monograph Archive. 13: 93-121. DOI: 10.1101/087969150.13.93 |
0.559 |
|
| 1982 |
Pabo CO, Krovatin W, Jeffrey A, Sauer RT. The N-terminal arms of lambda repressor wrap around the operator DNA. Nature. 298: 441-3. PMID 7088189 DOI: 10.1038/298441A0 |
0.647 |
|
| 1982 |
Sauer RT, Yocum RR, Doolittle RF, Lewis M, Pabo CO. Homology among DNA-binding proteins suggests use of a conserved super-secondary structure. Nature. 298: 447-51. PMID 6896364 DOI: 10.1038/298447A0 |
0.69 |
|
| 1982 |
Sauer RT, Ross MJ, Ptashne M. Cleavage of the lambda and P22 repressors by recA protein. The Journal of Biological Chemistry. 257: 4458-62. PMID 6461657 |
0.599 |
|
| 1982 |
Sauer RT, Krovatin W, Poteete AR, Berget PB. Phage P22 tail protein: gene and amino acid sequence. Biochemistry. 21: 5811-5. PMID 6295443 DOI: 10.1021/Bi00266A014 |
0.391 |
|
| 1982 |
Koshland D, Sauer RT, Botstein D. Diverse effects of mutations in the signal sequence on the secretion of beta-lactamase in Salmonella typhimurium. Cell. 30: 903-14. PMID 6183007 DOI: 10.1016/0092-8674(82)90295-1 |
0.345 |
|
| 1981 |
Sauer RT, Pan J, Hopper P, Hehir K, Brown J, Poteete AR. Primary structure of the phage P22 repressor and its gene c2. Biochemistry. 20: 3591-8. PMID 7260059 DOI: 10.1021/Bi00515A044 |
0.336 |
|
| 1981 |
Johnson AD, Poteete AR, Lauer G, Sauer RT, Ackers GK, Ptashne M. lambda Repressor and cro--components of an efficient molecular switch. Nature. 294: 217-23. PMID 6457992 DOI: 10.1038/294217A0 |
0.765 |
|
| 1981 |
Sauer RT, Allen DW, Niall HD. Amino acid sequence of p15 from avian myeloblastosis virus complex. Biochemistry. 20: 3784-91. PMID 6268146 DOI: 10.1021/Bi00516A018 |
0.329 |
|
| 1980 |
Johnson AD, Pabo CO, Sauer RT. Bacteriophage lambda repressor and cro protein: interactions with operator DNA. Methods in Enzymology. 65: 839-56. PMID 6445470 DOI: 10.1016/S0076-6879(80)65078-2 |
0.745 |
|
| 1980 |
Ptashne M, Jeffrey A, Johnson AD, Maurer R, Meyer BJ, Pabo CO, Roberts TM, Sauer RT. How the lambda repressor and cro work. Cell. 19: 1-11. PMID 6444544 DOI: 10.1016/0092-8674(80)90383-9 |
0.747 |
|
| 1979 |
Sauer RT, Pabo CO, Meyer BJ, Ptashne M, Backman KC. Regulatory functions of the lambda repressor reside in the amino-terminal domain. Nature. 279: 396-400. PMID 16068162 DOI: 10.1038/279396A0 |
0.783 |
|
| 1979 |
Pabo CO, Sauer RT, Sturtevant JM, Ptashne M. The lambda repressor contains two domains. Proceedings of the National Academy of Sciences of the United States of America. 76: 1608-12. PMID 287002 DOI: 10.1073/Pnas.76.4.1608 |
0.737 |
|
| 1978 |
Sauer RT. DNA sequence of the bacteriophage λ cI gene [33] Nature. 276: 301-302. PMID 714163 DOI: 10.1038/276301A0 |
0.334 |
|
| 1978 |
Sauer RT, Anderegg R. Primary structure of the lambda repressor. Biochemistry. 17: 1092-100. PMID 629949 DOI: 10.1021/Bi00599A024 |
0.352 |
|
| 1976 |
Ptashne M, Backman K, Humayun MZ, Jeffrey A, Maurer R, Meyer B, Sauer RT. Autoregulation and function of a repressor in bacteriophage lambda. Science (New York, N.Y.). 194: 156-61. PMID 959843 DOI: 10.1126/Science.959843 |
0.608 |
|
| 1971 |
Potts JT, Tregear GW, Keutmann HT, Niall HD, Sauer R, Deftos LJ, Dawson BF, Hogan ML, Aurbach GD. Synthesis of a biologically active N-terminal tetratriacontapeptide of parathyroid hormone. Proceedings of the National Academy of Sciences of the United States of America. 68: 63-7. PMID 4322265 DOI: 10.1073/Pnas.68.1.63 |
0.31 |
|
| 1970 |
Niall HD, Sauer R, Allen DW. The N-Terminal Amino Acid Sequence of Two Avian Leukosis Group Specific Antigens Proceedings of the National Academy of Sciences of the United States of America. 67: 1804-1809. PMID 4321347 DOI: 10.1073/Pnas.67.4.1804 |
0.339 |
|
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