| Structure and function of the 26S proteasome JAM Bard, EA Goodall, ER Greene, E Jonsson, KC Dong, A Martin Annual review of biochemistry 87 (1), 697-724, 2018 | 804 | 2018 |
| Complete subunit architecture of the proteasome regulatory particle GC Lander, E Estrin, ME Matyskiela, C Bashore, E Nogales, A Martin Nature 482 (7384), 186-191, 2012 | 757 | 2012 |
| Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines A Martin, TA Baker, RT Sauer Nature 437 (7062), 1115-1120, 2005 | 463 | 2005 |
| ClpX (P) generates mechanical force to unfold and translocate its protein substrates RA Maillard, G Chistol, M Sen, M Righini, J Tan, CM Kaiser, C Hodges, ... Cell 145 (3), 459-469, 2011 | 335 | 2011 |
| Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine SE Glynn, A Martin, AR Nager, TA Baker, RT Sauer Cell 139 (4), 744-756, 2009 | 325 | 2009 |
| Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding A Martin, TA Baker, RT Sauer Nature structural & molecular biology 15 (11), 1147-1151, 2008 | 324 | 2008 |
| Conformational switching of the 26S proteasome enables substrate degradation ME Matyskiela, GC Lander, A Martin Nature structural & molecular biology 20 (7), 781-788, 2013 | 313 | 2013 |
| Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation AH de la Peña, EA Goodall, SN Gates, GC Lander, A Martin Science 362 (6418), eaav0725, 2018 | 302 | 2018 |
| Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation EJ Worden, C Padovani, A Martin Nature structural & molecular biology 21 (3), 220-227, 2014 | 203 | 2014 |
| Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates A Martin, TA Baker, RT Sauer Molecular cell 29 (4), 441-450, 2008 | 181 | 2008 |
| Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase R Beckwith, E Estrin, EJ Worden, A Martin Nature structural & molecular biology 20 (10), 1164-1172, 2013 | 162 | 2013 |
| Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes A Martin, TA Baker, RT Sauer Nature structural & molecular biology 15 (2), 139-145, 2008 | 156 | 2008 |
| The ClpXP protease unfolds substrates using a constant rate of pulling but different gears M Sen, RA Maillard, K Nyquist, P Rodriguez-Aliaga, S Pressé, A Martin, ... Cell 155 (3), 636-646, 2013 | 155 | 2013 |
| Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease A Martin, TA Baker, RT Sauer Molecular cell 27 (1), 41-52, 2007 | 152 | 2007 |
| Semisynthesis of a homogeneous glycoprotein enzyme: ribonuclease C: part 2 C Piontek, D Varón Silva, C Heinlein, C Pöhner, S Mezzato, P Ring, ... Angewandte Chemie International Edition 48 (11), 1941-1945, 2009 | 149 | 2009 |
| The 26S proteasome utilizes a kinetic gateway to prioritize substrate degradation JAM Bard, C Bashore, KC Dong, A Martin Cell 177 (2), 286-298. e15, 2019 | 147 | 2019 |
| In-vitro selection of highly stabilized protein variants with optimized surface A Martin, V Sieber, FX Schmid Journal of molecular biology 309 (3), 717-726, 2001 | 143 | 2001 |
| Prolyl isomerization as a molecular timer in phage infection B Eckert, A Martin, J Balbach, FX Schmid Nature structural & molecular biology 12 (7), 619-623, 2005 | 142 | 2005 |
| Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome C Bashore, CM Dambacher, EA Goodall, ME Matyskiela, GC Lander, ... Nature structural & molecular biology 22 (9), 712-719, 2015 | 137 | 2015 |
| The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome MM Olszewski, C Williams, KC Dong, A Martin Communications Biology 2 (1), 29, 2019 | 125 | 2019 |
