| human | Q5 |
| P496 | ORCID iD | 0000-0003-0923-3284 |
| P214 | VIAF ID | 2105155769086327880005 |
| P69 | educated at | University of Bayreuth | Q702482 |
| P108 | employer | Howard Hughes Medical Institute | Q1512226 |
| P734 | family name | Martin | Q12035675 |
| Martin | Q12035675 | ||
| Martin | Q12035675 | ||
| P735 | given name | Andreas | Q4926263 |
| Andreas | Q4926263 | ||
| P106 | occupation | researcher | Q1650915 |
| P21 | sex or gender | male | Q6581097 |
| Q39720569 | A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNA Ala acceptor helix. |
| Q43891282 | An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome |
| Q36568548 | Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition. |
| Q36938901 | ClpX(P) generates mechanical force to unfold and translocate its protein substrates |
| Q28292908 | Conformational switching of the 26S proteasome enables substrate degradation |
| Q43151994 | Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. |
| Q31141217 | Evolutionary Stabilization of the Gene-3-protein of Phage fd Reveals the Principles that Govern the Thermodynamic Stability of Two-domain Proteins |
| Q33220550 | Evolutionary protein stabilization in comparison with computational design |
| Q27685325 | Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid |
| Q46163099 | Knots can impair protein degradation by ATP-dependent proteases |
| Q37625067 | Marching to the beat of the ring: polypeptide translocation by AAA+ proteases. |
| Q44269157 | Mechanisms and Functional Diversity of Macromolecular Remodeling by ATP-Dependent Motors. |
| Q54522876 | Proside: a phage-based method for selecting thermostable proteins. |
| Q46788602 | Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes. |
| Q37406494 | Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase |
| Q58024073 | Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C: Part 1 |
| Q58024076 | Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C: Part 2 |
| Q96128051 | Site-specific ubiquitination affects protein energetics and proteasomal degradation |
| Q83225722 | Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation |
| Q90623818 | Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation |
| Q27688973 | Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation |
| Q58024045 | Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation |
| Q42207755 | Substrate-translocating loops regulate mechanochemical coupling and power production in AAA+ protease ClpXP |
| Q92726626 | The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation |
| Q96429652 | The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity |
| Q61445961 | The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome |
| Q41890028 | The ClpXP protease unfolds substrates using a constant rate of pulling but different gears. |
| Q27309735 | The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. |
| Q48267632 | The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. |
| Q34623947 | The proteasome under the microscope: the regulatory particle in focus |
| Q36029605 | Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome. |
| Q35685098 | Vps4 disassembles an ESCRT-III filament by global unfolding and processive translocation |
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