My lab is a leader in understanding how cells maintain the integrity of the ribosome pool during and after assembly, both in terms of ribosome numbers as well as their structure and function. We are also tackling the question how misassembled ribosomes alter translation. To address these questions we use quantitative measurements in reconstituted systems, yeast biochemistry, genetics, genomics and structural tools including cryo-EM and RNA structure probing. The assays, reagents and technology we have developed are shared with and used by the community. By pioneering the study of ribosome assembly at the molecular level, my lab has transformed a field that was “too confusing” to study into a thriving research area that yields mechanistic insights. We have a history of making fundamental discoveries, including of a translation-like cycle during 40S subunit maturation, which couples quality control to maturation, ribosome remodeling under high salt/pH stress, where Rps26 is released in a chaperone-dependent manner to produce Rps26-deficient ribosomes, which have distinct mRNA specificities, and enable the response to high salt/pH stress, as well as ribosome repair, which enables replacement of damaged ribosomal proteins.