Abstract Anthropogenic carbon emissions and rising global energy demand are continuously intensifying the urgent need for immediate technological advancements for their mitigation. The electrochemical conversion of carbon dioxide (CO 2 ) and carbon monoxide (CO) into valuable chemicals, such as ethylene, acetate, ethanol and propanol is attracting significant attention as a solution to the CO 2 emissions and energy crisis. Electrocatalytic production of propanol from CO 2 /CO offers a more cost-effective alternative to conventional manufacturing processes. Yet, electrocatalytic CO 2 /CO-to-propanol synthesis is hindered by substantial thermodynamic barriers, low Faraday efficiency, poor energy efficiency, and complex coupling mechanisms between C 1 and C 2 active intermediates. Given these challenges, a deeper understanding of the CO 2 /CO-to-propanol conversion mechanism and the characteristics of effective catalysts is crucial. This timely review provides a comprehensive overview of the latest advancements in catalyst design, reaction conditions and electrode-electrolyte interface chemistry for CO 2 /CO reduction to propanol across a broad range of catalyst substrates. This review also highlights the fundamental limitations and prospects in propanol production through electrocatalytic reduction of CO 2 /CO, offering valuable insights into the emerging field.

Theranostics as a treatment strategy for individual patients encompasses a wide range of subjects, including personalized medicine, pharmacogenomics, and molecular imaging, in order to develop an efficient new targeted therapy and optimize drug selection via a better molecular understanding. Furthermore, theranostics aims to monitor the response to the treatment, to increase drug efficacy and safety, and to eliminate the unnecessary treatment of patients, resulting in significant cost savings for the overall healthcare system. Highly characteristic and nonrandom mutation patterns are found in well-studied oncogenes and tumor suppressor genes. Oncogenes are recurrently mutated at the same amino acid positions, leading to increased activity of the corresponding proteins.