Andreas Martin

The paper identifies two proteasomal mechanisms that target proteins with exposed cysteines, revealing their role in quality control and linking them to human diseases.

The paper identifies proteasomal substrates in yeast using photocrosslinking and mass spectrometry, revealing diverse substrates affected by ER stress.

This study identifies the mechanism by which antizyme mediates ubiquitin-independent degradation of yODC by the 26S proteasome through structural and biochemical analysis.

This study reveals how chaperones guide the conformational transitions of the 26S proteasome base subcomplex through intermediates to achieve ATPase activity.

This study identifies Blm10 as a proteasome-associated protein that modulates proteasome activity and maintains proteostasis and gamete quality in yeast.

This study identifies Faf1's role in enhancing p97-mediated ubiquitin-dependent protein unfolding by stabilizing the Ufd1-Npl4 cofactor through its UBX domain.

The paper identifies a novel ubiquitin-binding groove on the yeast 26S proteasome using photo-crosslinking mass spectrometry.

This study investigates how pore-1 loops of ATPase subunits in the 26S proteasome affect substrate degradation efficiency using biochemical and single-molecule assays with yeast proteasomes.

The paper solves high-resolution structures of TXNL1 bound to the human 26S proteasome, revealing conformation-specific binding and new insights into ATP hydrolysis and substrate translocation mechanisms.

This study shows Rpn11 acts as an allosteric ubiquitin sensor in the proteasome, enhancing substrate degradation by stabilizing the proteasome's engagement state.

This paper identifies how Nub1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome through a novel mechanism involving structural dynamics and proteasomal engagement.

The paper describes a method to incorporate a photo-crosslinkable amino acid into the 26S proteasome base subcomplex using recombinant expression in E. coli.

The paper identifies PITHD1 as an endogenous inhibitor of the 26S proteasome in dormant cells, revealing a triple-lock mechanism that prevents protein degradation during cellular dormancy.

The paper presents cryo-EM structures of the 26S proteasome in four conformational states to elucidate how ATP hydrolysis drives substrate translocation and deubiquitination.