Simon Alberti

Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome.

Molecular chaperones in the regulation of signal transduction.

BAG-1--a nucleotide exchange factor of Hsc70 with multiple cellular functions.

The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.

Cooperation of molecular chaperones with the ubiquitin/proteasome system.

BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.

Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays.

A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae.

A systematic survey identifies prions and illuminates sequence features of prionogenic proteins.

Prions, protein homeostasis, and phenotypic diversity.

Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast.

Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.

Prion formation by a yeast GLFG nucleoporin.

Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.

Molecular mechanisms of spatial protein quality control.

Protein disorder, prion propensities, and self-organizing macromolecular collectives.

A complete mass-spectrometric map of the yeast proteome applied to quantitative trait analysis.

Harnessing the power of yeast to unravel the molecular basis of neurodegeneration.

Aggregating the message to control the cell cycle.

Fission yeast does not age under favorable conditions, but does so after stress.

Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation.

HSP70-binding protein HSPBP1 regulates chaperone expression at a posttranslational level and is essential for spermatogenesis.

Fusion of protein aggregates facilitates asymmetric damage segregation.

Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation.

Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules.

Don't Go with the Cytoplasmic Flow.

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

Protein misfolding in Dictyostelium: Using a freak of nature to gain insight into a universal problem.

A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy.

Amyloid-like Self-Assembly of a Cellular Compartment.

Are aberrant phase transitions a driver of cellular aging?

A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism.