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The Journal of Cell Biology|March 11, 2018
One domain fits all: Using disordered regions to sequester misfolded proteinsEdgar E Boczek, Simon AlbertiTrends in Biochemical Sciences|October 29, 2024
Surviving the heat: the role of macromolecular assemblies in promoting cellular shutdownChristine Desroches Altamirano, Simon AlbertiDisease Models & Mechanisms|April 11, 2014
Barcoding heat shock proteins to human diseases: looking beyond the heat shock responseVaishali Kakkar, Melanie Meister-Broekema, Melania Minoia, et al.Plos One|March 23, 2011
BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicityAkinori Hishiya, Mortada Najem Salman, Serena Carra, et al.The Journal of Biological Chemistry|December 31, 2008
HspB8 participates in protein quality control by a non-chaperone-like mechanism that requires eIF2{alpha} phosphorylationSerena Carra, Jeanette F Brunsting, Herman Lambert, et al.Human Molecular Genetics|May 10, 2005
HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cellsSerena Carra, Mitchel Sivilotti, Aura T Chávez Zobel, et al.Trends in Cell Biology|January 15, 2010
Prions, protein homeostasis, and phenotypic diversityRandal Halfmann, Simon Alberti, Susan LindquistPhysical Chemistry Chemical Physics : PCCP|May 10, 2021
Hydrogen adsorption trends on two metal-doped Ni2P surfaces for optimal catalyst designLauri Partanen, Simon Alberti, Kari LaasonenBiochimica Et Biophysica Acta|January 19, 2013
Protein disorder, prion propensities, and self-organizing macromolecular collectivesLiliana Malinovska, Sonja Kroschwald, Simon AlbertiBiochimica Et Biophysica Acta|December 2, 2004
Cooperation of molecular chaperones with the ubiquitin/proteasome systemClaudia Esser, Simon Alberti, Jörg HöhfeldPageof 19