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Hsp90 as a capacitor for morphological evolution
It is reported that when Drosophila Hsp90 is mutant or pharmacologically impaired, phenotypic variation affecting nearly any adult structure is produced, with specific variants depending on the genetic background and occurring both in laboratory strains and in wild populations. Expand
The heat-shock response.
  • S. Lindquist
  • Biology, Medicine
  • Annual review of biochemistry
  • 1986
A comparison of different Organisms and Stages of Development and Heat-Induced Lethality and Thermotolerance and the role of RNA Processing are presented. Expand
The heat-shock proteins.
Roles moleculaires des proteines de choc thermique dans le fonctionnement des organismes a des temperatures normales et suite a des chocs thermiques; differents genes impliques
HSP90 and the chaperoning of cancer
Pharmacologically 'bribing' the essential guard duty of the chaperone HSP90 (heat-shock protein of 90 kDa) seems to offer a unique anticancer strategy of considerable promise. Expand
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Comprehensive understanding of how HSP90 functions promises not only to provide new avenues for therapeutic intervention, but to shed light on fundamental biological questions. Expand
A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins
A bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae found an unexpected amino acid bias in aggregation-prone candidates and discovered that 19 of these could also form prions. Expand
Hsp104, Hsp70, and Hsp40 A Novel Chaperone System that Rescues Previously Aggregated Proteins
It is concluded that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces. Expand
The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins.
The Lon Protease, DnaK.T URNOVER of AB ERR ANT PROT EINS in E. COLI, and more. Expand
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].
It is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the yeast non-Mendelian factor [psi+], and that a certain level of chaper one expression can cure cells of prions without affecting viability. Expand
Hsp90 as a capacitor of phenotypic variation
It is reported that, in Arabidopsis accessions and recombinant inbred lines, reducing Hsp90 function produces an array of morphological phenotypes, which are dependent on underlying genetic variation, and that HSp90 influences morphogenetic responses to environmental cues and buffers normal development from destabilizing effects of stochastic processes. Expand