A model depicting how accumulation of ER-resident misfolded membrane proteins would induce growth toxicity. (1) No growth toxicity is observed when misfolded membrane proteins aggregate but are not ubiquitinated. (2) No growth toxicity is observed when misfolded membrane proteins are ubiquitinated, but not aggregated. (3) Growth toxicity is observed when misfolded membrane proteins are both ubiquitinated and aggregated. ER, endoplasmic reticulum.</p
(A) WT, dfm1Δ, and rpn4Δ cells containing either GALpr-HMG2-GFP or EV were compared for growth by di...
AbstractThe endoplasmic reticulum (ER) is the eukaryotic organelle where most secretory proteins are...
The proper folding, assembly, and maintenance of cellular proteins is a highly regulated process and...
(A) WT, dfm1Δ, dfm1Δhrd1Δ, and dfm1Δdoa10Δ cells containing either GALpr-Hmg2-GFP, GALpr-STE6*-GFP, ...
(A) WT, dfm1Δ, and doa4Δ cells containing either GALpr-HMG2-GFP or EV were compared for growth by di...
The conversion of otherwise soluble proteins into insoluble amyloid aggregates is associated with a ...
(A) Western blot of monomeric ubiquitin in WT, dfm1Δ, and hrd1Δ cells. Anti-ubiquitin was used to bl...
<p>We propose that enhanced protein aggregate toxicity in Ub<sup>ext</sup>-expressing cells is due t...
Summary: To maintain secretory pathway fidelity, misfolded proteins are commonly retained in the end...
(A) Western blot of aggregated (pelleted) versus non-aggregated (soluble) membrane proteins at the E...
SummaryIt remains unclear how misfolded membrane proteins are selected and destroyed during endoplas...
In this paper, we discuss amyloidogenic proteins, their misfolding, resulting structures, and intera...
Protein homeostasis is maintained through a balance among protein synthesis, folding, assembly and d...
AbstractConformational diseases result from the failure of a specific protein to fold into its corre...
(A) WT, dfm1Δ, and rpn4Δ cells containing either GALpr-STE6*-GFP or EV were compared for growth by d...
(A) WT, dfm1Δ, and rpn4Δ cells containing either GALpr-HMG2-GFP or EV were compared for growth by di...
AbstractThe endoplasmic reticulum (ER) is the eukaryotic organelle where most secretory proteins are...
The proper folding, assembly, and maintenance of cellular proteins is a highly regulated process and...
(A) WT, dfm1Δ, dfm1Δhrd1Δ, and dfm1Δdoa10Δ cells containing either GALpr-Hmg2-GFP, GALpr-STE6*-GFP, ...
(A) WT, dfm1Δ, and doa4Δ cells containing either GALpr-HMG2-GFP or EV were compared for growth by di...
The conversion of otherwise soluble proteins into insoluble amyloid aggregates is associated with a ...
(A) Western blot of monomeric ubiquitin in WT, dfm1Δ, and hrd1Δ cells. Anti-ubiquitin was used to bl...
<p>We propose that enhanced protein aggregate toxicity in Ub<sup>ext</sup>-expressing cells is due t...
Summary: To maintain secretory pathway fidelity, misfolded proteins are commonly retained in the end...
(A) Western blot of aggregated (pelleted) versus non-aggregated (soluble) membrane proteins at the E...
SummaryIt remains unclear how misfolded membrane proteins are selected and destroyed during endoplas...
In this paper, we discuss amyloidogenic proteins, their misfolding, resulting structures, and intera...
Protein homeostasis is maintained through a balance among protein synthesis, folding, assembly and d...
AbstractConformational diseases result from the failure of a specific protein to fold into its corre...
(A) WT, dfm1Δ, and rpn4Δ cells containing either GALpr-STE6*-GFP or EV were compared for growth by d...
(A) WT, dfm1Δ, and rpn4Δ cells containing either GALpr-HMG2-GFP or EV were compared for growth by di...
AbstractThe endoplasmic reticulum (ER) is the eukaryotic organelle where most secretory proteins are...
The proper folding, assembly, and maintenance of cellular proteins is a highly regulated process and...