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2017
Under the unfolded protein response (UPR), transcripts encoding the endoplasmic reticulum (ER) chaperones are increased and those encoding proteins synthesized in the ER are decreased. To reproducibly detect such changes of an expression profile, homogeneous growth of plants is desired. In addition, uniform treatment with drugs inducing the UPR is also
Kazuki, Tabara +2 more
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Under the unfolded protein response (UPR), transcripts encoding the endoplasmic reticulum (ER) chaperones are increased and those encoding proteins synthesized in the ER are decreased. To reproducibly detect such changes of an expression profile, homogeneous growth of plants is desired. In addition, uniform treatment with drugs inducing the UPR is also
Kazuki, Tabara +2 more
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Molecular Biotechnology, 2006
The unfolded protein response (UPR) is a signal transduction network activated by inhibition of protein folding in the endoplasmic reticulum (ER). The UPR coordinates adaptive responses to this stress situation, including induction of ER resident molecular chaperone and protein foldase expression to increase the protein folding capacity of the ER ...
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The unfolded protein response (UPR) is a signal transduction network activated by inhibition of protein folding in the endoplasmic reticulum (ER). The UPR coordinates adaptive responses to this stress situation, including induction of ER resident molecular chaperone and protein foldase expression to increase the protein folding capacity of the ER ...
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Cross-talk unfolded: MARCKS proteins
Biochemical Journal, 2002The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and ...
Anna, Arbuzova +2 more
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1977
The folding of polypeptide chains into compact globular structures is often the supposition for the expression of their biological function in the cell. The determination of the spatial arrangement of the peptide chain by X-ray diffraction has given the most important information on the static properties of globular proteins. But the elucidation of the
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The folding of polypeptide chains into compact globular structures is often the supposition for the expression of their biological function in the cell. The determination of the spatial arrangement of the peptide chain by X-ray diffraction has given the most important information on the static properties of globular proteins. But the elucidation of the
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Trends in Biochemical Sciences, 2004
Protein unfolding is an important step in several cellular processes such as protein degradation by ATP-dependent proteases and protein translocation across some membranes. Recent studies have shown that the mechanisms of protein unfolding in vivo differ from those of the spontaneous unfolding in vitro measured by solvent denaturation.
Sumit, Prakash, Andreas, Matouschek
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Protein unfolding is an important step in several cellular processes such as protein degradation by ATP-dependent proteases and protein translocation across some membranes. Recent studies have shown that the mechanisms of protein unfolding in vivo differ from those of the spontaneous unfolding in vitro measured by solvent denaturation.
Sumit, Prakash, Andreas, Matouschek
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Science's STKE, 2001
One pathway involved in controlling apoptosis that has been characterized in Drosophila , but not other systems, is the pro-apoptotic pathway involving Reaper and the Reaper inhibitor Scythe. Scythe has a BAG domain, which is also present in the bcl-2 interacting protein BAG-1.
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One pathway involved in controlling apoptosis that has been characterized in Drosophila , but not other systems, is the pro-apoptotic pathway involving Reaper and the Reaper inhibitor Scythe. Scythe has a BAG domain, which is also present in the bcl-2 interacting protein BAG-1.
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Visualizing Protein Folding and Unfolding
Journal of Molecular Biology, 2019Protein folding/unfolding is a complicated process that defies high-resolution characterization by experimental methods. As an alternative, atomistic molecular dynamics simulations are now routinely employed to elucidate and magnify the accompanying conformational changes and the role of solvent in the folding process.
Jennifer, Ferina, Valerie, Daggett
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Heterogeneity in Protein Folding and Unfolding Reactions
Chemical Reviews, 2022Sandhya Bhatia, Jayant B Udgaonkar
exaly
1986
This chapter contains tabulated data of Gibbs energy changes (ΔGunf) enthalpy changes (ΔHunf), and heat capacity changes (ΔCp, unf) associated with protein unfolding. The data are relevant for various purposes, ranging from practical applications to theoretical considerations on structure stabilizing forces.
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This chapter contains tabulated data of Gibbs energy changes (ΔGunf) enthalpy changes (ΔHunf), and heat capacity changes (ΔCp, unf) associated with protein unfolding. The data are relevant for various purposes, ranging from practical applications to theoretical considerations on structure stabilizing forces.
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