HtpG, the E. coli homolog of Hsp90, is emerging as a valuable structural model of eukaryotic Hsp90. A first insight into the domain arrangement of HtpG is presented by Huai et al. (2005) in this issue of Structure
Understanding the mode of action of Hsp90 requires that molecular detail of its interactions with cl...
Heat shock protein 90 (Hsp90) is an ubiquitous molecular chaperone responsible for the assembly and ...
Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating many signaling prote...
Hsp90 is an abundant molecular chaperone involved in many biological systems. We report here the cry...
AbstractHsp90 is a ubiquitous, well-conserved molecular chaperone involved in the folding and stabil...
SummaryHsp90 is an abundant molecular chaperone involved in many biological systems. We report here ...
Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysi...
SummaryIn eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (h...
SummaryHsp90, an essential eukaryotic chaperone, depends upon its intrinsic ATPase activity for func...
<p>The topology and conserved structural regions of the Hsp90 dimer are shown for the crystal struct...
The molecular chaperone Hsp90 is an essential eukaryotic protein making up 1-2% of all cytosolic pro...
<p>The homodimer architecture of the full-length Hsp9p0 dimer is illustrated by the crystal structur...
Heat Shock Protein 90 (Hsp90) is an essential molecular chaperone that makes up 1-2% of all cytosoli...
Heat Shock Protein 90 (Hsp90) is an essential molecular chaperone that makes up 1-2% of all cytosoli...
The molecular chaperone Hsp90 interacts with around 10% of the proteome, facilitating folding and re...
Understanding the mode of action of Hsp90 requires that molecular detail of its interactions with cl...
Heat shock protein 90 (Hsp90) is an ubiquitous molecular chaperone responsible for the assembly and ...
Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating many signaling prote...
Hsp90 is an abundant molecular chaperone involved in many biological systems. We report here the cry...
AbstractHsp90 is a ubiquitous, well-conserved molecular chaperone involved in the folding and stabil...
SummaryHsp90 is an abundant molecular chaperone involved in many biological systems. We report here ...
Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysi...
SummaryIn eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (h...
SummaryHsp90, an essential eukaryotic chaperone, depends upon its intrinsic ATPase activity for func...
<p>The topology and conserved structural regions of the Hsp90 dimer are shown for the crystal struct...
The molecular chaperone Hsp90 is an essential eukaryotic protein making up 1-2% of all cytosolic pro...
<p>The homodimer architecture of the full-length Hsp9p0 dimer is illustrated by the crystal structur...
Heat Shock Protein 90 (Hsp90) is an essential molecular chaperone that makes up 1-2% of all cytosoli...
Heat Shock Protein 90 (Hsp90) is an essential molecular chaperone that makes up 1-2% of all cytosoli...
The molecular chaperone Hsp90 interacts with around 10% of the proteome, facilitating folding and re...
Understanding the mode of action of Hsp90 requires that molecular detail of its interactions with cl...
Heat shock protein 90 (Hsp90) is an ubiquitous molecular chaperone responsible for the assembly and ...
Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating many signaling prote...
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