2017
DOI: 10.1007/s13562-017-0409-7
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Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system

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Cited by 2 publications
(1 citation statement)
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“…The results with HSP70-based machinery are impressive because until recently only chaperones from the HSP100 family (for instance, CLPB in Escherichia coli and HSP104 in yeast) were known to act as disaggregases, and no representatives of this protein was found in metazoan. [8,23,32] Plants are among the organisms that present the canonical disaggregase HSP100 [33,34] and it is scientifically important to explore their HSP70-based machinery. Therefore, we asked whether a HSP110 from sorghum has the same functions as that of a mammalian HSP110, both alone and as part of a previously identified HSP70-based machinery.…”
mentioning
confidence: 99%
“…The results with HSP70-based machinery are impressive because until recently only chaperones from the HSP100 family (for instance, CLPB in Escherichia coli and HSP104 in yeast) were known to act as disaggregases, and no representatives of this protein was found in metazoan. [8,23,32] Plants are among the organisms that present the canonical disaggregase HSP100 [33,34] and it is scientifically important to explore their HSP70-based machinery. Therefore, we asked whether a HSP110 from sorghum has the same functions as that of a mammalian HSP110, both alone and as part of a previously identified HSP70-based machinery.…”
mentioning
confidence: 99%