Abstract: The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important roles in the control of normal growth of human cells and in promoting development of tumor cells. Hsp90s have become a currently important subject in cellular immunity, signal transduction, and anti-cancer research. Studies on the physiological functions of Hsp90s began much later in plants than in animals and fungi. Significant progress has been made in understanding complex mechanisms of HSP90s in plants, including ATPase-coupled conformational changes and interactions with cochaperon
Molecular chaperones are proteins that interact with and aid in stabilization and activation of othe...
The heat shock protein Hsp90 is a molecular chaperon that uses ATP and interacts with various co-cha...
Hsp90 is an evolutionarily conserved ATP-dependent molecular chaperone and is one of the most abunda...
The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important ro...
Abstract: The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays im...
Heat-shock protein 90 (HSP90) is a molecular chaperone that represents one of the most important pro...
Heat shock protein 90 (Hsp90) is a chaperone protein, that is involved in many cell functions. This ...
The molecular chaperone Hsp90 (90 kDa heat-shock protein) is a remarkably versatile protein involved...
SummaryA comprehensive understanding of the cellular functions of the Hsp90 molecular chaperone has ...
The ubiquitous and conserved cytosolic heat-shock proteins 90 (HSP90A) perform essential functions i...
AbstractHeat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital r...
Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not...
The molecular chaperone Hsp90 (90 kDa heat-shock protein) mediates many fundamental cellular pathwa...
The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved ...
90kDa heat shock proteins (HSP90) belong to a family of molecular chaperones involved in the mainten...
Molecular chaperones are proteins that interact with and aid in stabilization and activation of othe...
The heat shock protein Hsp90 is a molecular chaperon that uses ATP and interacts with various co-cha...
Hsp90 is an evolutionarily conserved ATP-dependent molecular chaperone and is one of the most abunda...
The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important ro...
Abstract: The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays im...
Heat-shock protein 90 (HSP90) is a molecular chaperone that represents one of the most important pro...
Heat shock protein 90 (Hsp90) is a chaperone protein, that is involved in many cell functions. This ...
The molecular chaperone Hsp90 (90 kDa heat-shock protein) is a remarkably versatile protein involved...
SummaryA comprehensive understanding of the cellular functions of the Hsp90 molecular chaperone has ...
The ubiquitous and conserved cytosolic heat-shock proteins 90 (HSP90A) perform essential functions i...
AbstractHeat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital r...
Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not...
The molecular chaperone Hsp90 (90 kDa heat-shock protein) mediates many fundamental cellular pathwa...
The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved ...
90kDa heat shock proteins (HSP90) belong to a family of molecular chaperones involved in the mainten...
Molecular chaperones are proteins that interact with and aid in stabilization and activation of othe...
The heat shock protein Hsp90 is a molecular chaperon that uses ATP and interacts with various co-cha...
Hsp90 is an evolutionarily conserved ATP-dependent molecular chaperone and is one of the most abunda...