Sentence examples for multiple client proteins from inspiring English sources

HSP90 is a chaperone essential for maturation and stabilization of multiple client proteins.

Hsp90 is a molecular chaperone responsible for the folding and stability of multiple client proteins, many of which are oncogenes, including Akt, c-Raf, and Her-2 [ 2].

Heat shock protein 90 (HSP90) is involved in folding and functions as a chaperone for multiple client proteins, many of which are important in tumorigenesis.

There are multiple client proteins of HSP90α, including steroid hormone receptors such as oestrogen receptor, protein kinases, cell cycle proteins and transcription factors that are essential targets in cancerous cell growth, survival, immortalisation, angiogenesis and metastasis [ 81].

This structural organization would ensure that the connected TPR and UCS domains retain their functional independence in the oligomeric state, allowing the simultaneous docking of multiple client proteins and cooperating chaperones to the UNC-45 chain.

In MM, Hsp90 inhibition has been shown to affect multiple client proteins involved in pathways critical to tumor development and progression, angiogenesis, and osteoclastogenesis, such as IGF1 and IL-6 receptors, and PI3K/Akt, STAT3, and MAPK signaling pathways; moreover, upregulation of Hsp90 has been observed in MM cells interacting with BMSCs [ 45– 45].

The great advantage of Hsp90 inhibitors should be the simultaneous depletion of multiple oncogenic client proteins [ 125].

The latter mechanism occurred through the acetylation of heat shock protein (HSP 90, causing its inactivation and loss of multiple HSP90 client proteins.

Inhibition of heat shock protein 90 (Hsp90) which promotes tumor cell survival and proliferation by stabilizing multiple oncogenic client proteins is a promising concept to overcome resistance of tumor cells to anticancer therapies.

Such activity can induce synergetic cytotoxic activity toward cancer cells by simultaneously decreasing multiple Hsp90 client proteins, providing a potent advantage over conventional Hsp90 inhibitors such as 17-AAG.

Although these proteins are unrelated, they all interact with a number of "client" proteins, undergo multiple conformational changes, and couple the hydrolysis of ATP to a downstream process that maintains the integrity of proteins in the cytoplasm.