client protein

client protein

A term of art for a protein which is manipulated or processed, as in the folding of a client protein by a chaperone.
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A potential application of AXL imaging is based on AXL's role as a client protein of HSP90 [31].
Effects of Gedunin on the Expression of Apoptotic Related and Heat Shock Protein (HSP90) and Its Client Protein Genes.
For instance, ERp44 could form a tandem with Ero1a or PRX4 but release these partners once they catalyze formation of mixed disulfide bond of ERp44 with a client protein. Another scenario could be envisaged in which the oxidative equivalents are provided in the form of a disulfide bond between two ERp44 proteins using the free (active site) cysteines.
Also a target protein, the glucocorticoid receptor (GR) protein, will be introduced to observe how the behaviour of each domain changes upon binding a client protein. Through observing the changes in chemical shifts and relaxation rates we will be able to identify specific regions in Hsp90 which are involved in the binding of client proteins.
ADX-1612 is a selective inhibitor of heat shock protein 90, a molecular chaperone that controls the folding and activation of client proteins involved in DNA repair and cell division.
However, the functionally relevant client proteins that sHSPs protect and the cellular processes they help to maintain remain unknown.
Scientists from the US, Argentina, Israel, India, and Europe discuss electron cryptomography and its application to bacterial chemoreceptor arrays, designing symmetric protein nanomaterials, weighted ensemble simulation, eukaryotic transcription initiation machinery, biophysical models of protein evolution, rate constants and mechanisms of protein-ligand binding, the integration of bacterial small RNAs in regulatory networks, recognition of client proteins by the proteasome, chemokine receptor structures and function, progress in human Tetrahymena telomerase structure determination, the theory and modeling of RNA structure and interactions with metal ions and small molecules, and reconstructing ancient proteins to understand the causes of structure and function.
Ganetespib, an investigational drug candidate, is a selective inhibitor of heat shock protein 90 (Hsp90), a molecular chaperone which controls the folding and activation of a number of client proteins that drive tumor development and progression, added the company.
Several mTOR signaling pathway components such as mTOR, AKT and LKB1 are HSP90 client proteins. Mechanistic data suggest the potential for improved efficacy through dual mTOR and HSP90 inhibition, which may also prevent the development of acquired resistant to this cancer therapy.
More specifically, HSP90 is one of the most abundant proteins (1-2%) in the cytoplasm of unstressed cells where it performs housekeeping functions, controlling the stability, maturation, activation, intracellular disposition and proteolytic turn-over of a plethora of proteins generally termed as 'client proteins'.
Hsp90 (heat shock protein 90) is a protein chaperone that binds to several sets of signaling proteins, known as "client proteins." These client proteins include a "who's who" list of cancer-relevant targets such as mutated p53, Bcr-Abl, Raf-1, ErbB2 and other kinases, as well as steroid hormone receptors.
Radicicol and geldanamycin frequently lead to a decrease in the activity or abundance of HSP9O's client proteins (Yen et al., 1994; Schulte et al., 1998).