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Showing 1 to 20 of 29 for “"heat shock protein 90"”.
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Heat shock protein 90, a potential biomarker for type I diabetes: mechanisms of release from pancreatic beta cells
Heat shock protein (HSP) 90 is a molecular chaperone that regulates diverse cellular processes by facilitating activities of various protein clients. Recent studies have shown serum levels of the alpha cytoplasmic HSP90 isoform are elevated in newly diagnosed type I diabetic patients, thus …
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Inhibition of Heat Shock Protein 90 Reduces Inflammatory Signal Transduction in Murine J774 Macrophage Cells and Lessens Disease in Autoimmune MRL/lpr Mice: What in vitro, in vivo, and in silico Models Reveal
Heat shock protein 90 (HSP90) is a molecular chaperone protein that protects proteins from degradation, repairs damaged proteins, and assists proteins in carrying out their functions. HSP90 has hundreds of clients, many of which are inflammatory signaling kinases. The mechanism by which HSP90 …
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Identification and Characterization of Novel Mycotoxin Degrading Enzymes
… radicicol. Radicicol inhibits the activity of Heat Shock Protein 90, however following enzymatic treatment, this activity was significantly attenuated. Identifying mycotoxin degradation activity supports continued agricultural production while preserving economic and health interests.
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Tracking buffers of mutation and noise to the genome
… For example, I found that substrates of Heat shock protein 90 (Hsp90), the best-understood source of buffering, tend to accumulate genetic changes in a manner that affects evolution. Hsp90 is also a proven buffer of developmental noise, so the mechanism by which this ability arises was …
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No-Independent Modulation of Soluble Guanylyl Cyclase (Sgc) Activity and Function
… to NO, investigators have identified a number of proteins that interact with sGC and modulate its function. For example, the interaction of sGC with ADP-ribosylation factor GTPase activating protein 1 (AGAP1) governs sGC’s intracellular distribution and therefore mediates localized production of …
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The Role of Prolactin in the Cellular Response to DNA Damaging Agents
… We previously identified that one isoform of heat shock protein-90 (HSP90), Hsp90alpha, is a prolactin-Janus kinase-2 (Jak2)-signal transducer and activator of transcription-5 (Stat5) regulated gene in breast cancer cells. We have now observed that prolactin increased the viability of breast …
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Identification of host cellular factors that regulate human norovirus replication
… for HuNoV replication. Secondly, the role of the heat shock protein 90 (Hsp90) on HuNoV replication was examined. While this molecular chaperone was previously reported to have a proviral effect on murine norovirus infection, in this current study, we observed that inhibition of the protein with …
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Bacterial expression of radio-labeled recombinant proteins for studying AHR signalling
… to AHR and ARNT there are at least three other proteins involved in AHR signaling. These proteins are the co-chaperone p23, Ara-9 and two molecules of Heat Shock Protein-90 (HSP-90). This study documents the production of Ara-9 and C∆418 (an ARNT deletion construct) in a modified thioredoxin …
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Studies toward the synthesis of celastrol and the late-stage hydroxylation of arenes mediated by 4,5-dichlorophthaloyl peroxide
… activities related to diseases characterized by protein misfolding including those associated with neuronal degradation, inflammation, and cancer. Relevant to cancer, celastrol functions as a non-ATP-competitive inhibitor of heat shock protein-90, providing a potential lead for the development of …
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The Dietary Isoprenoid Perillyl Alcohol Inhibits Telomerase Activity in Prostate Cancer Cells
… blot analysis revealed a decrease in hTERT protein levels in response to either agent that did not coincide wholly, with loss of telomerase activity suggesting a further level of regulation. Using immunoprecipitation we established the presence of a hTERT-mTOR-S6K (p70 S6 kinase)-Hsp90 (Heat …
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Total Syntheses of (+)-Geldanamycin, (-)-Ragaglitazar, and (+)-Kurasoin A and Phase-Transfer-Catalyzed Asymmetric Alkylation
… of geldanamycin (GA) to bind to the chaperone heat shock protein 90 (Hsp90). Despite its complicated functionality, the first total synthesis of GA was accomplished, which included two new reactions developed specifically to address the stereochemical features. The final step in the synthesis …
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Molecular characterization of tomato brown rugose fruit virus-host interactions and development of biocontrol strategies
… mutation analyses revealed that ToBRFV movement protein (MP) and coat protein (CP) contribute to ToBRFV local accumulation and are critical for systemic infectivity. Two highly conserved CP residues, D89 and R114, are essential for ToBRFV long-distance movement. Alanine substitutions of these two …
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Identification of small molecule inhibitors targeting Plasmodium falciparum Hsp70-Hop pathway
… its own molecular chaperones mainly the heat shock proteins (Hsps) in order to protect its protein constituents for survival. Heat shock protein 70 (Hsp70) together with heat shock protein 90 (Hsp90) are regarded as the most abundant cellular chaperones. Hsp70 and Hsp90 cooperate in order …
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Is my eye okay with OK lens?: comparative in vitro study depicting the effects of Orthokeratology (OK) lens treatment on the physiology of human corneal epithelial cells
… arrested. Proteomic analysis fully identified 5 proteins – annexin A3, pyridoxal kinase, peroxiredoxin-2, stathmin isoform A and heat shock protein 90-α, whose specific levels changed during treatment relative to the control, whilst 34 unidentified proteins were found to be up-regulated in …
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17-AAG and sihsp90α combinational therapy as a novel anti-cancer approach
Heat Shock Protein 90 (Hsp90) is a molecular chaperone which plays an active role in maintaining protein homeostasis. Hsp90 is known to be highly expressed in tumour cells where it regulates stability and function of several key oncogenic client proteins including Akt kinase, EGFR, CDK and PDGFR. …
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Hsp90 as a molecular target
Heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, has been proposed to play a vital role in tumorigenesis. Hsp90 has two isoforms, of which Hsp90α is the major isoform of the Hsp90 complex and has an inducible expression profile. The molecular chaperone Hsp90α has been …
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Amyotrophic Lateral Sclerosis: mechanism behind mutant SOD toxicity and improving current therapeutic strategies
… Inhibitors of the molecular chaperone heat shock protein 90 (Hsp90) have limited neuroprotection in some models of motor neuron degeneration. However the direct effect of Hsp90 inhibition on motor neurons is unknown. Here we show that Hsp90 inhibition induced motor neuron death through …
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Evaluating the Therapeutic Effect of an Hsp90 Inhibitor in Mouse Models of Alzheimer’s Disease
… by synaptic dysfunction. Strategies targeting heat shock protein 90 (Hsp90) inhibition have been widely investigated in the treatment of cancer for over two decades. Its application in the treatment of neurodegenerative diseases however, has emerged more recently in the last decade. The role of …
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Molecular Mechanisms by Which HSP90 Inhibition in the Spinal Cord Enhances Opioid Receptor Signaling
… the mu opioid receptor. Our lab has identified heat shock protein 90 (HSP90) as a key regulator of opioid signaling by demonstrating that when HSP90 is inhibited in spinal cord using 17-AAG, ERK MAPK signaling, and subsequent opioid anti-nociception is enhanced. Quantitative proteomic analysis …
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The Novel Role of Hematopoietic Lyn Substrate-1 Associated Protein X-1 in Cardiac Contractility and Cardioprotection
… cell-specific Lyn substrate associated protein-1 (HAX-1) was discovered in 1997 and suggested to play an anti-apoptotic role in B-cells. Although HAX-1 is ubiquitously expressed in all tissues, its role in the heart remains virtually unknown. Interestingly, recent studies demonstrate …
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