Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 25 for “"Unfolded proteins"”.
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Protein degradation from the endoplasmic reticulum in yeast
The majority proteins that misfold in the endoplasmic reticulum (ER) are dislocated to the cytoplasm for degradation by the proteasome. This process of dislocation and degradation occurs in several steps. First, unfolded proteins need to be recognized in the ER. Following recognition, unfolded …
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Regulation of mammalian IRE1α: Co-chaperones and their importance
When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER protein folding capacity to restore protein folding homeostasis. Unfolded proteins activate UPR signalling across the ER membrane to the nucleus by promoting oligomerisation of …
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Investigation of the kinetics of protein folding and the ensemble of conformations in non-native states of proteins by liquid NMR spectroscopy
… and the structure of the folded state, of unfolded and of non-native states of proteins and the kinetics of protein folding from the unfolded state to the folded state have to be determined. The focus of this PhD thesis was the development of novel NMR methodologies to study protein folding …
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Conformationally gated electron transfer studies of iso-1-cytochrome c
Protein folding is important because all proteins must fold to achieve their active conformer. In many cases, misfolding is the cause of disease and thus, understanding folding may lead to cures for disease. This thesis focuses on the dynamics and thermodynamics of partially unfolded states of …
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Conformationally gated electron transfer studies of iso-1-cytochrome c
Protein folding is important because all proteins must fold to achieve their active conformer. In many cases, misfolding is the cause of disease and thus, understanding folding may lead to cures for disease. This thesis focuses on the dynamics and thermodynamics of partially unfolded states of …
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The Endoplasmic Reticulum Udpase ENTPD5 Promotes Cancer Cell Growth and Survival in the PI3K/PTEN
… of protein folding and accumulation of unfolded proteins in the ER and finally lead to ER stress. How does cancer cell solve this problem of increased folding during rapid growth to avoid ER stress? We discovered that ENTPD5, an endoplasmic reticulum (ER) enzyme, is up-regulated in cell …
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Degradation of the E. coli small heat-shock proteins by the AAA+ protease lon : significance to protein quality-control
… and elimination of damaged and aggregated proteins requires the concerted effort of several branches of the protein quality-control network. This network includes refolding chaperones, disaggregases, holdases and proteases. Many years of investigation have led to a partial understanding of …
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The Role of BiP Nucleotide Exchange Factor Sil1 in Immunoglobulin Biosynthesis
… family that binds exposed hydrophobic regions of unfolded proteins. Substrates bound by BiP are protected from dangerous non-specific interaction with other unfolded proteins via their aggregation prone exposed hydrophobic regions, which are normally buried in the native state, and act as BiP …
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Uncovering Reversible AMPylation of BiP Mediated by dFic During ER Homeostasis
… ER stress but increases upon the reduction of unfolded proteins. Both dFic and BiP are transcriptionally activated upon ER stress induction, implicating a role for dFic in the UPR. We identified a conserved threonine residue, Thr366, as the AMPylation site, which is in close proximity to the …
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Uncovering Reversible AMPylation of BiP Mediated by dFic During ER Homeostasis
… ER stress but increases upon the reduction of unfolded proteins. Both dFic and BiP are transcriptionally activated upon ER stress induction, implicating a role for dFic in the UPR. We identified a conserved threonine residue, Thr366, as the AMPylation site, which is in close proximity to the …
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Interactions between the TatBC complex and Tat signal peptides during protein transport by the bacterial Tat pathway
… Sec pathways operate in parallel to translocate proteins across the prokaryotic cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. Unlike the Sec pathway, which translocates unfolded proteins, substrates of the Tat system are transported in a folded state. In Escherichia coli, …
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Regulation of the unfolded protein response by GADD34 and CReP
… the correct folding and assembling of proteins through the use of ER molecular chaperones. Homeostasis disruption of the ER leads to activation of the Unfolded Protein Response. The UPR is a three-arm pathway that plays a role in regulating ER stress and ultimately leads to cell …
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Stress-Induced Targeting of Molecular Chaperones In The Yeast Saccharomyces Cerevisiae
… response, expression of a battery of heat shock proteins (HSP) is induced, which act as molecular chaperones to assist in the repair or triage of unfolded proteins. The 90-kDa HSP (Hsp90) operates in the context of a multi-chaperone complex to promote the maturation of nuclear and cytoplasmic …
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Probing Order within Intrinsically Disordered Proteins
… understand the mechanisms behind how and why proteins fold, with natively unfolded proteins thought to be experimental artefacts. Today, the field of natively unfolded – or so-called intrinsically disordered – proteins, is rapidly developing. Protein disorder content has been positively …
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Characterising the early aggregation events of human lysozyme using single-molecule microscopy
… systemic amyloidosis. Given that a number of proteins, including lysozyme, can misfold and give rise to disorders such as Alzheimer’s disease, Parkinson’s disease, and type II diabetes, it is vital to understand the mechanistic features by which this process occurs, in order to attempt to cure …
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Stress-signal recognition in the unfolded protein response
The unfolded protein response (UPR) maintains protein folding homeostasis in the endoplasmic reticulum (ER) by adjusting its folding capacity to the load of unfolded proteins in the compartment. This critical feedback mechanism governs the functioning of the secretory pathway, impacting various …
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P4HB TARGETING HALTS TUMOR GROWTH AND RE-SENSITIZES RESISTANT MELANOMA CELLS TO DABRAFENIB AND TRAMETINIB STANDARD-OF-CARE THERAPY VIA IRE1-⍺ ACTIVATION AND AKT DOWNMODULATION
… by increasing accumulation of misfolded proteins and activating IRE1⍺ signalling pathway as part of the unfolded proteins response. This resulted in partial cellular death and autophagy induction. Additionally, P4HB knockdown and subsequent ER stress increment reduced AKT phosphorylation, …
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biological treatment options of multiple myeloma
… inhibitors is to inhibit the degradation of proteins within the cell nucleus leading to the accumulation of proteins within the endoplasmic reticulum, The build up of folded and unfolded proteins eventually triggers apoptosis. Monoclonal antibodies are available in various forms that …
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Characterisation and detection of viruses (Cucumovirus, Potyvirus) infecting vanilla in Réunion Island and Polynesian Islands
… isolate (VanMV-FP) had distinctly different coat proteins. The VanMV-FP CP N-terminus contained a stretch of amino-acid repeats (GTN) typical of natively unfolded proteins. This GTN stretch was located downstream of a DVG motif (which replaced the more common aphid transmission DAG motif), …
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Contribution of the Unfolded Protein Response to VEGF Expression
… interfere with the proper maturation of nascent proteins synthesized there. The resultant accumulation of unfolded proteins activates a signal transduction pathway known as the Unfolded Protein Response, which serves primarily to protect the cell during stress and helps restore homeostasis to …
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