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Showing 1 to 20 of 32 for “"disulfide bond formation"”.
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Disulfide Bond Formation: Identifying Roles of PDI Family Thiol Oxidoreductases and ER Oxidant Pathways
Protein disulfide isomerases (PDIs) catalyze the oxidation and isomerization of disulfide bonds in proteins passing through the endoplasmic reticulum (ER). Although as many as 20 enzymes are classified as PDI family members, their relative contributions to protein folding have remained an open …
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Adventitious disulfide bond formation in Escherichia coli and the involvement of thioredoxin and glutaredoxin in suppressing oxidative stress
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2025-12-01
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Oxidative Protein Folding Pathways In Gram-Positive Actinobacteria
<p>Disulfide bonds are important for the stability of many secreted proteins. These covalent linkages, which result from the oxidation of neighboring cysteine (Cys) residues, are often rate-limiting steps for protein folding and maturation. Disulfide bond formation is restricted to extracellular …
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The Role of Oxygen and Oxygen-Dependent Enzymes in Protein Folding, Metabolism, and Redox Homeostasis
… to utilize an oxygen dependent mechanism for disulfide bond formation required for proper folding, which represents a paradox when they are expressed under hypoxic conditions. Here we confirm the existence of oxygen independent pathways for disulfide bond formation. For the first time we …
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An investigation of the effect of cryoprotective agents on intermolecular disulfide formation
… also protect proteins against intermolecular disulfide bond formation? The model system Thiogel was used because of ease of measurement of intermolecular SS formation and lack of complicating factors found in living systems. Sulfhydryl groups on the protein molecules of Thiogel are oxidized …
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The role of ERO1 in oxidative protein folding in the endoplasmic reticulum
The formation of native disulfide bonds is critical for the folding and stability of many secreted proteins. We describe an essential S. cerevisiae gene, ER01, which encodes a conserved ER membrane protein required for disulfide bond formation in the er .doplasmic reticulum (ER). In a conditional …
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The Role of Periplasmic Disulfide Bond Status in the Regulation of the Salmonella SPI1 Type Three Secretion System
… regulators: HilD, HilC and RtsA. A periplasmic disulfide bond oxidoreductase DsbA is required for SPI1 T3SS function. RtsA directly activates dsbA and deletion of dsbA leads to loss of SPI1-dependent secretion. We have studied the dsbA phenotypes by monitoring expression of SPI1 regulatory, …
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Engineering streptavidin and its target ligands with both infinite binding affinity and reversible binding capability
… the streptavidin mutein and its binding tags. Disulfide bond formation allows immobilization of tagged proteins to streptavidin. Incubation with biotin in the presence of reducing agents allows stripping off tagged proteins from streptavidin.
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3-Hydroxy-3-methylglutaryl-coenzyme A lyase: investigation of cysteines mediating intersubunit disulfide formation and regulation by thiol/disulfide exchange and discovery of an extramitochondrial homolog
… the absence of reductant, cysteine 323 forms a disulfide bond with cysteine 323 on the adjacent monomer, blocking the substrate's access to the active site which results in diminished enzyme activity. The recently published crystal structure of the human enzyme indicates that cysteines 323 on …
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Insights Into The Reactivation, Regulation and Essentiality of Oxidative Protein Folding Pathways In Actinobacteria
<p>Accurate disulfide bond formation is important for proper folding, stability and function of exported proteins. The process of disulfide bond formation, termed oxidative protein folding, is catalyzed by thiol-disulfide oxidoreductase enzymes. Oxidative protein folding pathways influence …
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Purification of Global Regulator, Spx, and RNA Polymerase from Staphylococcus aureus for Use in In Vitro Transcription of Redox Genes
… stress. Its activity relies on reversible thiol-disulfide bond formation and binding RNA polymerase rather than DNA. The discovery that Staphylococcus aureus global virulence regulator, SarA, is more active upon cysteine reduction suggests that redox response could mediate virulence in this …
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Determination of disulfide bond connecting patterns via tandem mass spectrometry (MSn) and biomolecular ion/radical reactions
<p>Disulfide bond formation is one of the most common post translational modifications to occur in proteins and naturally occurring peptides. Disulfide bond formation plays a critical role in stabilizing their three-dimensional structure; therefore, it is very important to pinpoint the correct …
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Increasing Heterologous Protein Secretion From the Yeast S. Cerevisiae Through Manipulation of Cellular Redox Factors
… to be an electron acceptor from the E. coli disulfide bond formation chain, increased BPTI secretion from cultures overexpressing FMO, but under no other scenarios. A system has been set up to utilize the yeast surface display system to screen a cDNA library for factors that increase BPTI …
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The Effects of Selenium on Estrogen-regulated Gene Expression in LNCaP Prostate Cancer Cells
… may affect cancer risk is by catalyzing disulfide bond formation or otherwise complexing with reactive sulfhydryl groups in cellular proteins. The estrogen receptor (ER) contains cysteines in zinc (Zn) fingers that are susceptible to oxidation and internal disulfide formation, which can …
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Effects of glycosylation on the structure and fibrillization of prion protein fragments
… can play a major role modulating polypeptide conformation. It has also been shown that glycosylation can alter the thermodynamics of disulfide bond formation, favoring oxidation. To address the role of glycosylation on PrP, we have prepared glycosylated and unglycosylated peptides derived from …
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Disulfide Bridging the Gap between Src and Cortactin: A New Paradigm in SH2 Domain-mediated Signaling
… nucleation promoting factor that promotes the formation of stable branching networks within the actin cytoskeleton. Together, these proteins work in concert to promote the invasive and metastatic potential of tumor cells due to tyrosine phosphorylation of cortactin by Src. However, the …
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The degradation of membrane proteins from the mammalian endoplasmic reticulum
… pathway that cannot adopt their native conformation are targeted for dislocation from the endoplasmic reticulum (ER) membrane for subsequent degradation by the cytosolic proteasome. This thesis investigates factors influencing the catalyzed destruction of MHC class I molecules by the HCMV …
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The Role of Phospholamban Cysteines in the Activation of the Cardiac Sarcoplasmic Reticulum Ca2+ Pump by Nitroxyl (HNO)
… ~0.33 μM and evidence of reversible HNO induced disulfide bond formation. These studies provide important new insight into the mechanism of action of HNO on cardiac SR and thereby help evaluate the drug as a candidate therapy for congestive heart failure.
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Assessing Helicobacter pylori's HcpE and DsbK's Effects on Immunostimulation in Host Gastric Cells
… of Sel-Like Repeats (SLR) motifs–stabilized by disulfide bonds–which are important in protein-protein interactions and signal transduction. DsbK is key for HcpE’s disulfide bond formation and its secretion. Our aim was to identify the immunostimulatory effects of HcpE and DsbK, determine HcpE’s …
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Translational Frontiers for Chikungunya Virus: New World Epidemic, New Strains, New Therapeutic Targets
… are replete with structure-maintaining disulfide bonds, inhibitors to the host enzymes responsible for disulfide bond formation—protein disulfide isomerase (PDI) family chaperones—were utilized as a tool to potentiate PDI as an anti-CHIKV (and anti-alphavirus) drug target. PDI-inhibitors …
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