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 83 for “"molecular chaperones"”.
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Stress-Induced Targeting of Molecular Chaperones In The Yeast Saccharomyces Cerevisiae
… 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 clients. I have discovered that Hsp90 and …
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Analysis of axonal transport and molecular chaperones during neurodegeneration in drosophila
… pathologies are widely used to study particular molecular systems in early neurodegenerative changes. Axonal transport (AT) is perturbed in several prevalent neurodegenerative diseases. The development of a Huntington’s Disease (HD) model in Drosophila melanogaster larvae is described, in which …
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Molecular chaperones and telomerase expression profiles and inhibition: Clinical implications for Glioma
Glioma, an infrequent form of cancer, continues to confer poor prognosis despite advances in current therapeutic techniques. This research identified the presence of hsp90a in glioma and investigated its potential as a diagnostic or therapeutic marker. l-Isp90ct is emerging as an encouraging target …
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Effects of co-expression of chaperone combinations on production of soluble plasmodial protein PfAdoMetDC in E. coli
… in E. coli was developed based on the use of molecular chaperones as co-expression partners. For structural studies aimed at designing drugs or compounds obtaining a pure protein is crucial. Therefore, PfAdoMetDC was co-expressed with six different combinations of molecular chaperones. E. coli …
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The Role of Sacsin as a Molecular Chaperone
… fold, many proteins require the assistance of molecular chaperones. While substantial gains in our knowledge of the function of general chaperones have been made in the last two decades, the role of molecular chaperones in brain-specific processes is not clearly defined. In this study, we …
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Effects and dynamics of the UNC-45B molecular chaperone
… of self-folding and assembly. Instead, the molecular chaperones work in a precise network to allow a nascent polypeptide to be protected from aggregation and folded to the precisely native product. The assembly of this myosin into a thick filament can proceed largely from the self-directed …
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A novel system to study seed recalcitrance and dormancy - comparative proteomics between two Spartina species
… late embryogenesis abundant proteins (LEAs), molecular chaperones, antioxidants, cystatin, and glyceraldehyde-3-phosphate dehydrogenase. These data suggest that LEA prevention pathways, molecular chaperone rescue pathways, ubiquitin-proteasome and autophagy degradation pathways and …
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The UNC-45 molecular chaperone: Its interactions with myosin and its thermosensing properties
… however for others additional assistance of molecular chaperones is needed. The molecular chaperones are proteins which through interactions with the client proteins, prevent the formation of aggregates and promote the folding process without being present in their final structure. One of the …
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Neuronal Protection by a Novel C-terminal Hsp90 Modulator
… is compromised. Enhancing the activity of molecular chaperones such as the `heat shock' proteins (Hsp's) that re-fold or signal degradation of damaged proteins may help remove protein oligomers/aggregates and prevent cell death. The goal of our studies was to characterize a novel, non-toxic …
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Analysis of Aurora B Regulation and Signaling
… for future biochemical and structural work. Two molecular chaperones Hsp90 and Cdc37 assist the folding of a variety of kinases in vivo, among which Aurora B is also a candidate. This gave us the final idea of expressing Aurora B-INCENP complexes in bacteria via the coexpression of Hsp90-Cdc37 …
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Energy Stress Causes Chaperones to Assemble Into Cytoplasmic Complexes
<p>The majority of proteins require molecular chaperones to assist their folding into tertiary and quaternary structures. Certain stresses can compromise the weak hydrophobic forces responsible for these structures and lead to protein unfolding, misfolding, and aggregation. Aggregates of proteins …
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Yeast Prion Variants as Models of the Phenotypic and Pathological Consequences of Amyloid Polymorphism
… Additionally, in both humans and yeast, molecular chaperones act to process misfolded substrates. Here, I explore the interplay between molecular chaperones and prion variants and reveal novel determinants for how distinct aggregate structures can dictate phenotype.</p><p>Studies of the …
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Functional Analysis of Cytosolic Hsp70 Nucleotide Exchange Factor Networks In Yeast
<p>The Hsp70 class of molecular chaperones play critical roles in protein homeostasis via an ATP-dependent folding cycle. Cytosolic Hsp70s in the budding yeast <em>Saccharomyces cerevisiae, </em>Ssa and Ssb, interact with up to three distinct nucleotide exchange factors (NEFs) homologous to human …
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Functional analysis of Smyd1 and Myomesin in sarcomere organization in zebrafish embryos
… close interaction of sarcomeric proteins and molecular chaperones. Smyd1 is a lysine methyltransferase that plays important roles in myofibrillogenesis in both skeletal and cardiac muscles. Knockdown of smyd1 results in complete disruption of sarcomere organization. The molecular mechanism by …
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Comparative analysis of a chimeric Hsp70 of E. coli and Plasmodium falciparum origin relative to its wild type forms
… the protein quality control. Hsps are a group of molecular chaperones that are upregulated in response to cell stress and some are produced constitutively. The Hsp70 family also known as DnaK in Escherichia coli (E. coli) is the most well-known group of molecular chaperones. Structurally, Hsp70s …
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Deciphering The Role of Hsp110 Chaperones In Diseases of Protein Misfolding
<p>Molecular chaperones maintain protein homeostasis (proteostasis) by ensuring the proper folding of polypeptides. Loss of proteostasis has been linked to the onset of numerous neurodegenerative disorders including Alzheimer’s, Parkinson’s, and Huntington’s disease. Hsp110 is a member of the Hsp70 …
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Investigation of protein induction in vascular-targeted strategies.
… tumour survival and stress induced molecular chaperones. The inverse correlation of structural proteins, haemoglobin and heat shock molecular chaperones gave the required validation and identification to relate these responses to those seen in MALDI-MSI. The relationship pathways …
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The Myosin-Binding UCS Domain but not the Hsp90-Binding TPR Domain of the UNC-45 Chaperone is Essential for Myosin Accumulation and Assembly in Caenorhabditis elegans
The UNC-45 family of molecular chaperones is expressed in metazoan organisms from C. elegans to humans. The UNC-45 protein is essential in C. elegans for early body-wall muscle cell development and A band assembly. We show that the myosin-binding UCS domain of UNC-45 alone is sufficient to rescue …
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