Relevant bibliographies by topics / Protein misfolding and aggregation

Academic literature on the topic 'Protein misfolding and aggregation'

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Published: 10 December 2022
Last updated: 7 September 2023

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Journal articles on the topic "Protein misfolding and aggregation"

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Murphy, Regina M., and Brent S. Kendrick. "Protein Misfolding and Aggregation." Biotechnology Progress 23, no. 3 (September 5, 2008): 548–52. http://dx.doi.org/10.1021/bp060374h.

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Cuervo, Ana Maria, Esther S. P. Wong, and Marta Martinez-Vicente. "Protein degradation, aggregation, and misfolding." Movement Disorders 25, S1 (2010): S49—S54. http://dx.doi.org/10.1002/mds.22718.

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Popiel, H. Akiko, James R. Burke, Warren J. Strittmatter, Shinya Oishi, Nobutaka Fujii, Toshihide Takeuchi, Tatsushi Toda, Keiji Wada, and Yoshitaka Nagai. "The Aggregation Inhibitor Peptide QBP1 as a Therapeutic Molecule for the Polyglutamine Neurodegenerative Diseases." Journal of Amino Acids 2011 (June 30, 2011): 1–10. http://dx.doi.org/10.4061/2011/265084.

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Misfolding and abnormal aggregation of proteins in the brain are implicated in the pathogenesis of various neurodegenerative diseases including Alzheimer's, Parkinson's, and the polyglutamine (polyQ) diseases. In the polyQ diseases, an abnormally expanded polyQ stretch triggers misfolding and aggregation of the disease-causing proteins, eventually resulting in neurodegeneration. In this paper, we introduce our therapeutic strategy against the polyQ diseases using polyQ binding peptide 1 (QBP1), a peptide that we identified by phage display screening. We showed that QBP1 specifically binds to the expanded polyQ stretch and inhibits its misfolding and aggregation, resulting in suppression of neurodegeneration in cell culture and animal models of the polyQ diseases. We further demonstrated the potential of protein transduction domains (PTDs) for in vivo delivery of QBP1. We hope that in the near future, chemical analogues of aggregation inhibitor peptides including QBP1 will be developed against protein misfolding-associated neurodegenerative diseases.
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Ajmal, Mohammad Rehan. "Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response." Diseases 11, no. 1 (February 9, 2023): 30. http://dx.doi.org/10.3390/diseases11010030.

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Proteins are central to life functions. Alterations in the structure of proteins are reflected in their function. Misfolded proteins and their aggregates present a significant risk to the cell. Cells have a diverse but integrated network of protection mechanisms. Streams of misfolded proteins that cells are continuously exposed to must be continually monitored by an elaborated network of molecular chaperones and protein degradation factors to control and contain protein misfolding problems. Aggregation inhibition properties of small molecules such as polyphenols are important as they possess other beneficial properties such as antioxidative, anti-inflammatory, and pro-autophagic properties and help neuroprotection. A candidate with such desired features is important for any possible treatment development for protein aggregation diseases. There is a need to study the protein misfolding phenomenon so that we can treat some of the worst kinds of human ailments related to protein misfolding and aggregation.
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Wang, Chen-Yu, Hui-Ching Lin, Yi-Ping Song, Yu-Ting Hsu, Shu-Yu Lin, Pei-Chien Hsu, Chun-Hua Lin, et al. "Protein Kinase C-Dependent Growth-Associated Protein 43 Phosphorylation Regulates Gephyrin Aggregation at Developing GABAergic Synapses." Molecular and Cellular Biology 35, no. 10 (March 9, 2015): 1712–26. http://dx.doi.org/10.1128/mcb.01332-14.

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Growth-associated protein 43 (GAP43) is known to regulate axon growth, but whether it also plays a role in synaptogenesis remains unclear. Here, we found that GAP43 regulates the aggregation of gephyrin, a pivotal protein for clustering postsynaptic GABAAreceptors (GABAARs), in developing cortical neurons. Pharmacological blockade of either protein kinase C (PKC) or neuronal activity increased both GAP43-gephyrin association and gephyrin misfolding-induced aggregation, suggesting the importance of PKC-dependent regulation of GABAergic synapses. Furthermore, we found that PKC phosphorylation-resistant GAP43S41A, but not PKC phosphorylation-mimicking GAP43S41D, interacted with cytosolic gephyrin to trigger gephyrin misfolding and its sequestration into aggresomes. In contrast, GAP43S41D, but not GAP43S41A, inhibited the physiological aggregation/clustering of gephyrin, reduced surface GABAARs under physiological conditions, and attenuated gephyrin misfolding under transient oxygen-glucose deprivation (tOGD) that mimics pathological neonatal hypoxia. Calcineurin-mediated GAP43 dephosphorylation that accompanied tOGD also led to GAP43-gephyrin association and gephyrin misfolding. Thus, PKC-dependent phosphorylation of GAP43 plays a critical role in regulating postsynaptic gephyrin aggregation in developing GABAergic synapses.
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Cuanalo-Contreras, Karina, Abhisek Mukherjee, and Claudio Soto. "Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging." International Journal of Cell Biology 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/638083.

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The misfolding, aggregation, and tissue accumulation of proteins are common events in diverse chronic diseases, known as protein misfolding disorders. Many of these diseases are associated with aging, but the mechanism for this connection is unknown. Recent evidence has shown that the formation and accumulation of protein aggregates may be a process frequently occurring during normal aging, but it is unknown whether protein misfolding is a cause or a consequence of aging. To combat the formation of these misfolded aggregates cells have developed complex and complementary pathways aiming to maintain protein homeostasis. These protective pathways include the unfolded protein response, the ubiquitin proteasome system, autophagy, and the encapsulation of damaged proteins in aggresomes. In this paper we review the current knowledge on the role of protein misfolding in disease and aging as well as the implication of deficiencies in the proteostasis cellular pathways in these processes. It is likely that further understanding of the mechanisms involved in protein misfolding and the natural defense pathways may lead to novel strategies for treatment of age-dependent protein misfolding disorders and perhaps aging itself.
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Lu, Rui-Chun, Meng-Shan Tan, Hao Wang, An-Mu Xie, Jin-Tai Yu, and Lan Tan. "Heat Shock Protein 70 in Alzheimer’s Disease." BioMed Research International 2014 (2014): 1–8. http://dx.doi.org/10.1155/2014/435203.

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Alzheimer’s disease (AD) is the most common neurodegenerative disease that caused dementia which has no effective treatment. Growing evidence has demonstrated that AD is a “protein misfolding disorder” that exhibits common features of misfolded, aggregation-prone proteins and selective cell loss in the mature nervous system. Heat shock protein 70 (HSP70) attracts extensive attention worldwide, because it plays a crucial role in preventing protein misfolding and inhibiting aggregation and represents a class of proteins potentially involved in AD pathogenesis. Numerous studies have indicated that HSP70 could suppress the progression of AD within vitroandin vivoexperiments. Thus, targeting HSP70 and the related compounds might represent a promising strategy for the treatment of AD.
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Tan, Jeanne M. M., Esther S. P. Wong, and Kah-Leong Lim. "Protein Misfolding and Aggregation in Parkinson's Disease." Antioxidants & Redox Signaling 11, no. 9 (September 2009): 2119–34. http://dx.doi.org/10.1089/ars.2009.2490.

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Dobson, Christopher M. "Principles of protein folding, misfolding and aggregation." Seminars in Cell & Developmental Biology 15, no. 1 (February 2004): 3–16. http://dx.doi.org/10.1016/j.semcdb.2003.12.008.

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Lyubchenko, Yuri. "Nanoprobing immunoassay for protein misfolding and aggregation." Nanomedicine: Nanotechnology, Biology and Medicine 3, no. 4 (December 2007): 342. http://dx.doi.org/10.1016/j.nano.2007.10.033.

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Dissertations / Theses on the topic "Protein misfolding and aggregation"

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BROGGINI, LUCA. "MOLECULAR DETERMINANTS UNDERLYING PROTEIN MISFOLDING AND AGGREGATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/831967.

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Proteins have evolved to adopt distinctive and well-defined functional states under physiological conditions, either as monomers or complexes. The achievement of a three-dimensional structure allows proteins to exert their physiological functions. Nevertheless, when proteins lose – or fail to acquire – their spatial organization, they can convert into aggregated species that can be harmful to the organism. Conformational diseases gather all those pathologies characterized by the misfolding and aggregation of proteins. Indeed, while the formation and deposition of proteinaceous aggregates can be toxic to cells, the lack of active folded protein disrupts normal physiological pathways. Although considerable progresses have been made in the recent years, to date conformational diseases are still incurable. Indeed, the incomplete understanding of the causes guiding protein misfolding and aggregation prevents the development of efficient treatments. At the same time, the complexity and the diversity of the processes leading to the formation of aggregated species make the task extremely challenging. This PhD project was developed to provide a more comprehensive overview of the molecular bases underlying the conversion of soluble and functional states into aggregated and potentially toxic species. To reach such aims, we applied an integrative approach on two model systems, neuroserpin (NS) and beta-2 microglobulin (2m). In particular, we combined a series of biophysical, biochemical and structural techniques to study these two proteins which have been largely used as model systems for serpin polymerization and amyloid formation, respectively. We found that protein misfolding and aggregation processes depend on several molecular properties, including primary sequence, denatured state compactness, thermal stability, ability to form oligomers under physiological conditions, and the presence of post-translation modifications. The data presented in this PhD thesis add valuable information to depict the complex framework of protein misfolding and aggregation.
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Buell, Alexander Kai. "On the kinetics of protein misfolding and aggregation." Thesis, University of Cambridge, 2011. https://www.repository.cam.ac.uk/handle/1810/270324.

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Protein (mis)folding into highly ordered, fibrillar structures, amyloid fibrils, is a hallmark of several, mainly neurodegenerative, disorders. The mechanism of this supra-molecular self-assembly reaction, as well as its relationship to protein folding are not well understood. In particular, the molecular origin of the metastability of the soluble state of proteins with respect to the aggregated states has not been clearly established. In this dissertation, it is demonstrated, that highly accurate kinetic experiments, using a novel biosensing method, can yield fundamental insight into the dynamics of proteins in the region of the free energy landscape corresponding to protein aggregation. First, a section on Method development describes the extension and elaboration of the previously established kinetic assay relying on quartz crystal microbalance measurements for the study of amyloid fibril elongation (Chapter 3). This methodology is then applied in order to study in great detail the origin of the various contributions to the free energy barriers separating the soluble state of a protein from its aggregated state. In particular, the relative importance of residual structure, hydrophobicity (Chapter 4) and electrostatic interactions (Chapter 5) for the total free energy of activation are discussed. In the last part of this thesis (Chapter 6), it is demonstrated that this biosensing method can also be used to study the binding of small molecules to amyloid fibrils, a very useful feature in the framework of the quest for potential inhibitors of amyloid formation. In addition, it is shown that Thioflavin T, to-date the most frequently employed fluorescent label molecule for bulk solution kinetic studies, can in the presence of potential amyloid inhibitor candidates be highly unreliable as a means to quantify the effect of the inhibitor on amyloid formation kinetics. In summary, the work in this thesis contributes to both the fundamental and the applied aspects of the field of protein aggregation.
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Todorova, Nevena, and Nevena Todorova@rmit edu au. "Molecular modelling of peptide folding, misfolding and aggregation phenomena." RMIT University. Applied Science, 2009. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20091130.111240.

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In this thesis we present computer modelling studies that were implemented to investigate protein behavior in various environments causing their folding, unfolding and aggregation. Applications related to two important proteins - insulin and apolipoprotein C-II (ApoC-II) are presented. The use of atomistic simulation methodologies based on empirical force fields has enhanced our understanding of many physical processes governing protein structure and dynamics. However, the force fields used in classical modelling studies are often designed for a particular class of proteins and rely on continuous improvement and validation by comparison of simulations with experimental data. In Chapter 4 we present a comprehensive comparison of five popular force fields for simulation of insulin. The effect of each force field on the conformational evolution and structural properties of the protein is analysed in detail and compared with available experimental data. A fundamental phenomenon in nature is the ability of proteins to fold ab initio to their functional native conformation, also known as their biologically active state. Due to the heterogeneity and dimensionality of the systems involved, it is necessary to employ methodologies capable of accelerating rare events, specifically, configurational changes that involve the crossing of large free energy barriers. In Chapter 5, using the recently developed method BE-META we were able to identify the structural transitions and possible folding pathways of insulin. Another interesting phenomenon is the misfolding of proteins causing their aggregation, that may lead to formation of either amorphous compounds or structures of elongated-unbranched morphology known as amyloid fibrils. The deposition of amyloid fibrils in the human body may cause many debilitating diseases such as Alzheimer's and variant Creutzfeldt-Jakob diseases, thus making this field of research important and urgent. The human plasma protein apoC-II serves important roles in lipid transport, and it has been shown to form amyloid-like aggregates in solution. We have performed computational studies to investigate the effect of mutations, such as Met oxidation and the residue substitutions to hydrophobic Val and hydrophilic Gln, on dynamics of apoC-II(60-70) peptide. The conformation features relevant to the amyloidogenic propensities of the peptide were identified and presented in Chapter 6. The involvement of lipids at the various stages of development of amyloid diseases is becoming more evident in recent research efforts. In particular, micellar and sub-micellar concentrations have showed to have different effect on fibril growth and kinetics of native apoC-II and derived peptides. In Chapter 7 we investigated the influences of phospholipids at various concentrations on the structure of apoC-II(60-70) using MD and umbrella sampling methods. The molecular mechanisms of lipid effects on the peptide conformation and dynamics were identified. In Chapter 8 preliminary results on the structural stability of pre-formed oligomeric composites of apoC-II(60-70) peptide of different sizes and arrangements were also presented. The effects of mutation (oxidised Met, Met60Val and Met60Gln) on the most stable cluster was also investigated. To conclude, several ideas for continuation of research in the protein folding and aggregation field are discussed in the Future Work section of this thesis.
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Devlin, Glyn L. "The mechanisms of serpin misfolding and its inhibition." Monash University, Dept. of Biochemistry and Molecular Biology, 2003. http://arrow.monash.edu.au/hdl/1959.1/9469.

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Borgia, Madeleine Bridget Windsor. "Studies of the aggregation and misfolding of titin Ig-like domains." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609256.

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Freer, Rosie. "Molecular origins of tissue vulnerability to aberrant aggregation in protein misfolding diseases." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/275420.

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Neurodegenerative disorders, including Alzheimer’s disease (AD) and Parkinson’s disease (PD), are increasingly common in our ageing society, are remain incurable. A major obstacle encountered by researchers in their attempts to find effective therapies is represented by the current lack of understanding of the molecular origins of these disorders. It is becoming clear that, although the aggregation of specific proteins, including amyloid β (Aβ) and tau in AD and α-synuclein in PD, hallmark these disorders, such behaviour is a consequence of a wider, system-level disruption of protein homeostasis. In order to identify the genetic factors contributing to such a disruption, the transcriptional changes that occur during neurodegenerative disease progression have received considerable scientific attention in recent years. In our approach, we considered another hallmark of these diseases - their characteristic patterns of spreading across the brain - to identify the nature of the transcriptional signature which underlies tissue vulnerability to protein aggregation. By understanding why tissues succumb in their characteristic sequential pattern in neurodegenerative diseases, and why some tissues remain almost completely resistant throughout, we hoped to obtain insight into the molecular origins of these disorders. Our results show that the AD progression can be predicted from a transcriptional signature in healthy brains related to the protein aggregation homeostasis of Aβ, tau, and the wider proteome. We highlight a relationship between a specific subproteome at high risk of aggregation (formed by supersaturated proteins), and the vulnerability to neurodegenerative diseases. We thus identify an AD-specific supersaturated set of proteins - termed the metastable subproteome, whose expression in normal brains recapitulates the staging of AD, with more vulnerable tissues having higher metastable subproteome expression. We find evidence of these vulnerability signatures transcending the tissue level of interrogation, with cellular and subcellular analysis also showing elevated levels of proteins known and predicted to predispose the aberrant aggregation of Aβ and tau. These results characterise the key protein homeostasis pathways in the inception and progression of AD, and establish an approach with the potential to be applied to other protein misfolding diseases, in the brain and beyond.
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Xu, Mingming. "Discovery of inhibitors against a-synuclein aggregation." Thesis, Griffith University, 2020. http://hdl.handle.net/10072/392373.

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Abnormal protein aggregation has been linked to many neurodegenerative diseases, including Parkinson’s disease (PD). The main pathological hallmark of PD is the formation of Lewy bodies and Lewy neurites, both containing the pre-synaptic protein α-synuclein (α-syn). Native α-syn, under normal conditions, exists in a soluble unfolded state but undergoes misfolding and aggregation into toxic aggregates under pathological conditions. Toxic α-syn species can cause oxidative stress, membrane penetration, synaptic and mitochondrial dysfunction, leading to neuronal death and eventually neurodegeneration. Currently, early diagnosis and treatments targeting PD pathogenesis are urgently needed. Given its critical role in PD, α-syn is an attractive target for the development of both diagnostic tools and effective therapeutics. This thesis consists of a series of published and unpublished papers. In Chapter 1, which was published as a review, the progress towards discovering imaging probes and aggregation inhibitors for α-syn was summarized. Since a key property of such required therapeutic agents is specific binding to the target protein, relevant strategies and techniques in the discovery of α-syn-targeted drugs are discussed. As my PhD project aimed to screen small molecules capable of binding to α-syn specifically and then discover new α-syn aggregation inhibitors from the screened structures, relevant techniques were discussed at the end of Chapter 1. Mass spectrometry was chosen to discover specific α-syn binding molecules as this technique allows rapid detection of direct interactions between molecules and proteins. The materials and methods that were used in the included publications, were summarized in detail in Chapter 2. To provide sufficient protein for our study, the in-house α-syn having equally good quality as the commercial protein, was successfully generated in Chapter 3. Also, high yield of pure protein can be acquired from medium scale of bacteria culture, saving plenty of time and money for preparing proteins for large-scale screening. The protein expression and purification was a part of the supplementary data in the publication included in Chapter 4, where an automated screening system based on the connection of a mass spectrometer and the auto-sampler from a high performance liquid chromatograph was successfully established. This system allows computer-controlled sample loading and data acquisition with high stability and reproducibility. We first discovered a new inhibitor by screening over 4,300 pure molecules. The new compound, 3-[(3-methoxyphenyl)carbamoyl]-7-[(E)-2-phenylethenyl]-4,7- dihydropyrazolo [1,5-a]pyrimidine-5-carboxylic acid, not only significantly inhibited the misfolding and aggregation of α-syn, protected neuroblastoma cells from α-syn toxicity, but also has a more specific binding site compared with positive controls. The capability of the MS-based screening was further extended to the discovery of active components from natural products (manuscript in submission). A total of 29 marine fractions from our collaborators, were tested by MS and a new cholesterol derivative with significant inhibition of α-syn aggregation, was discovered and isolated from the active fraction. This MS-guided isolation of active components from natural products can also be applied to investigating traditional Chinese medicines with known therapeutic effects. Post-translational modifications (PTMs) of α-syn, especially enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the proteins hydroxylated amino acid residues, have been reported to affect the pathogenic self-assembly of α-syn. As such, manipulation of the proteins’ O-GlcNAcylation statuses has been proposed to offer a therapeutic route toward addressing PD. In Chapter 5, small peptides with different sequences and modification sites were synthesized by our collaborators. In the thioflavin-T assay, which is a golden standard for measuring α-syn aggregation, two peptides with O-GlcNAcylation at the serine site exhibited significant inhibition. Therefore, small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate α-syn aggregation (manuscript under review). Other sources of compounds including new analogs of anle138b, which is a well-studied α-syn aggregation modulator, were evaluated. Two derivatives of anle138b exerted promising effects on the aggregation of α-syn. Interestingly, these synthesized compounds and peptides did not form protein-ligand complexes in the mass spectra, indicating that these molecules, unlike the compounds we discovered in Chapter 4, may interact with α-syn aggregates instead of α-syn monomers. In the last chapter, general conclusions of the thesis were made and future directions were also discussed.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Environment and Sc
Science, Environment, Engineering and Technology
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Belfiore, Ramona. "Protein Misfolding and Aggregation in Neurodegeneration: In Vitro And In Vivo Study Cases." Doctoral thesis, Università di Catania, 2018. http://hdl.handle.net/10761/4178.

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Neurodegenerative diseases are nowadays increasing in incidence and widely distributed around the world. Despite those disorders show very different symptoms and morbidity, intracellular and extracellular protein misfolding and accumulation appears as a common pathological pathway. In the present thesis work I analyzed two cases of toxic protein deposition involved in ALS and AD. First, I looked at SOD1-G93A mutant protein, whose neuronal deposit is associated to familial and sporadic ALS. The mitochondrial porin VDAC1 has been proposed as a binding target of SOD1 mutant forms to mitochondria. By affinity studies we found that VDAC1 protein specifically binds SOD1-G93A but not wild type SOD1. Notably, it is known that the N-Terminal end of Hexokinase 1 (N-HK1) interacts with VDAC1: thus, we produced a synthetic peptide corresponding to the first 11 aa of human HK1 and tested its action as a potential interfering molecule between VDAC1/SOD1-G93A bond. Both in a protein-protein interaction and in a protein mitochondrial interaction we obtained a decrease of VDAC1/SOD1-G93A binding with respect of the increased N-HK1 peptide concentration. Summarizing, SOD1-G93A binds VDAC1 and impairs HK1 binding and our results suggest for N-HK1 peptide a neuroprotective potential in ALS patients. The second part of my thesis work was focused on Amyloid and tau protein accumulation in 3xTg-AD mice. In order to study neuropathology and cognitive deficits in (AD), several transgenic models of AD have been identified. Accumulation of Abeta and fibrillary tangles as well as impairments in working and learning memory are age-related hallmark of AD pathology. To produce a progressive characterization of Abeta and tau pathology in 3xTg-AD mice we aged female mice at 2, 6, 12 and 20 months of age. We tested mice in a behavioral assay named Morris Water Maze (MWM) and we used in vitro biochemical assays, to observe Abeta soluble and insoluble fraction as well as tau phosphorylation in both cortex and hippocampus of 3xTg-AD mice. Our data on MWM demonstrate a progressive impairment in learning with a strongly significant difference between 3xTg-AD mice and controls, from 6 months of age. Notably, we also found a progressive increase in both soluble and insoluble Abeta40 and Abeta42, an age dependent tau hyperphosphorylation at specific AD linked phospho-sites, and an intense glial reactivity. Overall, our data confirm that female 3xTg-AD mice consistently show AD-like pathology, therefore this transgenic mouse model can be used as an extremely powerful tool to investigate pathogenic mechanisms underlying Alzheimer s disease.
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Binger, Katrina Jean. "The reversibility of amyloid fibril formation." Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/4912.

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The aggregation of misfolded proteins into amyloid fibrils is implicated in the pathogenesis of several human degenerative diseases, including Alzheimer’s, Parkinson’s and Type II diabetes. Links between the deposition of amyloid fibrils and the progression of these diseases are poorly understood, with much of the current research focused on monomer misfolding and subsequent assembly of oligomers and mature fibrils. This project examines the formation of human apolipoprotein (apo) C-II amyloid fibrils, with a focus on the stability and reversibility of amyloid fibril assembly.
The initial stages of the project were to develop a model for apoC-II amyloid fibril formation. This was achieved by analysis of the concentration dependent kinetics of apoC-II amyloid fibril formation, and correlation of these data with the final size distribution of the fibrils, determined by sedimentation velocity experiments. On the basis of these studies, a new reversible model for apoC-II amyloid fibril formation is proposed that includes fibril breaking and re-joining as integral parts of the assembly mechanism. The model was tested by rigorous experimentation, with antibody-labelling transmission electron microscopy providing direct evidence for spontaneous fibril breaking and re-joining.
The development of this model for apoC-II fibril assembly provided the foundation for experiments to investigate factors that promote, inhibit or reverse amyloid fibril formation. Factors that were considered include a molecular chaperone protein, αB-crystallin, and a chemical modification, methionine oxidation. Investigations on the effect of αB-crystallin revealed that the inhibition of apoC-II fibril formation occurs by two distinct mechanisms: transient interaction with monomer preventing oligomerisation, and binding to mature fibrils, which inhibits fibril elongation. Studies on the effect of methionine oxidation on apoC-II fibril formation showed that both the assembly and stability of the fibrils was affected by this modification. ApoC-II contains two methionine residues (Met-9 and Met-60), and upon oxidation of these residues fibril formation was inhibited. In addition, the treatment of pre-formed fibrils with hydrogen peroxide caused dissociation of the fibrils via the oxidation of Met-60, located with the fibril core structural region. The final chapter details the development of antibodies that specifically recognise the conformation of apoC-II amyloid fibrils, which provide the foundation for future studies to examine the role that apoC-II amyloid fibrils play in disease.
Overall, this thesis reveals the dynamic and reversible nature of amyloid fibril formation. New insight is also obtained of the general stability of amyloid fibrils and the processes that may regulate their formation, persistence and disease pathogenesis in vivo.
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Daidone, Isabella. "Folding, misfolding and aggregation of proteins and peptides: a molecular dynamics study." Doctoral thesis, La Sapienza, 2005. http://hdl.handle.net/11573/917339.

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Books on the topic "Protein misfolding and aggregation"

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Muñoz, Victor, ed. Protein Folding, Misfolding and Aggregation. Cambridge: Royal Society of Chemistry, 2008. http://dx.doi.org/10.1039/9781847558282.

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N, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation, and conformational diseases. New York, N.Y: Springer Science+Business Media, 2006.

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N, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation and conformational diseases. New York: Springer, 2006.

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N, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation and conformational diseases. New York: Springer, 2007.

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Uversky, Vladimir N., and Anthony L. Fink, eds. Protein Misfolding, Aggregation, and Conformational Diseases. Boston, MA: Springer US, 2006. http://dx.doi.org/10.1007/b136464.

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Uversky, Vladimir N., and Anthony L. Fink, eds. Protein Misfolding, Aggregation, and Conformational Diseases. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-36534-3.

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Victor, Muñoz, ed. Protein folding, misfolding and aggregation: Classical themes and novel approaches. Cambridge, UK: Royal Society of Chemistry, 2008.

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B, O'Doherty Cian, and Byrne Adam C, eds. Protein misfolding. New York: Nova Science Publishers, 2008.

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Ramirez-Alvarado, Marina, Jeffery W. Kelly, and Christopher M. Dobson, eds. Protein Misfolding Diseases. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.

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Gomes, Cláudio M., ed. Protein Misfolding Diseases. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8820-4.

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Book chapters on the topic "Protein misfolding and aggregation"

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Cohen, Ehud, and Andrew Dillin. "Aging and Aggregation-Mediated Proteotoxicity." In Protein Misfolding Diseases, 631–44. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch29.

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Beckerman, Martin. "Protein Misfolding and Aggregation." In Biological and Medical Physics, Biomedical Engineering, 95–127. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22117-5_4.

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Wang, Yongting, and Jonathan A. King. "Cataract as a Protein-Aggregation Disease." In Protein Misfolding Diseases, 487–515. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch22.

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Li, Fang, and Richard M. Weinshilboum. "Thiopurine S-Methyltransferase Pharmacogenomics: Protein Misfolding, Aggregation, and Degradation." In Protein Misfolding Diseases, 453–68. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch20.

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Beckerman, Martin. "Protein Folding, Misfolding, and Aggregation." In Cellular Signaling in Health and Disease, 345–67. New York, NY: Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-98173-4_16.

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Wetzel, Ronald. "Misfolding and Aggregation in Huntington Disease and Other Expanded Polyglutamine Repeat Diseases." In Protein Misfolding Diseases, 305–24. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch14.

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Kikis, Elise A., Anat Ben-Zvi, and Richard I. Morimoto. "Caenorhabditis Elegans as a Model System to Study the Biology of Protein Aggregation and Toxicity." In Protein Misfolding Diseases, 175–90. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch9.

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Truscott, Roger John Willis. "Eye Lens Proteins and Cataracts." In Protein Misfolding, Aggregation, and Conformational Diseases, 435–47. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-36534-3_21.

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Ramirez-Alvarado, Marina, Janelle K. De Stigter, Elizabeth M. Baden, Laura A. Sikkink, Richard W. McLaughlin, and Anya L. Taboas. "Immunoglobulin Light Chain and Systemic Light-Chain Amyloidosis." In Protein Misfolding, Aggregation, and Conformational Diseases, 183–97. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-36534-3_9.

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LeVine, Harry. "Reporters of Amyloid Structure." In Protein Misfolding, Aggregation, and Conformational Diseases, 287–302. Boston, MA: Springer US, 2006. http://dx.doi.org/10.1007/0-387-25919-8_14.

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Conference papers on the topic "Protein misfolding and aggregation"

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Bellotti, Vittorio, and Monica Stoppini. "Nanotechnology drives a paradigm shift on protein misfolding diseases and amyloidosis." In THEORY AND APPLICATIONS IN COMPUTATIONAL CHEMISTRY: THE FIRST DECADE OF THE SECOND MILLENNIUM: International Congress TACC-2012. AIP, 2012. http://dx.doi.org/10.1063/1.4730667.

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Han, Yipeng, and Guangjie Chen. "A Method of Analyzing the Structures of Misfolding Proteins like Prion Protein." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering (ICBBE '08). IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.66.

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Pradhan, Chinmayee, and Subhankar Paul. "Investigation of the Role of Silver Nanoparticles in BSA Protein Misfolding Process." In 2011 International Conference on Nanoscience, Technology and Societal Implications (NSTSI). IEEE, 2011. http://dx.doi.org/10.1109/nstsi.2011.6111987.

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Hammarström, Per, Mikael Lindgren, and K. Peter R. Nilsson. "Luminescent conjugated oligothiophenes: optical dyes for revealing pathological hallmarks of protein misfolding diseases." In SPIE Photonic Devices + Applications, edited by Ruth Shinar and Ioannis Kymissis. SPIE, 2010. http://dx.doi.org/10.1117/12.859808.

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Giugliarelli, G. "Protein Folding and Aggregation Phenomena." In MODELING OF COMPLEX SYSTEMS: Seventh Granada Lectures. AIP, 2003. http://dx.doi.org/10.1063/1.1571330.

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Marasco, Daniela, Ettore Novellino, Giancarlo Morelli, and Sara La Manna. "Amyloidogenicity of regions of Nucleophosmin 1: a direct link between protein misfolding and Acute Myeloid Leukemia." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.038.

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Trusova, Valeriya M. "Amyloid fibrils: Dark side of protein aggregation." In 2015 International Young Scientists Forum on Applied Physics (YSF). IEEE, 2015. http://dx.doi.org/10.1109/ysf.2015.7333123.

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Vik, Cassidy, Lani Espinel, and Ashley Cannaday. "Using Angular Light Scattering to Measure Protein Aggregation." In Novel Techniques in Microscopy. Washington, D.C.: Optica Publishing Group, 2023. http://dx.doi.org/10.1364/ntm.2023.nw3c.4.

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Preliminary investigations were conducted to determine whether light scattering from proteins could be measured and fit to Mie theory. Distinct differences were observed in the scattering patterns from various aggregation sizes.
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Figueroa, Hector, and Deborah L. Heyl. "Running Interference on Protein Aggregation: Effects of Non-Specific Peptide Inhibitors of Amylin Aggregation." In The Twenty-Third American and the Sixth International Peptide Symposium. Prompt Scientific Publishing, 2013. http://dx.doi.org/10.17952/23aps.2013.130.

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Ikehara, Yuzuru, Sanae Ikehara, Hajime Sakakita, Takashi Yamaguchi, Jaeho Kim, Masahiro Yamagishi, Yoshihiro Akimoto, et al. "Plasmatreatment induces blood clot formation; protein aggregation and hemolysis." In 2016 IEEE International Conference on Plasma Science (ICOPS). IEEE, 2016. http://dx.doi.org/10.1109/plasma.2016.7534074.

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Reports on the topic "Protein misfolding and aggregation"

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Tzfira, Tzvi, Michael Elbaum, and Sharon Wolf. DNA transfer by Agrobacterium: a cooperative interaction of ssDNA, virulence proteins, and plant host factors. United States Department of Agriculture, December 2005. http://dx.doi.org/10.32747/2005.7695881.bard.

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Agrobacteriumtumefaciensmediates genetic transformation of plants. The possibility of exchanging the natural genes for other DNA has led to Agrobacterium’s emergence as the primary vector for genetic modification of plants. The similarity among eukaryotic mechanisms of nuclear import also suggests use of its active elements as media for non-viral genetic therapy in animals. These considerations motivate the present study of the process that carries DNA of bacterial origin into the host nucleus. The infective pathway of Agrobacterium involves excision of a single-stranded DNA molecule (T-strand) from the bacterial tumor-inducing plasmid. This transferred DNA (T-DNA) travels to the host cell cytoplasm along with two virulence proteins, VirD2 and VirE2, through a specific bacteriumplant channel(s). Little is known about the precise structure and composition of the resulting complex within the host cell and even less is known about the mechanism of its nuclear import and integration into the host cell genome. In the present proposal we combined the expertise of the US and Israeli labs and revealed many of the biophysical and biological properties of the genetic transformation process, thus enhancing our understanding of the processes leading to nuclear import and integration of the Agrobacterium T-DNA. Specifically, we sought to: I. Elucidate the interaction of the T-strand with its chaperones. II. Analyzing the three-dimensional structure of the T-complex and its chaperones in vitro. III. Analyze kinetics of T-complex formation and T-complex nuclear import. During the past three years we accomplished our goals and made the following major discoveries: (1) Resolved the VirE2-ssDNA three-dimensional structure. (2) Characterized VirE2-ssDNA assembly and aggregation, along with regulation by VirE1. (3) Studied VirE2-ssDNA nuclear import by electron tomography. (4) Showed that T-DNA integrates via double-stranded (ds) intermediates. (5) Identified that Arabidopsis Ku80 interacts with dsT-DNA intermediates and is essential for T-DNA integration. (6) Found a role of targeted proteolysis in T-DNA uncoating. Our research provide significant physical, molecular, and structural insights into the Tcomplex structure and composition, the effect of host receptors on its nuclear import, the mechanism of T-DNA nuclear import, proteolysis and integration in host cells. Understanding the mechanical and molecular basis for T-DNA nuclear import and integration is an essential key for the development of new strategies for genetic transformation of recalcitrant plant species. Thus, the knowledge gained in this study can potentially be applied to enhance the transformation process by interfering with key steps of the transformation process (i.e. nuclear import, proteolysis and integration). Finally, in addition to the study of Agrobacterium-host interaction, our research also revealed some fundamental insights into basic cellular mechanisms of nuclear import, targeted proteolysis, protein-DNA interactions and DNA repair.
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