Academic literature on the topic 'Protein misfolding and aggregation'
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Journal articles on the topic "Protein misfolding and aggregation"
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.
Full textCuervo, 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.
Full textPopiel, 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.
Full textAjmal, 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.
Full textWang, 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.
Full textCuanalo-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.
Full textLu, 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.
Full textTan, 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.
Full textDobson, 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.
Full textLyubchenko, 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.
Full textDissertations / Theses on the topic "Protein misfolding and aggregation"
BROGGINI, LUCA. "MOLECULAR DETERMINANTS UNDERLYING PROTEIN MISFOLDING AND AGGREGATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/831967.
Full textBuell, Alexander Kai. "On the kinetics of protein misfolding and aggregation." Thesis, University of Cambridge, 2011. https://www.repository.cam.ac.uk/handle/1810/270324.
Full textTodorova, 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.
Full textDevlin, 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.
Full textBorgia, 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.
Full textFreer, 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.
Full textXu, Mingming. "Discovery of inhibitors against a-synuclein aggregation." Thesis, Griffith University, 2020. http://hdl.handle.net/10072/392373.
Full textThesis (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.
Full textBinger, Katrina Jean. "The reversibility of amyloid fibril formation." Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/4912.
Full textThe 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.
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.
Full textBooks on the topic "Protein misfolding and aggregation"
Muñoz, Victor, ed. Protein Folding, Misfolding and Aggregation. Cambridge: Royal Society of Chemistry, 2008. http://dx.doi.org/10.1039/9781847558282.
Full textN, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation, and conformational diseases. New York, N.Y: Springer Science+Business Media, 2006.
Find full textN, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation and conformational diseases. New York: Springer, 2006.
Find full textN, Uversky Vladimir, and Fink Anthony L. 1943-, eds. Protein misfolding, aggregation and conformational diseases. New York: Springer, 2007.
Find full textUversky, 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.
Full textUversky, 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.
Full textVictor, Muñoz, ed. Protein folding, misfolding and aggregation: Classical themes and novel approaches. Cambridge, UK: Royal Society of Chemistry, 2008.
Find full textB, O'Doherty Cian, and Byrne Adam C, eds. Protein misfolding. New York: Nova Science Publishers, 2008.
Find full textRamirez-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.
Full textGomes, Cláudio M., ed. Protein Misfolding Diseases. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8820-4.
Full textBook chapters on the topic "Protein misfolding and aggregation"
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.
Full textBeckerman, 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.
Full textWang, 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.
Full textLi, 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.
Full textBeckerman, 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.
Full textWetzel, 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.
Full textKikis, 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.
Full textTruscott, 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.
Full textRamirez-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.
Full textLeVine, 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.
Full textConference papers on the topic "Protein misfolding and aggregation"
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.
Full textHan, 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.
Full textPradhan, 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.
Full textHammarström, 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.
Full textGiugliarelli, G. "Protein Folding and Aggregation Phenomena." In MODELING OF COMPLEX SYSTEMS: Seventh Granada Lectures. AIP, 2003. http://dx.doi.org/10.1063/1.1571330.
Full textMarasco, 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.
Full textTrusova, 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.
Full textVik, 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.
Full textFigueroa, 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.
Full textIkehara, 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.
Full textReports on the topic "Protein misfolding and aggregation"
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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