Academic literature on the topic 'Protein oligomers'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Protein oligomers.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Protein oligomers"
Schmid, J. A., H. Just, and H. H. Sitte. "Impact of oligomerization on the function of the human serotonin transporter." Biochemical Society Transactions 29, no. 6 (November 1, 2001): 732–36. http://dx.doi.org/10.1042/bst0290732.
Full textEisenberg, David, Arthur Laganowsky, Cong Liu, Michael Sawaya, Julian Whitelegge, Minglei Zhao, Angela Soriaga, et al. "Structural Studies of the Amyloid State of Proteins." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C797. http://dx.doi.org/10.1107/s205327331409202x.
Full textTanner, John J. "Empirical power laws for the radii of gyration of protein oligomers." Acta Crystallographica Section D Structural Biology 72, no. 10 (September 15, 2016): 1119–29. http://dx.doi.org/10.1107/s2059798316013218.
Full textVaikath, Nishant, Indulekha Sudhakaran, Ilham Abdi, Vijay Gupta, Nour Majbour, Simona Ghanem, Houari Abdesselem, Kostas Vekrellis, and Omar El-Agnaf. "Structural and Biophysical Characterization of Stable Alpha-Synuclein Oligomers." International Journal of Molecular Sciences 23, no. 23 (November 23, 2022): 14630. http://dx.doi.org/10.3390/ijms232314630.
Full textKreiser, Ryan P., Aidan K. Wright, Natalie R. Block, Jared E. Hollows, Lam T. Nguyen, Kathleen LeForte, Benedetta Mannini, Michele Vendruscolo, and Ryan Limbocker. "Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers." International Journal of Molecular Sciences 21, no. 22 (November 17, 2020): 8651. http://dx.doi.org/10.3390/ijms21228651.
Full textde Klerk, G. J., and D. Engelen. "Assembly of Agrostemma githago (corn-cockle) storage proteins and their precursor proteins into oligomers." Biochemical Journal 230, no. 1 (August 15, 1985): 269–72. http://dx.doi.org/10.1042/bj2300269.
Full textStoneman, Michael R., Naomi Raicu, Gabriel Biener, and Valerică Raicu. "Fluorescence-based Methods for the Study of Protein-Protein Interactions Modulated by Ligand Binding." Current Pharmaceutical Design 26, no. 44 (December 22, 2020): 5668–83. http://dx.doi.org/10.2174/1381612826666201116120934.
Full textLarson, Megan E., Susan J. Greimel, Fatou Amar, Michael LaCroix, Gabriel Boyle, Mathew A. Sherman, Hallie Schley, et al. "Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits." Proceedings of the National Academy of Sciences 114, no. 23 (May 22, 2017): E4648—E4657. http://dx.doi.org/10.1073/pnas.1704698114.
Full textWang, Yu, Karen S. L. Lam, Ming-hon Yau, and Aimin Xu. "Post-translational modifications of adiponectin: mechanisms and functional implications." Biochemical Journal 409, no. 3 (January 15, 2008): 623–33. http://dx.doi.org/10.1042/bj20071492.
Full textNEMOTO, Takayuki, and Nobuko SATO. "Oligomeric forms of the 90-kDa heat shock protein." Biochemical Journal 330, no. 2 (March 1, 1998): 989–95. http://dx.doi.org/10.1042/bj3300989.
Full textDissertations / Theses on the topic "Protein oligomers"
Andrade, Helena. "DNA Oligomers - From Protein Binding to Probabilistic Modelling." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2017. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-218709.
Full textRushworth, Joanne Valerie Humphrey. "The cellular prion protein as a receptor for amyloid-beta oligomers." Thesis, University of Leeds, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.581951.
Full textMa, Xin. "Ion Mobility Mass Spectrometry of DNA/SgrAI Nuclease Oligomers." Thesis, The University of Arizona, 2012. http://hdl.handle.net/10150/247282.
Full textLimbocker, Ryan Alexander. "Mitigating protein aggregation to reduce the toxicity inherent to Parkinson's and Alzheimer's diseases." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/284937.
Full textPhan, Jamie. "Investigating protein folding by the de novo design of an α-helix oligomer." Scholarly Commons, 2013. https://scholarlycommons.pacific.edu/uop_etds/859.
Full textXu, Xiaojun [Verfasser], and A. S. [Akademischer Betreuer] Ulrich. "Protein-protein interactions in oligomers studied by solid-state NMR in biomembranes / Xiaojun Xu. Betreuer: A. S. Ulrich." Karlsruhe : KIT-Bibliothek, 2016. http://d-nb.info/1108453198/34.
Full textPhan, Jamie. "Investigating protein folding by the de novo design of an α-helix oligomer : a thesis." Scholarly Commons, 2001. https://scholarlycommons.pacific.edu/uop_etds/859.
Full textZych, Andrew John. "Conformational characterization of abiotic secondary structure based on aromatic stacking /." Full text (PDF) from UMI/Dissertation Abstracts International, 2001. http://wwwlib.umi.com/cr/utexas/fullcit?p3008484.
Full textDe, Giorgi Marcella. "Design and synthesis of novel thienylpyridyl oligomers as alpha helix mimetics with protein-protein interaction disrupting activity and possible biological applications." Caen, 2012. http://www.theses.fr/2012CAEN4076.
Full textProtein-protein interactions (PPIs) are attractive targets for drug discovery. Indeed, most of cellular processes are composed or influenced by PPIs and their misregulation can result in numerous disease states. Even if proteins surfaces are generally large, some key elements are responsible of the interaction and the recognition (hot spots). The most common secondary structure in natural proteins is an alpha helix. Small molecules seem to be attractive candidates for stabilizing or disrupting protein-protein interactions based on alpha helices. We are particularly interested in Bcl-2 family proteins which are central regulators of apoptosis. They are overexpressed in many cancers and contribute to tumour initiation, progression and resistance to therapy. The aim of our study is to design small molecules able to interact with anti-apoptotic members and restore the intrinsic apoptosis mechanism. These foldamers would mimic only the key elements of a protein surface and potentially lead to small molecules having almost the full activity of a protein domain. For this, we synthesized a library of thienylpyridyl oligomers. Most of these compounds underwent molecular modeling studies based on radiocrystallography in order to evaluate the ability to mimic an alpha helix and the spatial orientation of different substituents. Moreover, biological tests have been done to evaluate the ability to induce apoptosis in cancer cells
Fluharty, Brian Richard. "Identification of novel cellular prion protein-based compounds to block the toxicity of amyloid-beta oligomers." Thesis, Boston University, 2013. https://hdl.handle.net/2144/12955.
Full textAlzheimer's disease (AD) is characterized by progressive dementia and accumulation of a cleavage product of the amyloid precursor protein, amyloid-β (Aβ) peptide, in the brain. Several lines of evidence suggest that soluble, oligomeric intermediates of Aβ are primarily responsible for synaptic dysfunction and the cognitive deficit observed in AD. The cellular prion protein (PrP^c), a cell surface glycoprotein involved in transmissible spongiform encephalopathies, was previously identified as a high affinity receptor for Aβ oligomers. It has been suggested that binding of Aβ oligomers to PrP^c transduces the synaptotoxic events seen in AD. The two reported binding sites of Aβ oligomers are located on the unstructured N-terminal tail of PrP^c. We show here that the soluble physiological cleavage fragment of PrP^c, N1, was necessary and sufficient for binding Aβ oligomers. This binding interaction was influenced by positively charged residues in the two binding sites and is dependent on the length ofthe sequence between them. Importantly, the addition of synthetic N1 peptide suppressed Aβ oligomer toxicity in cultured murine hippocampal neurons and in a mouse model of Aβ-induced memory dysfunction. Collectively, these data suggest that N1, or small peptides derived from it, could be potent inhibitors of Aβ oligomer toxicity by targeting Aβ oligomers and represent an entirely new class of therapeutic agents for AD. To directly target PrP^c as a toxicity receptor, in silica screening and molecular dynamics were used to generate small molecule ligands. We screened these ligands using biochemical and biophysical assays to identify high affinity ligands for PrP^c that block the binding of Aβ oligomers. We found one compound, called DS26 that bound to PrP^c with sub-micromolar affinity. Further, DS26 inhibited Aβ-dependent suppression of long-term potentiation in mouse hippocampal slices. Interestingly, we show that DS26 operated by an unexpected allosteric mechanism in which ligand binding to a site in the structured C-terminal half of PrP^c induced an intramolecular interaction with the N-terminal tail, thereby preventing Aβ binding. Together, these data demonstrate that pharmacologically targeting PrP^c can suppress Aβ toxicity. Additionally, this study clarifies previous conflicting studies regarding the role of PrP^c in AD.
Books on the topic "Protein oligomers"
Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.
Full textMoloshok, Thomas David. Oligogalacturonides as signals for plant defensive genes: Structure-activity relationships of oligomers for induction of proteinase inhibitors and for enhancement of plasma membrane protein phosphorylation. 1989.
Find full textWetzel, Ronald, and Rakesh Mishra. Structural Biology. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199929146.003.0012.
Full textSafar, Jiri G. Prion Paradigm of Human Neurodegenerative Diseases Caused by Protein Misfolding. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0005.
Full textLattman, Eaton E., Thomas D. Grant, and Edward H. Snell. Shape Reconstructions from Small Angle Scattering Data. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780199670871.003.0004.
Full textBook chapters on the topic "Protein oligomers"
Ferré, Sergi. "Allosterism Within GPCR Oligomers: Back to Symmetry." In G-Protein-Coupled Receptor Dimers, 433–50. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_17.
Full textSleno, Rory, Dominic Devost, and Terence E. Hébert. "Understanding the Physiological Significance of GPCR Dimers and Oligomers." In G-Protein-Coupled Receptor Dimers, 451–65. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_18.
Full textWang, Chunyu. "Solution NMR Studies of Aβ Monomers and Oligomers." In Protein and Peptide Folding, Misfolding, and Non-Folding, 389–411. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9781118183373.ch13.
Full textKandiyal, Pancham S., Ji Yoon Kim, Daniel L. Fortunati, and K. H. Mok. "Size Determination of Protein Oligomers/Aggregates Using Diffusion NMR Spectroscopy." In Methods in Molecular Biology, 173–83. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9678-0_13.
Full textHong, Dong-Pyo, Wenbo Zhou, Aaron Santner, and Vladimir N. Uversky. "Oligomers of α-Synuclein in the Pathogenesis of Parkinson’s Disease." In Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases, 189–216. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-2774-8_6.
Full textPalacio-Castañeda, Valentina, Roland Brock, and Wouter P. R. Verdurmen. "Generation of Protein-Phosphorodiamidate Morpholino Oligomer Conjugates for Efficient Cellular Delivery via Anthrax Protective Antigen." In Methods in Molecular Biology, 129–41. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2010-6_8.
Full textRosensweig, Clark, Kenjiro Ono, Kazuma Murakami, Devin K. Lowenstein, Gal Bitan, and David B. Teplow. "Preparation of Stable Amyloid β-Protein Oligomers of Defined Assembly Order." In Methods in Molecular Biology, 23–31. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-551-0_3.
Full textSakmar, Thomas P., Xavier Periole, and Thomas Huber. "Probing Self-Assembly of G Protein-Coupled Receptor Oligomers in Membranes Using Molecular Dynamics Modeling and Experimental Approaches." In G-Protein-Coupled Receptor Dimers, 385–414. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_15.
Full textMorales, Rodrigo, Claudia A. Duran-Aniotz, and Claudio Soto. "Role of Prion Protein Oligomers in the Pathogenesis of Transmissible Spongiform Encephalopathies." In Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases, 319–35. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-2774-8_10.
Full textBhaskar, Kiran, and Bruce T. Lamb. "The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s Disease." In Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases, 135–88. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-2774-8_5.
Full textConference papers on the topic "Protein oligomers"
Intze, A., M. E. Temperini, R. Polito, E. Zacco, G. G. Tartaglia, A. Pastore, M. Ortolani, and V. Giliberti. "Mid-infrared nanospectroscopy of individual DNA-binding protein oligomers." In 2022 47th International Conference on Infrared, Millimeter and Terahertz Waves (IRMMW-THz). IEEE, 2022. http://dx.doi.org/10.1109/irmmw-thz50927.2022.9895918.
Full textAbakumets, V. Y., and K. Ya Bulanava. "THE INFLUENCE OF INSULIN FIBRILLATION." In SAKHAROV READINGS 2021: ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2021. http://dx.doi.org/10.46646/sakh-2021-2-7-10.
Full textTemirov, Jamshid, James H. Werner, Peter M. Goodwin, and Andrew R. M. Bradbury. ""Sizing" the oligomers of Azami Green fluorescent protein with FCS and antibunching." In SPIE BiOS, edited by Jörg Enderlein, Zygmunt K. Gryczynski, Rainer Erdmann, Felix Koberling, and Ingo Gregor. SPIE, 2012. http://dx.doi.org/10.1117/12.906843.
Full textIde, J. P., D. R. Klug, W. Kuhlbrandt, and G. Porter. "Detergent effects upon the picosecond dynamics of higher plant light harvesting chlorophyll complex (LHC)." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.mf1.
Full textStoneman, M. R., D. R. Singh, and V. Raicu. "In vivo stoichiometry monitoring of G protein coupled receptor oligomers using spectrally resolved two-photon microscopy." In BiOS, edited by Ammasi Periasamy, Peter T. C. So, and Karsten König. SPIE, 2010. http://dx.doi.org/10.1117/12.843916.
Full textWu, Jeffrey, Prakash Ambady, DreeAnna Morris, Michael Pagel, Randy Woltjer, Joshua Walker, Leslie Muldoon, and Edward Neuwelt. "Abstract B38: Radiation enhances intracellular delivery of anti-MGMT oligomers to reduce protein expression in vitro and in a xenograft model." In Abstracts: AACR Special Conference on DNA Repair: Tumor Development and Therapeutic Response; November 2-5, 2016; Montreal, QC, Canada. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1557-3125.dnarepair16-b38.
Full textSabino, Luis G., Wellinson Gadelha Guimarães, Pedro Mikael Costa, Marta S. P. Carepo, Ana C. S. Gondim, Luiz G. F. Lopes, and Eduardo H. S. Sousa. "The application of low angle light scattering to evaluate qualitatively and quantitatively the dynamics of formation of oligomers in heme protein sensors." In SPIE BiOS, edited by Adam Wax and Vadim Backman. SPIE, 2016. http://dx.doi.org/10.1117/12.2213733.
Full textSavikhin, S., and W. S. Struve. "Optical coherences in light-harvesting chlorosomes from green photosynthetic bacteria." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1996. http://dx.doi.org/10.1364/up.1996.tue.21.
Full textSavikhir, S., Y. Zhu, S. Lin, R. E. Blankenship, and W. S. Struve. "Femtosecond energy transfer and coherent oscillations in BChl c light-harvesting antennae of chlorosomes from the green photosynthetic bacterium Chloroflexus aurantiacus." In International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/up.1994.tub.3.
Full textRak, K., J. Harsfalvi, M. Udavardy, I. Tornai, M. Misz, and Z. Boda. "ALTERATION OF PRIMARY HAEMOSTASIS IN PATIENTS WITH ATHEROSCLEROSIS: ITS POSSIBLE ROLE IN ATHEROGENESIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643082.
Full textReports on the topic "Protein oligomers"
Garcia, A. E., and G. Hummer. Theoretical studies of the interaction of water with DNA oligomers and proteins. Office of Scientific and Technical Information (OSTI), April 1996. http://dx.doi.org/10.2172/212500.
Full textSierks, Michael. Oligomeric Neuronal Protein Aggregates as Biomarkers for Traumatic Brain Injury (TBI) and Alzheimer Disease (AD). Fort Belvoir, VA: Defense Technical Information Center, October 2013. http://dx.doi.org/10.21236/ada591179.
Full textFleming, Karen G. Energetics and Structure Prediction of the Network of Homo- and Hetero-Oligomers Formed by the Transmembrane Domains of the ErbReceptor Family of Proteins. Fort Belvoir, VA: Defense Technical Information Center, June 2006. http://dx.doi.org/10.21236/ada456142.
Full textAzem, Abdussalam, George Lorimer, and Adina Breiman. Molecular and in vivo Functions of the Chloroplast Chaperonins. United States Department of Agriculture, June 2011. http://dx.doi.org/10.32747/2011.7697111.bard.
Full textValente, Pedro, Luis Rama, Hugo Sarmento, and Ana Teixeira. Cartilage Oligomeric Matrix Protein (COMP), a potential cartilage destruction biomarker in active and healthy individuals or athletes from different sports. A systematic review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, February 2021. http://dx.doi.org/10.37766/inplasy2021.2.0032.
Full text