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Gotowe bibliografie tematyczne / Β-amyloid structures

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Gotowa bibliografia na temat „Β-amyloid structures”

Autor: Grafiati

Data publikacji: 23 listopada 2024

Data aktualizacji: 31 lipca 2025

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Artykuły w czasopismach na temat "Β-amyloid structures"

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Taguchi, Yuzuru, Hiroki Otaki та Noriyuki Nishida. "Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains". Viruses 11, № 2 (2019): 110. http://dx.doi.org/10.3390/v11020110.

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The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc); however, achieving purification is difficult without affecting infectivity. Similar prion-like properties are recognized also in other disease-associated in-register parallel β-sheet amyloids including Tau and α-synuclein (αSyn) amyloids. Investigations into structures of those amyloids via solid-state nuclear magnetic resonance spectroscopy and

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M Smith, Margaret, and James Melrose. "Amyloid, A Jekyll and Hyde Molecule, Induces Neuronal Decline and Cognitive Dysfunction but is also a Unique Molecular Template used in Nano-Electronics, Light Capture Photovoltaics, Biosensors and in Neuromorphic Computing." International Journal of Nanotechnology and Nanomedicine 9, no. 2 (2024): 01–13. http://dx.doi.org/10.33140/ijnn.09.02.02.

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This study, examined the self-assembly of amyloid peptides β-40 or β-42 to form neurotoxic plaque and neurofibrillary tangles, neuronal dysfunction and diseases of cognitive decline (e.g. Alzheimer’s, Parkinson’s and Huntington's disease). However, not all amyloids are toxic, functional amyloids are non-toxic ordered structures that have been used in tissue engineering applications. Long and hollow amyloid fibres and flattened tube and spiral ribbon-like structures are diverse self-assembling structures that have found application in the development of next generation computers and biosensors,

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Chatani, Eri, Keisuke Yuzu, Yumiko Ohhashi, and Yuji Goto. "Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils." International Journal of Molecular Sciences 22, no. 9 (2021): 4349. http://dx.doi.org/10.3390/ijms22094349.

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Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure consisting of a backbone of hydrogen bonds, side-chain interactions also play an important role in determining their detailed structures and physicochemical properties. In amyloid fibrils comprising short peptide segments, a steric zipper where a pair of β-sheets with side chains interdigitate tightly is found as a fundamental motif. In amyloid fibrils

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Paulus, Agnes, Anders Engdahl, Yiyi Yang, et al. "Amyloid Structural Changes Studied by Infrared Microspectroscopy in Bigenic Cellular Models of Alzheimer’s Disease." International Journal of Molecular Sciences 22, no. 7 (2021): 3430. http://dx.doi.org/10.3390/ijms22073430.

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Alzheimer’s disease affects millions of lives worldwide. This terminal disease is characterized by the formation of amyloid aggregates, so-called amyloid oligomers. These oligomers are composed of β-sheet structures, which are believed to be neurotoxic. However, the actual secondary structure that contributes most to neurotoxicity remains unknown. This lack of knowledge is due to the challenging nature of characterizing the secondary structure of amyloids in cells. To overcome this and investigate the molecular changes in proteins directly in cells, we used synchrotron-based infrared microspec

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Sulatskaya, Anna I., Anastasiia O. Kosolapova, Alexander G. Bobylev та ін. "β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis". International Journal of Molecular Sciences 22, № 21 (2021): 11316. http://dx.doi.org/10.3390/ijms222111316.

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Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which th

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Gao, Yang, Sophia Schedin-Weiss та Lars O. Tjernberg. "A closer look at pathogenic amyloid-β in Alzheimer’s disease using cryo-electron microscopy: a narrative review". Advanced Technology in Neuroscience 1, № 2 (2024): 177–87. http://dx.doi.org/10.4103/atn.atn-d-24-00014.

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Alzheimer’s disease is a progressive neurodegenerative disorder that affects millions of people worldwide. The identification of amyloid-β in Alzheimer’s disease brains, together with the association of mutations in the amyloid-β precursor protein with Alzheimer’s disease pathology, is the basis of the amyloid cascade hypothesis, which suggests that amyloid-β plays a central role in Alzheimer’s disease pathogenesis. Recent studies have further highlighted the role of intraneuronal amyloid-β in Alzheimer’s disease development. Moreover, the success of anti-amyloid-β immunotherapies supports the

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Alperstein, Ariel M., Joshua S. Ostrander, Tianqi O. Zhang, and Martin T. Zanni. "Amyloid found in human cataracts with two-dimensional infrared spectroscopy." Proceedings of the National Academy of Sciences 116, no. 14 (2019): 6602–7. http://dx.doi.org/10.1073/pnas.1821534116.

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UV light and other factors damage crystallin proteins in the eye lens, resulting in cataracts that scatter light and affect vision. Little information exists about protein structures within these disease-causing aggregates. We examined postmortem lens tissue from individuals with and without cataracts using 2D infrared (2DIR) spectroscopy. Amyloid β-sheet secondary structure was detected in cataract lenses along with denatured structures. No amyloid structures were found in lenses from juveniles, but mature lenses with no cataract diagnosis also contained amyloid, indicating that amyloid struc

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Freitas, Raul O., Adrian Cernescu, Anders Engdahl, et al. "Nano-Infrared Imaging of Primary Neurons." Cells 10, no. 10 (2021): 2559. http://dx.doi.org/10.3390/cells10102559.

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Alzheimer’s disease (AD) accounts for about 70% of neurodegenerative diseases and is a cause of cognitive decline and death for one-third of seniors. AD is currently underdiagnosed, and it cannot be effectively prevented. Aggregation of amyloid-β (Aβ) proteins has been linked to the development of AD, and it has been established that, under pathological conditions, Aβ proteins undergo structural changes to form β-sheet structures that are considered neurotoxic. Numerous intensive in vitro studies have provided detailed information about amyloid polymorphs; however, little is known on how amylo

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Tycko, Robert. "Molecular structure of amyloid fibrils: insights from solid-state NMR." Quarterly Reviews of Biophysics 39, no. 1 (2006): 1–55. http://dx.doi.org/10.1017/s0033583506004173.

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1. Introduction 22. Sources of structural information in solid-state NMR data 52.1 General remarks 52.2 Chemical shifts, linewidths, and magic-angle spinning 62.3 Dipole–dipole couplings and dipolar recoupling 82.4 Tensor correlation techniques 122.5 Solid-state NMR of aligned samples 142.6 Indirect sources of structural information 152.7 Sample preparation for solid-state NMR 153. Levels of structure in amyloid fibrils 184. Molecular structure of β-amyloid fibrils 254.1 Self-propagating, molecular-level polymorphism in Aβ1–40 fibrils 254.2 Structural model for Aβ1-40 fibrils 284.3 Staggering

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Yakupova, Elmira I., Liya G. Bobyleva, Sergey A. Shumeyko, Ivan M. Vikhlyantsev, and Alexander G. Bobylev. "Amyloids: The History of Toxicity and Functionality." Biology 10, no. 5 (2021): 394. http://dx.doi.org/10.3390/biology10050394.

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Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures such as amyloid aggregates. Amyloids are rigid protein aggregates with the cross-β structure, resistant to most solvents and proteases. Because of their resistance to proteolysis, amyloid aggregates formed in the organism accumulate in tissues, promoting the development of various diseases called amyloidosis, for instance Alzheimer’s diseases (AD).

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Rozprawy doktorskie na temat "Β-amyloid structures"

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Newby, Francisco Nicolas. "Structural studies of the Alzheimer's amyloid β peptide". Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.607712.

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Siegemund, Thomas. "Structure and properties of drug-loaded polymeric nanoparticles targeting β-amyloid". Doctoral thesis, Universitätsbibliothek Leipzig, 2011. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-70212.

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Polymere Nanopartikel sind ein vielversprechender Ansatz für die Diagnose und Therapie von Krankheiten. Sie ermöglichen den Einsatz von schwerlöslichen oder instabilen Wirkstoffen. Ein weiterer Vorteil ist die Möglichkeit das Targetings, durch gezielte Modifikationen des Nanopartikels wird der Wirkstoff zum Zielort transportiert und kann dort in der gewünschten Form freigesetzt werden; dadurch könnten bei erhöhter Wirksamkeit die Nebenwirkungen von Medikamenten reduziert werden. Ziel dieser Arbeit war die Untersuchung von physikalischen und biochemischen Eigenschaften von Nanopartikeln besteh

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Daou, Dania. "Intégration de moteurs moléculaires photoactivables dans des gels supramoléculaires." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAF021.

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Cette thèse a exploré l'intégration de moteurs moléculaires synthétiques photoactivables dans des réseaux de gels supramoléculaires. L'objectif principal était d'obtenir un mouvement macroscopique réversible en exploitant à la fois la rotation unidirectionnelle des moteurs moléculaires et la nature réversible des interactions supramoléculaires. Des moteurs moléculaires hautement fonctionnalisés ont été synthétisés et intégrés comme unités de réticulation dans des réseaux de gel supramoléculaire de peptides de diphénylalanine et de poly(γ-benzyl-L-glutamate) et d'oligonucléotides d'ADN. L'activ

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Zhu, Maximillian. "Computational studies of the Alzheimer's amyloid-β peptide : from structural ensembles to therapeutic leads". Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.608056.

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Cozma, Claudia [Verfasser]. "Determination of Primary Structure and Affinity Characterization of Naturally Occurring β-Amyloid Autoantibodies / Claudia Cozma". Konstanz : Bibliothek der Universität Konstanz, 2014. http://d-nb.info/1079910271/34.

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Wißbrock, Amelie [Verfasser]. "Transient Heme-Protein Interactions: Structural and Functional Studies on Interleukin-36α and Amyloid-β / Amelie Wißbrock". Bonn : Universitäts- und Landesbibliothek Bonn, 2020. http://d-nb.info/1224270444/34.

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Paraschiv, Gabriela Ioana [Verfasser]. "Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods / Gabriela Ioana Paraschiv". Konstanz : Bibliothek der Universität Konstanz, 2012. http://d-nb.info/1025637240/34.

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Cerda, Muñoz Fabian Esteban [Verfasser], Wolfgang [Akademischer Betreuer] Baumeister, Bernd [Gutachter] Reif та Wolfgang [Gutachter] Baumeister. "Structural study of the Amyloid β cytotoxicity / Fabian Esteban Cerda Muñoz ; Gutachter: Bernd Reif, Wolfgang Baumeister ; Betreuer: Wolfgang Baumeister". München : Universitätsbibliothek der TU München, 2021. http://d-nb.info/1230552790/34.

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Dammers, Christina [Verfasser], Dieter [Gutachter] Willbold та Henrike [Gutachter] Heise. "Structural analysis and aggregation of Alzheimer’s disease related pyroglutamate-modified amyloid-β / Christina Dammers ; Gutachter: Dieter Willbold, Henrike Heise". Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2017. http://d-nb.info/1132771757/34.

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Dammers, Christina Verfasser], Dieter [Gutachter] [Willbold та Henrike [Gutachter] Heise. "Structural analysis and aggregation of Alzheimer’s disease related pyroglutamate-modified amyloid-β / Christina Dammers ; Gutachter: Dieter Willbold, Henrike Heise". Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2017. http://d-nb.info/1132771757/34.

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Części książek na temat "Β-amyloid structures"

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Tycko, Robert. "β-Amyloid Fibril Structures, In Vitro and In Vivo." In Proteopathic Seeds and Neurodegenerative Diseases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-35491-5_2.

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Bukauskas, V., V. Strazdienė, A. Šetkus, S. Bružytė, V. Časaitė, and R. Meškys. "β-Sheeted Amyloid Fibril Based Structures For Hybrid Nanoobjects On Solid Surfaces." In Springer Proceedings in Physics. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-95930-4_10.

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van Andel, A. C. J., P. R. Hol, J. H. van der Maas, E. T. G. Lutz, H. Krabbendam, and E. Gruys. "Reaggregation of Bovine Amyloid a Fibril Components to β-Pleated Sheet Fibrillar Structures." In Amyloidosis. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_5.

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Inouye, Hideyo, and Daniel A. Kirschner. "Refined Fibril Structures: The Hydrophobic Core in Alzheimer's Amyloid β-Protein and Prion as Revealed by X-ray Diffraction." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514924.ch3.

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Muñoz, Francisco J., and Nibaldo C. Inestrosa. "Acetylcholinesterase Enhances the Neurotoxicity of β-Amyloid Fibrils." In Structure and Function of Cholinesterases and Related Proteins. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_48.

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Meier, Beat H., and Anja Böckmann. "Solid-State NMR Structure of Amyloid-β Fibrils." In Methods in Molecular Biology. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2597-2_5.

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De Ferrari, Giancarlo V., and Nibaldo C. Inestrosa. "Identification of an Acetylcholinesterase Fragment that Promotes Alzheimer β-Amyloid Fibril Formation." In Structure and Function of Cholinesterases and Related Proteins. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_50.

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Gröbner, Gerhard, Clemens Glaubitz, Philip T. F. Williamson, Timothy Hadingham, and Anthony Watts. "Structural insight into the interaction of amyloid-β peptide with biological membranes by solid state NMR." In Focus on Structural Biology. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-017-2579-8_18.

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Pateras, Joseph, Ashwin Vaidya, and Preetam Ghosh. "Physics-Informed Bias Method for Multiphysics Machine Learning: Reduced Order Amyloid-β Fibril Aggregation." In Recent Advances in Mechanics and Fluid-Structure Interaction with Applications. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-14324-3_7.

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Keppler, Julia K., Timon R. Heyn, Jacqueline Lux, et al. "(Amyloid) Protein Aggregates from β-Lactoglobulin and Their Behavior Along the Process Chain." In Dispersity, Structure and Phase Changes of Proteins and Bio Agglomerates in Biotechnological Processes. Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-63164-1_7.

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Streszczenia konferencji na temat "Β-amyloid structures"

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Park, Jiyong, Byungnam Kahng та Wonmuk Hwang. "Supramolecular Structure and Stability of the GNNQQNY β-Sheet Bilayer Filament: A Computational Study". У ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-175588.

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Self-assembly of β-sheet forming peptides into filaments has drawn great interests in biomedical applications [1,2]; Hydrogels formed by filaments self-assembled from de novo designed peptides possess potential applications for cell culture scaffolds [3]. On the other hand, peptides derived from amyloidogenic proteins in neurodegenerative diseases such as Alzheimer’s and Parkinson’s also form similar β-sheet filaments in vitro. They share little sequence homology, yet filaments formed by these self-assembling peptides commonly have the cross-β structure, the key signature of the amyloid fibril

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Athamneh, Ahmad, and Justin Barone. "Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins." In ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-540.

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Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-β amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 μm in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein

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Shutikov, A. A., G. M. Arzumanyan, K. Z. Mamatkulov, E. Arynbek та D. S. Zakrytnaya. "ANALYSIS OF THE SECONDARY STRUCTURE OF AΒ (1-42) PEPTIDE IN THE AMIDE I REGION BY RAMAN SPECTROSCOPY". У X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-220.

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Amyloid fibrils found in plaques in Alzheimer’s disease (AD) brains are composed of amyloid-β peptides. Aβ peptides are formed from the transmembrane amyloid precursor protein (APP). They have pronounced fibrillogenic properties, and its oligomers are toxic to nerve cells, causing their degeneration and death. Oligomeric amyloid-β (1-42) is thought to play a critical role in neurodegeneration in AD. In this work, we analyzed the conformational transformation of Aβ (1-42) peptides embedded in membrane mimetics by Raman spectroscopy. The main goal of the scientific study was to investigate the s

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Souza, Giordana S., Samara O. Pinto та Ana Maria Marques da Silva. "Evaluation of MR-less in brain amyloid-β PET Centiloid quantification". У Biomedical Applications in Molecular, Structural, and Functional Imaging, редактори Barjor S. Gimi та Andrzej Krol. SPIE, 2022. http://dx.doi.org/10.1117/12.2611904.

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Lomakin, Aleksey, David B. Teplow, Daniel A. Kirschner та George B. Benedek. "Nucleation and Growth of Amyloid β-Protein Fibrils: Detection of Nuclei and Quantitation of Rate Constants". У Photon Correlation and Scattering. Optica Publishing Group, 1996. http://dx.doi.org/10.1364/pcs.1996.sab.3.

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Alzheimer's disease is a progressive, neurodegenerative disorder characterized by amyloid deposition in senile plaques in the cerebral parenchyma and vasculature.(1) These plaques are composed primarily of fibers of the amyloid β-protein, Aβ. A number of studies have provided information on the structure of fibrils formed both in vivo and in vitro, and on factors affecting fiber formation. Synthetic Aβ peptides also form fibers which are ultrastructurally indistinguishable from those isolated from the brain. These peptides have been utilized to examine how a variety of parameters, including te

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Silva, Letícia Freitas de Castro, Elisa Pinheiro Weber, Gleice Silva Toledo, and Josiane Fonseca Almeida. "New pharmacological strategies for the treatment of alzheimer’s disease." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.097.

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Introduction: Alzheimer’s disease (AD) is seen as the most important dementia, prevalent in the elderly over 60 years old. There is still no cure, and the pharmacological strategies are to delay the symptoms and development of the pathology. The pathophysiological mechanisms are: hyperphosphorylation of the tau protein and aggregation of amyloid-β. Update studies of the tested therapies target the main pathological mechanisms: accumulation of β amyloid (inhibitors and modulators of β-secretase and γ-secretase and active and passive anti-Aβ immunotherapies), tau protein (inhibition of abnormal

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Chiu, K. C., L. Y. Yu, J. N. Yih та S. J. Chen. "Investigating the structural changes of β-amyloid peptide aggregation using attenuated-total-reflection surface-enhanced Raman spectroscopy". У Biomedical Optics (BiOS) 2007, редактори Tuan Vo-Dinh та Joseph R. Lakowicz. SPIE, 2007. http://dx.doi.org/10.1117/12.701757.

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"818 BGRS/SB-2022 The low-molecular-weight ligands of human serum albumin, promoting its interaction with amyloid β peptide". У Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-475.

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"All-D-enantiomeric peptide designed for Alzheimer´s disease treatment dynamically interacts with amyloidogenic region of membrane-bound amyloid-β peptide precursor". У Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-175.

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"BGRS/SB-2022 779 In search for the peptide/protein ligands of human serum albumin able to affect its interaction with amyloid β peptide". У Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-449.

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Raporty organizacyjne na temat "Β-amyloid structures"

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Wing Hei Cheng, Cecily, Matthew Hai Heng Chung та Joseph Chi Fung Ng. Structural Dynamics of Amyloid-β Aggregation in Alzheimer’s Disease: Computational and Experimental Approaches. Journal of Young Investigators, 2016. http://dx.doi.org/10.22186/jyi.31.6.44-50.

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Zhang, Yu, Chaoliang Sun, Hengxi Xu, et al. Connectivity-Based Subtyping of De Novo Parkinson Disease: Biomarkers, Medication Effects and Longitudinal Progression. Progress in Neurobiology, 2024. http://dx.doi.org/10.60124/j.pneuro.2024.10.04.

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Parkinson's disease (PD) is characterized by divergent clinical symptoms and prognosis, suggesting the presence of distinct subtypes. Identifying these subtypes is crucial for understanding the underlying pathophysiology, predicting disease progression, and developing personalized treatments. In this study, we propose a connectivity-based subtyping approach, which measures each patient's deviation from the reference structural covariance networks established in healthy controls. Using data from the Parkinson's Progression Markers Initiative, we identified two distinct subtypes of de novo PD pa

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