Relevant bibliographies by topics / Tissue folding

Academic literature on the topic 'Tissue folding'

Author: Grafiati
Published: 25 May 2024

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Journal articles on the topic "Tissue folding"

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Zečić, Aleksandra, and Chadanat Noonin. "Whole-mount in situ hybridization: minimizing the folding problem of thin-sheet tissue-like crayfish haematopoietic tissue." Crustaceana 91, no. 1 (2018): 1–15. http://dx.doi.org/10.1163/15685403-00003745.

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Crayfish haematopoietic tissue (HPT) has a thin-sheet-like structure with a thickness of 100-160 μm and a width of approximately 1-2 cm. This structure makes HPT extremely easy to fold after removal from the animal. Therefore, it is difficult to handle the tissue without folding when processing for sectioning and histological study. The degree of tissue folding reflects the size of the tissue sections obtained, how complicated it is to interpret the location of each tissue section, and the accuracy of the interpretation of the location of a specific transcript. To facilitate the interpretation of a specific transcript location in the HPT, we optimized a whole-mount in situ hybridization technique to minimize tissue folding. This optimized protocol effectively reduced the tissue folding. Therefore, the location of a specific transcript in the HPT was easily and accurately defined. This protocol will be useful for whole-mount staining of other tissues with similar structure.
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Inoue, Yasuhiro, Itsuki Tateo, and Taiji Adachi. "Epithelial tissue folding pattern in confined geometry." Biomechanics and Modeling in Mechanobiology 19, no. 3 (November 14, 2019): 815–22. http://dx.doi.org/10.1007/s10237-019-01249-8.

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AbstractThe primordium of the exoskeleton of an insect is epithelial tissue with characteristic patterns of folds. As the insect develops from larva to pupa, the spreading of these folds produces the three-dimensional shape of the exoskeleton of the insect. It is known that the three-dimensional exoskeleton shape has already been encoded in characteristic patterns of folds in the primordium; however, a description of how the epithelial tissue forms with the characteristic patterns of folds remains elusive. The present paper suggests a possible mechanism for the formation of the folding pattern. During the primordium development, because of the epithelial tissue is surrounded by other tissues, cell proliferation proceeds within a confined geometry. To elucidate the mechanics of the folding of the epithelial tissue in the confined geometry, we employ a three-dimensional vertex model that expresses tissue deformations based on cell mechanical behaviors and apply the model to examine the effects of cell divisions and the confined geometry on epithelial folding. Our simulation results suggest that the orientation of the axis of cell division is sufficient to cause different folding patterns in silico and that the restraint of out-of-plane deformation due to the confined geometry determines the interspacing of the folds.
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Hookway, Tracy A. "Engineering Biology by Controlling Tissue Folding." Trends in Biotechnology 36, no. 4 (April 2018): 341–43. http://dx.doi.org/10.1016/j.tibtech.2018.02.003.

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Allen, Simon, Hassan Y. Naim, and Neil J. Bulleid. "Intracellular Folding of Tissue-type Plasminogen Activator." Journal of Biological Chemistry 270, no. 9 (March 3, 1995): 4797–804. http://dx.doi.org/10.1074/jbc.270.9.4797.

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Zartman, Jeremiah J., and Stanislav Y. Shvartsman. "Unit Operations of Tissue Development: Epithelial Folding." Annual Review of Chemical and Biomolecular Engineering 1, no. 1 (June 15, 2010): 231–46. http://dx.doi.org/10.1146/annurev-chembioeng-073009-100919.

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Hiraiwa, Tetsuya, Fu-Lai Wen, Tatsuo Shibata, and Erina Kuranaga. "Mathematical Modeling of Tissue Folding and Asymmetric Tissue Flow during Epithelial Morphogenesis." Symmetry 11, no. 1 (January 19, 2019): 113. http://dx.doi.org/10.3390/sym11010113.

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Recent studies have revealed that intrinsic, individual cell behavior can provide the driving force for deforming a two-dimensional cell sheet to a three-dimensional tissue without the need for external regulatory elements. However, whether intrinsic, individual cell behavior could actually generate the force to induce tissue deformation was unclear, because there was no experimental method with which to verify it in vivo. In such cases, mathematical modeling can be effective for verifying whether a locally generated force can propagate through an entire tissue and induce deformation. Moreover, the mathematical model sometimes provides potential mechanistic insight beyond the information obtained from biological experimental results. Here, we present two examples of modeling tissue morphogenesis driven by cell deformation or cell interaction. In the first example, a mathematical study on tissue-autonomous folding based on a two-dimensional vertex model revealed that active modulations of cell mechanics along the basal–lateral surface, in addition to the apical side, can induce tissue-fold formation. In the second example, by applying a two-dimensional vertex model in an apical plane, a novel mechanism of tissue flow caused by asymmetric cell interactions was discovered, which explained the mechanics behind the collective cellular movement observed during epithelial morphogenesis.
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Chan, Hon Fai, Ruike Zhao, German A. Parada, Hu Meng, Kam W. Leong, Linda G. Griffith, and Xuanhe Zhao. "Folding artificial mucosa with cell-laden hydrogels guided by mechanics models." Proceedings of the National Academy of Sciences 115, no. 29 (July 2, 2018): 7503–8. http://dx.doi.org/10.1073/pnas.1802361115.

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The surfaces of many hollow or tubular tissues/organs in our respiratory, gastrointestinal, and urogenital tracts are covered by mucosa with folded patterns. The patterns are induced by mechanical instability of the mucosa under compression due to constrained growth. Recapitulating this folding process in vitro will facilitate the understanding and engineering of mucosa in various tissues/organs. However, scant attention has been paid to address the challenge of reproducing mucosal folding. Here we mimic the mucosal folding process using a cell-laden hydrogel film attached to a prestretched tough-hydrogel substrate. The cell-laden hydrogel constitutes a human epithelial cell lining on stromal component to recapitulate the physiological feature of a mucosa. Relaxation of the prestretched tough-hydrogel substrate applies compressive strains on the cell-laden hydrogel film, which undergoes mechanical instability and evolves into morphological patterns. We predict the conditions for mucosal folding as well as the morphology of and strain in the folded artificial mucosa using a combination of theory and simulation. The work not only provides a simple method to fold artificial mucosa but also demonstrates a paradigm in tissue engineering via harnessing mechanical instabilities guided by quantitative mechanics models.
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Ko, Clint S., Vardges Tserunyan, and Adam C. Martin. "Microtubules promote intercellular contractile force transmission during tissue folding." Journal of Cell Biology 218, no. 8 (June 21, 2019): 2726–42. http://dx.doi.org/10.1083/jcb.201902011.

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During development, forces transmitted between cells are critical for sculpting epithelial tissues. Actomyosin contractility in the middle of the cell apex (medioapical) can change cell shape (e.g., apical constriction) but can also result in force transmission between cells via attachments to adherens junctions. How actomyosin networks maintain attachments to adherens junctions under tension is poorly understood. Here, we discovered that microtubules promote actomyosin intercellular attachments in epithelia during Drosophila melanogaster mesoderm invagination. First, we used live imaging to show a novel arrangement of the microtubule cytoskeleton during apical constriction: medioapical Patronin (CAMSAP) foci formed by actomyosin contraction organized an apical noncentrosomal microtubule network. Microtubules were required for mesoderm invagination but were not necessary for initiating apical contractility or adherens junction assembly. Instead, microtubules promoted connections between medioapical actomyosin and adherens junctions. These results delineate a role for coordination between actin and microtubule cytoskeletal systems in intercellular force transmission during tissue morphogenesis.
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Codd, S. L., R. K. Lambert, M. R. Alley, and R. J. Pack. "Tensile stiffness of ovine tracheal wall." Journal of Applied Physiology 76, no. 6 (June 1, 1994): 2627–35. http://dx.doi.org/10.1152/jappl.1994.76.6.2627.

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The epithelial folding that occurs during bronchoconstriction requires that the pressure on the muscle side of the folding membrane be greater than that on the lumen side. The pressure required for a given level of folding depends on the elastic properties of the tissue and on the geometry of the folding. To quantify the elastic properties, uniaxial tensile stiffness of the tracheal inner wall of nine sheep was measured in two directions: parallel to the tracheal axis and circumferentially. The tissue showed anisotropic behavior, being approximately three times stiffer longitudinally than circumferentially. Histological examination showed that collagen in the lamina propria was randomly arranged, whereas there were straight elastin fibers aligned with the tracheal axis. This observation could explain the observed elastic anisotropy. Mechanical removal of the epithelium had no effect on tensile stiffness. It was also found that the tissue was under tension in situ. When a strip was excised, its length decreased by > or = 30%. After allowing for the systematic errors inherent in this experiment, the in situ circumferential tensile stiffness is estimated to be > or = 20 kPa. If the equivalent tissue in the bronchioles has the same tensile stiffness as that in the trachea, the forces required to fold the membrane are significant at small transbronchial pressure differences and increase in the presence of membrane thickening such as that seen in asthma.
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Tozluoǧlu, Melda, and Yanlan Mao. "On folding morphogenesis, a mechanical problem." Philosophical Transactions of the Royal Society B: Biological Sciences 375, no. 1809 (August 24, 2020): 20190564. http://dx.doi.org/10.1098/rstb.2019.0564.

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Tissue folding is a fundamental process that sculpts a simple flat epithelium into a complex three-dimensional organ structure. Whether it is the folding of the brain, or the looping of the gut, it has become clear that to generate an invagination or a fold of any form, mechanical asymmetries must exist in the epithelium. These mechanical asymmetries can be generated locally, involving just the invaginating cells and their immediate neighbours, or on a more global tissue-wide scale. Here, we review the different mechanical mechanisms that epithelia have adopted to generate folds, and how the use of precisely defined mathematical models has helped decipher which mechanisms are the key driving forces in different epithelia. This article is part of a discussion meeting issue ‘Contemporary morphogenesis'.
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Dissertations / Theses on the topic "Tissue folding"

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Vasiev, Iskandar. "3D self-folding tissue engineering scaffold origami." Thesis, University of Glasgow, 2015. http://theses.gla.ac.uk/7071/.

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In the field of tissue engineering complex 3D architecture has become increasingly relevant in the pursuit of precisely engineered control over living tissue. It is needed to recreate the heterogeneous and complex arrangements of cells seen in nature, and to be able to influence their proliferation, differentiation and fate. A method for the 3D structuring of cells is therefore desired and is something standard lithographic methods cannot provide - the precision engineered 3D cellular niche. This work transfers traditional 2D lithographic techniques used in MEMS (E-beam lithography, photolithography, soft lithography and nanoimprint lithography) to the construction of 3D as well as complex hierarchical structures compatible with cell culture. To address this, hydrogel bilayers act as biocompatible, flexible and environmentally responsive hinges to fold the 2D structure into a 3D conformation. To achieve this, a rapid method of producing nanopatterns with the potential for large area patterning was developed. These were fluorinated ethylene propylene (FEP) and polydimethylsiloxane (PDMS) replica stamps with 2D and 2.5D hierarchical patterns. They were capable of bending and conforming to uneven and curved surfaces. These were used in a novel combinational lithography approach to construct complex hierarchical structures by photolithography through photomasks with nanopatterned transparent FEP inlays to create unfolded 3D cellular niches by a 2D method. Several different hydrogels were synthesised and patterned by photolithography to be used as bilayer hinges. Actuation mechanisms included thermoresponsive N-isopropylacrylamide (NIPAAm), and anionic acrylic acid (AA) monomers. Successful bilayers were formed using acrylate based photochemistry with poly(ethylene glycol) dimethacrylate (PEGDMA) and pH responsive polyacrylic acid (PAA) in a novel sacrificial layer functionalisation method. These structures would bend and roll due to differential swelling in neutral pH and when acting as a hinge would result in self-folding of photolithographically defined 2D structures into 3D containers. To test the compatibility of this method of manufacture with cell culture hESCs were trialled on the container materials, and showed excellent adhesion on the SU8 structures. More ambitiously to see if they could in the future be used for the directed differentiation of stem-cells, hESCs were cultured on nanopatterned injection moulded polymer substrates with varying nanofeature type. It was found that hESEs had improved adhesion on vitronectin coated nanotopographies even at extremely low vitronectin concentrations, and showed an increased 3D colony structure leading to the enhanced expression of certain lineage markers. It was found that hESC attachment could be mediated by feature height and substrate elasticity. This work has demonstrated as a proof-of-principle, a rapid and simple method of producing nanopatterned 3D self-folding containers, compatible with cell culture which could in the future serve as 3D self-folding nanopatterned cellular niches for tissue engineering.
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Vasquez, Claudia G. (Claudia Gabriela). "Mechanisms of myosin regulation and function during tissue folding." Thesis, Massachusetts Institute of Technology, 2015. http://hdl.handle.net/1721.1/101504.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.
Cataloged from PDF version of thesis. "September 2015."
Includes bibliographical references.
Throughout organismal development, precise three-dimensional organization of tissues is required for proper tissue function. These three-dimensional forms are generated by coordinated cell shape changes that induce global tissue shape changes, such as the transformation of an epithelial sheet into a tube. A model for this transformation occurs early in Drosophila development where approximately 1,000 cells on the ventral side of the embryo constrict their apical sides. Apical constriction drives the formation of a furrow that invaginates, forming a tube, and consequently, a new cell layer in the embryo. Constriction of ventral cells is driven by cycles of assembly and disassembly of actin-myosin networks at the cell apex, called pulses. Pulsatile myosin leads to phases of cellular contraction and cell shape stabilization that result in step-wise apical constriction. While many of the key components of the pathway have been identified, how pulsatile myosin is regulated was previously not well understood. The results presented in this thesis identify mechanisms of regulation of these myosin pulses. First, we demonstrated that cycles of phosphorylation and dephosphorylation of the myosin regulatory light chain are required for myosin pulsing and step-wise apical constriction. Uncoupling myosin from its upstream regulators resulted in loss of pulsatile myosin behavior and continuous, instead of incremental, apical constriction. A consequence of persistent, non-pulsatile myosin is a loss of myosin network integrity as the tissue invaginated. Thus, pulsatile myosin requires tight coordination between its activator and inactivator to generate cycles of myosin assembly, coupled to cellular constriction, and myosin disassembly, associated with cell shape stabilization. Second, we demonstrated that myosin motor activity is required for efficient apical constriction and for effective generation of tissue tension. This work defines essential molecular mechanisms that are required for proper cellular constriction and tissue invagination.
by Claudia G. Vasquez.
Ph. D.
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Nauli, Sehat. "Folding kinetics and redesign of Peptostreptococcal protein L and G /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/9237.

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Van, Leen Eric. "On the morphogenesis of the D. melanogaster pupa : a study on gene patterning and tissue folding." Electronic Thesis or Diss., Sorbonne université, 2020. http://www.theses.fr/2020SORUS387.

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Au cours du développement, la coordination des comportements cellulaires est essentielle à la formation d’organes complexes et fonctionnels. L’analyse de ces processus cellulaire est essentielle pour comprendre comment les tissues se forment au cours du développement. Pour ce faire, il est tout d’abord primordial d’identifier les gènes dont l’expression est corrélée avec chacun de ces processus cellulaires. Avec pour modèle la formation de l’épithélium dorsal (le notum) de la pupe de drosophile, mon travail de thèse a visé à identifier les mécanismes moléculaires qui gouvernent la régulation spatiale de la morphogenèse de l’échelle cellulaire à l’échelle de l’organisme. Dans un premier temps, j’ai mis en œuvre une analyse de transcriptomique spatiale qui m’a permis d’identifier de nouveaux gènes impliqués dans la morphogenèse du notum. Dans un second temps, j’ai développé un microscope confocal rotatif avec l’aide de la plateforme d’imagerie de l’Institut Curie. En appliquant cette nouvelle méthode au cours du développement de la pupe jusqu’au stade adulte, j’ai pu observer la morphogenèse de l’aile et du notum de manière simultanée. J’ai ainsi identifié un nouveau mouvement morphogénétique du notum entre 45-50 hAPF qui semble indépendant de la morphogenèse de l’aile dans le temps et dans l’espace. Enfin j’ai montré que ce mouvement est contrôlée par l’expression de sérine-protéases qui libèrent l’attachement de l’épithélium à la cuticule. Ce travail de thèse représente un apport important à une compréhension fine et intégrée de la régulation de la morphogenèse et de la coordination des dynamiques cellulaires au cours du développement
In order to achieve complex shapes during development, multicellular organisms need to coordinate cellular behaviors to form complex and functional organs. Identifying genes that are expressed in patterns that correlate with cellular processes is therefore primordial. Using the dorsal epithelium (the notum) of drosophila pupa as a model, my thesis aimed at uncovering the molecular mechanisms which control the spatial regulation of morphogenesis at the cell and tissue scale. First, I developed spatial transcriptomics which enabled the identification of new expression patterns involved in notum morphogenesis. Second, I developed, in collaboration with the imaging platform of Institut Curie, Rotating Sample Confocal Microscopy. Using this technique, I was able to simultaneously observe the morphogenesis of the notum, hinge and wing blade. This enabled the discovery of a new morphogenetic movement in the notum between 45-50hAPF. My results suggest that this extensive folding and elongation of the notum is independent of folding in the wing. Furthermore, I demonstrated that the expression of serine proteases regulate the attachment of the tissue to the cuticle which triggers the onset of the folding and determines the final shape of the tissue. Overall, this work increases our understanding of the spatial regulation of morphogenesis and contributes to the knowledge on how the extracellular matrix can regulate tissue shape
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Sukonina, Valentina. "Angiopoietin-like protein 4 : an unfolding chaperone regulating lipoprotein lipase activity." Doctoral thesis, Umeå : Univ, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1343.

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Fu, Josephine K. Y. "Functional characterization of the teleost multiple tissue (tmt) opsin family and their role in light detection." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:39bc18bb-16cb-4549-94cd-5f872daafe7e.

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In addition to a central circadian clock in the suprachiasmatic nucleus (SCN), zebrafish (Danio rerio) have local clock systems in their peripheral tissues. These peripheral tissues express a complement of clock genes that can be synchronized with the 24 h light/dark cycle and thus may be entrained by light. To date, teleost multiple tissue (tmt) opsin identified from Fugu rubripes and Danio rerio is the only opsin that has been proposed as a candidate to mediate this cellular photoentrainment (Moutsaki et al., 2003). Here we report the discovery of a multigene family of tmt opsins found not only in the teleost fishes, but in vertebrates,including amphibians, birds, reptiles, and some mammals. Phylogenetic analysis demonstrated that this gene family consists of three main classes, tmtI, tmtII and tmtIII, with each duplicating further to give two paralogues in the zebrafish genome. Their predicted amino acid sequences contain most of the characteristic features for the function of a photopigment opsin, as well as seven transmembrane segments indicative of a G protein coupled receptor (GPCR) superfamily. Significantly, reverse transcription polymerase chain reaction (RT-PCR) reveals that the tmt opsin genes in zebrafish are both temporally and spatially regulated. To investigate if these tmt photopigments mediate light-activated currents in cells, each opsin was expressed in vitro and the responses characterised by calcium imaging, whole-cell patch clamp electrophysiology, UV-Vis spectrophotometric analysis, and bioluminescence reporter assay. Collectively, these data suggest that some of the opsin photoproteins signal via Gi-type G protein pathway. Interestingly, the spectral analysis obtained shows that most tmt opsins tested are UV-sensitive when reconstituted in vitro with 11-cis and all-trans retinal, indicating an intrinsic bistable dynamics. Using site directed mutagenesis on one of the tmt opsins, tmt10, the potential spectral tuning sites involved in UV detection were tested. As part of this study, tmt opsin cDNAs were isolated from three populations of Mexican tetra (Astyanax mexicanus): surface, Pachon and Steinhardt. This allowed for a direct comparison between the tmt opsins present in the dark adapted species (cavefish) versus those of the light adapted species (zebrafish). It is hoped that the findings from this project will contribute to our understanding of non-visual light detection in fish and the evolution of their non-image forming photoreception.
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Scott, Henry Hepburne. "#alpha#B-crystallin expression, mutagenesis and immunoreactivity." Thesis, University of Reading, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284449.

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Books on the topic "Tissue folding"

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Clarke, Andrew. Water. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780199551668.003.0005.

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Liquid water is essential for life, and a metabolically active cell is ~70% water. The physical properties of liquid water, and their temperature dependence, are dictated to a significant extent by the properties of hydrogen bonds. From an ecological perspective, the important properties of liquid water include its high latent heats of fusion and vapourisation, its high specific heat, the ionisation, low dynamic viscosity and high surface tension. The solubility in water of oxygen, carbon dioxide and the calcium carbonate used to build skeletons in many invertebrates groups all increase with decreasing temperature. The hydrophobic interaction is important in the formation of cellular membranes and the folding of proteins; its strength increases with temperature, which may be a factor in the cold-denaturation of cellular macromolecules. The cell is extremely crowded with macromolecules. Coupled with the highly structured water close to membranes or protein surfaces and the hydration shells around ions, this means that the behaviour of water in cells is different from that of bulk water. The thermal behaviour of isolated cellular components studied in dilute aqueous buffers many not reflect accurately their behaviour in the intact cell or tissue.
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Book chapters on the topic "Tissue folding"

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Israelowitz, Meir, Birgit Weyand, Syed W. H. Rizvi, Christoph Gille, and Herbert P. von Schroeder. "Protein Modelling and Surface Folding by Limiting the Degrees of Freedom." In Computational Modeling in Tissue Engineering, 19–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/8415_2012_141.

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Spiegel, Holger, Stefan Schillberg, and Greta Nölke. "Production of Recombinant Proteins by Agrobacterium-Mediated Transient Expression." In Recombinant Proteins in Plants, 89–102. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2241-4_6.

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AbstractThe agroinfiltration of plant tissue is a robust method that allows the rapid and transient expression of recombinant proteins. Using wild-type plants as biomass, agroinfiltration exploits the ability of plants to synthesize even complex multimeric proteins that require oxidative folding and/or post-translational modifications, while avoiding the expensive and time-consuming creation of stably transformed plant lines. Here we describe a generic method for the transient expression of recombinant proteins in Nicotiana benthamiana at the small to medium laboratory scale, including appropriate binary vectors, the design and cloning of expression constructs, the transformation, selection, and cultivation of recombinant Agrobacterium tumefaciens, the infiltration of plants using a syringe or vacuum device, and finally the extraction of recombinant proteins from plant tissues.
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Bach, Anna Sofie. "The Affective Temporalities of Ovarian Tissue Freezing: Hopes, Fears, and the Folding of Embodied Time in Medical Fertility Preservation." In Reproductive Citizenship, 51–73. Singapore: Springer Nature Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-9451-6_3.

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Mehner, Philipp J., Tian Liu, Majid Bigdeli Karimi, Alyssa Brodeur, Juan Paniagua, Stephanie Giles, Patricia Richard, et al. "Toward engineering biological tissues by directed assembly and origami folding." In Origami⁶, 545–55. Providence, Rhode Island: American Mathematical Society, 2015. http://dx.doi.org/10.1090/mbk/095.2/17.

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Balusek, Curtis, Hyea Hwang, Anthony Hazel, Karl Lundquist, Anna Pavlova, and James C. Gumbart. "Diverse Protein-Folding Pathways and Functions of β-Hairpins and β-Sheets." In Quantitative Models for Microscopic to Macroscopic Biological Macromolecules and Tissues, 1–20. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-73975-5_1.

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Baum, Jean, and Barbara Brodsky. "Case study 2: Folding of the collagen triple-helix and its naturally occurring mutants." In Mechanisms of Protein Folding, 330–51. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637898.003.0012.

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Abstract Collagen comprises a family of extracellular matrix molecules responsible for the integrity and mechanical properties of connective tissue, including bone, tendon, skin, cartilage, and cornea (1-3). At least 19 distinct human collagens are known, the most abundant being found in fibrils with an axial 67 nm periodicity. In addition, collagen like domains are crucial to ligand binding and self-association in host-defence proteins such as Clq, mannose-binding protein, and the macrophage scavenger receptor (4, 5). Mutations in collagen are the cause of various connective tissue diseases, including osteogenesis imperfecta and hereditary aortic aneurysm (6-8). Altered folding of the collagen molecule and of fibril assembly have been implicated in the aetiology of these diseases, putting collagen in the context of protein folding and aggregation diseases (9-11).
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Covizzi, Ian Vilas Boas, Thatiana Scalon, João Renato Villas Bôas, Isadora Cucolo Oliveira, Tárik Abdalla dos Santos, Alba Regina de Abreu Lima, and Uderlei Doniseti Silveira Covizzi. "The incorrect folding of proteins and their involvement with pathological processes." In INNOVATION IN HEALTH RESEARCH ADVANCING THE BOUNDARIES OF KNOWLEDGE. Seven Editora, 2023. http://dx.doi.org/10.56238/innovhealthknow-033.

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During synthesis and the period in which they exert their cellular function, there is monitoring so that the proteins maintain a certain three-dimensional folding, where their energy levels are stabilized and their biological activity is maintained. Changes in cellular conditions can modify this structure, favoring its aggregation into insoluble complexes, called amyloidosis, depositing in the intra or extracellular environment. Recent data indicate that several types of proteins are involved in some type of amyloidosis, presenting a systemic character, or depositing in a specific tissue. The classification used for these cases considers the amyloid source, the pathology, and the organ affected. Protein fragments derived from immunoglobulin light and heavy chains are responsible for primary systemic amyloidosis. In secondary amyloidosis, there is the participation of circulating plasma protein, acting in inflammatory processes in different organs. Dialysis-related amyloidosis, on the other hand, is characterized by damage to bone tissues and joints in patients with chronic kidney disease. Most studies related to localized amyloidosis involve neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. These heterogeneous pathologies associated with the incorrect folding of proteins are subject to genetic influence, which is increasingly evidenced, despite their multifactorial character. Deficiencies in the cellular proteostasis processes, i.e., in the surveillance that confers the quality control of these proteins, leading to their recovery or sending them for recycling, tend to increase with age. For this reason, most of the time these amyloidoses are related to the individual's aging processes.
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Ahsan, Haseeb, Salman Ul Islam, Muhammad Bilal Ahmed, Adeeb Shehzad, Mazhar Ul Islam, Young Sup Lee, and Jong Kyung Sonn. "Principles of Supra Molecular Self Assembly and Use of Fiber mesh Scaffolds in the Fabrication of Biomaterials." In Biomaterial Fabrication Techniques, 218–42. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815050479122010012.

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Tissue engineering techniques aim to create a natural tissue architecture using biomaterials that have all the histological and physiological properties of human cells to replace or regenerate damaged tissue or organs. Nanotechnology is on the rise and expanding to all fields of science, including engineering, medicine, diagnostics and therapeutics. Nanostructures (biomaterials) specifically designed to mimic the physiological signals of the cellular/extracellular environment may prove to be indispensable tools in regenerative medicine and tissue engineering. In this chapter, we have discussed biomaterial design from two different perspectives. Supramolecular self-assembly is the bottom-up approach to biomaterials design that takes advantage of all the forces and interactions present in biomolecules and are responsible for their functional organization. This approach has the potential for one of the greatest breakthroughs in tissue engineering technology because it mimics the natural, complex process of coiling and folding biomolecules. In contrast, a fiber mesh scaffold is a top.down approach in which cells are seeded. The scaffolds form the cellular scaffold while the cells produce and release the desired chemical messengers to support the regeneration process. Therefore, both techniques, if efficiently explored, may lead to the development of ideal biomaterials produced by self-assembly or by the fabrication of optimal scaffolds with long shelf life and minimal adverse reactions.
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Fisch, Adam. "Surfaces of the Brain." In Neuroanatomy : Draw It to Know It, 272–93. Oxford University PressNew York, NY, 2009. http://dx.doi.org/10.1093/oso/9780195369946.003.0025.

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Abstract In This Chapter, we will draw the lateral, medial, and under surfaces of the brain,as well as the Sylvian fissure, and insular cortex. In addition, we will draw highlights of the Brodmann functional maps and Penfield’s somatotopic homunculus. On each cerebral surface, we will divide the brain into its lobes and then divide the lobes into their gyri and sulci. Close your fist, now, to represent the topography of the brain. The fingers represent the gyri and the grooves between them are the sulci. What advantage is there to this contour? It increases the brain surface’s area: approximately two-thirds of the brain’s surface lies within these sulcal valleys. The cerebellum, which was drawn in the preceding chapter, is a good example of how important tissue folding can be; it is condensed into a space much smaller than the remainder of the brain but its convolutions give it a larger surface area.
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Hawkins, Philip N. "Amyloidosis." In Oxford Textbook of Rheumatology, 1397–409. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0163.

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Amyloidosis is a disorder of protein folding in which normally soluble proteins are deposited in the interstitial space as insoluble and remarkably stable fibrils that progressively disrupt tissue structure and function of organs throughout the body. Protein misfolding and aggregation have increasingly been recognized in the pathogenesis of various other diseases, but amyloidosis—the disease directly caused by extracellular amyloid deposition—is a precise term with critical implications for patients with a specific group of life-threatening disorders. Amyloidosis may be acquired or hereditary and the pattern of organ involvement varies within and between types, though clinical phenotypes overlap greatly. Virtually any tissue other than the brain may be directly involved. Although histology remains the diagnostic gold standard, developments in scintigraphy and MRI technology often produce pathognomonic findings. Systemic amyloidosis is usually fatal, but the prognosis has improved as the result of increasingly effective treatments for many of the conditions that underlie it, notably the use of biologic anti-inflammatory agents in patients with AA amyloidosis and new immunomodulatory agents in patients with AL type. Better supportive care, including dialysis and solid organ transplantation, have also influenced the prognosis favourably. A range of specific novel therapies are currently in clinical development, including RNA inhibitors that suppress production of amyloid precursor proteins, drugs that promote their normal soluble conformation in the plasma, and immunotherapy approaches that directly target the amyloid deposits.
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Conference papers on the topic "Tissue folding"

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Shin, Jae-Won, and Jenny Sabin. "Tissue Architecture: Programmable Folding in Digital Responsive Skins." In ACADIA 2013: Adaptive Architecture. ACADIA, 2013. http://dx.doi.org/10.52842/conf.acadia.2013.443.

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Matsushima, Yuto, Dina Mikimoto, Minghao Nie, and Shoji Takeuchi. "Origami-Inspired Culture Device for Mechanical Folding Stimulation of Skin Tissue Equivalent." In 2024 IEEE 37th International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2024. http://dx.doi.org/10.1109/mems58180.2024.10439332.

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Joshi, Sagar D., and Lance A. Davidson. "Remote Control of Apical Epithelial Sheet Contraction by Laser Ablation or Nano-Perfusion: Acute Stimulus Triggers Rapid Remodeling of F-Actin Network in Apical Cortex." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-204904.

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Apical contraction is the major tissue movement during remodeling of epithelial sheets in development. During apical contraction, groups of cells narrow their apices to form bottle-shaped structures, driving events such as sea-urchin gastrulation [1], Drosophila ventral-furrow formation, vertebrate neurulation and wound healing [2]. Tissue-folding events such as invagination, ingression and involution involve this tissue movement in which cells actively build “rifts” and “tubes”. Epithelial cells integrate genetic information, mechanical signals, and biochemical gradients to build these structures, but how they do so is unknown [3]. Theoretical models [4] provide some mechanical explanation for these events. Here we experimentally induce apical contractions controllably for the first time in amphibian embryos. Two independent methods, namely, laser ablation of cell membranes and nano-perfusion with cell lysate induce cell contraction in tissue isolates and in whole embryos. We demonstrate a biochemical pathway that stimulates rapid actin-reorganization/ polymerization accompanied by increases in α-actinin. The F-actin remodeling correlates with increased levels of Ca++. Cell contraction begins within few seconds of laser ablation or nano-perfusion, peaks within a minute and is followed by a similar relaxation. Acute control of epithelial mechanics will allow us to better understand how molecular genetic processes drive shape change in tissues and will help future bioengineers build complex 3D epithelial organs.
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Wheeler, Charles M., and Martin L. Culpepper. "Soft Origami: Classification, Constraint, and Actuation of Highly Compliant Origami Structures." In ASME 2015 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/detc2015-46877.

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Herein we discuss the folding of highly compliant origami structures — “Soft Origami.” There are benefits to be had in folding compliant sheets (which cannot self-guide their motion) rather than conventional rigid origami. Example applications include scaffolds for artificial tissue generation and foldable substrates for flexible electronic assemblies. Highly compliant origami has not been contemplated by existing theory, which treats origami structures largely as rigid or semi-rigid mechanisms with compliant hinges — “Mechanism-Reliant Origami.” We present a quantitative metric — the Origami Compliance Metric — that aids in identifying proper modeling of a homogeneous origami structure based upon the compliance regime it falls into (Soft, Hybrid, or Mechanism-Reliant). We discuss the unique properties, applications, and design drivers for practical implementation of Soft Origami. We detail a theory of proper constraint by which an ideal soft structure’s number of degrees of freedom may be approximated as 3n, where n is the number of vertices of the fold pattern. Finally, we introduce a concept for a scalable process in which a few actuators and stretching membranes may be used to simultaneously fold many origami sub-structures that share common degrees of freedom.
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Higgins, Deborah L., and William E. Holmes. "CHARACTERIZATION OF RECOMBINANT HUMAN TISSUE-TYPE PLASMINOGEN ACTIVATOR MISSING THE FINGER DOMAIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643842.

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Site-specific mutagenesis was used to produce a mutant form of tissue-type plasminogen activator (t-PA) which was missing the first 44 amino acids. This domain has sequence homology with the type 1 regions in proteins such as fibronectin and is commonly called the finger domain. The mutant protein (des 1-44 t-PA) was expressed in Chinese Hampster Ovary cells, and was purified using chromatography on Zn-chelate sepharose and lysine-sepharose. Sequence analysis indicated that the resulting protein was homogeneous and started at amino acid 45 in the sequence of the normal protein. The two-chain forms of both des 1-44 t-PA and normal sequence t-PA exhibited similar kinetic constants with a small synthetic substrate (H-D-Isoleucyl-L- prolyl-L-arginyl-p-nitroani 1 ide). The ability of des 1-44 t-PA to activate plasminogen was decreased to 70% of the rate of normal t-PA. The rate of plasminogen activation by normal t-PA was stimulated 51-fold in the presence of fibrin, whereas with des 1-44 t-PA it was stimulated only 40-fold. Although des 1-44 t-PA bound to lysine-agarose, little (if any) binding was observed to either intact or degraded fibrin indicating that fibrin stimulation is due in part to the ability of t-PA to recognize plasminogen bound to fibrin as a preferable substrate. The mutant t-PA was capable of forming complexes in vitro with all of the inhibitors in blood which react with normal sequence t-PA. The rate of reaction with α2-macroglobulin, however, was slower with des 1-44 t-PA than with normal sequence t-PA. The similar resistance of des 1-44 t-PA and normal sequence t-PA to proteolysis and the ability to react with a battery of monoclonal antibodies suggests that the deletion did not cause perturbed folding, but rather that alterations in function of des 1-44 t-PA were due to the lack of the finger domain.
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Browe, Daniel P., Carrie A. Rainis, Patrick J. McMahon, and Richard E. Debski. "The Effect of Anterior Dislocation on the Mechanical Properties of the Inferior Glenohumeral Ligament." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80099.

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The glenohumeral joint is the most frequently dislocated major joint in the body with about 2% of the population dislocating their shoulders between the ages of 18 and 70 [1]. Instability due to permanent deformation of the glenohumeral capsule is commonly associated with dislocation [2]. Current surgical repair techniques for shoulder dislocations typically consist of plication of the glenohumeral capsule, or folding the tissue over on itself, to reduce redundancy in the capsule and restore stability to the shoulder. Up to 25% of patients who undergo surgery for a shoulder dislocation still experience pain, instability, and recurrent dislocation after surgery [3]. It is hypothesized that the mechanical properties of the glenohumeral capsule change in response to dislocation. In addition, the magnitude and location of these changes may have implications for the ideal location and extent of plication. Therefore, the objective of this study was to quantify the mechanical properties of the axillary pouch of the glenohumeral capsule in tension and shear after anterior dislocation.
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Kaufman, Randal J., David G. Bole, and Andrew J. Dorner. "THE INFLUENCE OF N-LINKED GLYCOSYLATION AND BINDING PROTEIN (BiP) ASSOCIATION IN THE SECRETION EFFICIENCY OF COMPLEX GLYCOPROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644016.

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We have studied the role of Binding Protein (BiP) or glucose regulated protein, GRP 78) in the processing and secretion of factor VIII (fVIII), von Willebrand factor (vWF), and tissue plasminogen activator(tPA) expressed in Chinese hamster ovary cell lines.fVIII is a 300 kDa protein which has a heavily glycosylated internal domain containing 20 clustered potential N-linked glycosylation sites.A significant proportion of the expressed fVIII is bound to BiP in the endoplasmic reticulum (ER) in a stable complex andnever secreted. Deletion of the heavily glycosylatedregion results in a lesser degree of association with BiP and increased secretion. Tunicamycin treatmentof cells producing the deleted form of fVIII resultsin stable association of the unglycosylated fVIII with BiP and inhibition of efficient secretion. vWF contains 17 potential N-linked glycosylation sites which are scattered throughout the molecule. vWF is transiently associated with BiP in the ER, demonstrating that CHO cells are competent to saecrete a complex glycoprotein. tPA, which contains 3 utilized N-linked glycosylation sites, exhibits low level association with BiP and is efficiently secreted. Disruptionof normal N-linked glycosylation of tPA, by site directed mutagenesis of the 3 Asn residues to Gin residues or by tunicamycin treatment of the tPA expressing CHO cells, results in reduced levels of secretion and increased association with BiP. This effect is enhanced by high levels of expression. The findings suggest that occupancy of glycosylation sites may effect protein folding and alter secretion efficiency by influencing the extent and stability of association with BiP.
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Mehraban, Arash, Jed Brown, Valeria Barra, Henry Tufo, Jeremy Thompson, and Richard Regueiro. "Efficient Residual and Matrix-Free Jacobian Evaluation for Three-Dimensional Tri-Quadratic Hexahedral Finite Elements With Nearly-Incompressible Neo-Hookean Hyperelasticity Applied to Soft Materials on Unstructured Meshes in Parallel, With PETSc and libCEED." In ASME 2020 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2020. http://dx.doi.org/10.1115/imece2020-24522.

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Abstract Soft materials such as rubber, elastomers, and soft biological tissues mechanically deform at large strain isochorically for all time, or during their initial transient (when a pore fluid, typically incompressible such as water, does not have time to flow out of the deforming polymer or soft tissue porous skeleton). Simulating these large isochoric deformations computationally, such as with the Finite Element Method (FEM), requires higher order (typically quadratic) interpolation functions and/or enhancements through hybrid/mixed methods to maintain stability. Lower order (linear) finite elements with hybrid/mixed formulation may not perform stably for all mechanical loading scenarios involving large isochoric deformations, whereas quadratic finite elements with or without hybrid/mixed formulation typically perform stably, especially when large bending or folding deformations are being simulated. For topology-optimization design of soft robotics, for instance, the FEM solid mechanics solver must run efficiently and stably. Stability is ensured by the higher order finite element formulation (with possible enhancement), but efficiency for higher order FEM remains a challenge. Thus, this paper addresses efficiency from the perspective of computer science algorithms and programming. The proposed efficient algorithm utilizes the Portable, Extensible Toolkit for Scientific Computation (PETSc), along with the libCEED library for efficient compiler optimized tensor-product-basis computation to demonstrate an efficient nonlinear solution algorithm. For preconditioning, a scalable p-multigrid method is presented whereby a hierarchy of levels is constructed. In contrast to classical geometric multigrid, also known as h-multigrid, each level in p-multigrid is related to a different approximation polynomial order, p, instead of the element size, h. A Chebyshev polynomial smoother is used on each multigrid level. Algebraic MultiGrid (AMG) is then applied to the assembled Q1 (linear) coarse mesh on the nodes of the quadratic Q2 (quadratic) mesh. This allows low storage that can be efficiently used to accelerate the convergence to solution. For a Neo-Hookean hyperelastic problem, we examine a residual and matrix-free Jacobian formulation of a tri-quadratic hexahedral finite element with enhancement. Efficiency estimates on AVX-2 architecture based on CPU time are provided as a comparison to similar simulation (and mesh) of isochoric large deformation hyperelasticity as applied to soft materials conducted with the commercially-available FEM software program ABAQUS. The particular problem in consideration is the simulation of an assistive device in the form of finger-bending in 3D.
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Liu, Yang, Jianquan Xu, and Hongqiang Ma. "Visualization of disrupted chromatin folding at nanoscale in early carcinogenesis via super-resolution microscopy." In Imaging, Manipulation, and Analysis of Biomolecules, Cells, and Tissues XIX, edited by James F. Leary, Attila Tarnok, and Irene Georgakoudi. SPIE, 2021. http://dx.doi.org/10.1117/12.2579259.

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Abakumets, 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.

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Violation of protein folding leads to the development of a number of systemic and neurodegenerative diseases-proteinopathy. In these pathologies, proteins acquire an incorrect conformation that differs from the native one, become functionally inactive, toxic, and prone to aggregation and deposition in various organs and tissues. There is a widespread hypothesis that the primary cytotoxic agents in the development of proteinopathies are protein oligomers that are prone to aggregation. These diseases include Parkinson’s disease, Creutzfeldt-Jakob disease, type 2 diabetes, and many others.
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