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Letteratura scientifica selezionata sul tema "Fibrils"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 26 luglio 2025

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Articoli di riviste sul tema "Fibrils"

Hagg, Rupert, Peter Bruckner, and Erik Hedbom. "Cartilage Fibrils of Mammals are Biochemically Heterogeneous: Differential Distribution of Decorin and Collagen IX." Journal of Cell Biology 142, no. 1 (1998): 285–94. http://dx.doi.org/10.1083/jcb.142.1.285.

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Cartilage fibrils contain collagen II as the major constituent, but the presence of additional components, minor collagens, and noncollagenous glycoproteins is thought to be crucial for modulating several fibril properties. We have examined the distribution of two fibril constituents—decorin and collagen IX—in samples of fibril fragments obtained after bovine cartilage homogenization. Decorin was preferentially associated with a population of thicker fibril fragments from adult articular cartilage, but was not present on the thinnest fibrils. The binding was specific for the gap regions of the

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Karunarathne, Kanchana, Nabila Bushra, Olivia Williams, et al. "Self-Assembly of Amyloid Fibrils Into 3D Gel Clusters Versus 2D Sheets." Biomolecules 13, no. 2 (2023): 230. http://dx.doi.org/10.3390/biom13020230.

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The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases. Fibril plaques are predominately composed of amyloid fibrils, characterized by their underlying cross beta-sheet architecture. Research into the mechanisms of amyloid formation has mostly focused on characterizing and modeling the growth of individual fibrils and associated oligomers from their monomeric precursors. Much less is known about the mechanisms causing individual fibrils to assemble into ordered fibrillar suprastructures. Elucidat

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Murvai, Ünige, Judit Somkuti, László Smeller, Botond Penke та Miklós SZ Kellermayer. "Structural and nanomechanical comparison of epitaxially and solution-grown amyloid β25-35 fibrils." Biochim Biophys Acta. 1854, № 5 (2015): 327–32. https://doi.org/10.1016/j.bbapap.2015.01.003.

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Aβ25-35, the fibril-forming, biologically active toxic fragment of the full-length amyloid β-peptide also forms fibrils on mica by an epitaxial assembly mechanism. Here we investigated, by using atomic force microscopy, nanomechanical manipulation and FTIR spectroscopy, whether the epitaxially grown fibrils display structural and mechanical features similar to the ones evolving under equilibrium conditions in bulk solution. Unlike epitaxially grown fibrils, solution-grown fibrils displayed a heterogeneous morphology and an apparently helical structure. While fibril assembly in soluti

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Liu, Yehe, Nelly Andarawis-Puri, and Steven J. Eppell. "Method to extract minimally damaged collagen fibrils from tendon." Journal of Biological Methods 3, no. 4 (2016): e54. http://dx.doi.org/10.14440/jbm.2016.121.

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A new method is presented to extract collagen fibrils from mammalian tendon tissue. Mammalian tendons are treated with a trypsin-based extraction medium and gently separated with tweezers in an aqueous solution. Collagen fibrils released in the solution are imaged using both dark-field light microscopy and scanning electron microscopy. The method successfully extracts isolated fibrils from rat tail and patellar tendons. To examine whether the method is likely to damage fibrils during extraction, sea cucumber dermis fibril lengths are compared against those obtained using only distilled water.

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Milton, Nathaniel G. N., and J. Robin Harris. "Human Islet Amyloid Polypeptide Fibril Binding to Catalase: A Transmission Electron Microscopy and Microplate Study." Scientific World JOURNAL 10 (2010): 879–93. http://dx.doi.org/10.1100/tsw.2010.73.

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The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrilsin vitroandin vivo. Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-β (Aβ) and prion protein (PrP) fibrils. Previous studies have shown that catalase binds to Aβ fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. This study presents a transmission electron microscopy (TEM)—based analysis of fibril formation and the binding of human erythrocyte catalas

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Carapeto, Ana P., Carlos Marcuello, Patrícia F. N. Faísca, and Mário S. Rodrigues. "Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis." Biomolecules 14, no. 9 (2024): 1091. http://dx.doi.org/10.3390/biom14091091.

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Atomic force microscopy (AFM) imaging enables the visualization of protein molecules with high resolution, providing insights into their shape, size, and surface topography. Here, we use AFM to study the aggregation process of protein S100A9 in physiological conditions, in the presence of calcium at a molar ratio 4Ca2+:S100A9. We find that S100A9 readily assembles into a worm-like fibril, with a period dimension along the fibril axis of 11.5 nm. The fibril’s chain length extends up to 136 periods after an incubation time of 144 h. At room temperature, the fibril’s bending stiffness was found t

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Pradhan, Tejaswini, Karthikeyan Annamalai, Riddhiman Sarkar та ін. "Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability". Journal of Biological Chemistry 295, № 52 (2020): 18474–84. http://dx.doi.org/10.1074/jbc.ra120.016006.

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Systemic antibody light chains (AL) amyloidosis is characterized by deposition of amyloid fibrils derived from a particular antibody light chain. Cardiac involvement is a major risk factor for mortality. Using MAS solid-state NMR, we studied the fibril structure of a recombinant light chain fragment corresponding to the fibril protein from patient FOR005, together with fibrils formed by protein sequence variants that are derived from the closest germline (GL) sequence. Both analyzed fibril structures were seeded with ex-vivo amyloid fibrils purified from the explanted heart of this patient. We

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Winklbauer, R., and C. Stoltz. "Fibronectin fibril growth in the extracellular matrix of the Xenopus embryo." Journal of Cell Science 108, no. 4 (1995): 1575–86. http://dx.doi.org/10.1242/jcs.108.4.1575.

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We show that the mechanism of fibronectin fibril formation on the blastocoel roof of the Xenopus embryo is comparable to that in other systems. Fibril assembly is inhibited by RGD peptide, by an amino-terminal fragment of fibronectin, and by cytochalasin B. When added exogenously, intact fibronectin, but not a 110 kDa cell binding fragment of fibronectin, is incorporated into fibrils. Thus, the blastocoel roof of Xenopus represents a valid model system for the study of fibronectin fibril formation in situ. Moreover, we show that fibril formation can be induced experimentally in this system. Ex

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KADLER, Karl E., David F. HOLMES, John A. TROTTER, and John A. CHAPMAN. "Collagen fibril formation." Biochemical Journal 316, no. 1 (1996): 1–11. http://dx.doi.org/10.1042/bj3160001.

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Collagen is most abundant in animal tissues as very long fibrils with a characteristic axial periodic structure. The fibrils provide the major biomechanical scaffold for cell attachment and anchorage of macromolecules, allowing the shape and form of tissues to be defined and maintained. How the fibrils are formed from their monomeric precursors is the primary concern of this review. Collagen fibril formation is basically a self-assembly process (i.e. one which is to a large extent determined by the intrinsic properties of the collagen molecules themselves) but it is also sensitive to cell-medi

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Nakata, Yui, Yuuto Kitazaki, Hitomi Kanaoka, et al. "Formation of Fibrils by the Periplasmic Molecular Chaperone HdeB from Escherichia coli." International Journal of Molecular Sciences 23, no. 21 (2022): 13243. http://dx.doi.org/10.3390/ijms232113243.

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The molecular chaperones HdeA and HdeB of the Escherichia coli (E. coli) periplasm protect client proteins from acid denaturation through a unique mechanism that utilizes their acid denatured states to bind clients. We previously demonstrated that the active, acid-denatured form of HdeA is also prone to forming inactive, amyloid fibril-like aggregates in a pH-dependent, reversible manner. In this study, we report that HdeB also displays a similar tendency to form fibrils at low pH. HdeB fibrils were observed at pH < 3 in the presence of NaCl. Similar to HdeA, HdeB fibrils could be resolubil

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Tesi sul tema "Fibrils"

Hernandez, Zurine. "Conditions required for spinning continuous fibres from cellulose nano-fibrils." Thesis, Edinburgh Napier University, 2012. http://researchrepository.napier.ac.uk/Output/5286.

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The thesis describes a programme of work to develop a novel cellulose based fibre. The most important innovative step in this work lies in the manufacture of the fibre from a chiral nematic suspension of plant based cellulose nano-fibrils. In the course of the project a number of key steps have been addressed in the development process. These included: • Developing a method for extraction of nano-fibrils from wood and cotton based pulp and filter paper; • Development of concentrated chiral nematic suspensions of the nano-fibrils suitable for extrusion (spinning); • Spinning a continuous fibre

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Rao, Shiva Priya. "Amyloid Fibrils in Bionanomaterials." Thesis, University of Canterbury. Biological Sciences, 2008. http://hdl.handle.net/10092/4415.

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Amyloid fibrils are a type of protein nanofibres that form when a normally soluble protein aggregates in a regular fashion via self-association. Their organised and repetitive β-sheet structure is thought to be a generic property of all proteins, depending on the environmental conditions. The nanometre size and high stability of these protein nanofibres are attractive features to exploit in bionanomaterials. This thesis aimed to manipulate insulin amyloid fibrils, as a model protein nanofibre system, through investigating the effect of chemical modification on insulin fibril formation in het

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Krebs, Mark R. H. "The chemical mystery of amyloid fibrils : hen lysozyme fibrils, seeding and cross-seeding." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249542.

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Smith, Jeffrey F. "Biophysical properties of amyloid fibrils." Thesis, University of Cambridge, 2006. https://www.repository.cam.ac.uk/handle/1810/251999.

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Hellewell, Andrew Leslie. "The cytoxocity of amyloid fibrils." Thesis, University of Leeds, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.581878.

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Amyloid assemblies consist of an organised cross ~-sheet structure and can be formed by many proteins or peptides regardless of peptide sequence. Amyloid has been utilised by many species for a variety of functions, however, inappropriate amyloid formation is associated with a spectrum of devastating amyloid diseases. The nature of the primary cytotoxic species in amyloid disease is widely debated, with the consensus favouring pre-fibrillar, oligomeric entities over mature end-stage fibrils, despite an increasing body of evidence that suggest at least some fibrils may be associated with cytoto

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Gras, Sally Louise. "Functionalised amyloid fibrils for bionanotechnology." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.614046.

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Povilonienė, Simona. "Investigation of amyloid fibrils forming proteins." Doctoral thesis, Lithuanian Academic Libraries Network (LABT), 2011. http://vddb.laba.lt/obj/LT-eLABa-0001:E.02~2011~D_20110607_092528-21563.

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Self-assembly of biomolecules into beta-sheet structures can be applied in the creation of nano-materials with novel electrical, optical, catalytical, or/and mechanical characteristics. This work was directed towards the construction of nano-derivatives based on amyloid fibrils forming proteins (Abeta40 peptide, a-Synuclein (a-Syn), equine lysozyme (EL)). Such nanostructures can be used to produce nanoscale functional systems. Herein, different mutant and hybrid proteins, which were able to form fibrillar structures, were constructed and the properties of fibrils were investigated. Designed cy

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Potter, Richard J. "Scrapie associated fibrils and polymeric PrP." Thesis, University of Leicester, 1998. http://hdl.handle.net/2381/29628.

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The conversion of PrPC, the normal form of the prion protein, to PrPSc, the protease-resistant disease specific form, is central to the pathogenesis of the transmissible spongiform encephalopathies. The mechanism underlying this conformational change remains elusive but the demonstration that PrPSc can infer protease-resistance to PrPc in-vitro in the presence of guanidine hydrochloride using a cell-free system offers a useful approach to investigating this process. The limitations of such systems however are that significant efficiencies of conversion are only observed in the presence of an e

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Rogers, Salman Samson. "Some physical properties of amyloid fibrils." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613906.

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剛貴, 田中, and Goki Tanaka. "Structural polymorphism of alpha-synuclein fibrils." Thesis, https://doors.doshisha.ac.jp/opac/opac_link/bibid/BB13115616/?lang=0, 2019. https://doors.doshisha.ac.jp/opac/opac_link/bibid/BB13115616/?lang=0.

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Più fonti

Libri sul tema "Fibrils"

Otzen, Daniel Erik, ed. Amyloid Fibrils and Prefibrillar Aggregates. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527654185.

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IARC Working Group on the Evaluation of Carcinogenic Risks to Humans. Silica, some silicates, coal dust and para-Aramid fibrils. IARC, 1997.

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Bock, Gregory R., and Jamie A. Goode, eds. Ciba Foundation Symposium 199 - The Nature and Origin of Amyloid Fibrils. John Wiley & Sons, Ltd., 1996. http://dx.doi.org/10.1002/9780470514924.

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Delmonte, John. Technology of carbon and graphite fiber composites. R.E. Krieger Pub. Co., 1987.

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Sidney, Mindess, ed. Fibre reinforced cementitious composites. Elsevier Applied Science, 1990.

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Sidney, Mindess, ed. Fibre reinforced cementitious composites. 2nd ed. Taylor & Francis, 2007.

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Calvin, Woodings, and Textile Institute (Manchester England), eds. Regenerated cellulose fibres. CRC Press, 2001.

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M, Gammon Luther, ed. Optical microscopy of fiber reinforced composites. ASM International, 2010.

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International Conference on Woodfiber-Plastic Composites (8th 2005 Madison, Wis.). Eighth International Conference on Woodfiber-Plastic Composites (and other natural fibers): May 23-25, 2005, Monona Terrace Community & Convention Center, Madison, Wisconsin, USA. Forest Products Society, 2005.

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Piggott, Michael R. Load bearing fibre composites. 2nd ed. MERP Enhanced Composites, 2001.

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Capitoli di libri sul tema "Fibrils"

Gooch, Jan W. "Fibrils." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_4881.

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Gras, Sally L., and Dennis Claessen. "Functional Amyloid Fibrils." In Natural Products Analysis. John Wiley & Sons, Inc, 2014. http://dx.doi.org/10.1002/9781118876015.ch16.

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Skeby, Katrine Kirkeby. "Amyloid and Amyloid Fibrils." In Computational Modelling of the Human Islet Amyloid Polypeptide. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20040-8_1.

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Galloway, John. "Structure of Collagen Fibrils." In Biology of Invertebrate and Lower Vertebrate Collagens. Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7636-1_6.

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Siddiqi, Mohammad Khursheed, Nabeela Majid, Sadia Malik, Parvez Alam, and Rizwan Hasan Khan. "Amyloid Oligomers, Protofibrils and Fibrils." In Subcellular Biochemistry. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-28151-9_16.

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Almendingen, M., P. V. Syversen, K. Sletten, and G. Husby. "Compositional Analyses of Amyloid Fibrils." In Amyloid and Amyloidosis 1990. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_137.

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Streeter, I., and N. H. Leeuw. "Atomistic Simulations of Collagen Fibrils." In IFMBE Proceedings. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-19044-5_11.

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Dobson, Christopher M. "The Amyloid Phenomenon and Its Significance." In Amyloid Fibrils and Prefibrillar Aggregates. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527654185.ch1.

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Cohen, Samuel I. A., Michele Vendruscolo, Christopher M. Dobson, and Tuomas P. J. Knowles. "The Kinetics and Mechanisms of Amyloid Formation." In Amyloid Fibrils and Prefibrillar Aggregates. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527654185.ch10.

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Hammarström, Per, Mikael Lindgren, and K. Peter R. Nilsson. "Fluorescence Spectroscopy as a Tool to Characterize Amyloid Oligomers and Fibrils." In Amyloid Fibrils and Prefibrillar Aggregates. Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527654185.ch11.

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Atti di convegni sul tema "Fibrils"

Harvey, MacAulay, Caylee MacDonald, Richard Cisek, et al. "Polarization-resolved Second Harmonic Generation Microscopy for Investigating Muscle and Collagen Fibrils." In Novel Techniques in Microscopy. Optica Publishing Group, 2025. https://doi.org/10.1364/ntm.2025.nm3c.2.

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Polarization-resolved second harmonic generation microscopy (PSHG) was used to determine baseline PSHG ρ and κ parameters for individual muscle and collagen fibrils, which can be used in future studies to further elucidate muscle and tissue structures.

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Intze, Antonia, Maria Eleonora Temperini, Giorgio Gregori, Federica Verde, Michele Ortolani, and Valeria Giliberti. "Effect of 0.6 THz irradiaton on protein fibrils monitored by mid-infrared nano-spectroscopy." In 2024 49th International Conference on Infrared, Millimeter, and Terahertz Waves (IRMMW-THz). IEEE, 2024. http://dx.doi.org/10.1109/irmmw-thz60956.2024.10697815.

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Babu, Aishwarya Chanady, Brian Vohnsen, and Ian A. Sigal. "Polarimetric Second-Harmonic Imaging of Collagen Fibrils in the Lamina Cribrosa of the Eye." In Frontiers in Optics. Optica Publishing Group, 2024. https://doi.org/10.1364/fio.2024.jw5a.44.

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The collagen-rich lamina cribrosa of the eye provides mechanical support to the neural tissues connecting the retina and brain. Here, we present second harmonic optical imaging of the lamina cribrosa using polarimetric sensing for orientational analysis to better understand lamina cribrosa architecture.

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Bourne, Jonathan W., and Peter A. Torzilli. "Collagen Molecular Conformation Exhibits Strain-Rate Dependent Response to Axial Deformation in Silico." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205534.

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Fibrillar collagens are a group of structural proteins that self assemble into a complex ordered structure of interconnected molecules to form supramolecular fibril structures. These collagens have three subgroups based on sequence similarity, of which clade A includes the most abundant fibrillar collagens, types I, II, and III. The fibrous hierarchical structures starts with individual collagen molecules that are crosslinked by enzymes to other collagen molecules to form micro fibrils, which aggregate and link to form sub fibrils, then larger fibrils and in some tissues continuing to assemble

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Shirazi, Reza, Pasquale Vena, Robert L. Sah, and Stephen M. Klisch. "A Novel Approach Towards Modeling the Collagen Fibril Network for Use in Nonlinear Anisotropic Polyconvex Mixture Models of Articular Cartilage." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19573.

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Despite distinct mechanical functions, biological soft tissues have a common microstructure in which a ground matrix is reinforced by a collagen (COL) fibril network. The highly anisotropic, heterogeneous, and asymmetric material properties caused by the microstructural nature of the COL fibril network suggest the importance, as well as the challenges, of accurately modeling soft tissue biomechanics. For soft fibrous tissues with multiple constituents, mathematical distribution functions have represented dispersed and continuous (i.e. non-discrete) fibrils oriented in all directions depending

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Dee, Derek, Fan Bu, Lanfang Shi, and Sara Zamani. "Comparing the structure and functionality of amyloid fibrils assembled from peanut, pea, lentil, and mung bean proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/kkyn7687.

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Protein structure dictates functionality, and one way to dramatically alter protein structure is to induce proteins to self-assemble into amyloid fibrils. Amyloid fibrils, or nanofibrils, are long (100–1000’s nm), narrow (10’s nm), highly-organized protein aggregates that hold promise for various applications in biotechnology and food. Converting plant proteins into fibrils may improve their functionality and create sustainable materials, yet most nanofibril research has focused on animal-derived proteins, so there is a need to learn more about fibrils derived from plant proteins. This project

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Cheng, Liang, William S. Oates, Ongi Englander, and Anant Paravastu. "A Computational Model for Structural Evolution of Protein Fibrils." In ASME 2010 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2010. http://dx.doi.org/10.1115/smasis2010-3649.

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A phase field modeling framework is developed to quantify structure evolution of protein fibrils in solution. The modeling framework employs a set of multi-physics constitutive relations to predict time dependent protein fibril structural evolution. The balance relations include chemical potential relations, microforces that govern local protein structure evolution, linear momentum and conservation of mass. Anisotropic formation of protein fibrils is controlled by protein monomer microforces and chemical fluxes to obtain long fibril growth from small seed particles. The theoretical model is im

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Li, L. P., M. D. Buschmann, and A. Shirazi-Adl. "A Fibril Reinforced Poroelastic Model of Articular Cartilage Including Depth Dependent Material Properties." In ASME 1999 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1999. http://dx.doi.org/10.1115/imece1999-0453.

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Abstract Articular cartilage is a highly nonhomogeneous, anisotropic and multiphase biomaterial consisting of mainly collagen fibrils, proteoglycans and water. Noncalcified cartilage is morphologically divided into three zones along the depth, i.e. superficial, transitional and radial zones. The thickness, density and alignment of collagen fibrils vary from the superficial zone, where fibrils are oriented parallel to the articular surface, to the radial zone where fibrils are perpendicular to the boundary between bone, and cartilage. The concentration of proteoglycans increases with the depth

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Harvey, MacAulay, Richard Cisek, Laurent Kreplak, and Danielle Tokarz. "Characterizing Hydration and Buckling in Individual Collagen Fibrils with Polarization Second Harmonic Generation Microscopy." In Optical Molecular Probes, Imaging and Drug Delivery. Optica Publishing Group, 2023. http://dx.doi.org/10.1364/omp.2023.om2e.3.

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Page, D. H., R. S. Seth, and F. El-Hosseiny. "Strength and Chemical Composition of Wood Pump Fibres." In Papermaking Raw Materials, edited by V. Punton. Fundamental Research Committee (FRC), Manchester, 1985. http://dx.doi.org/10.15376/frc.1985.1.77.

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An analysis of published work, together with new data, has clarified the effect of chemical composition on the strength of wood pulp fibres. Among fibres of low fibril angle, and in nondegrading pulping processes, strength (expressed as breaking stress) is directly proportional to α-cellulose content over a wide yield range. This implies that the cellulose fibrils are the sole tensile-load-bearing elements; hemicellulose and lignin only serve as a matrix that transfers the stress under shear from fibril to fibril. However, pulping to a yield corresponding to an α-cellulose content higher than

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Rapporti di organizzazioni sul tema "Fibrils"

Liang, Wenbin, and Charles R. Martin. Template-Synthesized Polyacetylene Fibrils Show Enhanced Supermolecular Order. Defense Technical Information Center, 1990. http://dx.doi.org/10.21236/ada228596.

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Nixdorf, R. D. Development of a Commercial Process for the Production of Silicon Carbide Fibrils. Office of Scientific and Technical Information (OSTI), 1999. http://dx.doi.org/10.2172/7914.

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Nixdorf, RD. Development of a Commercial Process for the Production of Silicon Carbide Fibrils - Draft Phase II Final Report. Office of Scientific and Technical Information (OSTI), 2002. http://dx.doi.org/10.2172/814172.

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Hollar, W. E. Jr, and W. H. Mills. Engineering scale development of the Vapor-Liquid-Solid (VLS) process for the production of silicon carbide fibrils. Office of Scientific and Technical Information (OSTI), 1993. http://dx.doi.org/10.2172/10125692.

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Ohnsorg, R. W., W. E. Jr Hollar, S. K. Lau, F. K. Ko, and K. Schatz. Engineering scale development of the vapor-liquid-solid (VLS) process for the production of silicon carbide fibrils. Phase 2. Office of Scientific and Technical Information (OSTI), 1995. http://dx.doi.org/10.2172/200670.

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จันทร์ประทีป, พีระศักดิ์, สุมลยา กาญจนะพังคะ, ประโยชน์ ตันติเจริญยศ та กัลยาณี ตันศฤงฆาร. ความเป็นมาและสถานภาพปัจจุบันของโรคสมองฟ่ามในโค (โคบ้า) : รายงานการวิจัย. จุฬาลงกรณ์มหาวิทยาลัย, 1998. https://doi.org/10.58837/chula.res.1998.81.

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โรคสมองฟ่ามหรือโคบ้า (Bovine Spongiform Encephalopathy, BSE) เป็นโรคระบาดร้ายแรงที่เกิดขึ้น.ในสหราชอาณาจักรเป็นส่วนใหญ่ ทำความเสียหายทางเศรษฐกิจอย่างมหาศาล จำเป็นต้องกำจัดโคถึง 1 ล้านตัวเพื่อกำจัด BSE ให้หมดไป ยิ่งไปกว่านั้น BSE อาจเป็นอันตรายแก่สุขภาพและชีวิตมนุษย์ด้วย BSE เป็นโรคหนึ่งใน transmissible spongiform encephalopathies (TSEs) โดยมี prion protein เป็นสารก่อโรคที่ทำความเสียหายแก่ระบบประสาท และทำให้คนหรือสัตว์ตายในที่สุด พบเนื้อสมองทั้งส่วน cerebrum และ cerebellum เป็นรูพรุน และอาจพบ plaques และ scrapie-associated fibrils (SAF) ในเนื้อสมองด้วย การศึกษาทางระบาดวิทยาชี้แนะว่าการแพร่ของ B

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Ivan, Jonas. Charge transport in fibrous/not fibrous alpha3-helical and variant peptides. ResearchHub Technologies, Inc., 2025. https://doi.org/10.55277/researchhub.5l4xo3fl.1.

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Dvorak, George J. Plasticity of Fibrous Composites. Defense Technical Information Center, 1987. http://dx.doi.org/10.21236/ada184637.

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OKAY, ERHAN, KORHAN OZKAN, Keith Baldwin, Alexandre Arkader, and Souroush Baghdadi. The clinical outcomes and current evidence in the surgical treatment of extremity-located fibrous dysplasia. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, 2023. http://dx.doi.org/10.37766/inplasy2023.5.0020.

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Review question / Objective: What are clinical outcomes and current evidence in the surgical treatment of extremity-located fibrous dysplasia? Condition being studied: Fibrous dysplasia is the fibro-osseous lesion of tissue where normal bone tissue is replaced by collagen fibroblast and varying amounts of osteoid cells which is caused by GNAS gene mutation. Surgery aims to correct deformities and avoid limb length discrepancies in symptomatic cases. Available options include curettage, grafting, corrective osteotomies, and using fixation materials. There is a need for an optimal surgical treat

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Smith, David R. Thermal conductivity of fibrous glass board :. National Bureau of Standards, 1997. http://dx.doi.org/10.6028/nist.tn.1391.

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