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Статті в журналах з теми "Amyloid Proteins (Amyloidosis)"
Bajic, Vladan P., Adil Salhi, Katja Lakota, Aleksandar Radovanovic, Rozaimi Razali, Lada Zivkovic, Biljana Spremo-Potparevic, et al. "DES-Amyloidoses “Amyloidoses through the looking-glass”: A knowledgebase developed for exploring and linking information related to human amyloid-related diseases." PLOS ONE 17, no. 7 (July 25, 2022): e0271737. http://dx.doi.org/10.1371/journal.pone.0271737.
Повний текст джерелаWisniowski, Brendan, and Ashutosh Wechalekar. "Confirming the Diagnosis of Amyloidosis." Acta Haematologica 143, no. 4 (2020): 312–21. http://dx.doi.org/10.1159/000508022.
Повний текст джерелаKoike, Haruki, and Masahisa Katsuno. "The Ultrastructure of Tissue Damage by Amyloid Fibrils." Molecules 26, no. 15 (July 29, 2021): 4611. http://dx.doi.org/10.3390/molecules26154611.
Повний текст джерелаAcquasaliente, Laura, and Vincenzo De Filippis. "The Role of Proteolysis in Amyloidosis." International Journal of Molecular Sciences 24, no. 1 (December 31, 2022): 699. http://dx.doi.org/10.3390/ijms24010699.
Повний текст джерелаGuan, Jian, Shikha Mishra, Rodney H. Falk, and Ronglih Liao. "Current perspectives on cardiac amyloidosis." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 3 (February 2012): H544—H552. http://dx.doi.org/10.1152/ajpheart.00815.2011.
Повний текст джерелаCzyżewska, Emilia. "Amyloidoses – pathogenesis, classification, diagnosis." Diagnostyka Laboratoryjna 56, no. 4 (July 9, 2021): 1–13. http://dx.doi.org/10.5604/01.3001.0015.0266.
Повний текст джерелаAblasser, Klemens, Nicolas Verheyen, Theresa Glantschnig, Giulio Agnetti, and Peter P. Rainer. "Unfolding Cardiac Amyloidosis –From Pathophysiology to Cure." Current Medicinal Chemistry 26, no. 16 (August 26, 2019): 2865–78. http://dx.doi.org/10.2174/0929867325666180104153338.
Повний текст джерелаRognoni, Paola, Giulia Mazzini, Serena Caminito, Giovanni Palladini, and Francesca Lavatelli. "Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics." Medicina 57, no. 9 (August 31, 2021): 916. http://dx.doi.org/10.3390/medicina57090916.
Повний текст джерелаKhoor, Andras, and Thomas V. Colby. "Amyloidosis of the Lung." Archives of Pathology & Laboratory Medicine 141, no. 2 (February 1, 2017): 247–54. http://dx.doi.org/10.5858/arpa.2016-0102-ra.
Повний текст джерелаSpodzieja, Marta, Sylwia Rodziewicz-Motowidło, and Aneta Szymanska. "Hyphenated Mass Spectrometry Techniques in the Diagnosis of Amyloidosis." Current Medicinal Chemistry 26, no. 1 (March 14, 2019): 104–20. http://dx.doi.org/10.2174/0929867324666171003113019.
Повний текст джерелаДисертації з теми "Amyloid Proteins (Amyloidosis)"
Bartlam, Mark Gerrard. "Structural studies of amyloid proteins." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342536.
Повний текст джерелаTerry, Carolyn Jane. "Structural studies of plasma proteins of medical interest." Thesis, University of Oxford, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302858.
Повний текст джерелаSkullerud, Andrine. "Characterization of antibodies specific for amyloid proteins." Thesis, Uppsala universitet, Institutionen för medicinsk cellbiologi, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-254597.
Повний текст джерелаFranco, Daniel A., Seth Truran, Volkmar Weissig, Diana Guzman-Villanueva, Nina Karamanova, Subhadip Senapati, Camelia Burciu, et al. "Monosialoganglioside-Containing Nanoliposomes Restore Endothelial Function Impaired by AL Amyloidosis Light Chain Proteins." WILEY-BLACKWELL, 2016. http://hdl.handle.net/10150/621716.
Повний текст джерелаNerelius, Charlotte. "Protein misfolding and amyloid formation : strategies for prevention /." Uppsala : Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, 2009. http://epsilon.slu.se/200941.pdf.
Повний текст джерелаSarlo, Katherine. "Some biological properties of the mouse acute phase reactant serum amyloid p-component /." The Ohio State University, 1985. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487262513407963.
Повний текст джерелаLannergård, Anders. "Serum Amyloid A Protein (SAA) in Healthy and Infected Individuals." Doctoral thesis, Uppsala University, Department of Medical Sciences, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-5774.
Повний текст джерелаSerum amyloid A protein (SAA) is an acute phase protein that has recently gained increasing interest as a potential marker for disease and treatment monitoring. We investigated SAA and CRP levels in (a) patients with various common infectious diseases (n=98), (b) patients with pyelonephritis (n=37) versus patients with cystitis (n=32), (c) healthy individuals of varying ages (n=231), (d) very immature newborn infants with or without nosocomial infections (NIs) (n=72) and (e) patients with bacterial infections treated with cefuroxime (n=81).
SAA significantly correlated with CRP in viral as well as in bacterial infections (for the total group: r2=0.757, p<0.0001) and showed a systemic inflammatory response in 90% of the patients with cystitis as compared with 23% for CRP. Equally high efficiencies (0.96 and 0.94 for SAA and CRP, respectively) were observed in discriminating between pyelonephritis and cystitis. SAA and high sensitive (hs) CRP were lower in umbilical cords (p<0.0001) and higher in elderly adults (p<0.0001-0.03) than in the other age groups; higher in immature newborn infants than in term infants; and higher in the NI group than in the non-NI group. Interindividual variabilities of the time course of the biomarkers SAA and CRP were considerable. Because of the smoothed distribution of SAA and CRP (i.e. elevations were both essentially unchanged during the first 3 days of cefuroxime treatment), these markers were not useful when deciding parenteral-oral switch of therapy, which occurred within this time period in most cases.
SAA is a sensitive systemic marker in cystitis. SAA and hsCRP in umbilical cord blood are close to the detection limit and increase with age. They increase in relation to NI in very immature newborn infants and might therefore be used in diagnosis and monitoring. Finally, SAA and CRP in adults with bacterial infections could not predict an early parenteral-oral switch of antimicrobial therapy.
Lundmark, Katarzyna. "Studies on pathogenesis of experimental AA amyloidosis : effects of amyloid enhancing factor and amyloid-like fibrils in rapid amyloid induction /." Linköping : Univ, 2001. http://www.bibl.liu.se/liupubl/disp/disp2001/med711s.pdf.
Повний текст джерелаBinger, Katrina Jean. "The reversibility of amyloid fibril formation." Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/4912.
Повний текст джерелаThe initial stages of the project were to develop a model for apoC-II amyloid fibril formation. This was achieved by analysis of the concentration dependent kinetics of apoC-II amyloid fibril formation, and correlation of these data with the final size distribution of the fibrils, determined by sedimentation velocity experiments. On the basis of these studies, a new reversible model for apoC-II amyloid fibril formation is proposed that includes fibril breaking and re-joining as integral parts of the assembly mechanism. The model was tested by rigorous experimentation, with antibody-labelling transmission electron microscopy providing direct evidence for spontaneous fibril breaking and re-joining.
The development of this model for apoC-II fibril assembly provided the foundation for experiments to investigate factors that promote, inhibit or reverse amyloid fibril formation. Factors that were considered include a molecular chaperone protein, αB-crystallin, and a chemical modification, methionine oxidation. Investigations on the effect of αB-crystallin revealed that the inhibition of apoC-II fibril formation occurs by two distinct mechanisms: transient interaction with monomer preventing oligomerisation, and binding to mature fibrils, which inhibits fibril elongation. Studies on the effect of methionine oxidation on apoC-II fibril formation showed that both the assembly and stability of the fibrils was affected by this modification. ApoC-II contains two methionine residues (Met-9 and Met-60), and upon oxidation of these residues fibril formation was inhibited. In addition, the treatment of pre-formed fibrils with hydrogen peroxide caused dissociation of the fibrils via the oxidation of Met-60, located with the fibril core structural region. The final chapter details the development of antibodies that specifically recognise the conformation of apoC-II amyloid fibrils, which provide the foundation for future studies to examine the role that apoC-II amyloid fibrils play in disease.
Overall, this thesis reveals the dynamic and reversible nature of amyloid fibril formation. New insight is also obtained of the general stability of amyloid fibrils and the processes that may regulate their formation, persistence and disease pathogenesis in vivo.
Bhogal, Ranjev. "The characterisation of binding sites for islet amyloid polypeptide and calcitonin gene-related peptide in mammalian lung." Thesis, Imperial College London, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.261471.
Повний текст джерелаКниги з теми "Amyloid Proteins (Amyloidosis)"
Sipe, Jean D. Amyloid proteins: The beta sheet conformation and disease. Weinheim: Wiley-VCH, 2005.
Знайти повний текст джерелаThomas, Scheibel, ed. Fibrous proteins. Austin, Tex: Landes Bioscience, 2008.
Знайти повний текст джерелаMarina, Ramirez-Alvarado, Kelly Jeffery W, and Dobson C. M, eds. Protein misfolding diseases: Current and emerging principles and therapies. Hoboken, N.J: Wiley, 2010.
Знайти повний текст джерелаIndu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part C. Amsterdam: Elsevier/Academic, 2006.
Знайти повний текст джерелаB, O'Doherty Cian, and Byrne Adam C, eds. Protein misfolding. New York: Nova Science Publishers, 2008.
Знайти повний текст джерелаIndu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part B. Amsterdam: Elsevier/Academic, 2006.
Знайти повний текст джерелаC, Dowler Brynn, ed. Endocytosis: Structural components, functions, and pathways. Hauppauge, N.Y: Nova Science Publishers, 2010.
Знайти повний текст джерелаSipe, Jean D. Amyloid Proteins: The Beta Sheet Conformation and Disease. Wiley-VCH, 2005.
Знайти повний текст джерелаLachmann, Helen J., and Giampaolo Merlini. The patient with amyloidosis. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0152.
Повний текст джерелаAmyloid Proteins Methods And Protocols. Humana Press, 2012.
Знайти повний текст джерелаЧастини книг з теми "Amyloid Proteins (Amyloidosis)"
Husby, Gunnar, and Knut Sletten. "Amyloid Proteins." In Amyloidosis, 23–34. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_2.
Повний текст джерелаWestermark, Per. "Endocrine Amyloid Fibril Proteins." In Amyloidosis, 39–42. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_4.
Повний текст джерелаEriksen, Nils, and Earl P. Benditt. "Protein AA and Associated Proteins in Type-AA Amyloid Substance." In Amyloidosis, 3–10. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_1.
Повний текст джерелаBenson, M. D. "Pathofibrillogenesis and Amyloid Proteins." In Amyloid and Amyloidosis 1990, 481–86. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_120.
Повний текст джерелаShinoda, Tomotaka, Fuyuki Kametani, Hiroshi Tonoike, and Shozo Kito. "Salient Structural Features of Low Molecular Weight Amyloid Fibril Proteins in Familial Amyloid Polyneuropathy of Japanese Origin." In Amyloidosis, 331–37. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_43.
Повний текст джерелаLinke, Reinhold P., Walter B. J. Nathrath, and Manfred Eulitz. "Classification of Amyloid Syndromes from Tissue Sections Using Antibodies Against Various Amyloid Fibril Proteins: Report of 142 Cases." In Amyloidosis, 599–605. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_75.
Повний текст джерелаSipe, J. D., F. C. De Beer, M. Pepys, A. Husebekk, B. Skogen, R. Kisilevsky, D. Selkoe, J. Buxbaum, R. P. Linke, and M. A. Gertz. "Report of Special Session on Bioassays and Standardization of Amyloid Proteins and Precursors." In Amyloid and Amyloidosis 1990, 883–89. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_216.
Повний текст джерелаBaba, Satoshi, Katsutoshi Miura, and Haruyuki Shirasawa. "In Vitro Assembly of Murine Amyloid a Protein, Two Murine Serum Amyloid a Proteins, and Normal Human Transthyretin to form Amyloid-Like Fibrils." In Amyloid and Amyloidosis 1990, 497–500. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_123.
Повний текст джерелаRygg, M., G. Husby, B. Dowton, and G. Marhaug. "Primary Structure of Two Rabbit Serum Amyloid a Proteins (SAA) Based on cDNA Sequence." In Amyloid and Amyloidosis 1990, 40–43. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_10.
Повний текст джерелаBellotti, V., A. Pucci, E. Arbustini, G. Merlini, M. Stoppin, G. Ferri, and E. F. Osserman. "High Molecular Weight Proteins, Sensitive to Collagenase Digestion are Intimate Constituents of Amyloid Deposits." In Amyloid and Amyloidosis 1990, 519–22. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_128.
Повний текст джерелаТези доповідей конференцій з теми "Amyloid Proteins (Amyloidosis)"
Gurian, Jordana Gaudie, Maria Ondina Machado Diniz, Amanda Nascimento Bispo, Aline Boaventura Ferreira, and Fernando Elias Borges. "Case report: amyloidosis." In XIV Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2023. http://dx.doi.org/10.5327/1516-3180.141s1.361.
Повний текст джерелаGonzalez, Deilys, Duncan Brown, Montserrat Vera Llonch, Aaron Yarlas, Kristen McCausland, and Asia Sikora Kessler. "Treatment satisfaction for gene silencing pharmacotherapies for the treatment of hereditary transthyretin amyloidosis with polyneuropathy." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.517.
Повний текст джерелаSenhorinha, Gláucia Maria, Arlys Emanuel Mendes da Silva Santos, and Douglas Daniel Dophine. "The role of metabolic syndrome in Alzheimer’s disease." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.319.
Повний текст джерелаЗвіти організацій з теми "Amyloid Proteins (Amyloidosis)"
Elmann, Anat, Orly Lazarov, Joel Kashman, and Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, March 2015. http://dx.doi.org/10.32747/2015.7597913.bard.
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