Literatura académica sobre el tema "Amyloid Proteins (Amyloidosis)"
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Artículos de revistas sobre el tema "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, n.º 7 (25 de julio de 2022): e0271737. http://dx.doi.org/10.1371/journal.pone.0271737.
Texto completoWisniowski, Brendan y Ashutosh Wechalekar. "Confirming the Diagnosis of Amyloidosis". Acta Haematologica 143, n.º 4 (2020): 312–21. http://dx.doi.org/10.1159/000508022.
Texto completoKoike, Haruki y Masahisa Katsuno. "The Ultrastructure of Tissue Damage by Amyloid Fibrils". Molecules 26, n.º 15 (29 de julio de 2021): 4611. http://dx.doi.org/10.3390/molecules26154611.
Texto completoAcquasaliente, Laura y Vincenzo De Filippis. "The Role of Proteolysis in Amyloidosis". International Journal of Molecular Sciences 24, n.º 1 (31 de diciembre de 2022): 699. http://dx.doi.org/10.3390/ijms24010699.
Texto completoGuan, Jian, Shikha Mishra, Rodney H. Falk y Ronglih Liao. "Current perspectives on cardiac amyloidosis". American Journal of Physiology-Heart and Circulatory Physiology 302, n.º 3 (febrero de 2012): H544—H552. http://dx.doi.org/10.1152/ajpheart.00815.2011.
Texto completoCzyżewska, Emilia. "Amyloidoses – pathogenesis, classification, diagnosis". Diagnostyka Laboratoryjna 56, n.º 4 (9 de julio de 2021): 1–13. http://dx.doi.org/10.5604/01.3001.0015.0266.
Texto completoAblasser, Klemens, Nicolas Verheyen, Theresa Glantschnig, Giulio Agnetti y Peter P. Rainer. "Unfolding Cardiac Amyloidosis –From Pathophysiology to Cure". Current Medicinal Chemistry 26, n.º 16 (26 de agosto de 2019): 2865–78. http://dx.doi.org/10.2174/0929867325666180104153338.
Texto completoRognoni, Paola, Giulia Mazzini, Serena Caminito, Giovanni Palladini y Francesca Lavatelli. "Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics". Medicina 57, n.º 9 (31 de agosto de 2021): 916. http://dx.doi.org/10.3390/medicina57090916.
Texto completoKhoor, Andras y Thomas V. Colby. "Amyloidosis of the Lung". Archives of Pathology & Laboratory Medicine 141, n.º 2 (1 de febrero de 2017): 247–54. http://dx.doi.org/10.5858/arpa.2016-0102-ra.
Texto completoSpodzieja, Marta, Sylwia Rodziewicz-Motowidło y Aneta Szymanska. "Hyphenated Mass Spectrometry Techniques in the Diagnosis of Amyloidosis". Current Medicinal Chemistry 26, n.º 1 (14 de marzo de 2019): 104–20. http://dx.doi.org/10.2174/0929867324666171003113019.
Texto completoTesis sobre el tema "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.
Texto completoTerry, 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.
Texto completoSkullerud, 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.
Texto completoFranco, 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.
Texto completoNerelius, 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.
Texto completoSarlo, 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.
Texto completoLannergård, 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.
Texto completoSerum 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.
Texto completoBinger, Katrina Jean. "The reversibility of amyloid fibril formation". Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/4912.
Texto completoThe 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.
Texto completoLibros sobre el tema "Amyloid Proteins (Amyloidosis)"
Sipe, Jean D. Amyloid proteins: The beta sheet conformation and disease. Weinheim: Wiley-VCH, 2005.
Buscar texto completoThomas, Scheibel, ed. Fibrous proteins. Austin, Tex: Landes Bioscience, 2008.
Buscar texto completoMarina, Ramirez-Alvarado, Kelly Jeffery W y Dobson C. M, eds. Protein misfolding diseases: Current and emerging principles and therapies. Hoboken, N.J: Wiley, 2010.
Buscar texto completoIndu, Kheterpal y Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part C. Amsterdam: Elsevier/Academic, 2006.
Buscar texto completoB, O'Doherty Cian y Byrne Adam C, eds. Protein misfolding. New York: Nova Science Publishers, 2008.
Buscar texto completoIndu, Kheterpal y Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part B. Amsterdam: Elsevier/Academic, 2006.
Buscar texto completoC, Dowler Brynn, ed. Endocytosis: Structural components, functions, and pathways. Hauppauge, N.Y: Nova Science Publishers, 2010.
Buscar texto completoSipe, Jean D. Amyloid Proteins: The Beta Sheet Conformation and Disease. Wiley-VCH, 2005.
Buscar texto completoLachmann, Helen J. y Giampaolo Merlini. The patient with amyloidosis. Editado por Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0152.
Texto completoAmyloid Proteins Methods And Protocols. Humana Press, 2012.
Buscar texto completoCapítulos de libros sobre el tema "Amyloid Proteins (Amyloidosis)"
Husby, Gunnar y Knut Sletten. "Amyloid Proteins". En Amyloidosis, 23–34. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_2.
Texto completoWestermark, Per. "Endocrine Amyloid Fibril Proteins". En Amyloidosis, 39–42. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_4.
Texto completoEriksen, Nils y Earl P. Benditt. "Protein AA and Associated Proteins in Type-AA Amyloid Substance". En Amyloidosis, 3–10. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_1.
Texto completoBenson, M. D. "Pathofibrillogenesis and Amyloid Proteins". En Amyloid and Amyloidosis 1990, 481–86. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_120.
Texto completoShinoda, Tomotaka, Fuyuki Kametani, Hiroshi Tonoike y Shozo Kito. "Salient Structural Features of Low Molecular Weight Amyloid Fibril Proteins in Familial Amyloid Polyneuropathy of Japanese Origin". En Amyloidosis, 331–37. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_43.
Texto completoLinke, Reinhold P., Walter B. J. Nathrath y Manfred Eulitz. "Classification of Amyloid Syndromes from Tissue Sections Using Antibodies Against Various Amyloid Fibril Proteins: Report of 142 Cases". En Amyloidosis, 599–605. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_75.
Texto completoSipe, J. D., F. C. De Beer, M. Pepys, A. Husebekk, B. Skogen, R. Kisilevsky, D. Selkoe, J. Buxbaum, R. P. Linke y M. A. Gertz. "Report of Special Session on Bioassays and Standardization of Amyloid Proteins and Precursors". En Amyloid and Amyloidosis 1990, 883–89. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_216.
Texto completoBaba, Satoshi, Katsutoshi Miura y 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". En Amyloid and Amyloidosis 1990, 497–500. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_123.
Texto completoRygg, M., G. Husby, B. Dowton y G. Marhaug. "Primary Structure of Two Rabbit Serum Amyloid a Proteins (SAA) Based on cDNA Sequence". En Amyloid and Amyloidosis 1990, 40–43. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_10.
Texto completoBellotti, V., A. Pucci, E. Arbustini, G. Merlini, M. Stoppin, G. Ferri y E. F. Osserman. "High Molecular Weight Proteins, Sensitive to Collagenase Digestion are Intimate Constituents of Amyloid Deposits". En Amyloid and Amyloidosis 1990, 519–22. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_128.
Texto completoActas de conferencias sobre el tema "Amyloid Proteins (Amyloidosis)"
Gurian, Jordana Gaudie, Maria Ondina Machado Diniz, Amanda Nascimento Bispo, Aline Boaventura Ferreira y Fernando Elias Borges. "Case report: amyloidosis". En XIV Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2023. http://dx.doi.org/10.5327/1516-3180.141s1.361.
Texto completoGonzalez, Deilys, Duncan Brown, Montserrat Vera Llonch, Aaron Yarlas, Kristen McCausland y Asia Sikora Kessler. "Treatment satisfaction for gene silencing pharmacotherapies for the treatment of hereditary transthyretin amyloidosis with polyneuropathy". En XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.517.
Texto completoSenhorinha, Gláucia Maria, Arlys Emanuel Mendes da Silva Santos y Douglas Daniel Dophine. "The role of metabolic syndrome in Alzheimer’s disease". En XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.319.
Texto completoInformes sobre el tema "Amyloid Proteins (Amyloidosis)"
Elmann, Anat, Orly Lazarov, Joel Kashman y Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, marzo de 2015. http://dx.doi.org/10.32747/2015.7597913.bard.
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