Littérature scientifique sur le sujet « Amyloid Proteins (Amyloidosis) »
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Articles de revues sur le sujet "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 (25 juillet 2022) : e0271737. http://dx.doi.org/10.1371/journal.pone.0271737.
Texte intégralWisniowski, Brendan, et Ashutosh Wechalekar. « Confirming the Diagnosis of Amyloidosis ». Acta Haematologica 143, no 4 (2020) : 312–21. http://dx.doi.org/10.1159/000508022.
Texte intégralKoike, Haruki, et Masahisa Katsuno. « The Ultrastructure of Tissue Damage by Amyloid Fibrils ». Molecules 26, no 15 (29 juillet 2021) : 4611. http://dx.doi.org/10.3390/molecules26154611.
Texte intégralAcquasaliente, Laura, et Vincenzo De Filippis. « The Role of Proteolysis in Amyloidosis ». International Journal of Molecular Sciences 24, no 1 (31 décembre 2022) : 699. http://dx.doi.org/10.3390/ijms24010699.
Texte intégralGuan, Jian, Shikha Mishra, Rodney H. Falk et Ronglih Liao. « Current perspectives on cardiac amyloidosis ». American Journal of Physiology-Heart and Circulatory Physiology 302, no 3 (février 2012) : H544—H552. http://dx.doi.org/10.1152/ajpheart.00815.2011.
Texte intégralCzyżewska, Emilia. « Amyloidoses – pathogenesis, classification, diagnosis ». Diagnostyka Laboratoryjna 56, no 4 (9 juillet 2021) : 1–13. http://dx.doi.org/10.5604/01.3001.0015.0266.
Texte intégralAblasser, Klemens, Nicolas Verheyen, Theresa Glantschnig, Giulio Agnetti et Peter P. Rainer. « Unfolding Cardiac Amyloidosis –From Pathophysiology to Cure ». Current Medicinal Chemistry 26, no 16 (26 août 2019) : 2865–78. http://dx.doi.org/10.2174/0929867325666180104153338.
Texte intégralRognoni, Paola, Giulia Mazzini, Serena Caminito, Giovanni Palladini et Francesca Lavatelli. « Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis : Contributions from Proteomics ». Medicina 57, no 9 (31 août 2021) : 916. http://dx.doi.org/10.3390/medicina57090916.
Texte intégralKhoor, Andras, et Thomas V. Colby. « Amyloidosis of the Lung ». Archives of Pathology & ; Laboratory Medicine 141, no 2 (1 février 2017) : 247–54. http://dx.doi.org/10.5858/arpa.2016-0102-ra.
Texte intégralSpodzieja, Marta, Sylwia Rodziewicz-Motowidło et Aneta Szymanska. « Hyphenated Mass Spectrometry Techniques in the Diagnosis of Amyloidosis ». Current Medicinal Chemistry 26, no 1 (14 mars 2019) : 104–20. http://dx.doi.org/10.2174/0929867324666171003113019.
Texte intégralThèses sur le sujet "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.
Texte intégralTerry, 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.
Texte intégralSkullerud, 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.
Texte intégralFranco, 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.
Texte intégralNerelius, 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.
Texte intégralSarlo, 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.
Texte intégralLannergård, 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.
Texte intégralSerum 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.
Texte intégralBinger, Katrina Jean. « The reversibility of amyloid fibril formation ». Connect to thesis, 2009. http://repository.unimelb.edu.au/10187/4912.
Texte intégralThe 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.
Texte intégralLivres sur le sujet "Amyloid Proteins (Amyloidosis)"
Sipe, Jean D. Amyloid proteins : The beta sheet conformation and disease. Weinheim : Wiley-VCH, 2005.
Trouver le texte intégralThomas, Scheibel, dir. Fibrous proteins. Austin, Tex : Landes Bioscience, 2008.
Trouver le texte intégralMarina, Ramirez-Alvarado, Kelly Jeffery W et Dobson C. M, dir. Protein misfolding diseases : Current and emerging principles and therapies. Hoboken, N.J : Wiley, 2010.
Trouver le texte intégralIndu, Kheterpal, et Wetzel Ronald, dir. Amyloid, prions, and other protein aggregates Part C. Amsterdam : Elsevier/Academic, 2006.
Trouver le texte intégralB, O'Doherty Cian, et Byrne Adam C, dir. Protein misfolding. New York : Nova Science Publishers, 2008.
Trouver le texte intégralIndu, Kheterpal, et Wetzel Ronald, dir. Amyloid, prions, and other protein aggregates Part B. Amsterdam : Elsevier/Academic, 2006.
Trouver le texte intégralC, Dowler Brynn, dir. Endocytosis : Structural components, functions, and pathways. Hauppauge, N.Y : Nova Science Publishers, 2010.
Trouver le texte intégralSipe, Jean D. Amyloid Proteins : The Beta Sheet Conformation and Disease. Wiley-VCH, 2005.
Trouver le texte intégralLachmann, Helen J., et Giampaolo Merlini. The patient with amyloidosis. Sous la direction de Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0152.
Texte intégralAmyloid Proteins Methods And Protocols. Humana Press, 2012.
Trouver le texte intégralChapitres de livres sur le sujet "Amyloid Proteins (Amyloidosis)"
Husby, Gunnar, et Knut Sletten. « Amyloid Proteins ». Dans Amyloidosis, 23–34. Dordrecht : Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_2.
Texte intégralWestermark, Per. « Endocrine Amyloid Fibril Proteins ». Dans Amyloidosis, 39–42. Dordrecht : Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-4309-4_4.
Texte intégralEriksen, Nils, et Earl P. Benditt. « Protein AA and Associated Proteins in Type-AA Amyloid Substance ». Dans Amyloidosis, 3–10. Boston, MA : Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_1.
Texte intégralBenson, M. D. « Pathofibrillogenesis and Amyloid Proteins ». Dans Amyloid and Amyloidosis 1990, 481–86. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_120.
Texte intégralShinoda, Tomotaka, Fuyuki Kametani, Hiroshi Tonoike et Shozo Kito. « Salient Structural Features of Low Molecular Weight Amyloid Fibril Proteins in Familial Amyloid Polyneuropathy of Japanese Origin ». Dans Amyloidosis, 331–37. Boston, MA : Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_43.
Texte intégralLinke, Reinhold P., Walter B. J. Nathrath et Manfred Eulitz. « Classification of Amyloid Syndromes from Tissue Sections Using Antibodies Against Various Amyloid Fibril Proteins : Report of 142 Cases ». Dans Amyloidosis, 599–605. Boston, MA : Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_75.
Texte intégralSipe, J. D., F. C. De Beer, M. Pepys, A. Husebekk, B. Skogen, R. Kisilevsky, D. Selkoe, J. Buxbaum, R. P. Linke et M. A. Gertz. « Report of Special Session on Bioassays and Standardization of Amyloid Proteins and Precursors ». Dans Amyloid and Amyloidosis 1990, 883–89. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_216.
Texte intégralBaba, Satoshi, Katsutoshi Miura et 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 ». Dans Amyloid and Amyloidosis 1990, 497–500. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_123.
Texte intégralRygg, M., G. Husby, B. Dowton et G. Marhaug. « Primary Structure of Two Rabbit Serum Amyloid a Proteins (SAA) Based on cDNA Sequence ». Dans Amyloid and Amyloidosis 1990, 40–43. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_10.
Texte intégralBellotti, V., A. Pucci, E. Arbustini, G. Merlini, M. Stoppin, G. Ferri et E. F. Osserman. « High Molecular Weight Proteins, Sensitive to Collagenase Digestion are Intimate Constituents of Amyloid Deposits ». Dans Amyloid and Amyloidosis 1990, 519–22. Dordrecht : Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_128.
Texte intégralActes de conférences sur le sujet "Amyloid Proteins (Amyloidosis)"
Gurian, Jordana Gaudie, Maria Ondina Machado Diniz, Amanda Nascimento Bispo, Aline Boaventura Ferreira et Fernando Elias Borges. « Case report : amyloidosis ». Dans XIV Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2023. http://dx.doi.org/10.5327/1516-3180.141s1.361.
Texte intégralGonzalez, Deilys, Duncan Brown, Montserrat Vera Llonch, Aaron Yarlas, Kristen McCausland et Asia Sikora Kessler. « Treatment satisfaction for gene silencing pharmacotherapies for the treatment of hereditary transthyretin amyloidosis with polyneuropathy ». Dans XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.517.
Texte intégralSenhorinha, Gláucia Maria, Arlys Emanuel Mendes da Silva Santos et Douglas Daniel Dophine. « The role of metabolic syndrome in Alzheimer’s disease ». Dans XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.319.
Texte intégralRapports d'organisations sur le sujet "Amyloid Proteins (Amyloidosis)"
Elmann, Anat, Orly Lazarov, Joel Kashman et Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, mars 2015. http://dx.doi.org/10.32747/2015.7597913.bard.
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