miércoles, 5 de abril de 2017

14 REFERENCIAS BIBLIOGRÁFICAS DE LA SANGRE Y OTROS FLUIDOS VITALES

  1. Abedin, M., & King, N. (2010). Diverse evolutionary paths to cell adhesion. Trends in Cell Biology, 20(12), 734–742.
  2. Adams, S. L. (1989). The medicinal leech: historical perspectives. In Seminars in thrombosis and hemostasis (Vol. 15, pp. 261–264). Copyright© 1989 by Thieme Medical Publishers, Inc.
  3. Alberts, B., Bray, D., Hopkin, K., Johnson, A., Lewis, J., & Raff, M. (2004). Tissues and cancer. Essential Cell Biology. New York, 698–706.
  4. Angelini, P., Villason, S., Chan Jr, A. V, & Diez, J. (1999). Normal and Anomalous Coronary Arteries in Humans. Part 1: Historical Background.
  5. Antonova, O., Yossifova, L., Staneva, R., Stevanovic, S., Dolashka, P., & Toncheva, D. (2015). Changes in the gene expression profile of the bladder cancer cell lines after treatment with Helix lucorum and Rapana venosa hemocyanin. J. BUON, 20(1), 180–187.
  6. Aw, T. Y. (1999). Intracellular compartmentation of organelles and gradients of low molecular weight species. International Review of Cytology, 192, 223–253.
  7. Azizi, M.-H., Nayernouri, T., & Azizi, F. (2008). A brief history of the discovery of the circulation of blood in the human body. Arch Iran Med, 11(3), 345–350.
  8. Bashkin, P., Doctrow, S., Klagsbrun, M., Svahn, C. M., Folkman, J., & Vlodavsky, I. (1989). Basic fibroblast growth factor binds to subendothelial extracellular matrix and is released by heparitinase and heparin-like molecules. Biochemistry, 28(4), 1737–1743.
  9. Berg, J. M., Tymoczko, J. L., & Stryer, L. (2002). Biochemical evolution. In Biochemistry (5th ed., pp. 56–82). Freeman. Retrieved from https://docs.google.com/file/d/0B0HRqdV3D7xIZGNlNmRmY2YtZGY3NS00YmJiLTkyYzQtNWFkOWYwMWVlNjA1/edit
  10. Boyanova, O., Dolashka, P., Toncheva, D., Rammensee, H., & Stevanović, S. (2013). In vitro effect of molluscan hemocyanins on CAL‑29 and T‑24 bladder cancer cell lines. Biomedical Reports, 1(2), 235–238.
  11. Bremer, P., Flint, S., Brooks, J., & Palmer, J. (2015). Introduction to Biofilms. Biofilms in the Dairy Industry, 1–16.
  12. Brewer, D. B. (2006). Max Schultze (1865), G. Bizzozero (1882) and the discovery of the platelet. British Journal of Haematology, 133(3), 251–258.
  13. Bright, G. R., Fisher, G. W., Rogowska, J., & Taylor, D. L. (1987). Fluorescence ratio imaging microscopy: temporal and spatial measurements of cytoplasmic pH. The Journal of Cell Biology, 104(4), 1019–1033.
  14. Brownlee, C. (2002). Role of the extracellular matrix in cell–cell signalling: paracrine paradigms. Current Opinion in Plant Biology, 5(5), 396–401.
  15. Brusca, R., Brusca, G. J., & Haver, N. J. (2003). Invertebrates (2nd ed.). Sinauer Associates.
  16. Burmester, T., & Hankeln, T. (2004). Neuroglobin: a respiratory protein of the nervous system. Physiology, 19(3), 110–113.
  17. Burmester, T., Weich, B., Reinhardt, S., & Hankeln, T. (2000). A vertebrate globin expressed in the brain. Nature, 407(6803), 520–523.
  18. Campbell, M. K., & Farrell, S. O. (2012). Biochemistry (7th ed.). Canadá: Brooks/Cole.
  19. Cate, J. H. D. (2001). Construction of low-resolution x-ray crystallographic electron density maps of the ribosome. Elsevier.
  20. Clegg, J. S. (1984). Properties and metabolism of the aqueous cytoplasm and its boundaries. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 246(2), R133–R151.
  21. Coates, C. J., & Nairn, J. (2014). Diverse immune functions of hemocyanins. Developmental & Comparative Immunology, 45(1), 43–55.
  22. Dalla Bona, F. (2004). Dolci pagine: la pasticceria napoletana nell´ opera di Matilde Serao. Revista de Italianística, (9), 149–154.
  23. Daniels, G. (2008). Human blood groups. John Wiley & Sons.
  24. De Duve, C., & Pizano, M. (1995). Polvo vital: origen y evolución de la vida en la tierra. Norma, Bogotá.
  25. Donlan, R. M. (2016). Microbial biofilms. Centers for Disease Control and Prevention.
  26. Doolittle, R. F. (1984). The plasma proteins.
  27. Doyle, L. (1989). Gabriel Andral (1797-1876) and the first reports of lymphangitis carcinomatosa. Journal of the Royal Society of Medicine, 82(8), 491.
  28. Ellis, R. J. (2001a). Macromolecular crowding: an important but neglected aspect of the intracellular environment. Current Opinion in Structural Biology, 11(1), 114–119.
  29. Ellis, R. J. (2001b). Macromolecular crowding: obvious but underappreciated. Trends in Biochemical Sciences, 26(10), 597–604.
  30. Elsholtz, J.-S. (1966). Clysmatica nova: sive ratio, qua in venam sectam medicamenta immitti possunt... ex Officina G. Schultzi.
  31. Friedman, M. T., West, K. A., & Bizargity, P. (2016). Immunohematology and Transfusion Medicine. Springer.
  32. Fröls, S. (2013). Archaeal biofilms: widespread and complex. Portland Press Limited.
  33. Gallagher, J. T., & Lyon, M. (2000). Molecular structure of heparan sulfate and interactions with growth factors and morphogens. Proteoglycans: Structure, Biology and Molecular Interactions, 27–59.
  34. Giangrande, P. L. F. (2000). The history of blood transfusion. British Journal of Haematology, 110(4), 758–767.
  35. Góngora-Biachi, R. A. (2005). La sangre en la historia de la humanidad. Rev Biomed, 16(4), 281–288.
  36. Goodenough, J., & McGuire, B. (2012). Biology of Humans, Concepts, Applications and Issues (4th ed.). San Francisco: Pearson, Benjamin Cummings.
  37. Guncheva, M., Paunova, K., Ossowicz, P., Rozwadowski, Z., Janus, E., Idakieva, K., … Apostolova, S. (2016). Rapana thomasiana hemocyanin modified with ionic liquids with enhanced anti breast cancer activity. International Journal of Biological Macromolecules, 82, 798–805.
  38. Hart, G. D. (2001). Descriptions of blood and blood disorders before the advent of laboratory studies. British Journal of Haematology, 115(4), 719–728.
  39. Harvey, W. (1959). De motu cordis. The American Journal of the Medical Sciences, 237(4), 543.
  40. Hay, E. D. (2013). Cell biology of extracellular matrix. Springer Science & Business Media.
  41. Hensch, T. K. (2005). Critical period mechanisms in developing visual cortex. Current Topics in Developmental Biology, 69, 215–237.
  42. Huleihel, L., Hussey, G. S., Naranjo, J. D., Zhang, L., Dziki, J. L., Turner, N. J., … Badylak, S. F. (2016). Matrix-bound nanovesicles within ECM bioscaffolds. Science Advances, 2(6), e1600502.
  43. Iozzo, R. V. (1998). Matrix proteoglycans: from molecular design to cellular function. Annual Review of Biochemistry, 67(1), 609–652.
  44. Ito, J., Parsons, H. T., & Heazlewood, J. L. (2014). The Arabidopsis cytosolic proteome: the metabolic heart of the cell.
  45. Izaguirre, A. R., & de Micheli, A. (2001). History of blood transfusion. Revista de Investigacion Clinica; Organo Del Hospital de Enfermedades de La Nutricion, 54(6), 552–558.
  46. Izaguirre-Ávila, R., & de Micheli, A. (2005). Evolución del conocimiento sobre la sangre y su movimiento: Parte II. El saber sobre su composición. Iatroquímica de la sangre. Revista de Investigación Clínica, 57(1), 85–97.
  47. Jaenicke, E., Pairet, B., Hartmann, H., & Decker, H. (2012). Crystallization and preliminary analysis of crystals of the 24-meric hemocyanin of the emperor scorpion (Pandinus imperator). PloS One, 7(3), e32548.
  48. Jaffe, L. F. (1993). Classes and mechanisms of calcium waves. Cell Calcium, 14(10), 736–745.
  49. Jaulin, P., & Lefrère, J. J. (2010). First French transfusions (1667-1668). Transfusion Clinique et Biologique: Journal de La Societe Francaise de Transfusion Sanguine, 17(4), 205–217.
  50. Kampen, K. R. (2012). The discovery and early understanding of leukemia. Leukemia Research, 36(1), 6–13.
  51. Kardong, K. V. (2011). Vertebrates, comparative anatomy, function, evolution (6th ed.). McGraw-Hill New York.
  52. Kardong, K. V. (2014). Vertebrates: Comparative Anatomy, Function, Evolution (7th ed.). McGraw-Hill Education.
  53. Karp, G. C. (2013). Cell and Molecular Biology, Concepts and Experiments (7th ed.). USA: Wiley Online Library.
  54. Khan, I. A., Daya, S. K., & Gowda, R. M. (2005). Evolution of the theory of circulation. International Journal of Cardiology, 98(3), 519–521.
  55. Kholodenko, B. N. (2003). Four-dimensional organization of protein kinase signaling cascades: the roles of diffusion, endocytosis and molecular motors. Journal of Experimental Biology, 206(12), 2073–2082.
  56. Kostakioti, M., Hadjifrangiskou, M., & Hultgren, S. J. (2013). Bacterial biofilms: development, dispersal, and therapeutic strategies in the dawn of the postantibiotic era. Cold Spring Harbor Perspectives in Medicine, 3(4), a010306.
  57. Kumar, V., Abbas, A. K., Fausto, N., & Aster, J. C. (2014). Robbins and Cotran pathologic basis of disease. Elsevier Health Sciences.
  58. Landau, M., & Fagien, S. (2015). Science of hyaluronic acid beyond filling: Fibroblasts and their response to the extracellular matrix. Plastic and Reconstructive Surgery, 136(5S), 188S–195S.
  59. Latzer, Y., Witztum, E., & Stein, D. (2008). Eating disorders and disordered eating in Israel: An updated review. European Eating Disorders Review, 16(5), 361–374.
  60. Learoyd, P. (2012). The history of blood transfusion prior to the 20th century–part 2. Transfusion Medicine, 22(6), 372–376.
  61. Lee, C., Collins-Hall, J., Hendrick, D., & Brabetz, B. (2016). Hemocyanin; Don’t Get in the Way of Blue Bloods.
  62. Linzen, B. (2013). Invertebrate oxygen carriers. Springer Science & Business Media.
  63. Love, W. E., Klock, P. A., Lattman, E. E., Padlan, E. A., Ward, K. B., & Hendrickson, W. A. (1972). The structures of lamprey and bloodworm hemoglobins in relation to their evolution and function. In Cold Spring Harbor symposia on quantitative biology (Vol. 36, pp. 349–357). Cold Spring Harbor Laboratory Press.
  64. Luby-Phelps, K. (1999). Cytoarchitecture and physical properties of cytoplasm: volume, viscosity, diffusion, intracellular surface area. International Review of Cytology, 192, 189–221.
  65. Luby-Phelps, K., Castle, P. E., Taylor, D. L., & Lanni, F. (1987). Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells. Proceedings of the National Academy of Sciences, 84(14), 4910–4913.
  66. MARKL, J. (1986). Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods. The Biological Bulletin, 171(1), 90–115.
  67. Mauseth, J, D. (2012). Botany: An Introduction to Plant Biology (5th ed.). Jones & Bartlett Learning.
  68. Maxfield, F. R., & Mondal, M. (2006). Sterol and lipid trafficking in mammalian cells. Portland Press Limited.
  69. McFadden, D. W., Riggs, D. R., Jackson, B. J., & Vona-Davis, L. (2003). Keyhole limpet hemocyanin, a novel immune stimulant with promising anticancer activity in Barrett’s esophageal adenocarcinoma. The American Journal of Surgery, 186(5), 552–555.
  70. Michel, G., Tonon, T., Scornet, D., Cock, J. M., & Kloareg, B. (2010). The cell wall polysaccharide metabolism of the brown alga Ectocarpus siliculosus. Insights into the evolution of extracellular matrix polysaccharides in Eukaryotes. New Phytologist, 188(1), 82–97.
  71. Moore, P. (2003). Blood and Justice: The 17 Century Parisian Doctor Who Made Blood Transfusion History. John Wiley & Sons.
  72. Moore, T. (2013). Novel Approach for Assessment and Mitigation of Heat-Stress Adverse Effects. Auburn University.
  73. Mory, R. N., Mindell, D., & Bloom, D. A. (2000). The leech and the physician: biology, etymology, and medical practice with Hirudinea medicinalis. World Journal of Surgery, 24(7), 878–883.
  74. Murray, R. K., Bender, D. A., Botham, K. M., Kennelly, P. J., Rodwell, V., & Weil, A. (2012). Harpers Illustrated Biochemistry (29th ed.). McGraw-Hill Medical.
  75. Newquist, H. P. (2012). The Book of Blood: From Legends and Leeches to Vampires and Veins. Houghton Mifflin Harcourt.
  76. Orell, A., Fröls, S., & Albers, S.-V. (2013). Archaeal biofilms: the great unexplored. Annual Review of Microbiology, 67, 337–354.
  77. Orlov, S. N., & Hamet, P. (2006). Intracellular monovalent ions as second messengers. The Journal of Membrane Biology, 210(3), 161–172.
  78. Orlova, E. V, Dube, P., Harris, J. R., Beckman, E., Zemlin, F., Markl, J., & van Heel, M. (1997). Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution. Journal of Molecular Biology, 271(3), 417–437.
  79. Paliwal, S., Fagien, S., Sun, X., Holt, T., Kim, T., Hee, C. K., … Messina, D. J. (2014). Skin extracellular matrix stimulation following injection of a hyaluronic acid–based dermal filler in a rat model. Plastic and Reconstructive Surgery, 134(6), 1224–1233.
  80. Pearson, H. A. (2002). History of pediatric hematology oncology. Pediatric Research, 52(6), 979–992.
  81. Pelletier, H., & Kraut, J. (1992). Crystal Structure of a Complex Between Electron Transfer. Science, 258, 1.
  82. Pesce, A., Bolognesi, M., Bocedi, A., Ascenzi, P., Dewilde, S., Moens, L., … Burmester, T. (2002). Neuroglobin and cytoglobin. EMBO Reports, 3(12), 1146–1151.
  83. Pesce, A., Dewilde, S., Nardini, M., Moens, L., Ascenzi, P., Hankeln, T., … Bolognesi, M. (2003). Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure, 11(9), 1087–1095.
  84. Peters, R. (2006). Introduction to nucleocytoplasmic transport: molecules and mechanisms. Xenopus Protocols: Cell Biology and Signal Transduction, 235–258.
  85. Pick, C., Scherbaum, S., Hegedüs, E., Meyer, A., Saur, M., Neumann, R., … Burmester, T. (2014). Structure, diversity and evolution of myriapod hemocyanins. FEBS Journal, 281(7), 1818–1833.
  86. Plopper, G. (2007). The extracellular matrix and cell adhesion. Cells.
  87. Prewitt, T. (1992). Unholy Anorexia: Blood Myth and the Signs of the Flesh. Semiotics, 300–319.
  88. Provance, D. W., McDowall, A., Marko, M., & Luby-Phelps, K. (1993). Cytoarchitecture of size-excluding compartments in living cells. Journal of Cell Science, 106(2), 565–577.
  89. Race, R. R., Sanger, R., & Fisher, R. (1962). Blood groups in man (Vol. 142). Blackwell scientific publications Oxford.
  90. Ratner, V. A., Zharkikh, A. A., Kolchanov, N., Rodin, S. N., Solovyov, V. V, & Antonov, A. S. (1996). Theoretical Analysis of the Evolution of Genes and Proteins. In Molecular Evolution (pp. 93–145). Springer.
  91. Rhoades, R. A., & Bell, D. R. (2013). Medical Physiology, Principles for Clinical Medicine (4th ed.). Baltimore: Lippincott Williams & Wilkins.
  92. Riggs, D. R., Jackson, B., Vona-Davis, L., & McFadden, D. (2002). In vitro anticancer effects of a novel immunostimulant: keyhole limpet hemocyanin. Journal of Surgical Research, 108(2), 279–284.
  93. Rolleston, H. (1934). The history of haematology. SAGE Publications.
  94. Roos, A., & Boron, W. F. (1981). Intracellular pH. Physiological Reviews, 61(2), 296–434.
  95. Ross, M. H., & Pawlina, W. (2011). Histology a text and atlas (6th ed.). Baltimore: Lippincott Williams & Wilkins.
  96. Ruoslahti, E. (1996). Brain extracellular matrix. Glycobiology, 6(5), 489–492.
  97. Scalettar, B. A., Abney, J. R., & Hackenbrock, C. R. (1991). Dynamics, structure, and function are coupled in the mitochondrial matrix. Proceedings of the National Academy of Sciences, 88(18), 8057–8061.
  98. Schultheiss, D., & Denil, J. (2002). History of the microscope and development of microsurgery: a revolution for reproductive tract surgery. Andrologia, 34(4), 234–241.
  99. Silverthorn, D. U., Bruce, B. R., Ober, W. C., Garrison, C. W., & Silverthorn, A. C. (2010). Human physiology an integrative aproach (5th ed.). San Francisco: Pearson, Benjamin Cummings.
  100. Starr, D. (2012). Blood: an epic history of medicine and commerce. Knopf.
  101. Stenzl, A., Dolashki, A., Stevanovic, S., Voelter, W., Aicher, W., & Dolashka, P. (2016). Cytotoxic Effects of Rapana venosa Hemocyanin on Bladder Cancer Permanent Cell Lines. Journal of US-China Medical Science, 13, 179–188.
  102. Stern, K. R., Bidlack, J. E., & Jansky, S. H. (2008). Introductory Plant Biology (11th ed.). McGraw-Hill New York.
  103. Storz, J. F., Opazo, J. C., & Hoffmann, F. G. (2011). Phylogenetic diversification of the globin gene superfamily in chordates. IUBMB Life, 63(5), 313–322.
  104. Suárez, P. D., Rojas, D. V., & Miranda, R. P. (2009). Análisis histórico–epistemológico de nomenclatura Química Inorgánica. TED: Tecné, Episteme Y Didaxis.
  105. Sussich, F., Skopec, C., Brady, J., & Cesàro, A. (2001). Reversible dehydration of trehalose and anhydrobiosis: from solution state to an exotic crystal? Carbohydrate Research, 334(3), 165–176.
  106. Swartz, A. M., Batich, K. A., Fecci, P. E., & Sampson, J. H. (2015). Peptide vaccines for the treatment of glioblastoma. Journal of Neuro-Oncology, 123(3), 433–440.
  107. Tam, J. P. (1988). Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system. Proceedings of the National Academy of Sciences, 85(15), 5409–5413.
  108. Tam, J. P., & Lu, Y.-A. (1989). Vaccine engineering: enhancement of immunogenicity of synthetic peptide vaccines related to hepatitis in chemically defined models consisting of T-and B-cell epitopes. Proceedings of the National Academy of Sciences, 86(23), 9084–9088.
  109. Tejero, J., & Gladwin, M. T. (2014). The globin superfamily: functions in nitric oxide formation and decay. Biological Chemistry, 395(6), 631–639.
  110. Terwilliger, N. B. (2015). Oxygen transport proteins in Crustacea: hemocyanin and hemoglobin. Physiology, 4, 359–390.
  111. Thanbichler, M., Wang, S. C., & Shapiro, L. (2005). The bacterial nucleoid: a highly organized and dynamic structure. Journal of Cellular Biochemistry, 96(3), 506–521.
  112. Ureta, T. (1985). Organización del metabolismo: Localización subcelular de enzimas glicolíticas. Arch. Biol. Med. Exp, 18(9).
  113. Vallone, B., Nienhaus, K., Brunori, M., & Nienhaus, G. U. (2004). The structure of murine neuroglobin: novel pathways for ligand migration and binding. Proteins: Structure, Function, and Bioinformatics, 56(1), 85–92.
  114. Verkman, A. S. (2002). Solute and macromolecule diffusion in cellular aqueous compartments. Trends in Biochemical Sciences, 27(1), 27–33.
  115. Voit, R., Feldmaier-Fuchs, G., Schweikardt, T., Decker, H., & Burmester, T. (2000). Complete Sequence of the 24-mer Hemocyanin of the TarantulaEurypelma californicum STRUCTURE AND INTRAMOLECULAR EVOLUTION OF THE SUBUNITS. Journal of Biological Chemistry, 275(50), 39339–39344.
  116. Wajcman, H., Kiger, L., & Marden, M. C. (2009). Structure and function evolution in the superfamily of globins. Comptes Rendus Biologies, 332(2), 273–282.
  117. Wang, Y., Meng, H., Yuan, X., Peng, J., Guo, Q., Lu, S., & Wang, A. (2014). Fabrication and in vitro evaluation of an articular cartilage extracellular matrix-hydroxyapatite bilayered scaffold with low permeability for interface tissue engineering. Biomedical Engineering Online, 13(1), 80.
  118. Wayne, R. (2009). Plant Cell Biology (1st ed.). San Diego: Elsevier.
  119. Weisiger, R. A. (2002). Cytosolic fatty acid binding proteins catalyze two distinct steps in intracellular transport of their ligands. In Cellular Lipid Binding Proteins (pp. 35–43). Springer.
  120. Weiss, J. N., & Korge, P. (2001). The Cytoplasm No Longer a Well-Mixed Bag. Circulation Research, 89, 108–110. Retrieved from http://circres.ahajournals.org/content/89/2/108.full#R1-094537
  121. Whitteridge, G., Pagel, W., & Keynes, G. (1972). William Harvey and the Circulation of the Blood.
  122. Wiggins, P. M. (1990). Role of water in some biological processes. Microbiological Reviews, 54(4), 432–449.
  123. Wikipedia, S. (2013). Hemoproteins: Arc System, Catalase, Chlorocruorin, Chromoprotein, Cytochrome B6f Complex. University-Press Org.
  124. Winey, M., Mamay, C. L., O’toole, E. T., Mastronarde, D. N., Giddings Jr, T. H., McDonald, K. L., & McIntosh, J. R. (1995). Three-dimensional ultrastructural analysis of the Saccharomyces cerevisiae mitotic spindle. Journal of Cell Biology, 129(6), 1601–1616.
  125. Wittenberg, J. B., & Wittenberg, B. A. (1990). Mechanisms of cytoplasmic hemoglobin and myoglobin function. Annual Review of Biophysics and Biophysical Chemistry, 19(1), 217–241.
  126. Yeates, T. O., Crowley, C. S., & Tanaka, S. (2010). Bacterial microcompartment organelles: protein shell structure and evolution. Annual Review of Biophysics, 39, 185–205.

Fluidos vitales // Principal // Siguiente

No hay comentarios:

Publicar un comentario