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Books on the topic 'Sialic Acid Binding Proteins'

Author: Grafiati
Published: 6 September 2023

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1

Glatz, Jan F. C., and Ger J. Van Der Vusse, eds. Cellular Fatty Acid-binding Proteins. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-3936-0.

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2

C, Glatz Jan F., and Vusse, G. J. van der., eds. Cellular fatty-acid binding proteins. Dordrecht: Kluwer Academic Publishers, 1990.

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3

Glatz, Jan F. C., and Ger J. van der Vusse, eds. Cellular Fatty Acid-Binding Proteins II. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3096-1.

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4

Conference on High Affinity Metal-Binding Proteins in Non-Mammalian Species (1984 : Research Triangle Park) and Conference on phthalic acid esters (1984 : Guildford, England)., eds. Metal-binding proteins: Phthalic acid esters. Research Triangle Park, N.C: National Institute of Environmental Health Sciences, National Institutes of Health, Dept. of Health and Human Services, 1986.

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5

Younis, Rafal R. Sabir. Improved assays for the reactive hexose and sialic acid contents of glycoproteins. Dublin: University College Dublin, 1996.

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6

C, Glatz Jan F., and Vusse, G. J. van der., eds. Cellular fatty acid-binding proteins: Proceedings of the 2nd International Workshop on Fatty Acid-Binding Proteins, Maastricht, August 31 and September 1, 1992. Dordrecht: Kluwer Academic Publishers, 1993.

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7

Asim, Dutta-Roy, and Sener Friedrich, eds. Cellular proteins and their fatty acids in health and disease. Weinheim: Wiley-VCH, 2003.

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8

W, Wang, and United States. National Aeronautics and Space Administration., eds. A novel kinesin-like protein with a calmodulin-binding domain. [Washington, DC: National Aeronautics and Space Administration, 1996.

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9

Huang, Wei-chün. Structural studies of enzymes in biotin and fatty acid biosynthesis. Uppsala: Dept. of Molecular Biology, Swedish University of Agricultural Sciences, 1996.

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10

Khuri, Lamya Raja Tannous. The role of retinoids and retinoid binding proteins in the differentiation of the cervix. [New York]: [Columbia University], 1993.

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11

Mallory, Raburn M. Changes in cellular retinoic acid binding proteins and nuclear retinoic acid receptors in murine melanoma cell lines following retinoic acid exposure. [New Haven, Conn: s.n.], 1997.

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12

Singh, Juswinder. Atlas of protein side-chain interactions. Oxford: IRL Press at Oxford University Press, 1992.

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13

M, Thornton Janet, ed. Atlas of protein side-chain interactions. Oxford: IRL Press at Oxford University Press, 1992.

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14

Saluz, H. P. A laboratory guide for in vivo studies of DNA methylation and protein/DNA interactions. Basel: Birkhäuser Verlag, 1990.

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15

Allen, Geoffrey. Proteins: Nucleic Acid Binding Proteins. JAI Press, 1995.

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16

Ger J. van der Vusse and Jan F. C. Glatz. Cellular Fatty Acid-Binding Proteins. Springer London, Limited, 2012.

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17

Ger J. van der Vusse and Jan F. C. Glatz. Cellular Fatty Acid-Binding Proteins. Springer London, Limited, 2012.

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18

Metal-binding proteins: Phthalic acid esters. Research Triangle Park, N.C: National Institute of Environmental Health Sciences, National Institutes of Health, Dept. of Health and Human Services, 1986.

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19

C, Glatz Jan F., ed. Cellular lipid binding proteins. Dordrecht: Kluwer Academic Pub., 2002.

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20

Cellular Lipid Binding Proteins. Springer, 2011.

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21

Jansen, Jan. Cellular Lipid Binding Proteins. Springer London, Limited, 2012.

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22

Glatz, Jan F. C., and A. T. M. Jansen. Cellular Lipid Binding Proteins. Springer London, Limited, 2012.

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23

Ger J. van der Vusse and Jan F. C. Glatz. Cellular Fatty Acid-Binding Proteins II: Proceedings of the 2nd International Workshop on Fatty Acid-Binding Proteins, Maastricht, August 31 and September 1 1992. Springer London, Limited, 2012.

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24

Waring, Michael J., and Jonathan B. Chaires. Drug-Nucleic Acid Interactions. Elsevier Science & Technology Books, 2001.

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25

Glatz, Jan F. C. Cellular Fatty Acid-Binding Proteins II: Proceedings of the 2nd International Workshop on Fatty Acid-Binding Proteins, Maastricht, August 31 and ... in Molecular and Cellular Biochemistry ). Springer, 2012.

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26

Jan F.C. Glatz (Editor) and Ger J. van der Vusse (Editor), eds. Cellular Fatty-Acid Binding Proteins (Developments in Molecular and Cellular Biochemistry). Springer, 2007.

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27

Bailey, John Stuart. Characterization of two distinct cellular retinoic acid-binding proteins from rodent tissue. 1989.

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28

Jan F.C. Glatz (Editor) and Ger J. van der Vusse (Editor), eds. Cellular Fatty-Acid-Binding Proteins II (Developments in Molecular and Cellular Biochemistry). Springer, 1993.

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29

(Editor), Jonathan B. Chaires, and Michael J. Waring (Editor), eds. Drug-Nucleic Acid Interactions (Methods in Enzymology, Volume 340) (Methods in Enzymology). Academic Press, 2001.

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30

DNA-Ligand Interactions:From Drugs to Proteins. Springer, 1987.

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31

Richardson, Charles C., and I. Robert Lehman. Molecular Mechanisms in Deoxyribonucleic Acid Replication and Recombination (UCLA Symposia on Molecular and Cellular Biology, New Series). John Wiley & Sons Inc, 1990.

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32

Cellular retinoic acid binding proteins -I and -II: Expression during mouse embryogenesis and modulation of the retinoid signal. Ottawa: National Library of Canada, 1993.

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33

Wagner, Carsten A., and Olivier Devuyst. Renal acid–base homeostasis. Edited by Robert Unwin. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0024.

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The kidney is central to acid–base homeostasis. Major processes are reabsorption of filtered bicarbonate, de novo synthesis of bicarbonate from ammoniagenesis, and net excretion of protons. The latter requires buffers such as ammonium, phosphate, citrate and other bases binding protons (so-called titratable acids). The proximal tubule is the major site of bicarbonate reabsorption and only site of ammoniagenesis. The thick ascending limb and the distal convoluted tubule handle ammonia/ammonium and complete bicarbonate reabsorption. The collecting duct system excretes protons and ammonium, but may switch to net bicarbonate secretion. The kidney displays a great plasticity to adapt acid or bicarbonate excretion. Angiotensin II, aldosterone and endothelin are involved in regulating these processes, and they induce morphological changes along the nephron. Inborn and acquired disorders of renal acid–base handling are caused by mutations in acid–base transport proteins or by dysregulation of adaptive mechanisms.
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34

DNA Structure and Recognition (IN FOCUS). Oxford University Press, USA, 1994.

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35

Halperin, Mitchell L., and Kamel S. Kamel. Approach to the patient with metabolic acidosis or alkalosis. Edited by Robert Unwin. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0035_update_001.

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The pathophysiology, clinical approach, and management of the common causes of metabolic acidosis and alkalosis are discussed. In metabolic acidosis, a quantitative estimate of the extracellular volume (ECFV) is required to determine its content of bicarbonate in a patient with ECFV contraction. Buffering of H+ must occur by the bicarbonate buffer system in muscle to avoid binding to intracellular proteins, this requires low muscle capillary PCO2; acid gain type of metabolic acidosis is detected by the finding of new anions in blood and/or urine. The urine osmolal gap is the best indirect test to assess [NH4+] in urine. In metabolic alkalosis, Cl− depletion alkalosis is misleading. Deficits must be defined as HCl, KCl, and/or NaCl. A quantitative assessment of ECFV helps determine the contribution of individual deficits of Cl− salts. There is no tubular maximum for HCO3− reabsorption. Angiotensin II and the usual pH in proximal convoluted tubule cells, the two major stimuli for NaHCO3 reabsorption, must be removed/ changed for NaHCO3 to be excreted.
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