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Books on the topic 'Proton transporter'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Nelson, Nathan. Organellar proton-ATPases. New York: Springer-Verlag, 1995.

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2

Borka, D. Channeling of protons through carbon nanotubes. Hauppauge, N.Y: Nova Science Publishers, 2011.

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3

Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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4

Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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5

Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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6

Tripathi, Ratikanta. Proton-nucleus elastic cross sections using two-body in-medium scattering amplitudes. Hampton, Va: National Aeronautics and Space Administration, Langley Research Center, 2001.

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7

author, Mak M. W., ed. Machine learning for protein subcellular localization prediction. Boston: De Gruyter, 2015.

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8

R, Westwood Olwyn M., ed. Protein targeting and secretion. Oxford, OX: IRL Press at Oxford University Press, 1991.

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9

Richard, Zimmermann. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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10

An introduction to the passage of energetic particles through matter. Boca Raton: Taylor & Francis, 2007.

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11

J, McIlhinney R. A., and Hooper N. M, eds. Lipids, rafts and traffic: Biochemical Society symposium no. 72, held at BioScience2004, Glasgow, July 2004. London: Portland Press, 2005.

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12

service), ScienceDirect (Online, ed. Mitochondrial function: Mitochondrial protein kinases, protein phosphatases and mitochondrial diseases. San Diego, Calif: Academic Press/Elsevier, 2009.

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13

Trafficking inside cells: Pathways, mechanisms, and regulation. Austin, Tex: Landes Bioscience, 2009.

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14

C, Mobley William, Christen Yves, and SpringerLink (Online service), eds. Intracellular Traffic and Neurodegenerative Disorders. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009.

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15

Transcription factors: Methods and protocols. New York: Humana Press, 2010.

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16

C, Baxter R., Gluckman Peter D, and Rosenfeld Ron G, eds. The insulin-like growth factors and their regulatory proteins: Proceedings of the Third International Symposium on Insulin-Like Growth Factors, Sydney, 6-10 February 1994. Amsterdam: Excerpta Medica, 1994.

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17

Nelson, Nathan. Organellar Proton-ATPases. Springer, 2013.

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18

Symposium, CIBA Foundation. Proton Passage Across Cell Membranes. John Wiley & Sons, 1989.

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19

Gregory, Bock, Marsh Joan, Ciba Foundation, and Symposium on Proton Passage Across Cell Membranes (1988 : Ciba Foundation), eds. Proton passage across cell membranes. Chichester, Sussex, UK: Wiley, 1988.

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20

H, Durham John, Hardy Marcos A, and New York Academy of Sciences., eds. Bicarbonate, chloride, and proton transport systems. New York, N.Y: New York Academy of Sciences, 1989.

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21

Quick, Michael W. Transmembrane Transporters. Wiley & Sons, Incorporated, John, 2008.

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22

W, Quick Michael, ed. Transmembrane transporters. New York: Wiley-Liss, 2002.

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23

Quick, Michael W. Transmembrane Transporters. Wiley & Sons, Incorporated, John, 2003.

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24

Parameterized spectral distributions for meson production in proton-proton collisions. [Washington, DC]: NASA, 1995.

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25

(Editor), Tetsuro Urushidani, John G. Forte (Editor), and George Sachs (Editor), eds. Mechanisms and Consequences of Proton Transport. Springer, 2002.

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26

Tetsuro, Urushidani, Forte John G, and Sachs George 1935-, eds. Mechanisms and consequences of proton transport. Boston, MA: Kluwer Academic Publishers, 2002.

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27

Molecular bioenergetics: Simulations of electron, proton, and energy transfer. Washington, DC: American Chemical Society, 2004.

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28

Molecular Bioenergetics: Simulations of Electron, Proton, and Energy Transfer (Acs Symposium Series). An American Chemical Society Publication, 2004.

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29

Sebastio, Gianfranco, Manuel Schiff, and Hélène Ogier de Baulny. Lysinuric Protein Intolerance and Hartnup Disease. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0025.

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Lysinuric protein intolerance (LPI) is an inherited aminoaciduria caused by defective cationic amino acid transport at the basolateral membrane of epithelial cells in intestine and kidney. LPI is caused by mutations in the SLC7A7 gene, which encodes the y+LAT-1 protein, the catalytic light chain subunit of a complex belonging to the heterodimeric amino acid transporter family. Symptoms usually begin after weaning with refusal of feeding, vomiting, and consequent failure to thrive. Hepatosplenomegaly, hematological anomalies, and neurological involvement including hyperammonemic coma will progressively appear. Lung involvement (specifically pulmonary alveolar proteinosis), chronic renal disease that may lead to end stage renal disease, and hemophagocytic lymphohistiocytosis with macrophage activation all represent complications of LPI that may appear at any time from childhood to adulthood. The great variability of the clinical presentation frequently causes misdiagnosis or delayed diagnosis. The basic therapy of LPI consist of a low-protein diet, low-dose citrulline supplementation, nitrogen-scavenging compounds to prevent hyperammonemia, lysine, and carnitine supplements.

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30

Rabier, Daniel. Amino Acids. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0083.

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Amino acids present in the different biological fluids belong to two groups: the protein group, with the 21 classical amino acids constituting the backbone of the protein, and the nonprotein group, appearing in different metabolic pathways as intermediate metabolites. It is important to know and to be able to recognize the latter, as they are the markers of many inherited metabolic diseases. Three kinds of pathways must be considered: the catabolic pathways, the synthesis pathways, and the transport pathways. A disorder on a catabolic pathway induces an increase of all metabolites upstream and so an increase of the starting amino acid in all fluids. Any disorder on the synthetic pathway of a particular amino acid will induce a decrease of this amino acid in all fluids. When a transporter is located on a plasma membrane, its deficiency will result in normal or low concentration in plasma concomitant to a high excretion in urine.

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31

(Editor), Ross Dalbey, and Gunnar von Heijne (Editor), eds. Protein Targetting, Transport, and Translocation. Academic Press, 2002.

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32

(Editor), Ross Dalbey, and Gunnar von Heijne (Editor), eds. Protein Targetting, Transport, and Translocation. Academic Press, 2002.

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33

J, Bean Andrew, ed. Protein trafficking in neurons. Amsterdam: Elsevier/Academic Press, 2007.

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34

Vesicle Trafficking In Cancer. Springer-Verlag New York Inc., 2013.

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35

Kortgen, Andreas, and Michael Bauer. The effect of acute hepatic failure on drug handling in the critically ill. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0197.

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Impaired hepatic function is a common event in intensive care unit patients and as the liver plays a central role in drug metabolism and excretion this may lead to profound changes in pharmacokinetics. Underlying mechanisms are altered enzyme function of phase I and phase II metabolism, altered transporter protein function together with cholestasis and hepatic perfusion disorders. Moreover, multidrug therapy may lead to induction and inhibition of these enzymes and transporter proteins. In addition, changes in plasma protein binding and volumes of distribution of drugs are common. Altogether, these changes may not only lead to sometimes unpredictable plasma levels of xenobiotics, but also to drug-induced liver injury when hepatocellular accumulation of noxious substances occurs. Concomitant renal dysfunction may further complicate this situation. Pharmacodynamic alterations might also occur. In conclusion, the clinician must carefully evaluate medication given to patients with hepatic failure. Therapeutic drug monitoring should be performed wherever available to guide therapy.

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36

Eichler, Jerry. Protein Movement Across Membranes. Springer, 2011.

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37

Eichler, Jerry. Protein Movement Across Membranes. Springer, 2005.

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38

Coordination Chemistry In Protein Cages Principles Design And Applications. John Wiley & Sons Inc, 2013.

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39

Carron, N. J. An Introduction to the Passage of Energetic Particles through Matter. Taylor & Francis, 2006.

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40

Protein movement across membranes. Georgetown, TX: Landes Bioscience / Eurekah.com, 2006.

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41

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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42

Isett, Philip. Transport-Elliptic Estimates. Princeton University Press, 2017. http://dx.doi.org/10.23943/princeton/9780691174822.003.0027.

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This chapter solves the underdetermined, elliptic equation ∂ⱼQsuperscript jl = Usuperscript l and Qsuperscript jl = Qsuperscript lj (Equation 1069) in order to eliminate the error term in the parametrix. For the proof of the Main Lemma, estimates for Q and the material derivative as well as its spatial derivatives are derived. The chapter finds a solution to Equation (1069) with good transport properties by solving it via a Transport equation obtained by commuting the divergence operator with the material derivative. It concludes by showing the solutions, spatial derivative estimates, and material derivative estimates for the Transport-Elliptic equation, as well as cutting off the solution to the Transport-Elliptic equation.

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43

L, Audus Kenneth, and Raub Thomas J, eds. Biological barriers to protein delivery. New York: Plenum Press, 1993.

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44

(Editor), Lynda M. Sanders, and R. Wayne Hendren (Editor), eds. Protein Delivery: Physical Systems (Pharmaceutical Biotechnology). Springer, 1997.

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45

The Band 3 proteins: Anion transporters, binding proteins, and senescent antigens. Amsterdam: Elsevier, 1992.

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46

1966-, Jahn Thomas P., and Bienert Gerd P. 1978-, eds. MIPS and their role in the exchange of metalloids. New York, N.Y: Springer Science+Business Media/Landes Bioscience, 2010.

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47

D, Zimmermann Richard Ph, ed. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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48

Nava, Segev, ed. Trafficking inside cells: Pathways, mechanisms, and regulation. Austin, Tex: Landes Bioscience, 2009.

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49

Segev, Nava, Aixa Alfonso, and Gregory S. Payne. Trafficking Inside Cells: Pathways, Mechanisms and Regulation. Springer, 2011.

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50

D, Zimmermann Richard Ph, ed. Protein transport into the endoplasmic reticulum. Austin, Tex: Landes Bioscience, 2009.

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