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Pyrophosphatasen (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Pyrophosphatasen" in German language version.

refsWebsite
Global rank German rank
23doi.org
2nd place
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2bioinformatics.org
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1qmul.ac.uk
1,735th place
3,053rd place
1jstor.org
26th place
153rd place
1nature.com
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1web.archive.org
1st place
1st place

bioinformatics.org

doi.org

  • Alexander A. Baykov, Anssi M. Malinen, Heidi H. Luoto, Reijo Lahti: Pyrophosphate-Fueled Na+ and H+ Transport in Prokaryotes. In: Microbiology and Molecular Biology Reviews. Band 77, Nr. 2, 2013, S. 267–276, doi:10.1128/MMBR.00003-13 (englisch).
  • Tommi Kajandera, Juho Kellosalob, Adrian Goldman: Inorganic pyrophosphatases: One substrate, three mechanisms. In: FEBS Letters. Band 587, Nr. 13, 2013, S. 1863–1869, doi:10.1016/j.febslet.2013.05.003 (englisch).
  • Shih-Ming Lin, Jia-Yin Tsai, Chwan-Deng Hsiao, Yun-Tzu Huang, Chen-Liang Chiu, Mu-Hsuan Liu, Jung-Yu Tung, Tseng-Huang Liu, Rong-Long Pan, Yuh-Ju Sun: Crystal structure of a membrane-embedded H+-translocating pyrophosphatase. In: Nature. Band 484, Nr. 7394, 2012, S. 399–403, doi:10.1038/nature10963 (englisch).
  • Heidi H. Luoto, Georgiy A. Belogurov, Alexander A. Baykov, Reijo Lahti, Anssi M. Malinen: Na+-translocating Membrane Pyrophosphatases Are Widespread in the Microbial World and Evolutionarily Precede H+-translocating Pyrophosphatases. In: Journal of Biological Chemistry. Band 286, Nr. 11, 2011, S. 21633–21642, doi:10.1074/jbc.M111.244483 (englisch).
  • Toni Sivula, Anu Salminen, Alexey N. Parfenyev, Pekka Pohjanjoki, Adrian Goldman, Barry S. Cooperman, Alexander A. Baykov, Reijo Lahti: Evolutionary aspects of inorganic pyrophosphatase. In: FEBS Letters. Band 454, Nr. 1–2, 1999, S. 75–80, doi:10.1016/S0014-5793(99)00779-6 (englisch).
  • A. Kunitz: Crystalline inorganic pyrophosphatase isolated from baker's yeast. In: The Journal of General Physiology. Band 35, Nr. 3, 1952, S. 423–450, doi:10.1085/jgp.35.3.423 (englisch).
  • Lana J. McMillana, Nathaniel L. Hepowit, Julie A. Maupin-Furlow: Archaeal Inorganic Pyrophosphatase Displays Robust Activity under High-Salt Conditions and in Organic Solvents. In: Applied and Environmental Microbiology. Band 82, Nr. 2, 2016, S. 538–548, doi:10.1128/AEM.03055-15 (englisch).
  • María R Gómez‐García, Manuel Losada, Aurelio Serrano: Comparative biochemical and functional studies of family I soluble inorganic pyrophosphatases from photosynthetic bacteria. In: FEBS Journal. Band 274, Nr. 15, 2007, S. 3948–3959, doi:10.1111/j.1742-4658.2007.05927.x (englisch).
  • Marco Zancani, Valentino Casolo, Carlo Peresson, Giorgio Federici, Andrea Urbani, Francesco Macrı̀, Angelo Vianello: The β-subunit of pea stem mitochondrial ATP synthase exhibits PPiase activity. In: Mitochondrion. Band 3, Nr. 2, 2003, S. 111–118, doi:10.1016/S1567-7249(03)00105-3 (englisch).
  • Chathurada S. Gajadeera, Xinyi Zhang, Yinan Wei, Oleg V. Tsodikov: Structure of inorganic pyrophosphatase from Staphylococcus aureus reveals conformational flexibility of the active site. In: Journal of Structural Biology. Band 189, Nr. 2, 2015, S. 81–86, doi:10.1016/j.jsb.2014.12.003 (englisch).
  • Laura M. Barge, Ivria J. Doloboff, Michael J. Russell, David VanderVelde, Lauren M. White, Galen D. Stucky, Marc M. Baum, John Zeytounian, Richard Kidd, Isik Kanik: Pyrophosphate synthesis in iron mineral films and membranes simulating prebiotic submarine hydrothermal precipitates. In: Geochimica et Cosmochimica Acta. Band 128, 2014, S. 42705, doi:10.1016/j.gca.2013.12.006 (englisch).
  • Jennifer Moyle, Roy Mitchell, Peter Mitchell: Proton-translocating pyrophosphatase of Rhodospirillum rubrum. In: FEBS Letters. Band 23, Nr. 2, 1972, S. 233–236, doi:10.1016/0014-5793(72)80349-1 (englisch).
  • Roberto Docampo, Wanderley de Souza, Kildare Miranda, Peter Rohloff, Silvia N. J. Moreno: Acidocalcisomes? conserved from bacteria to man. In: Nature Reviews Microbiology. Band 3, Nr. 3, 2005, S. 251–261, doi:10.1038/nrmicro1097 (englisch).
  • Manfredo Seufferheld, Christopher R. Lea, Mauricio Vieira, Eric Oldfield, Roberto Docampo: The H+-pyrophosphatase of Rhodospirillum rubrum is predominantly located in Polyphosphate-rich Acidocalcisomes. In: Journal of Biological Chemistry. Band 279, 2004, S. 51193–51202, doi:10.1074/jbc.M406099200 (englisch).
  • Juho Kellosalo, Tommi Kajander, Konstantin Kogan, Kisun Pokharel, Adrian Goldman: The Structure and Catalytic Cycle of a Sodium-Pumping Pyrophosphatase. In: Science. Band 337, Nr. 6093, 2012, S. 473–476, doi:10.1126/science.1222505 (englisch).
  • Shih-Ming Lin, Jia-Yin Tsai, Chwan-Deng Hsiao, Yun-Tzu Huang, Chen-Liang Chiu, Mu-Hsuan Liu, Jung-Yu Tung, Tseng-Huang Liu, Rong-Long Pan, Yuh-Ju Sun: Crystal structure of a membrane-embedded H+-translocating pyrophosphatase. In: Nature. Band 484, Nr. 7394, 2012, S. 399–403, doi:10.1038/nature10963 (englisch). Grafik vgl. A working model for proton pumping in VrH+-PPase
  • Nils G. Holm, Herrick Baltscheffsky: Links between hydrothermal environments, pyrophosphate, Na+, and early evolution. In: Origins of Life and Evolution of Biospheres. Band 41, Nr. 5, 2011, S. 483–493, doi:10.1007/s11084-011-9235-4 (englisch).
  • Tommi Kajandera, Juho Kellosalob, Adrian Goldman: Inorganic pyrophosphatases: One substrate, three mechanisms. In: FEBS Letters. Band 587, Nr. 13, 2013, S. 1866 f., doi:10.1016/j.febslet.2013.05.003 (englisch).
  • Armen Y. Mulkidjanian, Pavel Dibrov, Michael Y. Galperin: The past and present of sodium energetics: May the sodium-motive force be with you. In: Biochimica et Biophysica Acta (BBA) – Bioenergetics. Band 1777, Nr. 7–8, 2008, S. 985–992, doi:10.1016/j.bbabio.2008.04.028 (englisch).
  • Armen Y Mulkidjanian, Michael Y Galperin, Kira S Makarova, Yuri I Wolf, Eugene V Koonin: Evolutionary primacy of sodium bioenergetics. In: Biology Direct. Band 3, Nr. 13, 2008, doi:10.1186/1745-6150-3-13 (englisch).
  • Armen Y Mulkidjanian, Kira S Makarova, Michael Y Galperin, Eugene V Koonin: Inventing the dynamo machine: the evolution of the F-type and V-type ATPases. In: Nature Reviews Microbiology. Band 5, Nr. 11, 2007, S. 892–899, doi:10.1038/nrmicro1767 (englisch, dieser Artikel bei Uni Osnabrück: Perspectives (Memento vom 31. Oktober 2008 im Internet Archive) [PDF]).
  • Suzanne J. Admiraal, Daniel Herschlag: Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis. In: Chemistry & Biology. Band 2, Nr. 11, 1995, S. 729–739, doi:10.1016/1074-5521(95)90101-9 (englisch).
  • Lucien Bettendorff, Pierre Wins: Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors. In: FEBS Journal. Band 276, Nr. 11, 2009, S. 2917–2925, doi:10.1111/j.1742-4658.2009.07019.x (englisch).

jstor.org

  • Herrick Baltscheffsky, Lars-Victor von Stedingk, Hans-Walter Heldt, Martin Klingenberg: Inorganic Pyrophosphate: Formation in Bacterial Photophosphorylation (Inorganic pyrophosphate is identified as the major product of photophosphorylation by isolated chromatophores from Rhodospirillum rubrum in the absence of added nucleotides.). In: Science. Band 274, Nr. 3740, 1966, S. 1120–1122, JSTOR:1719164 (englisch).

nature.com

  • Shih-Ming Lin, Jia-Yin Tsai, Chwan-Deng Hsiao, Yun-Tzu Huang, Chen-Liang Chiu, Mu-Hsuan Liu, Jung-Yu Tung, Tseng-Huang Liu, Rong-Long Pan, Yuh-Ju Sun: Crystal structure of a membrane-embedded H+-translocating pyrophosphatase. In: Nature. Band 484, Nr. 7394, 2012, S. 399–403, doi:10.1038/nature10963 (englisch). Grafik vgl. A working model for proton pumping in VrH+-PPase

qmul.ac.uk

  • Laut IUBMB gilt für (anorganische) Pyrophosphatasen die Bezeichnung (inorganic) diphosphatase [1] [2]

web.archive.org