Results 111 to 120 of about 172,406 (192)

Mammalian NADH:ubiquinone oxidoreductase (Complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H2O2—Implications for their role in disease, especially cancer [PDF]

A Cittadini, A Kim, A Le, A Okado-Matsumoto, A Pedersen, A Pedersen, A Terman, A Volbeda, A Volbeda, AA Toye, AC Nulton-Persson, AJ Lambert, AJ Lambert, AJ Lambert, AJ Lambert, AJ Meijer, Alfred J. Meijer, AS Galkin, AT Kowal, AY Andreyev, B Lippitt, B Persson, B Westermann, BA Diwan, BAC Ackrell, BG Heerdt, BM Madhok, C Broeke Van den, C Hunte, C Kuiper, C Paech, C Rossi, C Yip, C-W Lu, CI Ragan, CI Ragan, CI Ragan, CJ Lusty, DH Flint, DJ Morgan, DM Miller, DR Mole, DW Parsons, E Cadenas, E Linden Van der, E Linden Van der, ED Michelakis, EL Arkblad, EW Miller, FA Armstrong, FL Muller, G Belevich, G Dooijewaard, G Hofhaus, G Krishnamoorthy, G Peng, GD Eytan, GL Semenza, GL Semenza, H Beinert, H Beinert, H Beinert, H Freeman, H Freeman, H Zhang, HC Freeman, HG Heidrich, HJ Knowles, I Papandreou, IM Fearnley, IS Gostimskaya, J Carroll, J Hirst, J Hirst, J Li, J Lind, J Rydström, J Rydström, J Rydström, J Rydström, J Rydström, J Vásquez-Vivar, Jan Rydström, JB Hoek, JB Jackson, JC Fontecilla-Camps, JC Salerno, JE Walker, JG Pastorino, JM Berrisford, JM Berrisford, JM McCord, JM McCord, JM Robinson, JYY Wong, K Aston-Mourney, K Kim, K Leonard, K Luciaková, K Shinzawa-Itoh, K Zwicker, KA Vincent, KR Pryde, KS Suslick, KS Suslick, L Chin, L Ernster, L Grgic, L Jong De, L Jong De, L Kussmaul, L Sinegina, LA Sazanov, LB Chen, M Finel, M Finel, M Forkink, M Gutman, M Ivan, M Kato, M Kawakita, M Murai, M Wikström, MA Aon, MA Tocilescu, MA Tocilescu, MCM Vissers, MCM Vissers, MD Brand, MP Murphy, MP Murphy, MR Stratton, MS Sharpley, N Grigorieff, N Kashani-Poor, N Parker, N Yamamoto, N Yamamoto, NPJ Cotton, NR Orme-Johnson, NV Dudkina, O Warburg, O Warburg, O Warburg, O Warburg, P Borst, P Jiang, PC Hinkle, PD Mitchell, PJ Pollard, PK Jensen, PL Pedersen, PT Bakker, PW Ellyard, R Belzen Van, R Belzen Van, R Djafarzadeh, R Scherz-Shouval, RC Sun, RF Anderson, RG Efremov, RL Ringler, RL Ringler, RP Happe, RW Estabrook, S Bonnet, S Jitrapakdee, S Jones, S Kurkin, S Papa, S Whitehouse, S-H Jo, SI Taylor, Simon P. J. Albracht, SJ George, SP Mathupala, SP Mathupala, SPJ Albracht, SPJ Albracht, SPJ Albracht, SPJ Albracht, SPJ Albracht, SPJ Albracht, ST Ohnishi, T Bizouarn, T Cremona, T Ohnishi, T Ohnishi, T Yagi, T-T Huang, T-T Huang, TC Bruice, V Guénebaut, V Guénebaut, V Zickermann, VD Sled, VR Fantin, W Bursch, W Cao, W Koppenol, W Watt, WG Kaelin Jr, WJ Ingledew, Y Chen, Y Chen, Y Hatefi, Y Hatefi, Y Hatefi, Y Hatefi, Y Nakashima, Y Zhang   +210 more
core   +1 more source

[Characterization and properties of two dehydroquinate hydro-lyases in higher plants].

Planta, 1975
Two dehydroquinate hydro-lyases (E.C. 4.2.1.10) have been routinely separated from different organs of Zea mays L. by chromatography on Cellex-D Bio-Rad or hydroxypatite using linear salt gradients. Dehydroquinate hydro-lyase 1 is associated with shikimate: NADP(+) oxidoreductase (E.C. 1.1.1.25).
A. Boudet, R. Lécussan, A. Boudet
semanticscholar   +5 more sources

The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases.

European Journal of Biochemistry, 1987
d‐Altronate hydratase and d‐mannonate hydratase belong to a class of Fe2+‐requiring enzymes, but the function of iron in these enzymes is largely unknown. Methods are described for the convenient preparation of both these hydratases from Escherichia coli and studies related to metal activation are presented.
Jean-Luc Dreyer
semanticscholar   +4 more sources

Indoleacetaldoxime hydro-lyase (4.2.1.29)

Archives of Biochemistry and Biophysics, 1970
The purification and some properties of the enzyme indoleacetaldoxime hydrolyase (EC 4.2.1.29) from the fungus Gibberella fujikuroi, which dehydrates indoleacetaldoxime (IAOX) to indoleacetonitrile (IAN), are described. The enzyme activity in the fungus is present only under certain culture conditions.
P.S. Shukla, S. Mahadevan
openalex   +4 more sources

3-Dehydroshikimate hydro-lyase ofPhaseolus mungo seedlings

The Botanical Magazine Tokyo, 1972
3-Dehydroshikimate hydro-lyase was extracted and partially purified by ammonium sulfate fractionation from the hypocotyls of etiolatedPhaseolus mungo seedings. The enzyme was most active at pH 7.0 and the Km for DHS was 1.4 mM. Enzyme activity was inhibited byp-chloromercuribenzoate and arsenite, the inhibition being reversed by reduced glutathione ...
T. Tateoka
openalex   +2 more sources

Association of the quinate : NAD+ oxidoreductase with one dehydroquinate hydro-lyase isoenzyme in corn seedlings

Plant and Cell Physiology, 1980
Annick Graziana, Annie Boudet, Alain M. Böudet   +2 more
openalex   +2 more sources

[43] d-Deoxy-5-ketoglucarate hydro-lyase (Decarboxylating)

, 1975
S. Dagley, Roger Jeffcoat
openalex   +2 more sources

Über die Reaktion von Carbonat-Hydro-Lyase mit p-Nitrophenylacetat

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1963
Friedhelm Schneider, Manfred Liefländer
openalex   +2 more sources

Über die Reaktion von Carbonat-Hydro-Lyase in schwerem Wasser (D₂O)

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1963
Manfred Liefländer
openalex   +2 more sources

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Characteristics and applications of alginate lyases: A review.

International Journal of Biological Macromolecules, 2020
Brown algae, as the main source of alginate, are a type of marine biomass with a very high output. Alginate, a polysaccharide composed of β-D-mannuronic acid (M) and α-L-guluronic acid (G), has great potential for applications in the food, cosmetic and ...
Danyang Cheng, Chengcheng Jiang, Jiachao Xu, Zhen Liu, Xiangzhao Mao   +4 more
semanticscholar   +1 more source