Artykuły w czasopismach na temat „NADH molecules”
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Wos, M. L., i P. C. Pollard. "Cellular nicotinamide adenine dinucleotide (NADH) as an indicator of bacterial metabolic activity dynamics in activated sludge". Water Science and Technology 60, nr 3 (1.07.2009): 783–91. http://dx.doi.org/10.2166/wst.2009.393.
Pełny tekst źródłaTsai, Hsieh-Chin, Cheng-Hung Hsieh, Ching-Wen Hsu, Yau-Heiu Hsu i Lee-Feng Chien. "Cloning and Organelle Expression of Bamboo Mitochondrial Complex I Subunits Nad1, Nad2, Nad4, and Nad5 in the Yeast Saccharomyces cerevisiae". International Journal of Molecular Sciences 23, nr 7 (6.04.2022): 4054. http://dx.doi.org/10.3390/ijms23074054.
Pełny tekst źródłaQi, Xiangying, Kaiqi Wang, Liping Yang, Zhenshan Deng i Zhihong Sun. "The complete mitogenome sequence of the coral lily (Lilium pumilum) and the Lanzhou lily (Lilium davidii) in China". Open Life Sciences 15, nr 1 (31.12.2020): 1060–67. http://dx.doi.org/10.1515/biol-2020-0102.
Pełny tekst źródłaCronholm, T. "Hydrogen transfer between ethanol molecules during oxidoreduction in vivo". Biochemical Journal 229, nr 2 (15.07.1985): 315–22. http://dx.doi.org/10.1042/bj2290315.
Pełny tekst źródłaJeong, Kang Hwa, Hyun Jin Lee, Young Woo Park i Jae Young Lee. "Structural Basis of Redox-Sensing Transcriptional Repressor Rex with Cofactor NAD+ and Operator DNA". International Journal of Molecular Sciences 23, nr 3 (29.01.2022): 1578. http://dx.doi.org/10.3390/ijms23031578.
Pełny tekst źródłaKolappan, Subramaniapillai, David L. Shen, Renee Mosi, Jianyu Sun, Ernest J. McEachern, David J. Vocadlo i Lisa Craig. "Structures of lactate dehydrogenase A (LDHA) in apo, ternary and inhibitor-bound forms". Acta Crystallographica Section D Biological Crystallography 71, nr 2 (23.01.2015): 185–95. http://dx.doi.org/10.1107/s1399004714024791.
Pełny tekst źródłaKim, Youngnyun, L. O. Ingram i K. T. Shanmugam. "Dihydrolipoamide Dehydrogenase Mutation Alters the NADH Sensitivity of Pyruvate Dehydrogenase Complex of Escherichia coli K-12". Journal of Bacteriology 190, nr 11 (28.03.2008): 3851–58. http://dx.doi.org/10.1128/jb.00104-08.
Pełny tekst źródłaLiao, Yuqin, Ruiyun You, Min Fan, Shangyuan Feng, Dechan Lu i Yudong Lu. "Determination of NADH by Surface Enhanced Raman Scattering Using Au@MB@Ag NPs". Australian Journal of Chemistry 74, nr 10 (2021): 722. http://dx.doi.org/10.1071/ch21178.
Pełny tekst źródłaTedokon, M., K. Suzuki, Y. Kayamori, S. Fujita i Y. Katayama. "Enzymatic Assay of Inorganic Phosphate with Use of Sucrose Phosphorylase and Phosphoglucomutase". Clinical Chemistry 38, nr 4 (1.04.1992): 512–15. http://dx.doi.org/10.1093/clinchem/38.4.512.
Pełny tekst źródłaRuiz, Lorena, Miguel Gueimonde, Patricia Ruas-Madiedo, Angela Ribbera, Clara G. de los Reyes-Gavilán, Marco Ventura, Abelardo Margolles i Borja Sánchez. "Molecular Clues To Understand the Aerotolerance Phenotype of Bifidobacterium animalis subsp. lactis". Applied and Environmental Microbiology 78, nr 3 (18.11.2011): 644–50. http://dx.doi.org/10.1128/aem.05455-11.
Pełny tekst źródłaWang, Pinpin, Kai Liu, Huanqing Ma, Hao Nian, Yawen Li, Qingfang Li, Lin Cheng i Liping Cao. "Synthesis and aqueous anion recognition of an imidazolium-based nonacationic cup". Chemical Communications 57, nr 98 (2021): 13377–80. http://dx.doi.org/10.1039/d1cc05603d.
Pełny tekst źródłaSingh, Ruchi, Rajesh K. Yadav, Ravindra K. Shukla, Satyam Singh, Atul P. Singh, Dilip K. Dwivedi, Ahmad Umar i Navneet K. Gupta. "Highly Selective Nitrogen-Doped Graphene Quantum Dots/Eriochrome Cyanine Composite Photocatalyst for NADH Regeneration and Coupling of Benzylamine in Aerobic Condition under Solar Light". Catalysts 13, nr 1 (14.01.2023): 199. http://dx.doi.org/10.3390/catal13010199.
Pełny tekst źródłaMaeda, K., K. Truscott, X. L. Liu i R. K. Scopes. "A thermostable NADH oxidase from anaerobic extreme thermophiles". Biochemical Journal 284, nr 2 (1.06.1992): 551–55. http://dx.doi.org/10.1042/bj2840551.
Pełny tekst źródłaГорбунова, И. А., М. Э. Сасин i О. С. Васютинский. "Достижение субпикосекундного временного разрешения при исследовании процессов анизотропной релаксации биологических молекул". Письма в журнал технической физики 46, nr 4 (2020): 7. http://dx.doi.org/10.21883/pjtf.2020.04.49041.18062.
Pełny tekst źródłaDi Spiridione, Carmela, Michele Aresta i Angela Dibenedetto. "Improving the Enzymatic Cascade of Reactions for the Reduction of CO2 to CH3OH in Water: From Enzymes Immobilization Strategies to Cofactor Regeneration and Cofactor Suppression". Molecules 27, nr 15 (2.08.2022): 4913. http://dx.doi.org/10.3390/molecules27154913.
Pełny tekst źródłaTrisolini, Lucia, Nicola Gambacorta, Ruggiero Gorgoglione, Michele Montaruli, Luna Laera, Francesco Colella, Mariateresa Volpicella, Anna De Grassi i Ciro Leonardo Pierri. "FAD/NADH Dependent Oxidoreductases: From Different Amino Acid Sequences to Similar Protein Shapes for Playing an Ancient Function". Journal of Clinical Medicine 8, nr 12 (2.12.2019): 2117. http://dx.doi.org/10.3390/jcm8122117.
Pełny tekst źródłaEl-Sayed, Ivan, Xiaohua Huang, Fima Macheret, Joseph Oren Humstoe, Randall Kramer i Mostafa El-Sayed. "Effect of Plasmonic Gold Nanoparticles on Benign and Malignant Cellular Autofluorescence: A Novel Probe for Fluorescence Based Detection of Cancer". Technology in Cancer Research & Treatment 6, nr 5 (październik 2007): 403–12. http://dx.doi.org/10.1177/153303460700600505.
Pełny tekst źródłaKmita, H., O. Stobienia i J. Michejda. "The access of metabolites into yeast mitochondria in the presence and absence of the voltage dependent anion selective channel (YVDAC1)." Acta Biochimica Polonica 46, nr 4 (31.12.1999): 991–1000. http://dx.doi.org/10.18388/abp.1999_4124.
Pełny tekst źródłaZhao, Li-Jun, Ruo-Can Qian, Wei Ma, He Tian i Yi-Tao Long. "Electrocatalytic Efficiency Analysis of Catechol Molecules for NADH Oxidation during Nanoparticle Collision". Analytical Chemistry 88, nr 17 (9.08.2016): 8375–79. http://dx.doi.org/10.1021/acs.analchem.6b02365.
Pełny tekst źródłaHarbut, Michael B., Baiyuan Yang, Renhe Liu, Takahiro Yano, Catherine Vilchèze, Bo Cheng, Jonathan Lockner i in. "Small Molecules Targeting Mycobacterium tuberculosis Type II NADH Dehydrogenase Exhibit Antimycobacterial Activity". Angewandte Chemie 130, nr 13 (22.02.2018): 3536–40. http://dx.doi.org/10.1002/ange.201800260.
Pełny tekst źródłaHarbut, Michael B., Baiyuan Yang, Renhe Liu, Takahiro Yano, Catherine Vilchèze, Bo Cheng, Jonathan Lockner i in. "Small Molecules Targeting Mycobacterium tuberculosis Type II NADH Dehydrogenase Exhibit Antimycobacterial Activity". Angewandte Chemie International Edition 57, nr 13 (22.02.2018): 3478–82. http://dx.doi.org/10.1002/anie.201800260.
Pełny tekst źródłaCho, Eun Jeong, Ashwini K. Devkota, Gabriel Stancu, Ramakrishna Edupunganti, Garth Powis i Kevin N. Dalby. "A Fluorescence-Based High-Throughput Assay for the Identification of Anticancer Reagents Targeting Fructose-1,6-Bisphosphate Aldolase". SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, nr 1 (18.08.2017): 1–10. http://dx.doi.org/10.1177/2472555217726325.
Pełny tekst źródłaShidhi, Pattayampadam Ramakrishnan, Vadakkemukadiyil Chellappan Biju, Sasi Anu, Chandrasekharan Laila Vipin, Kumar Raveendran Deelip i Sukumaran Nair Achuthsankar. "Genome Characterization, Comparison and Phylogenetic Analysis of Complete Mitochondrial Genome of Evolvulus alsinoides Reveals Highly Rearranged Gene Order in Solanales". Life 11, nr 8 (30.07.2021): 769. http://dx.doi.org/10.3390/life11080769.
Pełny tekst źródłaFu, Yan-Hua, Zhen Wang, Kai Wang, Guang-Bin Shen i Xiao-Qing Zhu. "Evaluation and comparison of antioxidant abilities of five bioactive molecules with C–H and O–H bonds in thermodynamics and kinetics". RSC Advances 12, nr 42 (2022): 27389–95. http://dx.doi.org/10.1039/d2ra04839f.
Pełny tekst źródłaAndrade, Susana L. A., Eric V. Patridge, James G. Ferry i Oliver Einsle. "Crystal Structure of the NADH:Quinone Oxidoreductase WrbA from Escherichia coli". Journal of Bacteriology 189, nr 24 (19.10.2007): 9101–7. http://dx.doi.org/10.1128/jb.01336-07.
Pełny tekst źródłaCafaro, Valeria, Viviana Izzo, Roberta Scognamiglio, Eugenio Notomista, Paola Capasso, Annarita Casbarra, Piero Pucci i Alberto Di Donato. "Phenol Hydroxylase and Toluene/o-Xylene Monooxygenase from Pseudomonas stutzeri OX1: Interplay between Two Enzymes". Applied and Environmental Microbiology 70, nr 4 (kwiecień 2004): 2211–19. http://dx.doi.org/10.1128/aem.70.4.2211-2219.2004.
Pełny tekst źródłaZabolotny, M. A., Yu M. Barabash, N. P. Kulish, O. P. Dmitrenko i M. O. Kuzmenko. "Conformational states of NADH molecules in a hydrated shell under weak electromagnetic irradiation". Biophysics 60, nr 1 (styczeń 2015): 35–42. http://dx.doi.org/10.1134/s0006350915010261.
Pełny tekst źródłaBloem, Audrey, Isabelle Sanchez, Sylvie Dequin i Carole Camarasa. "Metabolic Impact of Redox Cofactor Perturbations on the Formation of Aroma Compounds in Saccharomyces cerevisiae". Applied and Environmental Microbiology 82, nr 1 (16.10.2015): 174–83. http://dx.doi.org/10.1128/aem.02429-15.
Pełny tekst źródłaHòa, Lê Thanh, Nguyễn Thị Khuê, Nguyễn Thị Bích Nga, Đỗ Thị Roan, Đỗ Trung Dũng, Lê Thị Kim Xuyến i Đoàn Thị Thanh Hương. "Genetic characterization of mitochondrial genome of the small intestinal fluke, Haplorchis taichui (Trematoda: Heterophyidae), Vietnamese sample". Vietnam Journal of Biotechnology 14, nr 2 (30.06.2016): 215–24. http://dx.doi.org/10.15625/1811-4989/14/2/9333.
Pełny tekst źródłaSchneckenburger, H., P. Gessler i I. Pavenstädt-Grupp. "Measurements of mitochondrial deficiencies in living cells by microspectrofluorometry." Journal of Histochemistry & Cytochemistry 40, nr 10 (październik 1992): 1573–78. http://dx.doi.org/10.1177/40.10.1527376.
Pełny tekst źródłaChen, Siqi, Yuanbing Wang, Kongfu Zhu i Hong Yu. "Mitogenomics, Phylogeny and Morphology Reveal Ophiocordyceps pingbianensis Sp. Nov., an Entomopathogenic Fungus from China". Life 11, nr 7 (14.07.2021): 686. http://dx.doi.org/10.3390/life11070686.
Pełny tekst źródłaHeslop, Kareem A., Pieter Burger, Monika Gooz, Amandine Rovini, Thomas Benton, Catherine Mills, Patrick Woster i Eduardo N. Maldonado. "Small molecules targeting the VDAC-NADH binding pocket modulate mitochondrial metabolism in cancer cells". Biophysical Journal 121, nr 3 (luty 2022): 316a. http://dx.doi.org/10.1016/j.bpj.2021.11.1175.
Pełny tekst źródłaNowall, Wilbur B., i Werner G. Kuhr. "Electrocatalytic Surface for the Oxidation of NADH and Other Anionic Molecules of Biological Significance". Analytical Chemistry 67, nr 19 (październik 1995): 3583–88. http://dx.doi.org/10.1021/ac00115a031.
Pełny tekst źródłaValentini, Federica, Silvia Orlanducci, M. L. Terranova i Giuseppe Palleschi. "Fabrication Routes of Microsized Electrochemical Biosensors Based on Single-Walled Carbon Nanotubes". Materials Science Forum 539-543 (marzec 2007): 1098–103. http://dx.doi.org/10.4028/www.scientific.net/msf.539-543.1098.
Pełny tekst źródłaYoshioka, Shota, Sota Nimura, Masayuki Naruto i Susumu Saito. "Reaction of H2 with mitochondria-relevant metabolites using a multifunctional molecular catalyst". Science Advances 6, nr 43 (październik 2020): eabc0274. http://dx.doi.org/10.1126/sciadv.abc0274.
Pełny tekst źródłaMikšanová, Markéta, Jiří Hudeček, Jan Páca i Marie Stiborová. "To the Mechanism of Horseradish Peroxidase-Mediated Degradation of a Recalcitrant Dye Remazol Brilliant Blue R". Collection of Czechoslovak Chemical Communications 66, nr 4 (2001): 663–75. http://dx.doi.org/10.1135/cccc20010663.
Pełny tekst źródłaAllali, Naoual, Veronika Urbanova, Mathieu Etienne, Xavier Devaux, Martine Mallet, Brigitte Vigolo, Jean-Joseph Adjizian i in. "Accurate control of the covalent functionalization of single-walled carbon nanotubes for the electro-enzymatically controlled oxidation of biomolecules". Beilstein Journal of Nanotechnology 9 (26.10.2018): 2750–62. http://dx.doi.org/10.3762/bjnano.9.257.
Pełny tekst źródłaMatic, Sandra, Daniela A. Geisler, Ian M. Møller, Susanne Widell i Allan G. Rasmusson. "Alamethicin permeabilizes the plasma membrane and mitochondria but not the tonoplast in tobacco (Nicotiana tabacum L. cv Bright Yellow) suspension cells". Biochemical Journal 389, nr 3 (26.07.2005): 695–704. http://dx.doi.org/10.1042/bj20050433.
Pełny tekst źródłaHeslop, Kareem A., Pieter Burger, Christiana Kappler, Ashish K. Solanki, Monika Gooz, Yuri K. Peterson, Catherine Mills i in. "Small molecules targeting the NADH-binding pocket of VDAC modulate mitochondrial metabolism in hepatocarcinoma cells". Biomedicine & Pharmacotherapy 150 (czerwiec 2022): 112928. http://dx.doi.org/10.1016/j.biopha.2022.112928.
Pełny tekst źródłaYu, Steve S. F., Kelvin H. C. Chen, Mandy Y. H. Tseng, Yane-Shih Wang, Chiu-Feng Tseng, Yu-Ju Chen, Ded-Shih Huang i Sunney I. Chan. "Production of High-Quality Particulate Methane Monooxygenase in High Yields from Methylococcus capsulatus (Bath) with a Hollow-Fiber Membrane Bioreactor". Journal of Bacteriology 185, nr 20 (15.10.2003): 5915–24. http://dx.doi.org/10.1128/jb.185.20.5915-5924.2003.
Pełny tekst źródłaPérez-Pinzón, Miguel A., Patricia L. Mumford, VeróAnica Carranza i Thomas J. Sick. "Calcium Influx from the Extracellular Space Promotes NADH Hyperoxidation and Electrical Dysfunction after Anoxia in Hippocampal Slices". Journal of Cerebral Blood Flow & Metabolism 18, nr 2 (luty 1998): 215–21. http://dx.doi.org/10.1097/00004647-199802000-00013.
Pełny tekst źródłaNakatani, Yoshio, Wanting Jiao, David Aragão, Yosuke Shimaki, Jessica Petri, Emily J. Parker i Gregory M. Cook. "Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 Å". Acta Crystallographica Section F Structural Biology Communications 73, nr 10 (23.09.2017): 541–49. http://dx.doi.org/10.1107/s2053230x17013073.
Pełny tekst źródłaMa, Liang, Shuting Lv, Jianxin Tang, Jianxin Liu, Wen Li, Jing Deng, Yan Deng, Jingjing Du, Xueying Liu i Xiaoxi Zeng. "Study on bioactive molecules involved in extracellular biosynthesis of silver nanoparticles by Penicillium aculeatum Su1". Materials Express 9, nr 5 (1.08.2019): 475–83. http://dx.doi.org/10.1166/mex.2019.1508.
Pełny tekst źródłaBottoni, Patrizia, Giulia Gionta i Roberto Scatena. "Remarks on Mitochondrial Myopathies". International Journal of Molecular Sciences 24, nr 1 (21.12.2022): 124. http://dx.doi.org/10.3390/ijms24010124.
Pełny tekst źródłaKaragüler, N. G., R. B. Sessions, B. Binay, E. B. Ordu i A. R. Clarke. "Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH". Biochemical Society Transactions 35, nr 6 (23.11.2007): 1610–15. http://dx.doi.org/10.1042/bst0351610.
Pełny tekst źródłaLaroussi, Arwa, Małgorzata Kot, Jan Ingo Flege, Noureddine Raouafi i Vladimir Mirsky. "Self-Assembled Monolayers from Symmetrical Di-Thiols: Preparation, Characterization and Application for the Assembly of Electrochemically Active Films". Engineering Proceedings 6, nr 1 (17.05.2021): 17. http://dx.doi.org/10.3390/i3s2021dresden-10112.
Pełny tekst źródłaBlatter, E. E., M. L. Tasayco, G. Prestwich i R. Pietruszko. "Chemical modification of aldehyde dehydrogenase by a vinyl ketone analogue of an insect pheromone". Biochemical Journal 272, nr 2 (1.12.1990): 351–58. http://dx.doi.org/10.1042/bj2720351.
Pełny tekst źródłaMoreau, Patrice L. "Diversion of the Metabolic Flux from Pyruvate Dehydrogenase to Pyruvate Oxidase Decreases Oxidative Stress during Glucose Metabolism in Nongrowing Escherichia coli Cells Incubated under Aerobic, Phosphate Starvation Conditions". Journal of Bacteriology 186, nr 21 (1.11.2004): 7364–68. http://dx.doi.org/10.1128/jb.186.21.7364-7368.2004.
Pełny tekst źródłaOhnishi, S. Tsuyoshi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa i Tomoko Ohnishi. "EPR detection of protein-associated ubiquinone molecules in purified bovine heart NADH–ubiquinone oxidoreductase (complex I)". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1797 (lipiec 2010): 21–22. http://dx.doi.org/10.1016/j.bbabio.2010.04.082.
Pełny tekst źródłaFolkerts, O., i M. R. Hanson. "The male sterility-associated pcf gene and the normal atp9-1 gene in Petunia are located on different mitochondrial DNA molecules." Genetics 129, nr 3 (1.11.1991): 885–95. http://dx.doi.org/10.1093/genetics/129.3.885.
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