Relevant bibliographies by topics / NAD-bound

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'NAD-bound'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "NAD-bound"

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Kalinina, Sviatlana, Christian Freymueller, Nilanjon Naskar, et al. "Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques." International Journal of Molecular Sciences 22, no. 11 (2021): 5952. http://dx.doi.org/10.3390/ijms22115952.

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Metabolic FLIM (fluorescence lifetime imaging) is used to image bioenergetic status in cells and tissue. Whereas an attribution of the fluorescence lifetime of coenzymes as an indicator for cell metabolism is mainly accepted, it is debated whether this is valid for the redox state of cells. In this regard, an innovative algorithm using the lifetime characteristics of nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD) to calculate the fluorescence lifetime induced redox ratio (FLIRR) has been reported so far. We extended the FLIRR approach and present
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Kim, Yong Ju. "A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase." Acta Crystallographica Section F Structural Biology Communications 74, no. 5 (2018): 277–82. http://dx.doi.org/10.1107/s2053230x18004557.

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the thr
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Galloway, T. S., R. M. Tait, and S. van Heyningen. "Photolabelling of cholera toxin by NAD+." Biochemical Journal 242, no. 3 (1987): 927–30. http://dx.doi.org/10.1042/bj2420927.

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When cholera toxin is incubated under u.v. light with NAD+ labelled in either the adenine or the nicotinamide moiety, radioactivity becomes covalently bound to the protein. The reaction is specific for cholera toxin, and is inhibited by excess unlabelled NAD+ or NAD analogues. Only the active A 1 chain of the toxin is labelled. The u.v.-absorption spectrum of the product is very similar to that of NAD+, and shows the same reaction with cyanide. The nature of the product is therefore different from that found when diphtheria toxin is photolabelled [Carroll & Collier (1984) Proc. Natl. Acad.
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Bell, Charles E., Todd O. Yeates, and David Eisenberg. "Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: A comparison with NAD bound to the oxidoreductase enzymes." Protein Science 6, no. 10 (2008): 2084–96. http://dx.doi.org/10.1002/pro.5560061004.

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Aguilar-Arnal, Lorena, Suman Ranjit, Chiara Stringari, Ricardo Orozco-Solis, Enrico Gratton, and Paolo Sassone-Corsi. "Spatial dynamics of SIRT1 and the subnuclear distribution of NADH species." Proceedings of the National Academy of Sciences 113, no. 45 (2016): 12715–20. http://dx.doi.org/10.1073/pnas.1609227113.

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Sirtuin 1 (SIRT1) is an NAD+-dependent deacetylase that functions as metabolic sensor of cellular energy and modulates biochemical pathways in the adaptation to changes in the environment. SIRT1 substrates include histones and proteins related to enhancement of mitochondrial function as well as antioxidant protection. Fluctuations in intracellular NAD+ levels regulate SIRT1 activity, but how SIRT1 enzymatic activity impacts on NAD+ levels and its intracellular distribution remains unclear. Here, we show that SIRT1 determines the nuclear organization of protein-bound NADH. Using multiphoton mic
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Hu, Yumei, Weidong Liu, Satish R. Malwal, et al. "Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms." Angewandte Chemie 127, no. 51 (2015): 15698–702. http://dx.doi.org/10.1002/ange.201508310.

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Hu, Yumei, Weidong Liu, Satish R. Malwal, et al. "Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms." Angewandte Chemie International Edition 54, no. 51 (2015): 15478–82. http://dx.doi.org/10.1002/anie.201508310.

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Cummings, M. D., T. N. Hart, B. Hazes, and R. J. Read. "Modeling the structure of NAD bound to pertussis toxin." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C88. http://dx.doi.org/10.1107/s0108767396095566.

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Thomas, Leonard M., Angelica R. Harper, Whitney A. Miner, et al. "Structure ofEscherichia coliAdhP (ethanol-inducible dehydrogenase) with bound NAD." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 7 (2013): 730–32. http://dx.doi.org/10.1107/s1744309113015170.

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Niesner, R., P. Narang, H. Spiecker, V. Andresen, K. H. Gericke, and M. Gunzer. "Selective Detection of NADPH Oxidase in Polymorphonuclear Cells by Means of NAD(P)H-Based Fluorescence Lifetime Imaging." Journal of Biophysics 2008 (November 16, 2008): 1–13. http://dx.doi.org/10.1155/2008/602639.

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NADPH oxidase (NOX2) is a multisubunit membrane-bound enzyme complex that, upon assembly in activated cells, catalyses the reduction of free oxygen to its superoxide anion, which further leads to reactive oxygen species (ROS) that are toxic to invading pathogens, for example, the fungus Aspergillus fumigatus. Polymorphonuclear cells (PMNs) employ both nonoxidative and oxidative mechanisms to clear this fungus from the lung. The oxidative mechanisms mainly depend on the proper assembly and function of NOX2. We identified for the first time the NAD(P)H-dependent enzymes involved in such oxidativ
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Dissertations / Theses on the topic "NAD-bound"

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Naylor, Claire. "X-ray crystallographic studies of glucose 6-phosphate dehydrogenase." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.360467.

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Vanhooke, Janeen LaVay. "E. coli UDP-galactose 4-epimerase active site nucleotide content, oxidation of enzyme-bound NADH and the effect of uridine nucleotide binding on the classical raman spectrum of enzyme-bound [4-²H]NAD⁺ /." 1993. http://catalog.hathitrust.org/api/volumes/oclc/31387367.html.

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Raclavský, Marek. "Algebraické nerovnice nad reálnými čísly." Master's thesis, 2017. http://www.nusl.cz/ntk/nusl-357111.

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This thesis analyses the semialgebraic sets, that is, a finite union of solu- tions to a finite sequence of polynomial inequalities. We introduce a notion of cylindrical algebraic decomposition as a tool for the construction of a semialge- braic stratification and a triangulation of a semialgebraic set. On this basis, we prove several important and well-known results of real algebraic geometry, such as Hardt's semialgebraic triviality or Sard's theorem. Drawing on Morse theory, we finally give a proof of a Thom-Milnor bound for a sum of Betti numbers of a real algebraic set. 1
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Book chapters on the topic "NAD-bound"

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Askerlund, Per, Christer Larsson, and Susanne Widell. "Localisation of Donor and Acceptor Sites of NAD(P)H Dehydrogenase(S) Using “Inside-Out” and “Right-Side-Out” Plant Plasma Membrane Vesicles, and Characterization of Plasma Membrane-Bound b-Cytochromes." In Plasma Membrane Oxidoreductases in Control of Animal and Plant Growth. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-8029-0_44.

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Okada, Hirosuke, and Itaru Urabe. "[4] Polymerizable NAD derivative and model enzyme reactor with recycling of polyethylene glycol-bound NAD." In Immobilized Enzymes and Cells, Part C. Elsevier, 1987. http://dx.doi.org/10.1016/s0076-6879(87)36006-9.

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Conference papers on the topic "NAD-bound"

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Sharick, Joe T., Peter F. Favreau, Amani A. Gillette, Sophia M. Sdao, Matthew J. Merrins, and Melissa C. Skala. "Protein-bound NAD(P)H lifetime is sensitive to multiple fates of glucose carbon (Conference Presentation)." In Biophysics, Biology and Biophotonics III: the Crossroads, edited by Adam Wax and Vadim Backman. SPIE, 2018. http://dx.doi.org/10.1117/12.2287873.

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You might also be interested in the extended bibliographies on the topic 'NAD-bound' for particular source types:
Journal articles
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