Log in

Relevant bibliographies by topics / NAD-bound

Contents

Journal articles
Dissertations / Theses
Book chapters
Conference papers

Academic literature on the topic 'NAD-bound'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'NAD-bound.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "NAD-bound"

1

Kalinina, Sviatlana, Christian Freymueller, Nilanjon Naskar, Bjoern von Einem, Kirsten Reess, Ronald Sroka, and Angelika Rueck. "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 (May 31, 2021): 5952. http://dx.doi.org/10.3390/ijms22115952.

Full text

Abstract:

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 new results, which includes FLIM data of the various enzymes, such as NAD(P)H, FAD, as well as flavin mononucleotide (FMN). Our algorithm uses a two-exponential fitting procedure for the NAD(P)H autofluorescence and a three-exponential fit of the flavin signal. By extending the FLIRR approach, we introduced FLIRR1 as protein-bound NAD(P)H related to protein-bound FAD, FLIRR2 as protein-bound NAD(P)H related to free (unbound) FAD and FLIRR3 as protein-bound NAD(P)H related to protein-bound FMN. We compared the significance of extended FLIRR to the metabolic index, defined as the ratio of protein-bound NAD(P)H to free NAD(P)H. The statistically significant difference for tumor and normal cells was found to be highest for FLIRR1.

APA, Harvard, Vancouver, ISO, and other styles

2

Kim, Yong Ju. "A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase." Acta Crystallographica Section F Structural Biology Communications 74, no. 5 (April 16, 2018): 277–82. http://dx.doi.org/10.1107/s2053230x18004557.

Full text

Abstract:

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 three-dimensional crystal structure of GAPDH treated with trehalose is reported at 2.0 Å resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose-bound ecGAPDH was compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure.

APA, Harvard, Vancouver, ISO, and other styles

3

Galloway, T. S., R. M. Tait, and S. van Heyningen. "Photolabelling of cholera toxin by NAD+." Biochemical Journal 242, no. 3 (March 15, 1987): 927–30. http://dx.doi.org/10.1042/bj2420927.

Full text

Abstract:

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. Sci. U.S.A. 81, 3307-3311] in that the yield is lower, but both moieties of the NAD molecule become bound.

APA, Harvard, Vancouver, ISO, and other styles

4

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 (December 31, 2008): 2084–96. http://dx.doi.org/10.1002/pro.5560061004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

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 (October 24, 2016): 12715–20. http://dx.doi.org/10.1073/pnas.1609227113.

Full text

Abstract:

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 microscopy in live cells, we show that free and bound NADH are compartmentalized inside of the nucleus, and its subnuclear distribution depends on SIRT1. Importantly, SIRT6, a chromatin-bound deacetylase of the same class, does not influence NADH nuclear localization. In addition, using fluorescence fluctuation spectroscopy in single living cells, we reveal that NAD+ metabolism in the nucleus is linked to subnuclear dynamics of active SIRT1. These results reveal a connection between NAD+ metabolism, NADH distribution, and SIRT1 activity in the nucleus of live cells and pave the way to decipher links between nuclear organization and metabolism.

APA, Harvard, Vancouver, ISO, and other styles

6

Hu, Yumei, Weidong Liu, Satish R. Malwal, Yingying Zheng, Xinxin Feng, Tzu-Ping Ko, Chun-Chi Chen, et al. "Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms." Angewandte Chemie 127, no. 51 (November 13, 2015): 15698–702. http://dx.doi.org/10.1002/ange.201508310.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Hu, Yumei, Weidong Liu, Satish R. Malwal, Yingying Zheng, Xinxin Feng, Tzu-Ping Ko, Chun-Chi Chen, et al. "Structures of Iridoid Synthase fromCantharanthus roseuswith Bound NAD+, NADPH, or NAD+/10-Oxogeranial: Reaction Mechanisms." Angewandte Chemie International Edition 54, no. 51 (November 13, 2015): 15478–82. http://dx.doi.org/10.1002/anie.201508310.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

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 (August 8, 1996): C88. http://dx.doi.org/10.1107/s0108767396095566.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Thomas, Leonard M., Angelica R. Harper, Whitney A. Miner, Helen O. Ajufo, Katie M. Branscum, Lydia Kao, and Paul A. Sims. "Structure ofEscherichia coliAdhP (ethanol-inducible dehydrogenase) with bound NAD." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 7 (June 27, 2013): 730–32. http://dx.doi.org/10.1107/s1744309113015170.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

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.

Full text

Abstract:

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 oxidative mechanisms by means of biexponential NAD(P)H-fluorescence lifetime imaging (FLIM). A specific fluorescence lifetime of 3670±140 picoseconds as compared to 1870 picoseconds for NAD(P)H bound to mitochondrial enzymes could be associated with NADPH bound to oxidative enzymes in activated PMNs. Due to its predominance in PMNs and due to the use of selective activators and inhibitors, we strongly believe that this specific lifetime mainly originates from NOX2. Our experiments also revealed the high site specificity of the NOX2 assembly and, thus, of the ROS production as well as the dynamic nature of these phenomena. On the example of NADPH oxidase, we demonstrate the potential of NAD(P)H-based FLIM in selectively investigating enzymes during their cellular function.

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "NAD-bound"

1

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

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

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "NAD-bound"

1

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, 397–98. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-8029-0_44.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

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, 34–45. Elsevier, 1987. http://dx.doi.org/10.1016/s0076-6879(87)36006-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "NAD-bound"

1

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!