Results 271 to 280 of about 125,071 (335)

Keeping up with the nicotinamides: NADP(H), the forgotten circadian cofactor that keeps metabolic time. [PDF]

Life Metab
Palluth L, Takahashi JS, Green CB.
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Emerging Roles of De Novo Proline Biosynthesis in Human Diseases. [PDF]

FASEB Bioadv
Pei E, Ma J.
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Oxidative Stress Induces the Phosphorylation of NAD⁺ to NADP⁺ by NAD Kinase in Cultured Primary Rat Astrocytes. [PDF]

Neurochem Res
Willker JE, Watermann P, Dringen R.
europepmc   +1 more source

Structural organization of photosynthetic apparatus in mesophyll and bundle sheath chloroplasts of C4 plants of NADP-ME subtype

, 2013
Alicja Buczyńska, Wioleta Wasilewska-Dębowska, Anna Drožak, Elżbieta Romanowska   +3 more
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Binding of NAD and NADP dimers to NAD- and NADP-dependent dehydrogenases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Interaction of the electrolytically prepared dimers of nicotinamide adenine nucleotide, (NAD)2, and nicotinamide adenine nucleotide phosphate, (NADP)2, with lactate, alcohol, glyceraldehyde 3-phosphate, alpha-glycerophosphate, glutamate and glucose-6-phosphate dehydrogenase has been studied using the quenching of protein fluorescence, kinetics of ...
J, Kovár, H, Klukanová
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NADP regulates the light activation of NADP-dependent malate dehydrogenase

Planta, 1983
The chloroplastic NADP-dependent malate-dehydrogenase (EC 1.1.1.82) activity is modulated by light and dark. The enzyme is activated upon illumination of intact or broken chloroplasts or by incubation with dithiothreitol, whereas dark has the opposite effect.
R, Scheibe, J P, Jacquot
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Thio-NADP is not an antagonist of NAADP

Cell Biochemistry and Biophysics, 1998
Nicotinic acid adenine dinucleotide phosphate (NAADP) is a metabolite of NADP, which can release Ca2+ from stores that are distinct from those activated by either cyclic ADP-ribose or inositol 1,4,5-trisphosphate (IP3). It has previously been suggested that thio-NADP is a specific antagonist of NAADP (Chini et al. [1995] J. Biol. Chem. 270, 3216-3223).
Dickey, DM, Aarhus, R, Walseth, TF, Lee, HC   +3 more
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Affinity labeling of spinach ferredoxin-NADP+ oxidoreductase with periodate-oxidized NADP+

Archives of Biochemistry and Biophysics, 1984
Periodate-oxidized NADP+ (dialdehyde-NADP+) inactivated soluble ferredoxin-NADP+ oxidoreductase and combined covalently to the enzyme. This inactivation was first order with respect to dialdehyde-NADP+ and followed saturation kinetics, indicating that the enzyme initially forms a reversible complex with the inactivator.
R L, Chan, N, Carrillo
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Complex formation by ferredoxin-NADP+ reductase with ferredoxin or NADP+

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
Abstract Complex formation by ferredoxin-NADP + reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.99.4) with ferredoxin was measured by the independent methods based on the changes of circular dichroism, fluorescence intensity and the chromatographic behavior on a Sephadex G-75 column of the two proteins after mixing.
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