Results 121 to 130 of about 9,389 (177)

First Experience with Hypothermic Oxygenated Perfusion in Human Uteri: Feasibility and Metabolic Characterization. [PDF]

J Clin Med
Sun K, Eshraghi N, Fernandes FW, Satish S, Jiao C, Yildirim FS, Crasta G, Karakaya OF, Takase K, Horie H, Keslar KS, Isaacson D, Baldwin W, Fairchild RL, Hashimoto K, Pita A, Wee A, AlHilli M, Miller C, Eltemamy M, Falcone T, Tzakis A, Richards E, Schlegel A.   +23 more
europepmc   +1 more source

A Novel POR G88S Mutation Causes Severe PORD and Establishes a Critical Pharmacogenomic Risk Profile.

J Clin Endocrinol Metab
Rojas Velazquez MN, Lopez Dacal J, Jørgensen FS, Sanguineti N, Sharma K, Marino R, Pérez Garrido N, Vaiani E, Ramírez P, Scaglia P, Izquierdo A, Sansó G, Ropelato MG, Bergadá I, Rey RA, Grinspon RP, Pandey AV.   +16 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Direct evolution of riboflavin kinase significantly enhance flavin mononucleotide synthesis by design and optimization of flavin mononucleotide riboswitch

Bioresource Technology, 2023
Flavin mononucleotide (FMN) is the active form of riboflavin. It has a wide range of application scenarios in the pharmaceutical and food additives. However, there are limitations in selecting generic high-throughput screening platforms that improve the properties of enzymes.
Xuewei Pan, Rongshuai Zhu, Jiajia You
exaly   +3 more sources

Flavin mononucleotide reductase of luminous bacteria

Molecular and Cellular Biochemistry, 1975
NAD(P)H: FMN oxidoreductase (flavin reductase) couples in vitro to bacterial luciferase. This reductase, which is also postulated to supply reduced flavin mononucleotide in vivo as a substrate for the bioluminescent reaction, has been partially purified and characterized from two species of luminous bacterial.
W, Duane, J W, Hastings
openaire   +2 more sources

Analysis of the reduction of nitroxides by flavin mononucleotide

Biochimica et Biophysica Acta (BBA) - General Subjects, 1990
This article describes a simple method to prepare hydroxylamines from nitroxides by photo-activated flavin mononucleotide. The half-time of reduction varied from 2 to 38.4 s for a series of nitroxides. For most nitroxides short exposures to light (min) were sufficient to produce significant amounts of hydroxylamine; longer periods of exposure increased
P D, Morse, E K, Ruuge, M J, Petro, H M, Swartz   +3 more
openaire   +2 more sources

Bacterial Flavin Mononucleotide Riboswitches as Targets for Flavin Analogs

2013
Roseoflavin is a toxic riboflavin (vitamin B2) analog and naturally is produced by Streptomyces davawensis. Roseoflavin is converted to roseoflavin mononucleotide (RoFMN) by promiscuous flavokinases (EC 2.7.1.26). Flavin mononucleotide (FMN) riboswitches control the expression of genes involved in riboflavin biosynthesis and/or transport.
Danielle Biscaro, Pedrolli, Matthias, Mack   +1 more
openaire   +2 more sources

The enthalpy of oxidation of flavin mononucleotide

Archives of Biochemistry and Biophysics, 1974
Abstract The oxidation enthalpy of reduced flavin mononucleotide at pH 7.0 in 0.2 m phosphate buffer has been studied by determining the heat associated with the reaction: FMNH 2 + 2 Fe(CN) −3 6 ⇌ FMN + 2 Fe(CN) −4 6 + 2 H + . (a) (The quinone, semiquinone, and hydroquinone forms of FMN are represented as FMN, FMNH, and FMNH 2 , respectively.)
Norman V. Beaudette, Neal Langerman
openaire   +1 more source

Flavin Mononucleotide-Binding Fluorescent Proteins

2013
Flavin mononucleotide (FMN)-binding fluorescent proteins (FbFPs) are novel reporters for cell microscopy, outperforming green fluorescent proteins (GFP) and derivatives in anaerobic or microaerobic environments (Figure 1). Furthermore they are better suited for incorporation into small-sized genomes and for following viral infections, protein ...
Losi, Aba, Viappiani, Cristiano
openaire   +5 more sources