We never got in on any of the fad areas.

And fad or not, many people say they are worth a try.

Could this be the first big fad of the 2000's?

For a while it was a fad to read his work.

But it could turn out to be just a fad.

I wonder what new fad he has taken up now?

Its long history suggested that the business was not just a fad.

Does that make it a fad or something here to stay?

I remember when ice was a fad a few years back.

What looked like a private fad has become a public function.

The popularity of these works has not been a fad.

"We did not want to be caught up in a fad."

Maybe it was a woman who had joined in the fad.

And she was always on some sort of fad diet.

I think it's pretty clear now that the Internet is not a fad.

Some people said it was just a fad and would disappear.

At the time, many people dismissed it as a California fad.

In recent months the game has become a fad on college campuses.

"The shoe business is too difficult to go with a fad."

IT is a phenomenon, too big to be called just a fad.

Which is what fad phrases are soon likely to become.

He is not at all concerned with fashion or fad.

After all, radio could turn out to be only a passing fad.

Is this some fad that I've somehow been left out of?

The economic fad of the moment is "make America more competitive in the world."

Thus, riboflavin is not technically a nucleotide; the name flavin adenine dinucleotide is a misnomer.

Other coenzymes, flavin adenine dinucleotide (FAD), biotin, and lipoamide, for instance, are covalently bound.

In order to work as a catalyst, GOx requires a cofactor, flavin adenine dinucleotide (FAD).

In 1949 he synthesized adenosine triphosphate (ATP) and flavin adenine dinucleotide (FAD).

In biochemistry, flavin adenine dinucleotide (FAD) is a redox cofactor involved in several important reactions in metabolism.

Inside the mitochondria, AIF folds into its functional configuration by the help of the co-factor, flavin adenine dinucleotide (FAD).

The PHR domain can bind to the flavin adenine dinucleotide (FAD) cofactor and a light-harvesting chromophore.

The renalase protein consists of a secretory signal peptide, a flavin adenine dinucleotide (FAD)-binding region, and an amine oxidase domain.

Similar experiments with D-amino acid oxidase led to the identification of flavin adenine dinucleotide (FAD) as a second form of flavin utilised by enzymes.

Raiczyk GB, Dutta P, Pinto J. Chlorpromazine and quinacrine inhibit flavin adenine dinucleotide biosynthesis in skeletal muscle.

Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin: the flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).

These electron transport proteins are complementary to the non-metal electron transporters nicotinamide adenine dinucleotide (NAD) and flavin adenine dinucleotide (FAD).

Flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) function as coenzymes for a wide variety of oxidative enzymes and remain bound to the enzymes during the oxidation-reduction reactions.

However, two B vitamins, niacin and riboflavin, bind with adenine to form the essential cofactors nicotinamide adenine dinucleotide (NAD) and flavin adenine dinucleotide (FAD), respectively.

Flavin adenine dinucleotide is a group bound to many enzymes including ferredoxin-NADP+ reductase, monoamine oxidase, D-amino acid oxidase, glucose oxidase, xanthine oxidase, and acyl CoA dehydrogenase.

Other names in common use include FAD pyrophosphatase, riboflavin adenine dinucleotide pyrophosphatase, flavin adenine dinucleotide pyrophosphatase, riboflavine adenine dinucleotide pyrophosphatase, and flavine adenine dinucleotide pyrophosphatase.

The flavin moiety is often attached with an adenosine diphosphate to form flavin adenine dinucleotide (FAD), and, in other circumstances, is found as flavin mononucleotide (or FMN), a phosphorylated form of riboflavin.

Defined by their mechanisms, two main classes of histone demethylases exist: a flavin adenine dinucleotide (FAD)-dependent amine oxidase, and an Fe(II) and α-ketoglutarate-dependent dioxygenase, with the general proposed mechanisms shown in the figure below.

Siderophore decomposition or other biological mechanisms can also release iron., especially in the case of catecholates such as ferric-enterobactin, whose reduction potential is too low for reducing agents such as flavin adenine dinucleotide, hence enzymatic degradation is needed to release the iron.

Complex II consists of four protein subunits and contains a bound flavin adenine dinucleotide (FAD) cofactor, iron-sulfur clusters, and a heme group that does not participate in electron transfer to coenzyme Q, but is believed to be important in decreasing production of reactive oxygen species.

University Grants Commission (UGC) Award 1985 for the research paper entitled, 'Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme' which was adjudged as the best publication in 1985 in fundamental research in the field of Biological Sciences in Bangladesh.