enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Nicotinamide phosphoribosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_phosphoribosy...

    Because cancer cells utilize increased glycolysis, and because NAD enhances glycolysis, iNAMPT is often amplified in cancer cells. [33] [34] APO866 is an experimental drug that inhibits this enzyme. [35] It is being tested for treatment of advanced melanoma, cutaneous T-cell lymphoma (CTL), and refractory or relapsed B-chronic lymphocytic leukemia.

  3. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    Glycosylation is the process by which a carbohydrate is covalently attached to a target macromolecule, typically proteins and lipids. This modification serves various functions. [5] For instance, some proteins do not fold correctly unless they are glycosylated. [2]

  4. Nicotinamide adenine dinucleotide phosphate - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    NADPH is the reduced form, whereas NADP + is the oxidized form. NADP + is used by all forms of cellular life. NADP + is essential for life because it is needed for cellular respiration. [3] NADP + differs from NAD + by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety.

  5. Phosphoinositide 3-kinase - Wikipedia

    en.wikipedia.org/wiki/Phosphoinositide_3-kinase

    The distinct feature of Class II PI3Ks is the C-terminal C2 domain. This domain lacks critical Asp residues to coordinate binding of Ca 2+, which suggests class II PI3Ks bind lipids in a Ca 2+-independent manner. Class II comprises three catalytic isoforms (C2α, C2β, and C2γ), but, unlike Classes I and III, no regulatory proteins.

  6. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [3]

  7. Pentose phosphate pathway - Wikipedia

    en.wikipedia.org/wiki/Pentose_phosphate_pathway

    While the pentose phosphate pathway does involve oxidation of glucose, its primary role is anabolic rather than catabolic. The pathway is especially important in red blood cells (erythrocytes). The reactions of the pathway were elucidated in the early 1950s by Bernard Horecker and co-workers. [2] [3] There are two distinct phases in the pathway.

  8. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    For example, in the enzyme-catalyzed reactions of glycolysis, accumulation phosphoenol is catalyzed by pyruvate kinase into pyruvate. Alanine is an amino acid which is synthesized from pyruvate also inhibits the enzyme pyruvate kinase during glycolysis. Alanine is a non-competitive inhibitor, therefore it binds away from the active site to the ...

  9. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    Glycolysis is an essential process of glucose degrading into two molecules of pyruvate, through various steps, with the help of different enzymes. It occurs in ten steps and proves that phosphorylation is a much required and necessary step to attain the end products.