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Positive cofactor

TBP TATA box binding protein, TAF TATA box binding protein associated factor, SRB suppressor of RNA polymerase B, CTD C-terminal domain of RNA polymerase II, PC positive cofactor, NC negative cofactor, HMG high mobihty group proteins, UAS upstream activating sequence. [Pg.50]

J. D. Fondell, M. Guermah, S. Malik, and R G. Roeder. Thyroid hormone receptor-associated proteins and general positive cofactors mediate thyroid hormone receptor function in the absence of the TATA box-binding protein-associated factors of TFIID. Proc Nad Acad. Sci, VSA, 96 (5), 1959-1964, 1999. [Pg.208]

Taken together, PARP-1 seems to be an essential structural/ architectural positive cofactor of NF-kB, which could act in concert with p300 to help facilitating the formation and subsequent activation of the pre-initiation complex (PIC) during pathological processes in inflammatory disorders, in a stimuli-dependent manner. [Pg.83]

Query Proteins with significant similarity (bacterial genus— GenBank/NCBI identifier) Identity (positives ) Cofactor... [Pg.432]

Figure Bl.15.16. Two-pulse ESE signal intensity of the chemically reduced ubiqumone-10 cofactor in photosynthetic bacterial reaction centres at 115 K. MW frequency is 95.1 GHz. One dimension is the magnetic field value Bq, the other dimension is the pulse separation x. The echo decay fiinction is anisotropic with respect to the spectral position. Figure Bl.15.16. Two-pulse ESE signal intensity of the chemically reduced ubiqumone-10 cofactor in photosynthetic bacterial reaction centres at 115 K. MW frequency is 95.1 GHz. One dimension is the magnetic field value Bq, the other dimension is the pulse separation x. The echo decay fiinction is anisotropic with respect to the spectral position.
A different mechanism operates in the wheat germ enzyme. 2,3-Bisphosphoglycerate is not a cofactor. Instead, the enzyme carries out intra-molecular phosphoryl group transfer (Figure 19.25). The C-3 phosphate is transferred to an active-site residue and then to the C-2 position of the original substrate molecule to form the product, 2-phosphoglycerate. [Pg.628]

The human PR exists as two functionally distinct isoforms PRA and PRB transcribed from two promoters from a single gene. PRA lacks the N-terminal 164 aa and is a 769 aa protein. PRB functions as a transcriptional activator in most cell and promoter contexts. In contrast, PRA is transcriptionally inactive and functions as a strong ligand-dependent transdominant repressor of SHR transcriptional activity. Different cofactor interactions were demonstrated for PRA and PRB, probably due to an inhibitory domain within the first 140 aa of PRA, which is masked in PRB. Both PR isoforms however, repress estradiol-induced ER activity when liganded. Several other mRNA isoforms are present in PR-positive tissues such as breast cancer with unknown clinical significance. [Pg.1130]

The best cofactors are typically flavonoid derivatives that contain many hydroxyl groups, the most favorable at position 3 of the flavones. The strongest cofactors have electron-rich systems that associate with electron-poor compounds such as the flavylium cation. [Pg.265]

Many dehydrogenase enzymes catalyze oxidation/reduction reactions with the aid of nicotinamide cofactors. The electrochemical oxidation of nicotinamide adeniiw dinucleotide, NADH, has been studied in depthThe direct oxidation of NADH has been used to determine concentration of ethanol i s-isv, i62) lactate 157,160,162,163) pyTuvate 1 ), glucose-6-phosphate lactate dehydrogenase 159,161) alanine The direct oxidation often entails such complications as electrode surface pretreatment, interferences due to electrode operation at very positive potentials, and electrode fouling due to adsorption. Subsequent reaction of the NADH with peroxidase allows quantitation via the well established Clark electrode. [Pg.65]

Figure 18.4 Structures of heme/Cu oxidases at different levels of detail, (a) Position of the redox-active cofactors relative to the membrane of CcO (left, only two obligatory subunits are shown) and quinol oxidase (right), (b) Electron transfer paths in mammalian CcO. Note that the imidazoles that ligate six-coordinate heme a and the five-coordinate heme are linked by a single amino acid, which can serve as a wire for electron transfer from ferroheme a to ferriheme as. (c) The O2 reduction site of mammalian CcO the numbering of the residues corresponds to that in the crystal structure of bovine heart CcO. The subscript 3 in heme as and heme 03 signifies the heme that binds O2. The structures were generated using coordinates deposited in the Protein Data Bank, lari [Ostermeier et al., 1997] Ifft [Abramson et al., 2000] (a) and locc [Tsukihara et al., 1996] (b, c). Figure 18.4 Structures of heme/Cu oxidases at different levels of detail, (a) Position of the redox-active cofactors relative to the membrane of CcO (left, only two obligatory subunits are shown) and quinol oxidase (right), (b) Electron transfer paths in mammalian CcO. Note that the imidazoles that ligate six-coordinate heme a and the five-coordinate heme are linked by a single amino acid, which can serve as a wire for electron transfer from ferroheme a to ferriheme as. (c) The O2 reduction site of mammalian CcO the numbering of the residues corresponds to that in the crystal structure of bovine heart CcO. The subscript 3 in heme as and heme 03 signifies the heme that binds O2. The structures were generated using coordinates deposited in the Protein Data Bank, lari [Ostermeier et al., 1997] Ifft [Abramson et al., 2000] (a) and locc [Tsukihara et al., 1996] (b, c).
Trace elements are essential cofactors for numerous biochemical processes. Trace elements that are added routinely to PN include zinc, selenium, copper, manganese, and chromium. There are various commercial parenteral trace element formulations that can be added to PN admixtures (e.g., MTE-5 ). Zinc is important for wound healing, and patients with high-output fistulas, diarrhea, burns, and large open wounds may require additional zinc supplementation. Patients may lose as much as 12 to 17 mg zinc per liter of gastrointestinal (GI) output (e.g., from diarrhea or enterocutaneous fistula losses) however, others have demonstrated that 12 mg/day may be adequate to maintain these patients in positive zinc balance.18 Patients with chronic diarrhea, malabsorption, and short-gut syndrome may have increased selenium losses and may require additional selenium supplementation. Patients with severe cholestasis should have copper and manganese... [Pg.1498]


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See also in sourсe #XX -- [ Pg.82 , Pg.83 ]




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Cofactor

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