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Topic: Ribonucleotide reductase

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	r2
		If the mechanism of ribonucleotide reductase could be fully understood, the knowledge could be used to restrict DNA synthesis, and therefore restrict the growth of tumors or virus replications (Sjöberg 1983).
		Ribonucleotide diphosphate reductase from aerobic E. coli is archetypal of these enzymes, which contain a diiron cluster and a tyrosyl radical (Stubbe 1989).
		Ribonucleotide reductase is quite puzzling, due to the necessity of both R1 and R2 to form the catalytically active protein.
	www.chem.umn.edu /groups/stankovich/R2.html (2407 words)

	Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia ...
		Mutations in the dnaAN locus increase the expression of the nrdAB operon.
		by overexpressing ribonucleotide reductase and that this suppression
		by the suppressor mutations or by overexpression of ribonucleotide
	www.pnas.org /cgi/content/full/101/19/7439 (4655 words)

	A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase
		Ribonucleotide reductase initiates de nova DNA biosynthesis through the reduction of nucleotides to their corresponding 2$/sp/prime$-deoxynucleotides.
		The active reductase is composed of a catalytic portion (the R1 enzyme) and a cofactor (R2).
		Purine reduction by murine ribonucleotide reductase is shown to be regulated by modulation of the catalytic rate constant (allosteric V system).
	repository.upenn.edu /dissertations/AAI9727295 (372 words)

	Ribonucleotide reductase R2 component is a novel malignancy determinant that cooperates with activated oncogenes to ...
		Ribonucleotide reductase R2 component is a novel malignancy determinant that cooperates with activated oncogenes to determine transformation and malignant potential -- Fan et al.
		Ribonucleotide reductase R2 component is a novel malignancy determinant that cooperates with activated oncogenes to determine transformation and malignant potential
		Ribonucleotide reductase is a highly regulated cell cycle-controlled activity that is essential for DNA synthesis and repair.
	www.pnas.org /cgi/content/full/93/24/14036 (3931 words)

	Synergistic antiviral action of ribonucleotide reductase inhibitors and 3'-azido-3'-deoxythymidine on HIV type 1 ...
		Ribonucleotide reductase inhibitors reduce the cellular supply of DNA precursors(dNTP) by interfering with their de novo synthesis.
		Earlier we demonstrated that ribonucleotide reductase inhibitors--hydroxyurea, and two deoxycytidine analogs specifically active in lymphoid cells--increased the phosphorylation of AZT in CEM cells by prolonging the S phase of the cell cycle.
		A clear synergism between AZT and ribonucleotide reductase inhibitors was observed at nontoxic doses that induced only minor changes in the cellular parameters measured.
	www.aegis.com /aidsline/1996/dec/M96C0638.html (500 words)

	Exposure to Cigarette Tar Inhibits Ribonucleotide Reductase and Blocks Lymphocyte Proliferation -- McCue et al. 165 ...
		Characterization of the free radical of mammalian ribonucleotide reductase.
		Inactivation of ribonucleotide reductase in tumour cells and inhibition of tumour cell growth by p-alkoxyphenols.
		Quenching of the tyrosyl free radical of ribonucleotide reductase by nitric oxide: relationship to cytostasis induced in tumor cells by cytotoxic macrophages.
	www.jimmunol.org /cgi/content/full/165/12/6771 (3641 words)

	Ribonucleotide reductase R2 structure
		Ribbon representation of the oxidised ribonucleotide reductase R2 chain A structure (PDB code 1RIB).
		Nordlund, P. and Eklund, H. Structure and function of the Escherichia coli ribonucleotide reductase protein R2.
		Bibliography on structural studies of ribonucleotide reductase R2type proteins
	metallo.scripps.edu /PROMISE/1RIB.html (196 words)

	Pfam 18.0 : Ribonuc_red_lgC (Site not responding. Last check: 2007-10-12)
		Ribonucleotide reductase (EC:1.17.4.1) MEDLINE:3286319, MEDLINE:8511586 catalyzes the reductivesynthesis of deoxyribonucleotides from their corresponding ribonucleotides.
		Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain MEDLINE:11875520.
		There are several regions of similarity in the sequence of the large chain of prokaryotes, eukaryotes and viruses spread across 3 domains: an N-terminal domain common to the mammalian and bacterial enzymes; a C-terminal domain common to the mammalian and viral ribonucleotide reductases; and a central domain common to all three MEDLINE:9309223.
	pfam.wustl.edu /cgi-bin/getdesc?name=Ribonuc_red_lgC (594 words)

	Expression of an Altered Ribonucleotide Reductase Activity Associated with the Replication of Murine Cytomegalovirus in ...
		Ribonucleotide reductase (RNR) is an essential enzyme for the de novo synthesis of both cellular and viral DNA and catalyzes
		Ribonucleotide reductase encoded by herpes simplex virus is a determinant of the pathogenicity of the virus in mice and a valid antiviral target.
		Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks.
	jvi.asm.org /cgi/content/full/74/24/11557 (7041 words)

	[No title] (Site not responding. Last check: 2007-10-12)
		to the ribonucleotide reductase gene of the microorganism under conditions such that the expression of the ribonucleotide reductase gene is inhibited.
		The term "ribonucleotide reductase gene" or the "ribonucleoside diphosphate reductase gene" refers to any gene which encodes a protein that either reduces the four main ribonucleotides to the corresponding deoxyribonucleotides involved in DNA synthesis or encodes a subunit of a multimeric enzyme which reduces the four main ribonucleotides to the corresponding deoxyribonucleotides.
		The oligonucleotides may be used as hybridization probes to detect the presence of the ribonucleotide reductase gene or the secA gene in the microorganism.
	www.wipo.int /cgi-pct/guest/getbykey5?KEY=99/02673.990121&ELEMENT_SET=DECL (8138 words)

	Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase - Nature Structural ...
		Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides into deoxyribonucleotides, which constitute the precursor pools used for DNA synthesis and repair.
		Beck, W.S. Regulation of cobamide-dependent ribonucleotide reductase by allosteric effectors and divalent cations.
		B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli.
	www.nature.com /nsmb/journal/v11/n11/full/nsmb838.html (5533 words)

	Purine and Pyrimidine Metabolism
		Deoxyribonucleotides are synthesized by reduction of the corresponding ribonucleotides.
		The enzyme dihydrofolate reductase is responsible for the regeneration of tetrahydrofolate from dihydrofolate.
		Deoxyribonucleotides are synthesized from ribonucleotides by the enzyme ribonucleotide reductase
	www.db.uth.tmc.edu /faculty/alevine/1521_2000/deoxyribo.htm (1174 words)

	InterPro: IPR000358 Ribonucleotide reductase (Site not responding. Last check: 2007-10-12)
		Ribonucleotide reductase (1.17.4.1) [ 1, 2 ] catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides:
		Ribonucleotide reductase is an oligomeric enzyme composed of a large subunit (700 to 1000 residues) and a small subunit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain [ 3 ].
		The regions of the sequence that contain the metal-binding residues and the active site tyrosine are conserved in ribonucleotide reductase small chain from prokaryotes, eukaryotes and viruses.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR000358 (2999 words)

	The Ribonucleotide Reductase R1 Homolog of Murine Cytomegalovirus Is Not a Functional Enzyme Subunit but Is Required ...
		A ribonucleotide reductase homolog of cytomegalovirus and endothelial cell tropism.
		The human cytomegalovirus ribonucleotide reductase homolog UL45 is dispensable for growth in endothelial cells, as determined by a BAC-cloned clinical isolate of human cytomegalovirus with preserved wild-type characteristics.
		Expression of an altered ribonucleotide reductase activity associated with the replication of murine cytomegalovirus in quiescent fibroblasts.
	jvi.asm.org /cgi/content/full/78/8/4278 (7699 words)

	A Megaplasmid-Borne Anaerobic Ribonucleotide Reductase in Alcaligenes eutrophus H16 -- Siedow et al. 181 (16): 4919 -- ...
		Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cystein residues in ribonucleotide reduction.
		The redox centres of ribonucleotide reductase of Escherichia coli.
		The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681.
	jb.asm.org /cgi/content/full/181/16/4919 (3694 words)

	Re: Why isn’t the inhibition of ribonucleotide reductase
		The herpes simplex virus type 1 ribonucleotide reductase is required for acute retinal disease.
		Ribonucleotide reductase: an important enzyme in the replication of herpes simplex virus type 1 and a target for antiviral chemotherapy.
		Induction of ribonucleotide reductase activity in cells infected with African swine fever virus.
	www.madsci.org /posts/archives/2005-05/1116598331.Vi.r.html (195 words)

	Radiation Inactivation of Ribonucleotide Reductase, an Enzyme with a Stable Free Radical -- Bolger et al. 79 (4): 2155 ...
		The ribonucleotide reductases (RR) are enzymes that catalyze the conversion of ribonucleoside 5'-diphosphate to the corresponding
		Herpes simplex virus type 1-induced ribonucleotide reductase activity is dispensable for virus growth and DNA synthesis: isolation and characterization of an ICP6 lac Z insertion mutant.
		The herpes simplex virus type 1 ribonucleotide reductase is a tight complex of the type alpha 2 beta 2 composed of 40K and 140K proteins, of which the latter shows multiple forms due to proteolysis.
	www.biophysj.org /cgi/content/full/79/4/2155 (4141 words)

	Adenovirus-Mediated Ribonucleotide Reductase R1 Gene Therapy of Human Colon Adenocarcinoma -- Cao et al. 9 (12): 4553 ...
		Fan H., Villegas C., Wright J. Ribonucleotide reductase R2 component is a novel malignancy determinant that cooperates with activated oncogenes to determine transformation and malignant potential, Proc..
		Zhou B. S., Hsu N. Y., Pan B. C., Doroshow J. H., Yen Y. Overexpression of ribonucleotide reductase in transfected human KB cells increases their resistance to hydroxyurea: M2 but not M1 is sufficient to increase resistance to hydroxyurea in transfected cells..
		Chabes A., Thelander L. Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks..
	clincancerres.aacrjournals.org /cgi/content/full/9/12/4553 (5352 words)

	The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a ...
		Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides, an essential step in DNA biosynthesis and repair.
		Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides in all organisms and, therefore, serve an essential function in DNA replication and repair.
		Nordlund, P., Sjöberg, B.M. and Eklund, H. Three-dimensional structure of the free radical protein of ribonucleotide reductase.
	www.nature.com /nsmb/journal/v9/n4/full/nsb774.html (5445 words)

	Structural studies of ribonucleotide reductase R2-type proteins
		Bollinger, J.M., Jr., Edmondson, D.E., Huynh, B.H., Filley, J., Norton, J.R. and Stubbe, J. Mechanism of assembly of the tyrosyl radicaldinuclear iron cluster cofactor of ribonucleotide reductase.
		Sjöberg, B.M., SandersLoehr, J. and Loehr, T.M. Identification of a hydroxide ligand at the iron center of ribonucleotide reductase by resonance Raman spectroscopy.
		Stemmler, T.L., Sossong, T.M., Jr., Goldstein, J.I., Ash, D.E., Elgren, T.E., Kurtz, D.M., Jr., and PennerHahn, J.E. EXAFS comparison of the dimanganese core structures of manganese catalase, arginase, and manganesesubstituted ribonucleotide reductase and hemerythrin.
	metallo.scripps.edu /promise/RNRR2_REF.html (3485 words)

	In Vivo and In Vitro Comparison of the Short-Term Hematopoietic Toxicity Between Hydroxyurea and Trimidox or Didox, ...
		Biochemical and antitumor activity of trimidox, a new inhibitor of ribonucleotide reductase.
		Effective use of ribonucleotide reductase inhibitors (Didox and Trimidox) alone or in combination with didanosine (ddI) to suppress disease progression and increase survival in murine acquired immunodeficiency syndrome (MAIDS).
		The inhibition of ribonucleoside diphosphate reductase by hydroxyurea, guanazole and pyrazoloimidazole (IMPY).
	stemcells.alphamedpress.org /cgi/content/full/17/6/345 (4990 words)

	The Ribonucleotide Reductase R1 Homolog of Murine Cytomegalovirus Is Not a Functional Enzyme Subunit but Is Required ...
		The Ribonucleotide Reductase R1 Homolog of Murine Cytomegalovirus Is Not a Functional Enzyme Subunit but Is Required for Pathogenesis -- Lembo et al.
		The Ribonucleotide Reductase R1 Homolog of Murine Cytomegalovirus Is Not a Functional Enzyme Subunit but Is Required for Pathogenesis
		Ribonucleotide reductase (RNR) is the key enzyme in the biosynthesis
	jvi.asm.org /cgi/content/abstract/78/8/4278 (446 words)

	A Megaplasmid-Borne Anaerobic Ribonucleotide Reductase in Alcaligenes eutrophus H16 -- Siedow et al. 181 (16): 4919 -- ...
		A Megaplasmid-Borne Anaerobic Ribonucleotide Reductase in Alcaligenes eutrophus H16 -- Siedow et al.
		reductases is dependent on a stable radical at a glycine residue
		Tamarit, J., Gerez, C., Meier, C., Mulliez, E., Trautwein, A., Fontecave, M. The Activating Component of the Anaerobic Ribonucleotide Reductase from Escherichia coli.
	jb.asm.org /cgi/content/abstract/181/16/4919 (249 words)

	BioMed Central \| Full text \| Rational polynomial representation of ribonucleotide reductase activity
		Recent data suggest that ribonucleotide reductase (RNR) exists not only as a heterodimer R1 of R1 and R2 homodimers, but also as tetramers R1 and hexamers R1 Recent data also suggest that ATP binds the R1 subunit at a previously undescribed hexamerization site, in addition to its binding to previously described dimerization and tetramerization sites.
		Quaternary states of R1 Ribonucleotide reductase (RNR) is a key component of de novo deoxynucleotide (dNTP) metabolism and an important target of cancer therapies [1].
		Recent data [3-6] suggest that ribonucleotide reductase (RNR) exists not only as a heterodimer R1 of R1 and R2 homodimers [2], but also as a R1 tetramer and as a R1 hexamer, where hexamer formation is driven by ATP binding to a previously undescribed hexamerization site.
	www.biomedcentral.com /1471-2091/6/8 (1828 words)

	Phase I and Pharmacokinetic Study of the Ribonucleotide Reductase Inhibitor, 3-Aminopyridine-2-Carboxaldehyde ...
		Hurta RA, Wright JA: Alterations in the activity and regulation of mammalian ribonucleotide reductase by chlorambucil, a DNA damaging agent.
		Fan H, Villegas C, Wright JA: Ribonucleotide reductase R2 component is a novel malignancy determinant that cooperates with activated oncogenes to determine transformation and malignant potential.
		Thelander L, Graslund A: Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone: Destruction of the tyrosine free radical of the enzyme in an oxygen-requiring reaction.
	www.jco.org /cgi/content/full/22/9/1553 (6118 words)

	Corynebacterium ammoniagenes class Ib ribonucleotide reductase: transcriptional regulation of an atypical genomic ...
		Ribonucleotide reductases (RNRs) catalyse the reduction of ribonucleotides
		Breidbach, T., Krauth-Siegelb, R. and Steverdinga, D. Ribonucleotide reductase is regulated via the R2 subunit during the life cycle of Trypanosoma brucei.
		Filpula, D. and Fuchs, J. Regulation of the synthesis of ribonucleoside diphosphate reductase in Escherichia coli: specific activity of the enzyme in relationship to perturbations of DNA replication.
	mic.sgmjournals.org /cgi/content/full/149/4/1011 (4931 words)

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