Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase.
about
Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin functionStructural basis of cellular redox regulation by human TRP14Structure of the yeast ribonucleotide reductase Y2Y4 heterodimerDisplacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray dataPreorganization of molecular binding sites in designed diiron proteins2.6 Å X-ray Crystal Structure of Human p53R2, a p53-Inducible Ribonucleotide Reductase,Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assemblyArtificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle StructureMicrobial biosynthesis of alkanesThe structural basis for the allosteric regulation of ribonucleotide reductase.Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light.Selenoproteins: molecular pathways and physiological roles.Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4.The role of the RB tumour suppressor pathway in oxidative stress responses in the haematopoietic system.A 2.8 Å Fe-Fe separation in the Fe2(III/IV) intermediate, X, from Escherichia coli ribonucleotide reductaseProton-coupled electron flow in protein redox machinesProton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology.Rapid X-ray photoreduction of dimetal-oxygen cofactors in ribonucleotide reductase.Proton-coupled electron transfer in biology: results from synergistic studies in natural and model systems.Dissection of the radical reactions linked to fetal hemoglobin reveals enhanced pseudoperoxidase activity.Perturbations of aromatic amino acids are associated with iron cluster assembly in ribonucleotide reductase.Identification of a conserved protein involved in anaerobic unsaturated fatty acid synthesis in Neiserria gonorrhoeae: implications for facultative and obligate anaerobes that lack FabA.Synthetic analogues of cysteinate-ligated non-heme iron and non-corrinoid cobalt enzymesAn approach to the site-selective deoxygenation of hydroxy groups based on catalytic phosphoramidite transferRe(bpy)(CO)3CN as a probe of conformational flexibility in a photochemical ribonucleotide reductase.Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case studyClass I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.Replacement of Y730 and Y731 in the alpha2 subunit of Escherichia coli ribonucleotide reductase with 3-aminotyrosine using an evolved suppressor tRNA/tRNA-synthetase pair.Biosynthesis of the [FeFe] Hydrogenase H Cluster: A Central Role for the Radical SAM Enzyme HydGMechanism of assembly of the dimanganese-tyrosyl radical cofactor of class Ib ribonucleotide reductase: enzymatic generation of superoxide is required for tyrosine oxidation via a Mn(III)Mn(IV) intermediateBranched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis.The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state.Radical-translocation intermediates and hurdling of pathway defects in "super-oxidized" (Mn(IV)/Fe(IV)) Chlamydia trachomatis ribonucleotide reductase.Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: diiron or dimanganese?Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study.The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years.Exploring oxidative modifications of tyrosine: an update on mechanisms of formation, advances in analysis and biological consequences.Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Oxidative pathways in the sickle cell and beyond.Clinical pharmacology and clinical trials of ribonucleotide reductase inhibitors: is it a viable cancer therapy?
P2860
Q24299385-CCED0AE8-08A5-4CBB-BEF1-E0EFEB3164FAQ24303332-2D32962B-B2BA-49E9-A6B6-5FDC2D76210CQ27634566-870D52DD-F5C9-411C-BEE2-B42E9DF08CF9Q27640658-CB2A5359-23A0-44CA-8479-1D34B1BC4B50Q27640786-B49E7DB1-9D31-45FF-9A07-084ED13CA4EFQ27657290-25497BBE-9444-498F-957B-A17222FF6BA0Q27931632-D65E236F-89EC-4783-A960-4104DEAEE352Q28830531-ADD6DA42-D4D7-423C-9A25-3FF373B472C4Q29617243-73A8E468-4339-4AA0-83E6-881D6F2F8244Q33762296-77428475-B917-412E-9628-FAD8C4134C38Q33862999-E4385867-72CA-4410-B81E-68D274CBA0C5Q33913069-EA01C11C-BB91-4ABE-B6D7-DF562146E5AAQ33942942-D9888E80-007E-4C70-8C61-5F87B929C33AQ34341080-14E81930-331A-4A98-ABBB-E3B6B3A30FC3Q34406248-4BB382C7-9111-4BF2-B016-F622D1D9145AQ34423826-29B56D40-B0B9-4E7D-A0CC-BD81A5C67A5AQ34551745-DCC13AC7-F67B-4484-BA0E-E4F38F159634Q34582760-8F856505-F03D-4517-A0E2-990FD76C4057Q34974036-AE704EEA-79C0-42F8-899C-B5C0CE05767AQ35104057-A7F9EF89-82A6-40B1-A2F3-4C2EED3E063CQ35189803-FD33E82A-D98C-4087-B1C9-0B66BE2CFE88Q35332481-3C26C422-19CE-4082-A4DD-F8FD09266758Q35660884-4CE03848-52F4-4171-86F8-E9D5000E9E36Q35871115-49CD6682-CD7F-42BF-9978-2B73BE8AC8B9Q35922912-B0D5AF4D-3A39-4E0C-968A-1A22CFA2B8FDQ36369017-7C1DBD04-326D-49B3-B183-E11D82DFC315Q36435630-7ECA9B5D-BCC2-4D31-AE9A-3BB4EBF1DD3DQ36461216-E8FA449C-673A-4118-9B0D-79026E88CEC9Q36659198-9D77B4D4-B64F-45FF-883D-B697E49FD3A2Q37085040-E3D52DFA-3F5A-4084-8D16-833736C83249Q37189692-14BE0893-C948-4A24-A9B7-5DD3C65587A0Q37407853-017946A1-570C-4407-A306-DB947E67AF82Q37597145-8C577CD3-0219-495A-98E6-F50D1A2ACA85Q37826997-25D7DEB6-7D5D-4250-B4D9-DAEDE6AAA796Q37855926-998D8B85-E913-4AFE-9E19-F48CD5F71B62Q38012192-FB303D56-F78C-4977-9BA9-43AD2437CA27Q38392128-DDF00BB5-173D-4ECF-92DD-BA850C139FFFQ39048193-B86BD8DC-DA26-4861-A9DE-0849A75A8482Q39336717-3239C353-6D77-4348-85AB-6EA4ABA8F00CQ39380445-42435395-C125-49F8-8F01-59AD938EB24A
P2860
Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase.
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@ast
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@en
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@nl
type
label
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@ast
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@en
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@nl
prefLabel
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@ast
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@en
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@nl
P1476
Harnessing free radicals: form ...... l in ribonucleotide reductase.
@en
P2093
Riggs-Gelasco P
P304
P356
10.1016/S0968-0004(98)01296-1
P577
1998-11-01T00:00:00Z