About: Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase

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About: Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase Goto Sponge NotDistinct Permalink

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) im Jahr 1993 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Nature (en) Նեյչրում հրատարակված հոդված (hy) наукова стаття, опублікована в Nature в січні 1993 (uk)
publication date	wds:Q59067456-CDEBEC2A-9F7F-45B3-AE8B-3A1334037244
publication date	1993-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59067456-A915C0DF-BFDC-48F0-90E5-E4CEB35B6503
language of work or name	English
exact match	wds:Q59067456-74ADECC5-DA10-4948-9E04-2626AB1A7B10
exact match	https://scigraph.springernature.com/pub.10.1038/361276a0
cites work	wds:Q59067456-0BB0C2EF-2573-4E48-80DF-58AC941EE354 wds:Q59067456-27206BDB-AA83-4665-A5F7-336667CE0EAF wds:Q59067456-30521D83-5905-4145-AE15-6682DA3F662C wds:Q59067456-5B61CE4E-4897-4969-9869-2A3100232B25 wds:Q59067456-5C6F6608-27FC-4740-8307-AF75CFE378B8 wds:Q59067456-6D7A5089-99E3-41CB-9534-D22FE9B81D05 wds:Q59067456-73B49BEE-B0CC-4CF2-997E-BE3C205C7D04 wds:Q59067456-7FFBBB35-3885-408A-B577-3921790EF1EC wds:Q59067456-87D0D4D5-F83A-478F-9BAE-315879841F6C wds:Q59067456-A30F9C82-1BA4-4BFD-B580-05BBDE15199E wds:Q59067456-AC63FA54-DB53-4C25-BD47-8E4069366EB4 wds:Q59067456-D843D2B5-912C-483E-A55B-BD0803705DC3 wds:Q59067456-D9774107-55F4-4ED9-8B11-1357A6967ED5 wds:Q59067456-DAAD589C-7FD2-47F5-9658-A03F42D17887 wds:Q59067456-DD3AC3FA-5D02-42EA-BE53-A9514A486B7B
cites work	Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives Three-dimensional structure of the free radical protein of ribonucleotide reductase Protein radical involvement in biological catalysis? Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins Hydrogen bonding in globular proteins Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution Long-range structural changes in proteinase K triggered by calcium ion removal. Crystallographic R factor refinement by molecular dynamics The structure and function of the aspartic proteinases Nicotinic acetylcholine receptor superfamily of ligand-gated ion channels Crystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine Crystal structure of demetallized concanavalin A: the metal-binding region Changes in the three-dimensional structure of concanavalin A upon demetallization New crystal forms of the small subunit of ribonucleotide reductase from Escherichia coli.
author name string	wds:Q59067456-9BCB6A50-8C2B-42FD-A785-62885111B956 wds:Q59067456-B4B90DA3-027D-4127-98CA-E003455B885C wds:Q59067456-C737997B-86C4-45E9-B1C2-1CEDE9CE894F
author name string	Aberg A Nordlund P Eklund H
rdfs:label	Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (en) Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (nl)
skos:prefLabel	Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (en) Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (nl)
name	Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (en) Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (nl)
title	wds:Q59067456-92F14DDA-1842-463E-9F35-640D859A3D24
title	Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase (en)
page(s)	wds:Q59067456-2E5704AC-BCC3-4891-A588-3FCC0F092B88
page(s)	276-278
instance of	wds:Q59067456-36B332F3-1683-451A-8C75-F127275BCAC9
instance of	scholarly article
PubMed ID	wds:Q59067456-ED570BF9-0841-49FE-BF68-6CF4B43A65F8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8423856
PubMed ID	8423856
published in	wds:Q59067456-852109BE-2C25-4C4C-A48D-CD59B17A740F
published in	Nature
issue	wds:Q59067456-CBE0765F-CB81-4E5A-B0DB-D94B568AB830
volume	wds:Q59067456-F77731C3-A626-43BB-811E-272412079B71
issue	6409
volume	361
DOI	wds:Q59067456-DF6FFAA2-0578-4EAB-B480-639DA5842A2B
DOI	http://dx.doi.org/10.1038/361276A0
DOI	10.1038/361276A0
Dimensions Publication ID	wds:Q59067456-1EDF4DB5-953E-4094-B1E3-D8EBDEFFCD78
Dimensions Publication ID	1052057387
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59067456
is cites work of	Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates Structure and function of the radical enzyme ribonucleotide reductase Residues Important for Radical Stability in Ribonucleotide Reductase fromEscherichia coli Proton and metal ion-dependent assembly of a model diiron protein New insight into the structure and function of the alternative oxidase Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound Identification of the ferroxidase centre of Escherichia coli bacterioferritin Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site An unusual buried polar cluster in a family of fungal lipases Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of p K a Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase Tyrosyl radical cofactors Structural Basis for Assembly of the Mn IV /Fe III Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatis Direct observation of structurally encoded metal discrimination and ether bond formation in a heterodinuclear metalloprotein Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity Density functional theory analysis of structure, energetics, and spectroscopy for the Mn-Fe active site of Chlamydia trachomatis ribonucleotide reductase in four oxidation states Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins DFT calculations for intermediate and active states of the diiron center with a tryptophan or tyrosine radical in Escherichia coli ribonucleotide reductase Perturbations of aromatic amino acids are associated with iron cluster assembly in ribonucleotide reductase Mössbauer properties of the diferric cluster and the differential iron(II)-binding affinity of the iron sites in protein R2 of class Ia Escherichia coli ribonucleotide reductase: a DFT/electrostatics study Charge compensated binding of divalent metals to bacterioferritin: H+ release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites Class Id ribonucleotide reductase utilizes a Mn2(IV,III) cofactor and undergoes large conformational changes on metal loading

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