1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1
about
Structure of the yeast ribonucleotide reductase Y2Y4 heterodimerInterplay of structure and disorder in cochaperonin mobile loopsPoint and deletion mutations eliminate one or both methyl group transfers catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase.Yeast Sml1, a protein inhibitor of ribonucleotide reductase.Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit.Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletionEnzymatically active mammalian ribonucleotide reductase exists primarily as an alpha6beta2 octamerMouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysisCloning and characterization of the R1 and R2 subunits of ribonucleotide reductase from Trypanosoma brucei.Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase.Targeting ribonucleotide reductase for cancer therapy.Caspase-dependent Proteolysis of Human Ribonucleotide Reductase Small Subunits R2 and p53R2 during Apoptosis.Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanismsMethodology to probe subunit interactions in ribonucleotide reductases.Crystal structure of the biologically active form of class Ib ribonucleotide reductase small subunit from Mycobacterium tuberculosis.Orientation of the tyrosyl radical in Salmonella typhimurium class Ib ribonucleotide reductase determined by high field EPR of R2F single crystals.Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase.Demonstration of segmental mobility in the functionally essential carboxyl terminal part of ribonucleotide reductase protein R2 from Escherichia coli.
P2860
Q27634566-E63E1154-0355-4394-AA78-0A5C2F0658A0Q27733719-4F398953-3ECB-466F-92F9-47778FF3820CQ27933570-D30B733B-B73D-4E5E-9387-97E2584B1BBAQ27934371-F44FF19E-9FA0-4A34-A250-7FD72512002BQ27939596-70FFFFB0-69B9-4C17-B436-A2E8E641C5A5Q28301052-F9AFE71F-CA23-422A-83BB-AD2CF1D9F4DCQ28511319-B97E2033-8A77-4F82-BD55-CF9CCF6A0FFDQ28512497-51AC7848-168B-4198-BA6D-B94530F502DFQ36244421-58A2841B-24BE-42C6-B940-F4008299CA00Q36283688-D868F01E-8C66-487A-86FA-84CBE3C4EEDAQ38148222-E016C665-2A87-4FA9-9845-C2E9F6E2824FQ38886653-D42C1F99-EABF-47AB-AC81-698C85D84515Q39895340-474FAB54-B9A5-4B84-909F-E284F56CCC27Q41938227-4DBA04ED-02FF-4CC7-8905-860825054DA9Q47268451-32936877-0107-49A3-835E-8432E3FA8224Q50078797-6AF891B1-F7C0-41BB-A30F-BA6F44339423Q54601627-B9F4B1BC-1337-4E8E-9037-E7157F94FB73Q54608177-B4E0049A-39A3-41F6-8B0F-577A5CC4B944
P2860
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1
description
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1994
@ast
im März 1994 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 1994/03/15)
@nl
наукова стаття, опублікована в березні 1994
@uk
مقالة علمية (نشرت في 15-3-1994)
@ar
name
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@ast
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@en
type
label
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@ast
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@en
prefLabel
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@ast
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@en
P2093
P356
P1433
P1476
1H NMR studies of mouse ribonu ...... in the presence of protein R1
@en
P2093
A. Gräslund
L. Thelander
P. O. Lycksell
R. Ingemarson
P304
P356
10.1021/BI00176A013
P407
P577
1994-03-15T00:00:00Z