Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers.
about
Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriaeMetal stoichiometry and functional studies of the diphtheria toxin repressorSolution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor proteinCorepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulatorStructure of the metal-ion-activated diphtheria toxin repressor/tox operator complexFunctional studies of the Mycobacterium tuberculosis iron-dependent regulatorGenetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation.Isolation and characterization of iron-independent positive dominant mutants of the diphtheria toxin repressor DtxRBiology and molecular epidemiology of diphtheria toxin and the tox gene.The conformations of the manganese transport regulator of Bacillus subtilis in its metal-free state.Disordered to ordered folding in the regulation of diphtheria toxin repressor activity.Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor.Both Corynebacterium diphtheriae DtxR(E175K) and Mycobacterium tuberculosis IdeR(D177K) are dominant positive repressors of IdeR-regulated genes in M. tuberculosis.Mechanism of metal ion activation of the diphtheria toxin repressor DtxR.The src homology 3-like domain of the diphtheria toxin repressor (DtxR) modulates repressor activation through interaction with the ancillary metal ion-binding siteCharacterization of the role of the divalent metal ion-dependent transcriptional repressor MntR in the virulence of Staphylococcus aureusMetalloregulatory proteins: metal selectivity and allosteric switching.Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidumIntracellular Zn(II) Intoxication Leads to Dysregulation of the PerR Regulon Resulting in Heme Toxicity in Bacillus subtilis.Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor.Treponema denticola TroR is a manganese- and iron-dependent transcriptional repressor.Architectural accommodation in the complex of four p53 DNA binding domain peptides with the p21/waf1/cip1 DNA response element.Iron-regulatory proteins DmdR1 and DmdR2 of Streptomyces coelicolor form two different DNA-protein complexes with iron boxes.The SH3-like domain switches its interaction partners to modulate the repression activity of mycobacterial iron-dependent transcription regulator in response to metal ion fluctuations
P2860
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P2860
Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Transition metal ion activatio ...... ormation of stable homodimers.
@ast
Transition metal ion activatio ...... ormation of stable homodimers.
@en
Transition metal ion activatio ...... ormation of stable homodimers.
@nl
type
label
Transition metal ion activatio ...... ormation of stable homodimers.
@ast
Transition metal ion activatio ...... ormation of stable homodimers.
@en
Transition metal ion activatio ...... ormation of stable homodimers.
@nl
prefLabel
Transition metal ion activatio ...... ormation of stable homodimers.
@ast
Transition metal ion activatio ...... ormation of stable homodimers.
@en
Transition metal ion activatio ...... ormation of stable homodimers.
@nl
P2093
P2860
P356
P1476
Transition metal ion activatio ...... ormation of stable homodimers.
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.15.6803
P407
P577
1995-07-01T00:00:00Z