The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
about
X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibilitySelf-Assembly and Conformational Heterogeneity of the AXH Domain of Ataxin-1: An Unusual Example of a Chameleon FoldCrystal Structure of the N-terminal Domain of the Yeast General Corepressor Tup1p and Its Functional ImplicationsRPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylationBacteriophage protein-protein interactionsNMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.Regulation of high affinity nickel uptake in bacteria. Ni2+-Dependent interaction of NikR with wild-type and mutant operator sites.Non-independence of Mnt repressor-operator interaction determined by a new quantitative multiple fluorescence relative affinity (QuMFRA) assay.Structure-functional intimacies of transient receptor potential channels.Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzymeContributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor.An undecided coiled coil: the leucine zipper of Nek2 kinase exhibits atypical conformational exchange dynamicsSingle-molecule observation of helix staggering, sliding, and coiled coil misfolding.Doxorubicin-triggered self-assembly of native amphiphilic peptides into spherical nanoparticles.Breaking symmetry in protein dimers: designs and functions.Genome-wide association analysis identifies genetic variations in subjects with myalgic encephalomyelitis/chronic fatigue syndrome.Nature and mechanism of the in vivo oligomerization of nucleoid protein H-NS.Mutagenic dissection of the sequence determinants of protein folding, recognition, and machine function.Geometric principles in the assembly of α-helical bundles.TRPC Channel Structure and Properties.Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex.
P2860
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P2860
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@ast
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@en
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@nl
type
label
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@ast
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@en
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@nl
prefLabel
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@ast
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@en
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@nl
P2093
P356
P1476
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
@en
P2093
P304
P356
10.1038/11531
P50
P577
1999-08-01T00:00:00Z