about
The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteinsNogo goes in the pure water: solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regenerationThe solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin bindingDetermination of Multicomponent Protein Structures in Solution Using Global Orientation and Shape RestraintsStructure and Function of AvtR, a Novel Transcriptional Regulator from a Hyperthermophilic Archaeal LipothrixvirusStructural Studies of E73 from a Hyperthermophilic Archaeal Virus Identify the “RH3” Domain, an Elaborated Ribbon–Helix–Helix Motif Involved in DNA RecognitionThe Transcription Factor AmrZ Utilizes Multiple DNA Binding Modes to Recognize Activator and Repressor Sequences of Pseudomonas aeruginosa Virulence Genes3D solution structure of copper and silver-substituted yeast metallothioneinsStructure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifsThe Pseudomonas aeruginosa ribbon-helix-helix DNA-binding protein AlgZ (AmrZ) controls twitching motility and biogenesis of type IV piliAmrZ beta-sheet residues are essential for DNA binding and transcriptional control of Pseudomonas aeruginosa virulence genesOverview of protein structural and functional folds.Identification, cloning and characterization of a new DNA-binding protein from the hyperthermophilic methanogen Methanopyrus kandleriRegulation of high affinity nickel uptake in bacteria. Ni2+-Dependent interaction of NikR with wild-type and mutant operator sites.Contributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor.A genetically economical family of plasmid-encoded transcriptional repressors involved in control of plasmid copy numberThe structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator.The nickel-responsive regulator NikR controls activation and repression of gene transcription in Helicobacter pylori.Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy.The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain.NikR is a ribbon-helix-helix DNA-binding proteinMutagenic dissection of the sequence determinants of protein folding, recognition, and machine function.The A-kinase anchoring domain of type IIalpha cAMP-dependent protein kinase is highly helical.Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex.LSF and NTF-1 share a conserved DNA recognition motif yet require different oligomerization states to form a stable protein-DNA complex.
P2860
Q24533570-C7718313-AAAA-481E-A218-9EB51C173ED7Q24647661-635441BD-3B33-4E4B-B791-29362E3CCDB7Q27646891-4BEF2067-4D88-4E58-88D1-E3C01408FE8EQ27657269-221E0A0F-AAF6-48D1-81B6-D3BC8ABC2F41Q27674412-A7047471-1834-4777-96D6-E477AE1A6A7BQ27678006-AE5C62A3-9AC4-4C3E-B2D4-119DD4E9343EQ27678592-D41AA191-FBCA-4080-9183-AC040D1C9B63Q27732534-F70C38C3-724E-48D5-96B8-0232B303A086Q28485127-E9CE78EC-F165-4B06-A67E-267B9D3AAA2DQ28492694-F9E97B82-085C-458C-83F8-EE40A6858D74Q28493255-E578146F-F3ED-478D-9904-A85BF312F1C0Q30368988-E3B14E9F-DFD1-4C8E-85E9-2EF0E28D7876Q33559624-DA8017A5-0C87-4F97-8E7D-D78397F9FE99Q33899958-7D678489-9D53-4AD9-B669-A69633D58DD8Q34454118-69E6AD4D-1574-4097-9CF8-E05CF73B26D5Q34794815-F8F8B2A4-2A0B-4939-8610-0F4F81CDEE45Q38330387-4D699BAF-6B0F-410E-BD70-3AF2B8677620Q39392051-99C79025-9B1F-433E-8553-313BDDB4D9B1Q40954112-D7B8213F-DB97-45C5-99C6-096BFE6ACEC9Q42816012-88639E7E-93E5-44D4-8307-7FD5EEEF6FE0Q42846792-5F5DAB23-CF9C-4F47-BC5B-6BE130382E25Q42881980-0B784160-56F4-429E-A91A-AB7E11DC7F9AQ44190110-37669E26-34B2-4DFA-9799-91BD5F848FDDQ47742823-AE27F363-F411-4FD9-87B5-9C1D78351431Q47827900-A35C261B-B904-4DC2-985E-9DC8C7034E7F
P2860
description
1994 nî lūn-bûn
@nan
1994 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Solution structure of dimeric Mnt repressor (1-76)
@ast
Solution structure of dimeric Mnt repressor (1-76)
@en
Solution structure of dimeric Mnt repressor (1-76)
@nl
type
label
Solution structure of dimeric Mnt repressor (1-76)
@ast
Solution structure of dimeric Mnt repressor (1-76)
@en
Solution structure of dimeric Mnt repressor (1-76)
@nl
prefLabel
Solution structure of dimeric Mnt repressor (1-76)
@ast
Solution structure of dimeric Mnt repressor (1-76)
@en
Solution structure of dimeric Mnt repressor (1-76)
@nl
P2093
P356
P1433
P1476
Solution structure of dimeric Mnt repressor (1-76)
@en
P2093
D E Gilbert
K L Knight
M J Burgering
P304
P356
10.1021/BI00254A012
P407
P577
1994-12-20T00:00:00Z