The crystal structure of the Sox4 HMG domain-DNA complex suggests a mechanism for positional interdependence in DNA recognition
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Combinatorial control of gene expressionReprogramming cells with synthetic proteinsDe novo SOX11 mutations cause Coffin-Siris syndromeDeciphering the Sox-Oct partner code by quantitative cooperativity measurementsAssessment of algorithms for inferring positional weight matrix motifs of transcription factor binding sites using protein binding microarray data.Structure-function relationships in human testis-determining factor SRY: an aromatic buttress underlies the specific DNA-bending surface of a high mobility group (HMG) box.SOXE transcription factors form selective dimers on non-compact DNA motifs through multifaceted interactions between dimerization and high-mobility group domainsImproved models for transcription factor binding site identification using nonindependent interactionsA Model for Dimerization of the SOX Group E Transcription Factor Family.Structure and decoy-mediated inhibition of the SOX18/Prox1-DNA interactionThe high mobility group box: the ultimate utility player of a cell.The role of SRY-related HMG box transcription factor 4 (SOX4) in tumorigenesis and metastasis: friend or foe?DNA-mediated cooperativity facilitates the co-selection of cryptic enhancer sequences by SOX2 and PAX6 transcription factors.DNAproDB: an interactive tool for structural analysis of DNA-protein complexes.Crystallization and X-ray diffraction analysis of the HMG domain of the chondrogenesis master regulator Sox9 in complex with a ChIP-Seq-identified DNA element.Nucleocytoplasmic shuttling of SOX14A and SOX14B transcription factorsStability selection for regression-based models of transcription factor-DNA binding specificity.Conformational and thermodynamic hallmarks of DNA operator site specificity in the copper sensitive operon repressor from Streptomyces lividans.Sox transcription factors require selective interactions with Oct4 and specific transactivation functions to mediate reprogramming.Diversity among POU transcription factors in chromatin recognition and cell fate reprogramming.Probing the role of intercalating protein sidechains for kink formation in DNA.
P2860
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P2860
The crystal structure of the Sox4 HMG domain-DNA complex suggests a mechanism for positional interdependence in DNA recognition
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
The crystal structure of the S ...... rdependence in DNA recognition
@ast
The crystal structure of the S ...... rdependence in DNA recognition
@en
The crystal structure of the S ...... rdependence in DNA recognition
@nl
type
label
The crystal structure of the S ...... rdependence in DNA recognition
@ast
The crystal structure of the S ...... rdependence in DNA recognition
@en
The crystal structure of the S ...... rdependence in DNA recognition
@nl
prefLabel
The crystal structure of the S ...... rdependence in DNA recognition
@ast
The crystal structure of the S ...... rdependence in DNA recognition
@en
The crystal structure of the S ...... rdependence in DNA recognition
@nl
P2093
P2860
P3181
P356
P1433
P1476
The crystal structure of the S ...... rdependence in DNA recognition
@en
P2093
Calista K L Ng
Kamesh Narasimhan
Prasanna R Kolatkar
Ralf Jauch
P2860
P3181
P356
10.1042/BJ20111768
P407
P577
2012-04-01T00:00:00Z