A global transcription cofactor bound to juxtaposed strands of unwound DNA.
about
Structures of apo- and ssDNA-bound YdbC from Lactococcus lactis uncover the function of protein domain family DUF2128 and expand the single-stranded DNA-binding domain proteomeCrystallographic analysis of an RNA polymerase σ-subunit fragment complexed with −10 promoter element ssDNA: quadruplex formation as a possible tool for engineering crystal contacts in protein–ssDNA complexesStructural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprAStructural features of the single-stranded DNA-binding protein MoSub1 from Magnaporthe oryzaeGenome-wide location analysis reveals a role for Sub1 in RNA polymerase III transcription.Recruitment of RNA polymerase II cofactor PC4 to DNA damage sitesMolecular determinants of the interactions between proteins and ssDNA.PC4 promotes genome stability and DNA repair through binding of ssDNA at DNA damage sites.Yeast transcription co-activator Sub1 and its human homolog PC4 preferentially bind to G-quadruplex DNA.Cooperation between SMYD3 and PC4 drives a distinct transcriptional program in cancer cells.A biochemical and biophysical model of G-quadruplex DNA recognition by positive coactivator of transcription 4.Sub1/PC4, a multifaceted factor: from transcription to genome stability.Peptide-protein interactions suggest that acetylation of lysines 381 and 382 of p53 is important for positive coactivator 4-p53 interaction.Activation of p53 function by human transcriptional coactivator PC4: role of protein-protein interaction, DNA bending, and posttranslational modifications.Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.The Sub1 nuclear protein protects DNA from oxidative damageIdentification of the ssDNA-binding protein of bacteriophage T5: Implications for T5 replication.Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics.Transcription cofactor PC4 plays essential roles in collaboration with the small subunit of general transcription factor TFIIE.Chemical shift assignments of the homodimer protein SP_0782 (7-79) from Streptococcus pneumoniae.
P2860
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P2860
A global transcription cofactor bound to juxtaposed strands of unwound DNA.
description
2006 nî lūn-bûn
@nan
2006年の論文
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2006年学术文章
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2006年学术文章
@zh-cn
2006年学术文章
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2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
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2006年學術文章
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name
A global transcription cofactor bound to juxtaposed strands of unwound DNA.
@en
type
label
A global transcription cofactor bound to juxtaposed strands of unwound DNA.
@en
prefLabel
A global transcription cofactor bound to juxtaposed strands of unwound DNA.
@en
P2860
P356
P1476
A global transcription cofactor bound to juxtaposed strands of unwound DNA.
@en
P2093
Dino Moras
Sebastiaan Werten
P2860
P2888
P304
P356
10.1038/NSMB1044
P577
2006-01-15T00:00:00Z
P6179
1005721717