Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.

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Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.

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Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.

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Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.

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P1476

Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.

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P2093

Dan Huang

http://www.w3.org/2001/XMLSchema#string

Huaian Liu

http://www.w3.org/2001/XMLSchema#string

Ian A Taylor

http://www.w3.org/2001/XMLSchema#string

Jinguang Huang

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Junfeng Liu

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Wensheng Zhao

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Xiankun Cheng

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Yanxiang Zhao

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You-Liang Peng

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P2860

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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 proteome

Structural features of the single-stranded DNA-binding protein MoSub1 from Magnaporthe oryzae

Bacteriophage T5 encodes a homolog of the eukaryotic transcription coactivator PC4 implicated in recombination-dependent DNA replication

C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site

XDS

Clustal W and Clustal X version 2.0

Overview of the CCP4 suite and current developments

P2888

srep08789

P304

8789

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P31

scholarly article

P356

10.1038/SREP08789

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P407

English

P478

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P577

2015-03-05T00:00:00Z

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P5875

273149641

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P698

25739870

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P932

4350104

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