Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis.

about

The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage.NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains.

P2860

Q47617004-4959F03E-589A-45DB-BFCE-52B2CE8FDF19 Q50333817-449A7EEC-D1C2-44BA-9509-489B50F847CD

P2860

Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis.

Item

http://www.wikidata.org/entity/Q50898029

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@en

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@nl

type

Item

label

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@en

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@nl

prefLabel

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@en

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@nl

P1476

Purification of DNA Damage-Dep ...... ural and Biochemical Analysis.

@en

P2093

Amanda A Riccio

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

Jamin D Steffen

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

John M Pascal

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

Michael McCauley

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

P2860

A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation

Crystal Structures of Poly(ADP-ribose) Polymerase-1 (PARP-1) Zinc Fingers Bound to DNA: STRUCTURAL AND FUNCTIONAL INSIGHTS INTO DNA-DEPENDENT PARP-1 ACTIVITY

Structural Basis for DNA Damage-Dependent Poly(ADP-ribosyl)ation by Human PARP-1

PARP inhibition: PARP1 and beyond

PARP-2 and PARP-3 are selectively activated by 5' phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1.

The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.

New facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases.

The PARP superfamily.

PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage

The diverse roles and clinical relevance of PARPs in DNA damage repair: current state of the art.

P304

431-444

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

P31

scholarly article

P356

10.1007/978-1-4939-6993-7_27

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

P407

English

P478

1608

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

P50

Marie-France Langelier

P577

2017-01-01T00:00:00Z

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

P698

28695525

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

P921

Escherichia coli

Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis.

about

P2860

P2860

Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P50

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P50

P577

P698

P921