A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.

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A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.

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A macrodomain-linked immunosorbent assay

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A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.

@en

A macrodomain-linked immunosorbent assay

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A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.

@en

A macrodomain-linked immunosorbent assay

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P1476

A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.

@en

P2093

Albert T Lam

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Jingwen Chen

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Yong Zhang

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P2860

RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling

PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation

PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1

The macro domain is an ADP-ribose binding module

Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains

Intracellular Mono-ADP-Ribosylation in Signaling and Disease

Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination

Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitors

P304

132-139

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P31

scholarly article

P356

10.1016/J.AB.2017.12.019

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English

P478

543

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P577

2017-12-13T00:00:00Z

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P698

29247608

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P932

5826802

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