PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1 (Q24338323)

Karyopherin subunit beta 1

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

Roberto Buccione

4

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author name string

Simone Di Paola

1

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Massimo Micaroni

2

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Giuseppe Di Tullio

3

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Maria Di Girolamo

Creative Commons Attribution 4.0 International

5

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language of work or name

English

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publication date

2012

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published in

PLOS One

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volume

7

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issue

6

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page(s)

e37352

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copyright license

start time

11 June 2012

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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describes a project that uses

ImageJ

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3372510/fullTextXML

inferred from PubMed Central ID database lookup

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30 May 2018

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ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress

30 May 2018

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30 May 2018

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30 May 2018

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30 May 2018

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30 May 2018

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21 January 2018

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21 January 2018

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12 December 2020

Endogenous ADP-ribosylation of the G protein beta subunit prevents the inhibition of type 1 adenylyl cyclase

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ADP-ribosyltransferase type A from turkey erythrocytes modifies actin at Arg-95 and Arg-372

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[Use of atomic force microscopy to study the morphology and structure of viruses]

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Protein modification by ADP-ribose via acid-labile linkages

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Noncovalent protein interaction with poly(ADP-ribose).

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A human melanoma line heterogeneous with respect to metastatic capacity in athymic nude mice

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The family of bacterial ADP-ribosylating exotoxins

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7 January 2021