Characterization of chemical inhibitors of brefeldin A-activated mono-ADP-ribosylation. (Q41108978)

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3 November 2019

title

Characterization of chemical inhibitors of brefeldin A-activated mono-ADP-ribosylation (English)

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3 November 2019

2

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Roberto Buccione

4

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3 November 2019

Daniela Corda

12

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3 November 2019

Alberto Luini

14

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3 November 2019

author name string

R Weigert

1

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3 November 2019

A Mironov

3

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C Cericola

5

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3 November 2019

M G Sciulli

6

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3 November 2019

G Santini

7

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S Flati

8

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A Fusella

9

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J G Donaldson

10

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M Di Girolamo

11

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M A De Matteis

13

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language of work or name

English

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publication date

1 May 1997

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Journal of Biological Chemistry

3 November 2019

number of pages

8

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based on heuristic

inferred from page(s)

published in

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volume

272

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issue

22

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3 November 2019

page(s)

14200-14207

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3 November 2019

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Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins

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Brefeldin A: insights into the control of membrane traffic and organelle structure

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Stimulation of endogenous ADP-ribosylation by brefeldin A.

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Evidence that the 50-kDa substrate of brefeldin A-dependent ADP-ribosylation binds GTP and is modulated by the G-protein beta gamma subunit complex

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Early and late transformations occurring at organelles of the Golgi area under the influence of brefeldin A: an ultrastructural and lectin cytochemical study

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Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes

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The morphology but not the function of endosomes and lysosomes is altered by brefeldin A

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In AtT20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties

21 January 2018

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Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic

21 January 2018

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Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators

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Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes

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LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function

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Golgi spectrin: identification of an erythroid beta-spectrin homolog associated with the Golgi complex.

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Guanine nucleotides modulate the effects of brefeldin A in semipermeable cells: regulation of the association of a 110-kD peripheral membrane protein with the Golgi apparatus

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Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein

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