Posttranslational isoprenylation of rho protein is a prerequisite for its interaction with mastoparan and other amphiphilic agents (Q48455064)

11 February 2018

title

Posttranslational isoprenylation of rho protein is a prerequisite for its interaction with mastoparan and other amphiphilic agents (English)

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11 February 2018

author name string

Koch G

1

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11 February 2018

Mohr C

2

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11 February 2018

Just I

3

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11 February 2018

Aktories K

4

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11 February 2018

language of work or name

English

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publication date

1 July 1992

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11 February 2018

Biochemical and Biophysical Research Communications

published in

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11 February 2018

volume

186

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11 February 2018

issue

1

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11 February 2018

page(s)

448-454

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11 February 2018

https://api.crossref.org/works/10.1016%2FS0006-291X%2805%2980828-9

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Purification of the 22 kDa protein substrate of botulinum ADP-ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene product

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Microinjection of recombinant p21rho induces rapid changes in cell morphology

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Morphological alterations of Xenopus oocytes induced by valine-14 p21rho depend on isoprenylation and are inhibited by Clostridium botulinum C3 ADP-ribosyltransferase

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Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/rac

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ADP-ribosylation of rho proteins is inhibited by melittin, mast cell degranulating peptide and compound 48/80

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Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes

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Botulinum C2 toxin ADP-ribosylates actin

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A geranylgeranyltransferase for rhoA p21 distinct from the farnesyltransferase for ras p21S.

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10.1016/S0006-291X(05)80828-9

7 January 2021

Identifiers

DOI

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11 February 2018

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11 February 2018