In a cell-free assay, Thr148-ADP-ribosylated actin polymerized rapidly to curled F-actin bundles even in the presence of thymosin β4.
In plain wordsIn lab tests, actin changed by a bacterial toxin still formed bundles when thymosin β4 was present.
- Peptide
- Thymosin beta-4 (human)
- Outcome
- Not applicablePolymerization of ADP-ribosylated actin in presence of Tβ4
- Study
n: not reported in source
purified actin, TIRF microscopy- Outcome group
- Receptor activity and mechanism · Whole body
Source sentences
TIRF microscopy demonstrates rapid polymerization of Thr148-ADP-ribosylated actin to curled F-actin bundles even in the presence of thymosin β4, gelsolin or G1-3.
1 context sentence(design, population, supporting numbers)
Here, we used morphological and biochemical procedures to analyse the mechanism of TccC3 intoxication.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).