Exoenzyme S from P. aeruginosa ADP Ribosylates rab4 and Inhibits Transferrin Recycling in SLO-Permeabilized Reticulocytes
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 244, Issue: 2, Page: 336-341
1998
- 19Citations
- 21Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations19
- Citation Indexes19
- 19
- CrossRef11
- Captures21
- Readers21
- 21
Article Description
ADP-ribosylation of rab proteins by exoenzyme S (Exo S) of P. aeruginosa was studied using reticulocytes. 14-3-3 protein, the eukaryotic cofactor that is obligatory for Exo S activity, was found in association with reticulocyte endocytic vesicles and exosomes, vesicles previously shown to be enriched with rab4. Incubation of purified endocytic vesicles with Exo S triggered rab4 ADP-ribosylation. Transferrin recycling in SLO-permeabilized reticulocytes was highly impaired when Exo S was added to the cells, suggesting that ADP-ribosylation affected rab4 function. Moreover, in vitro ADP-ribosylation of different rab proteins was studied using the cofactor activity extracted from reticulocytes.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X98982638; http://dx.doi.org/10.1006/bbrc.1998.8263; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0032539766&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9514923; https://linkinghub.elsevier.com/retrieve/pii/S0006291X98982638; https://dx.doi.org/10.1006/bbrc.1998.8263
Elsevier BV
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