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N-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris

Overview of attention for article published in SpringerPlus, August 2014
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Title
N-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris
Published in
SpringerPlus, August 2014
DOI 10.1186/2193-1801-3-436
Pubmed ID
Authors

Kaia Kukk, Sergo Kasvandik, Nigulas Samel

Abstract

Prostaglandin H synthases (PGHSs) are N-glycosylated membrane proteins that catalyse the committed step in prostaglandin synthesis. Unlike PGHS-2, the production of recombinant PGHS-1 in non-mammalian expression systems is complicated. The majority of the heterologous enzyme is inactive due to misfolding. Correct N-glycosylation is proposed to be obligatory for proper folding of mammalian PGHSs. In this study, human PGHS-1 and -2 (hPGHS-1 and -2) were expressed in the yeast Pichia pastoris. Recombinant hPGHS-2 was catalytically active, whereas hPGHS-1 was inactive. Accumulation of non-glycosylated hPGHSs was not observed in the crude lysate of the yeast cells. The N-glycosylation patterns of the purified recombinant proteins were characterised using nano-LC/MS/MS. The isoforms exhibited similar N-glycosylation site occupancy. The results indicate that there are more complex grounds for the inactivity of the recombinant hPGHS-1 produced in yeast.

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The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 18 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 6%
Unknown 17 94%

Demographic breakdown

Readers by professional status Count As %
Researcher 3 17%
Student > Ph. D. Student 2 11%
Student > Bachelor 2 11%
Lecturer > Senior Lecturer 1 6%
Other 1 6%
Other 2 11%
Unknown 7 39%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 44%
Agricultural and Biological Sciences 3 17%
Chemistry 1 6%
Unknown 6 33%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 30 August 2014.
All research outputs
#20,235,415
of 22,761,738 outputs
Outputs from SpringerPlus
#1,461
of 1,852 outputs
Outputs of similar age
#193,904
of 230,674 outputs
Outputs of similar age from SpringerPlus
#91
of 103 outputs
Altmetric has tracked 22,761,738 research outputs across all sources so far. This one is in the 1st percentile – i.e., 1% of other outputs scored the same or lower than it.
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