↓ Skip to main content

PLOS

The Crystal Structure of Toxoplasma gondii Pyruvate Kinase 1

Overview of attention for article published in PLOS ONE, September 2010
Altmetric Badge

Mentioned by

wikipedia
2 Wikipedia pages

Citations

dimensions_citation
19 Dimensions

Readers on

mendeley
34 Mendeley
Title
The Crystal Structure of Toxoplasma gondii Pyruvate Kinase 1
Published in
PLOS ONE, September 2010
DOI 10.1371/journal.pone.0012736
Pubmed ID
Authors

Rebecca Bakszt, Amy Wernimont, Abdellah Allali-Hassani, Man Wai Mok, Tanya Hills, Raymond Hui, Juan C. Pizarro

Abstract

Pyruvate kinase (PK), which catalyzes the final step in glycolysis converting phosphoenolpyruvate to pyruvate, is a central metabolic regulator in most organisms. Consequently PK represents an attractive therapeutic target in cancer and human pathogens, like Apicomplexans. The phylum Aplicomplexa, a group of exclusively parasitic organisms, includes the genera Plasmodium, Cryptosporidium and Toxoplasma, the etiological agents of malaria, cryptosporidiosis and toxoplasmosis respectively. Toxoplasma gondii infection causes a mild illness and is a very common infection affecting nearly one third of the world's population.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 34 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 3%
China 1 3%
Pakistan 1 3%
Australia 1 3%
Unknown 30 88%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 9 26%
Researcher 6 18%
Student > Master 6 18%
Student > Doctoral Student 3 9%
Student > Bachelor 2 6%
Other 5 15%
Unknown 3 9%
Readers by discipline Count As %
Agricultural and Biological Sciences 15 44%
Biochemistry, Genetics and Molecular Biology 4 12%
Medicine and Dentistry 4 12%
Nursing and Health Professions 1 3%
Chemical Engineering 1 3%
Other 4 12%
Unknown 5 15%