Anion binding sites in the active center of D-glyceraldehyde-3-phosphate dehydrogenase

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The structural basis for catalytic function of GMD and RMD, two closely related enzymes from the GDP-D-rhamnose biosynthesis pathway.

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DNA Polymerase α has cyclobutane pyrimidine dimer translesion activity that is suppressed during normal replication.

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Anion binding sites in the active center of D-glyceraldehyde-3-phosphate dehydrogenase

Related Concept Videos

Rare genetic variants suggest dysregulation of signaling pathways in low- and high-risk patients developing severe ovarian hyperstimulation syndrome.

A distinctive epigenetic ageing profile in human granulosa cells.

Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion.

Structure of southern bean mosaic virus at 2.8 A resolution.

The structural basis for catalytic function of GMD and RMD, two closely related enzymes from the GDP-D-rhamnose biosynthesis pathway.

Structure and morphogenesis of bacteriophage T4.

Auto-S-fatty acylation of PKM2 regulates its tetramerization and glycolytic metabolism in cancer cells.

MEK/ERK signaling and Bcl-2 family protein changes in influenza-infected cells with differing sulfatide levels.

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Graphitic Carbon Nitride (g-C3N4)-Catalysed Green Synthesis of Heterocycles: Progress, Mechanistic Insights, and Future Perspectives.

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Anion binding sites in the active center of D-glyceraldehyde-3-phosphate dehydrogenase

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