A modified form of Green Fluorescent Protein integrated into an ammonium transporter provides a sensor that can be used to monitor transport activity in vivo.

A new cellular transport mechanism splits the substrate and separately translocates its fragments to achieve selectivity.

Metabolomics and stable isotope labelling studies of virulent Mycobacterium tuberculosis reveal a de-centralised metabolic network able to utilise various amino acids as nitrogen sources to a better extent than ammonium.

In order to enter a cell, an ammonium ion must first dissociate to form an ammonia molecule and a hydrogen ion (a proton), which then pass through the cell membrane separately and recombine inside.

Human hippocampal cornu ammonis 3 damage impairs both recent and remote autobiographical episodic memory, and disrupts functional integration in medial temporal lobe subsystem regions of the default network.

Building on previous work (De Michele et al., 2013), we report the development of dual-emission AmTrac sensors for in vivo analysis of transporter activity.

The architecture of a gene regulatory network determines the effect of evolutionary changes in transcription factor binding.

Peptide and nitrate transporters have been converted into fluorescent reporters of transport activity and have been used to measure various transport properties including the dual affinity of the nitrate transceptor