Detailed analysis of transporter expression and glucose uptake rates shows that carbohydrate import at the blood–brain barrier is adapted via TGF-βsignaling-dependent transcriptional regulation of carbohydrate transporters to protect the brain form effects of nutrient shortage.

Computational models and mutagenesis study reveal a conserved carbohydrate recognition motif of two therapeutically important purinergic receptors to help understand the carbohydrate regulation of G-protein coupled receptors.

The balanced utilization of energy sources, namely carbohydrates and fats, by mitochondria, is critically important for the long-term maintenance of both skeletal muscle and heart health.

Integration of clinical patient data, pathogen information and a multi-omic analysis of the gut microbiome reveals key determinants of disease in C. difficile-colonized patients.

The putative carbohydrate-binding protein gene Cs9g12620 by PthA4-mediated induction of CsLOB1 during Xcc infection.

A highly sophisticated and adaptive interplay between modulation of myosin II function by light chain phosphorylation and environmentally controlled formin availability, is critical for a successful cytokinesis during respiratory carbohydrate metabolism in the fission yeast Schizosaccharomyces pombe.

The E2F/Dp transcription factors, which are key cell cycle regulators, can also mediate the regulation of carbohydrate metabolism in larva by controlling both systemic trehalose homeostasis and fat storage.

General stress response factors Msn2 and Msn4 activate glycolytic genes and promote acetyl-CoA accumulation to stimulate growth and proliferation of yeast cells under a nutrient-limiting condition, suggesting the unexpected interrelationship between carbohydrate metabolism and stress response.

Increasing levels of atmospheric carbon dioxide reduce the mineral content but increase the levels of starch and sugars found in crop plants; which could exacerbate both obesity and malnutrition in some human populations.

The MIR domain of protein-O-mannosyltransferases participates in glycosylation by binding mannosylated peptides and regulates enzyme processivity.