Building competency to deal with environmental health challenges: experiences and a proposal.

The global landscape of professional training in environmental health, encompassing ecological public health or environmental public health, lacks consistent global implementation for training programs for public health practitioners, clinical professionals, and individuals across various disciplines, as well as standardized curricula for undergraduates. This training gap is related to the overall lack of capacity in addressing the population impacts of the triple challenge of pollution, biodiversity loss, and climate change, impeding the worldwide transition to and development of ecological sustainability. This paper reviews existing approaches and their potential to address implementation challenges within the necessarily tight timescale.

A new environmental public health practice to manage current and future global health challenges through education, training, and capacity building.

Unsustainable globalisation of economic activities, lifestyles and social structures has contributed to environmental degradation, posing major threats to human health at the local and global levels. All these problems including climate change, pollution, and biodiversity loss represent challenges that are unlikely to be met with existing approaches, capabilities and tools. This article acknowledges the need for well-prepared practitioners from many walks of life to contribute to environmental public health (EPH) functions thus strengthening society's capacity and capability to respond effectively and in a timely manner to such complex situations and multiple challenges.

Structural response of G protein binding to the cyclodepsipeptide inhibitor FR900359 probed by NMR spectroscopy.

The cyclodepsipeptide FR900359 (FR) and its analogs are able to selectively inhibit the class of G proteins by blocking GDP/GTP exchange. The inhibitor binding site of G has been characterized by X-ray crystallography, and various binding and functional studies have determined binding kinetics and mode of inhibition. Here we investigate isotope-labeled FR bound to the membrane-anchored G protein heterotrimer by solid-state nuclear magnetic resonance (ssNMR) and in solution by liquid-state NMR.