The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical question of
how water specifically crosses biological membranes. In the kidney, at least seven …

Our understanding of the movement of water through cell membranes has been greatly
advanced by the discovery of a family of water-specific, membrane-channel proteins—the …

“Real time” molecular dynamics simulations of water permeation through human aquaporin-
1 (AQP1) and the bacterial glycerol facilitator GlpF are presented. We obtained time …

The aquaporins (AQPs) are a family of small membrane-spanning proteins (monomer size∼
30 kDa) that are expressed at plasma membranes in many cells types involved in fluid …

▪ Abstract The high water permeability characteristic of mammalian red cell membranes is
now known to be caused by the protein AQP1. This channel freely permits movement of …

Aquaporin channel-forming integral protein (CHIP) is the first characterized water channel
protein (genome symbol AQP1), but the molecular structure of the aqueous pathway through …

Based on their unique combination of offering high water permeability and high solute
rejection aquaporin proteins have attracted considerable interest over the last years as …

Aquaporins (AQPs) are membrane proteins that transport water and, in some cases, also
small solutes such as glycerol. AQPs are expressed in many fluid-transporting tissues, such …

Aquaporins (AQP) are integral membrane proteins that serve as channels in the transfer of
water, and in some cases, small solutes across the membrane. They are conserved in …

The rat thyroid Na+/I− symporter (NIS) was expressed inXenopus laevis oocytes and
characterized using electrophysiological, tracer uptake, and electron microscopic methods …