Structure and function of aquaporin water channels.
By A. Verkman, A. Mitra. AJP - Renal Physiology, 2000
715 citations recorded by the source corpus.
Subfields: Molecular Biology, Surgery
View Paper: https://www.semanticscholar.org/paper/f0bcee9ec6c5aa2d6b43093bdc910cba9fac0af0
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In Molecular Biology
- A. Verkman
- M. C. Papadopoulos
- Anthony Gordon Fane
- C. Tang
- C. Hélix-Nielsen
- Steve Tyerman
- R. Deane
- Maiken Nedergaard
In Surgery
- C. Hélix-Nielsen
- Anthony Gordon Fane
- C. Tang
- R. Deane
- Maiken Nedergaard
- Jeffrey J. Iliff
- Minghuan Wang
Citations in the corpus
- Plant aquaporins: multifunctional water and solute channels with expanding roles. (2002, background): “This density is typical of MIP densities in membranes (Verkman & Mitra 2000) and is actually less than that estimated by Rivers et al. (1997) for NOD26 (approximately 150 000 per µm2).”
- Impairment of paravascular clearance pathways in the aging brain (2014, background): “Paravascular CSF recirculation and ISF solute clearance are dependent upon the astroglial AQP4 water channel,(4) which is localized primarily to perivascular astrocytic endfeet and astrocytic processes of the glial limitans and reduces the resistance to water flux across astrocytic endfeet.(33) Reac”
- Biomimetic aquaporin membranes coming of age (2015, background): “In living organisms selective water transport across membrane is facilitated by a specialized class of proteins – aquaporins (AQPs), also referred to as Major Intrinsic Proteins (MIPs) – or water channels, a family of integral membrane proteins that are expressed broadly throughout the animal and pl”
- Aquaporin‐4 facilitates reabsorption of excess fluid in vasogenic brain edema (2004, background): “Because water flow through AQP4 is bidirectional (18, 19), we hypothesized that AQP4 deletion may impair the elimination of edema fluid, particularly when water enters the brain substance independent of AQP4, as is the case in vasogenic (noncellular) brain edema.”