Results 51 to 60 of about 52,178 (309)

Aquaporin-Incorporated Biomimetic Membranes [PDF]

open access: yes, 2016
Aquaporin, a transmembrane protein, has attracted attention globally since its serendipitous discovery by Peter Agre in 1992 (Agre 2006). Its facilitation in rapid and selective water transport has inspired many scientists to utilize this unique function
Guofei Sun   +9 more
core   +1 more source

Carbonic anhydrase 12 mutation modulates membrane stability and volume regulation of aquaporin 5

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2019
Patients carrying the carbonic anhydrase12 E143K mutation showed the dry mouth phenotype. The mechanism underlying the modulation of aquaporin 5 and function in the salivary glands by carbonic anhydrase12 remains unknown. In this study, we identified the
Soyoung Hwang   +4 more
doaj   +1 more source

Aquaporins in endothelia [PDF]

open access: yesKidney International, 2006
Aquaporin-1 (AQP1) water channels are expressed widely in microvascular endothelia outside of the central nervous system, including renal vasa recta and tumor microvessels, as well as in non-vascular endothelia in pleura, peritoneum, cornea, and lymphatics.
openaire   +2 more sources

Aquaporins at a glance [PDF]

open access: yesJournal of Cell Science, 2011
With a concentration of 55,000 mM, water is by far the most prevalent molecule in biological systems. For many years it was assumed that biological membranes are freely water permeable, so that the existence of a family of water channels would not have been predicted.
openaire   +2 more sources

Aquaporin‐3 and aquaporin‐5 impact the development of pancreatic ductal adenocarcinoma spheroids

open access: yesFEBS Open Bio, EarlyView.
Schematic representation of the role of aquaporin‐3 (AQP3) and aquaporin‐5 (AQP5) in pancreatic ductal adenocarcinoma (PDAC). Both proteins are upregulated in PDAC and are associated with tumor progression and metastatic potential. Silencing AQP3 or AQP5 in PDAC spheroids results in decreased diameter, area, and overall growth, underscoring their key ...
Catarina Pimpão   +3 more
wiley   +1 more source

Towards a structural and functional understanding of human aquaporin 9 [PDF]

open access: yes, 2007
Human aquaporin 9 (hAQP9) is one of the glycerol channels that are a member of the aquaporin family. AQP9 have been shown to have the broadest specificity among the aquaporins. Except for glycerol and water it facilitates the transport of urea, arsenite,
Lindkvist-Petersson, Karin,   +4 more
core   +2 more sources

Paramagnetic Rim Lesions Are Associated With Trans‐Synaptic Degeneration of the Visual Pathway in Multiple Sclerosis

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objectives Retrograde trans‐synaptic degeneration (rTSD) from posterior visual pathway lesions in multiple sclerosis (MS) is characterized by hemi‐macular ganglion cell‐inner plexiform layer (GCIPL) thinning and contralateral visual field loss.
Abdul Jaber Tayem   +17 more
wiley   +1 more source

Aquaporin-4

open access: yesRinsho Shinkeigaku, 2008
In human body, there are thirteen water channels but their expression patterns are tissue specific. Aquaporin-4 (AQP4) is a predominantly expressed water channel in the mammalian brain and an important drug target for treatment of cerebral edema, bipolar disorder, and mesial temporal lobe epilepsy.
Tani, Kazutoshi   +2 more
openaire   +3 more sources

Understanding Further the Phenotypic Spectrum of Central Nervous System Inflammatory Demyelinating Disorders Using Unsupervised Clustering

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Background Central nervous system (CNS) inflammatory demyelinating syndromes, including multiple sclerosis (MS), aquaporin‐4 antibody–positive neuromyelitis optica spectrum disorder (AQP4 + NMOSD), and myelin oligodendrocyte glycoprotein (MOG) antibody–associated disease (MOGAD), occasionally overlap.
Bade Gulec   +6 more
wiley   +1 more source

2D-crystallization and 3D-structures of membrane channels and transporters [PDF]

open access: yes, 2004
Membrane proteins are responsible for a broad spectrum of biological functions such as signal transduction, structural functions, energy conversion or transport of matter across the membranes.
Braun, Thomas
core   +1 more source

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