Results 51 to 60 of about 57,369 (303)

Impact of the anti-aquaporin-4 autoantibody on inner retinal structure, function and structure-function associations in Japanese patients with optic neuritis - Fig 1

, 2017
Representative cases of aquaporin-4 antibody (AQP4 Ab)-positive (A−C) and -negative (D−F) optic neuritis in the left eye. Shown are optic nerve head maps (A, D) and GCC significance maps (B, E) from RTVue optical coherence tomography analyses, and gray ...
Sotaro Mori (3749752), Yoshiko Matsumoto (3749764), Takuji Kurimoto (3749761), Akiyasu Kanamori (3749749), Makoto Nakamura (199152), Yuko Yamada (3749758), Ichiro Nakashima (3574049), Kaori Ueda (3749755)   +7 more
core   +1 more source

AQP4 (aquaporin 4) [PDF]

, 2013
Review on AQP4 (aquaporin 4), with data on DNA, on the protein encoded, and where the gene is ...
Ribatti, D, RIBATTI, Domenico, NICO, Beatrice, Nico, B   +3 more
core   +1 more source

Aquaporins in Plants

Physiological Reviews, 2015
Aquaporins are membrane channels that facilitate the transport of water and small neutral molecules across biological membranes of most living organisms. In plants, aquaporins occur as multiple isoforms reflecting a high diversity of cellular localizations, transport selectivity, and regulation properties.
Maurel, Christophe, Boursiac, Yann, Luu, Doan, Santoni, Veronique, Shahzad, Zaigham, Verdoucq, Lionel   +5 more
openaire   +5 more sources

Comparative Effectiveness and Safety of Inebilizumab Versus Rituximab in AQP4‐IgG‐Positive NMOSD

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Rituximab (anti‐CD20, RTX) and inebilizumab (anti‐CD19, INE) represent B‐cell‐depleting therapies used for aquaporin‐4 antibody‐positive (AQP4‐IgG+) neuromyelitis optica spectrum disorder (NMOSD); however, direct comparative evidence remains limited.
Jie Lin, Binbin Xue, Dewei Xie, Jia Li, Juyuan Pan, Lanbing Zhu, Qiaowen Tong, Jing Lin, Ruofan Zhu, Xu Zhang, Junhui Xia, Xiang Li   +11 more
wiley   +1 more source

The AQP2 mutation V71M causesnephrogenic diabetes insipidus in humans but does not impair the function of a bacterial homolog

FEBS Open Bio, 2015
Several point mutations have been identified in human aquaporins, but their effects on the function of the respective aquaporins are mostly enigmatic. We analyzed the impact of the aquaporin 2 mutation V71M, which causesnephrogenic diabetes insipidus in ...
Noreen Klein, Nadine Kümmerer, Dominika Hobernik, Dirk Schneider   +3 more
doaj   +1 more source

The physiological response of Populus tremula x alba leaves to the down-regulation of PIP1 aquaporin gene expression under no water stress.

Frontiers in Plant Science, 2013
In order to study the role of PIP1 aquaporins in leaf water and CO2 transport, several lines of PIP1-deficient transgenic Populus tremula x alba were generated using a reverse genetic approach. These transgenic lines displayed no visible developmental or
Francesca eSecchi, Maciej Andrzej Zwieniecki   +1 more
doaj   +1 more source

Characterization of an Aquaporin Gene ZpPIP2 from Zygophyllum potaninii [PDF]

Mongolian Journal of Biological Sciences, 2016
Zygophyllum potaninii Maxim. is a medicinal plant, distributed in arid regions of southern Mongolia. Full length of a cDNA clone, which was identifi ed as a stress induced gene by suppression subtractive hybridization was obtained by 5’RACEPCR, and ...
Bayarmaa Gun-Aajav, Munkhbileg Enkhbat, Oyuntsetseg Batlai   +2 more
doaj   +1 more source

Finding Aquaporins in Annelids: An Evolutionary Analysis and a Case Study

Cells, 2021
Aquaporins (AQPs) are a family of membrane channels facilitating diffusion of water and small solutes into and out of cells. Despite their biological relevance in osmoregulation and ubiquitous distribution throughout metazoans, the presence of AQPs in ...
Serena Mucciolo, Andrea Desiderato, Marika Salonna, Tomasz Mamos, Viviane Prodocimo, Maikon Di Domenico, Francesco Mastrototaro, Paulo Lana, Carmela Gissi, Giuseppe Calamita   +9 more
doaj   +1 more source

A refined structure of human aquaporin-1 [PDF]

, 2001
A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 A resolution and a multiple ...
Grubmüller, H., Bert L. de Groot, Engel, A., Grubmüller, Helmut, de Groot, Bert, de Groot, B., Helmut Grubmüller, Grubmueller, H., de Groot, B. L., Andreas Engel, Engel, Andreas, de Groot, Bert L.   +11 more
core   +1 more source

“Low‐Positive” MOG‐IgG Cases Among Adults With a First Event Suggestive of Multiple Sclerosis

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective To determine the prevalence and clinical characteristics of patients with “low‐positive” (LP) MOG‐IgG (titres 1:160–1:320) among adults with a first demyelinating event (FDE) suggestive of multiple sclerosis (MS). Methods From the Barcelona CIS inception cohort, we included adult patients with serum collected ≤ 6 months from the FDE.
Javier Villacieros‐Álvarez, Carmen Espejo, Georgina Arrambide, Mireia Castillo, Marta Rodriguez, Helena Ariño, Iker Elosua, Carmen Tur, Angela Vidal‐Jordana, Andreu Vilaseca, Joaquín Castilló, Ingrid Galán, Luciana Midaglia, Carlos Nos, Breogan Rodríguez‐Acevedo, Ana Zabalza, Luca Bollo, Agustín Pappolla, René Carvajal, Neus Mongay‐Ochoa, Jordi Rio, Jaume Sastre‐Garriga, Manuel Comabella, Gesualdina Busiello, Sofia Sceppacuercia, Àlex Rovira, Xavier Montalban, Mar Tintoré, Cristina Auger, Álvaro Cobo‐Calvo   +29 more
wiley   +1 more source