نتایج جستجو برای: aquaporin membrane

تعداد نتایج: 393406  

Journal: :Plant physiology 1997
P. Fleurat-Lessard N. Frangne M. Maeshima R. Ratajczak J. L. Bonnemain E. Martinoia

Mature motor cells of Mimosa pudica that exhibit large and rapid turgor variations in response to external stimuli are characterized by two distinct types of vacuoles, one containing large amounts of tannins (tannin vacuole) and one without tannins (colloidal or aqueous vacuole). In these highly specialized cells we measured the abundance of two tonoplast proteins, a putative water-channel prot...

Journal: :Current Biology 2002
Richard J. Law Mark S.P. Sansom

A high-resolution X-ray structure of an aquaporin has revealed water molecules bound within the transmembrane pore and provided new clues to the mechanisms of rapid water transport and high selectivity in this important class of membrane proteins.

Journal: :Physiological reviews 2015
Christophe Maurel Yann Boursiac Doan-Trung Luu Véronique Santoni Zaigham Shahzad Lionel Verdoucq

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. Plant aquaporins are localized in the plasma membrane, endoplasmic reticulum, vacuoles, p...

Journal: :Physical chemistry chemical physics : PCCP 2014
Xian Kong Shanshan Qin Diannan Lu Zheng Liu

While the surface tension of a cell membrane, or a plasma membrane, regulates cell functions, little is known about its effect on the conformational changes of the lipid bilayer and hence the resulting changes in the cell membrane. To obtain some insights into the phase transition of the lipid bilayer as a function of surface tension, we used a 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)...

2016
Maria del Carmen Martínez-Ballesta Micaela Carvajal

In recent years, a number of studies have been focused on the structural evaluation of protein complexes in order to get mechanistic insights into how proteins communicate at the molecular level within the cell. Specific sites of protein-aquaporin interaction have been evaluated and new forms of regulation of aquaporins described, based on these associations. Heterotetramerizations of aquaporin...

2014
J.P. Fryer V.A. Lennon S.J. Pittock S.M. Jenkins P. Fallier-Becker S.L. Clardy E. Horta E.A. Jedynak C.F. Lucchinetti E.A. Shuster B.G. Weinshenker D.M. Wingerchuk A. McKeon

OBJECTIVE To compare performance of contemporary aquaporin-4-immunoglobulin (Ig) G assays in clinical service. METHODS Sera from neurologic patients (4 groups) and controls were tested initially by service ELISA (recombinant human aquaporin-4, M1 isoform) and then by cell-based fluorescence assays: fixed (CBA, M1-aquaporin-4, observer-scored) and live (fluorescence-activated cell sorting [FAC...

2010
Lei Kai Ralf Kaldenhoff Jiazhang Lian Xiangcheng Zhu Volker Dötsch Frank Bernhard Peilin Cen Zhinan Xu

The continuous progress in the structural and functional characterization of aquaporins increasingly attracts attention to study their roles in certain mammalian diseases. Although several structures of aquaporins have already been solved by crystallization, the challenge of producing sufficient amounts of functional proteins still remains. CF (cell free) expression has emerged in recent times ...

Journal: :PLoS Biology 2003
David F Savage Pascal F Egea Yaneth Robles-Colmenares Joseph D. O'Connell III Robert M Stroud

Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity res...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید