Results 291 to 300 of about 66,670 (341)
An atlas of plant selenium metabolism
Summary Selenium (Se) is not only a rare and toxic element but also an essential micronutrient for humans and animals that is often in short supply. Terrestrial plants do not require Se, but it can have growth‐promoting or negative effects, depending on the exposure level.
Jeroen van der Woude +3 more
wiley +1 more source
ABSTRACT Heat stress significantly damages crop yield and quality. PLATZ (PLANT A/T‐RICH SEQUENCE‐AND ZINC‐BINDING PROTEIN) transcription factors play pivotal roles in plant growth, development, and environmental stress responses. While the functions of PLATZ members in response to drought and salt stress are well characterised, their roles in heat ...
Xue Gong +7 more
wiley +1 more source
Abstract Restriction of fetal substrate supply has an adverse effect on surfactant maturation in the lung and thus affects the transition from in utero placental oxygenation to pulmonary ventilation ex utero. However, the consequences of reduced fetal substrate supply are dependent on the timing of gestation, severity and duration.
Mitchell C. Lock +5 more
wiley +1 more source
Bulky residues constrict the central pore of WT SoPIP2;1, generating high energy barriers for both O2 and CO2 and preventing gas permeation. ABSTRACT Aquaporins (AQPs) are classical water channels that also conduct small gas molecules such as O2$$ {\mathrm{O}}_2 $$ and CO2$$ {\mathrm{CO}}_2 $$ across the membrane.
Ahmad Raeisi Najafi +5 more
wiley +1 more source
A novel interaction between aquaporin 1 and caspase-3 in pulmonary arterial smooth muscle cells.
Niedermeyer S +8 more
europepmc +1 more source
Accumulation of Astrocytic Aquaporin 4 and Aquaporin 1 in Prion Protein Plaques
openaire
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Structural determinants of water permeation through aquaporin-1
Nature, 2000Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues
Murata, K. +7 more
openaire +5 more sources

