Results 111 to 120 of about 156,233 (327)

In situ analysis of pH gradients in mosquito larvae using non-invasive, self-referencing, pH-sensitive microelectrodes

open access: yes, 2001
The alkaline environment, pH approximately 11, in the anterior midgut lumen of mosquito larvae is essential for normal nutrition and development. The mechanism of alkalization is, however, unknown.
Boudko, D.Y.   +5 more
core  

Regulatory assembly of the vacuolar proton pump VOV1-ATPase in yeast cells by FLIM-FRET

open access: yes, 2010
We investigate the reversible disassembly of VOV1-ATPase in life yeast cells by time resolved confocal FRET imaging. VOV1-ATPase in the vacuolar membrane pumps protons from the cytosol into the vacuole. VOV1-ATPase is a rotary biological nanomotor driven
Batisse, Claire   +4 more
core   +1 more source

Metallofullerenol Sc3N@C80(OH)18: A New Generation Radioprotector Protecting Human Erythrocytes Against Multiple Biochemical Damage Modes Upon Gamma Irradiation, Identifying It as a Scavenger of Short‐ and Long‐Lived Radicals

open access: yesAdvanced Healthcare Materials, EarlyView.
Metallofullerenol Sc3N@C80(OH)18 demonstrates strong radioprotective properties as a scavenger of both short‐ and long‐lived radicals. The study reveals protection of human erythrocytes from γ‐radiation–induced biochemical damage via post‐irradiation removal of primary and secondary reactive oxidants, supported by pulse radiolysis kinetics.
Jacek Grebowski   +6 more
wiley   +1 more source

コウボ エキホウマク ATPase ノ コウゾウ ト キノウ [PDF]

open access: yes, 2005
The yeast vacuolar membrane H+-ATPase (V-ATPase) is the first member of "vacuolar type" ATPase family that has been successively identified in various endocytic and exocytic membrane compartments of eukaryotic cells.
Yasuhiro Anraku   +2 more
core  

Expanding tole for V-ATPases

open access: yesTrends in Genetics, 2000
Vacuolar proton-conducting ATPases (V-ATPases) are key components in the control of pH and ionic homeostasis in eukaryotes. They feature centrally in plant cell biology because, in plants, proton gradients support the bulk of secondary active transport of solutes and ions. However, genetic analysis of V-ATPase function in plants has been lacking.
openaire   +2 more sources

Redefining Therapies for Drug‐Resistant Tuberculosis: Synergistic Effects of Antimicrobial Peptides, Nanotechnology, and Computational Design

open access: yesAdvanced Healthcare Materials, EarlyView.
Antimicrobial peptide (AMP)‐loaded nanocarriers provide a multifunctional strategy to combat drug‐resistant Mycobacterium tuberculosis. By enhancing intracellular delivery, bypassing efflux pumps, and disrupting bacterial membranes, this platform restores phagolysosome fusion and macrophage function.
Christian S. Carnero Canales   +11 more
wiley   +1 more source

Lysosomal dysfunction by inactivation of V-ATPase drives innate immune response in C. elegans

open access: yesCell Reports
Summary: Pathogens target vacuolar ATPase (V-ATPase) to inhibit lysosomal acidification or lysosomal fusion, causing lysosomal dysfunction. However, it remains unknown whether cells can detect dysfunctional lysosomes and initiate an immune response.
Xuepiao Pu, Bin Qi
doaj   +1 more source

DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase

open access: yeseLife, 2014
Escherichia coli DNA polymerase V (pol V), a heterotrimeric complex composed of UmuD′2C, is marginally active. ATP and RecA play essential roles in the activation of pol V for DNA synthesis including translesion synthesis (TLS). We have established three
Aysen L Erdem   +5 more
doaj   +1 more source

Fehérjék membránba ágyazódásának, szerveződésének és lipidekkel való kölcsönhatásának biofizikája = Biophysics of protein insertion and folding in membranes and their interaction with lipids [PDF]

open access: yes, 2007
1. A vakuólum ATPáz (V-ATPáz). Ez a membránkötött molekuláris motor az ATP hidrolízisből nyert kémiai energia révén protonokat pumpál a membránon keresztül, ami miatt a csontritkulás potenciális terápiájában ez az egyik kulcs target enzim.
Bérczi, Alajos   +5 more
core  

Cytosolic Glucosylceramide regulates endolysosomal function in Niemann-Pick type C disease [PDF]

open access: yes, 2019
A new paradigm for Niemann-Pick C disease is presented where lysosomal storage leads to a deficit in cytoplasmic glucosylceramide (GlcCer) where it performs important functions.
Bhardwaj, Meenakshi   +5 more
core   +1 more source

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