Results 61 to 70 of about 5,860 (202)

Canonical and non‐canonical functions of proteins regulating mitochondrial dynamics in mammalian physiology

open access: yesThe Journal of Physiology, EarlyView.
Abstract figure legend Mitochondria are highly dynamic organelles that continuously remodel their architecture through coordinated cycles of fusion and fission. This review examines the four key GTPases that orchestrate mitochondrial dynamics in mammals: MFN1, MFN2, OPA1, and DRP1.
Rémi Chaney   +4 more
wiley   +1 more source

P4 ATPases: Flippases in Health and Disease

open access: yes, 2013
P4 ATPases catalyze the translocation of phospholipids from the exoplasmic to the cytosolic leaflet of biological membranes, a process termed "lipid flipping".
Oude Elferink, Ronald P. J.   +5 more
core   +1 more source

Ischemia–Reperfusion Injury: Molecular Mechanisms and Therapeutic Interventions

open access: yesMedComm, Volume 7, Issue 7, July 2026.
Multiorgan ischemia–reperfusion injury begins with ischemia‐induced ATP depletion and ionic imbalance, followed by reperfusion‐triggered mitochondrial ROS/RNS bursts, regulated cell death, and DAMP release. Sterile inflammation converges on endothelial–immune–coagulation crosstalk, where NETs drive immunothrombosis, no‐reflow, and remote organ injury ...
Peng An   +4 more
wiley   +1 more source

Physiological and pharmacological characterizations of the larval Anopheles albimanus rectum support a change in protein distribution and/or function in varying salinities [PDF]

open access: yes, 2010
Ion regulation is a biological process crucial to the survival of mosquito larvae and a major organ responsible for this regulation is the rectum. The recta of anopheline larvae are distinct from other subfamilies of mosquitoes in several ways, yet have ...
Valenti, Micheala L.   +4 more
core   +1 more source

Redox signals and oxidative stress in the control of mitochondrial protein import

open access: yesProtein Science, Volume 35, Issue 7, July 2026.
Abstract Mitochondrial protein import is essential for organelle biogenesis and cellular homeostasis. It operates in an environment that is intrinsically shaped by redox chemistry. Mitochondria are major sources of reactive oxygen species (ROS), which arise as by‐products of oxidative phosphorylation. Cells therefore maintain sophisticated ROS‐handling
Lidwina Hasberg   +3 more
wiley   +1 more source

Distinct functional roles for the Menkes and Wilson copper translocating P-type ATPases in Human Placental Cells

open access: yes, 2007
Distinct functional roles for the Menkes and Wilson copper translocating P-type ATPases in Human Placental ...
Agnes Michalczyk (13056828)   +5 more
core  

Investigating the proton-transolcating subunit of the rotary A-type ATPase

open access: yes, 2016
All forms of life are dependent on proton gradients as a source of energy to power essential cellular processes, and they all store this energy in the form of the nucleotide adenosine triphosphate (ATP).
Laming, Elise
core   +1 more source

Intracellular proton pumps as targets in chemotherapy: V-ATPases and cancer [PDF]

open access: yes, 2012
Cancer cells show a metabolic shift that makes them overproduce protons; this has the potential to disturb the cellular acid-base homeostasis. However, these cells show cytoplasmic alkalinisation, increased acid
Hernández López, Agustín   +3 more
core   +1 more source

Integrated genomic and transcriptomic approaches reveal oxidative stress adaptation mechanisms in a mesotrione‐resistant Amaranthus tuberculatus biotype

open access: yesPest Management Science, Volume 82, Issue 7, Page 6387-6398, July 2026.
Integrated GWAS and transcriptomics in a Canadian waterhemp biotype reveal mesotrione resistance is polygenic and metabolically driven. Significant SNPs and 187 herbicide‐responsive genes point to enhanced redox homeostasis, glutathione‐linked detoxification, lipid/secondary metabolism, and oxidative stress responses. Resistance arises from coordinated,
Martin Laforest   +6 more
wiley   +1 more source

Features of V-ATPases that distinguish them from F-ATPases

open access: yes, 2001
The general structure of F- and V-ATPases is quite similar and they may share a common mechanism of action that involves mechanochemical energy transduction. Both holoenzymes are composed of catalytic sectors, F1 and V1 respectively, and membrane sectors,
Nelson, Nathan   +7 more
core   +1 more source

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