Results 21 to 30 of about 156,998 (303)
Duelling functions of the V‐ATPase [PDF]
The EMBO Journal, 2011 The V‐ATPase, the major cellular proton pump, is comprised of the peripheral sector V1 catalysing ATP hydrolysis and the membrane integral sector V0 translocating protons. Ten years ago, Andreas Mayer9s group made the surprising observation that proteolipids of the V0 transmembrane sector are implicated in membrane fusion, but deeper analysis proved to
Scott Cameron C +2 more
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Development of RNAi methods for Peregrinus maidis, the corn planthopper. [PDF]
PLoS ONE, 2013 The corn planthopper, Peregrinus maidis, is a major pest of agronomically-important crops. Peregrinus maidis has a large geographical distribution and transmits Maize mosaic rhabdovirus (MMV) and Maize stripe tenuivirus (MSpV).
Jianxiu Yao +4 more
doaj +1 more source
Reciprocal Regulation of V-ATPase and Glycolytic Pathway Elements in Health and Disease
Frontiers in Physiology, 2019 The ability of cells to adapt to fluctuations in glucose availability is crucial for their survival and involves the vacuolar proton-translocating ATPase (V-ATPase), a proton pump found in all eukaryotes.
Summer R. Hayek +2 more
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Regulation of vacuolar H+-ATPase activity by the Cdc42 effector Ste20 in Saccharomyces cerevisiae [PDF]
, 2012 In the budding yeast Saccharomyces cerevisiae, the Cdc42 effector Ste20 plays a crucial role in the regulation of filamentous growth, a response to nutrient limitation.
Höfken, T, Kane, PM, Li, SC, Lin, M
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The evolutionary conserved TLDc domain defines a new class of (H+)V-ATPase interacting proteins
Scientific Reports, 2021 We recently found that nuclear receptor coactivator 7 (Ncoa7) and Oxr1 interact with the proton-pumping V-ATPase. Ncoa7 and Oxr1 belong to a group of proteins playing a role in the oxidative stress response, that contain the conserved “TLDc” domain. Here
A. F. Eaton, D. Brown, M. Merkulova
doaj +1 more source
Covalent targeting of the vacuolar H+-ATPase activates autophagy via mTORC1 inhibition. [PDF]
, 2019 Autophagy is a lysosomal degradation pathway that eliminates aggregated proteins and damaged organelles to maintain cellular homeostasis. A major route for activating autophagy involves inhibition of the mTORC1 kinase, but current mTORC1-targeting ...
Berdan, Charles A +7 more
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Translational Neurodegeneration, 2020 Background Lysosomes digest extracellular material from the endocytic pathway and intracellular material from the autophagic pathway. This process is performed by the resident hydrolytic enzymes activated by the highly acidic pH within the lysosomal ...
Qiaoyun Song +3 more
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Wheat V-H+-ATPase subunit genes significantly affect salt tolerance in Arabidopsis thaliana. [PDF]
PLoS ONE, 2014 Genes for V-H(+)-ATPase subunits were identified and cloned from the salt-tolerant wheat mutant RH8706-49. Sequences of these genes are highly conserved in plants.
Xiaoliang He +3 more
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Regulation of proton-translocating V-ATPases [PDF]
Journal of Experimental Biology, 1997 ABSTRACT Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning Vo domain.
H, Merzendorfer +4 more
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mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H+-ATPase [PDF]
, 2011 The mTOR complex 1 (mTORC1) protein kinase is a master growth regulator that is stimulated by amino acids. Amino acids activate the Rag guanosine triphosphatases (GTPases), which promote the translocation of mTORC1 to the lysosomal surface, the site of ...
Bar-Peled, Liron +5 more
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