Results 81 to 90 of about 10,440,305 (287)

V-ATPase subunit B plays essential roles in the molting process of the Chinese mitten crab, Eriocheir sinensis

open access: yesBiology Open, 2020
Vacuolar ATPase (V-ATPase) is a proton pump driven by ATP hydrolysis, and it plays an important role in numerous biological processes, such as protein degradation and synthesis, cell growth, and cell autophagy.
Xin Hou   +6 more
doaj   +1 more source

Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein. [PDF]

open access: yesPLoS Pathogens, 2017
Intracellular pathogenic bacteria evade the immune response by replicating within host cells. Legionella pneumophila, the causative agent of Legionnaires' Disease, makes use of numerous effector proteins to construct a niche supportive of its replication
Jianhua Zhao   +11 more
doaj   +1 more source

Genetic dissection of human ABCE1 in yeast reveals separable requirements for ribosome recycling and suppression of aberrant reinitiation

open access: yesFEBS Open Bio, EarlyView.
Human ABCE1 cannot functionally replace its yeast ortholog. Yeast–human chimera analysis identified NBD1 as a major interspecies barrier. Genetic screening yielded hABCE1 revertants that rescue yeast viability but fail to suppress aberrant translation reinitiation in the 3′ UTR.
Eriko Nakata   +3 more
wiley   +1 more source

Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids

open access: yesFrontiers in Cell and Developmental Biology, 2020
Luminal pH and the distinctive distribution of phosphatidylinositol phosphate (PIP) lipids are central identifying features of organelles in all eukaryotic cells that are also critical for organelle function.
Subhrajit Banerjee, Patricia M. Kane
doaj   +1 more source

Infrared spectroscopic studies on the V-ATPase

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2015
V-ATPase is an ATP-driven rotary motor that vectorially transports ions. Together with F-ATPase, a homologous protein, several models on the ion transport have been proposed, but their molecular mechanisms are yet unknown. V-ATPase from Enterococcus hirae forms a large supramolecular protein complex (total molecular weight: ~700,000) and ...
Kandori, Hideki   +2 more
openaire   +2 more sources

Identification and characterization of a gene conferring stress resistance in Escherichia coli and cyanobacteria

open access: yesFEBS Open Bio, EarlyView.
Functional screening identified PcSyn14890, a cyanobacteria‐specific protein that enhances growth and stress resistance in E. coli and Synechocystis PCC6803. Although we expected it to function as a molecular chaperone, it was unable to protect against thermal aggregation of GAPDH.
Akiyo Yamada   +7 more
wiley   +1 more source

Yeast V-ATPase Regulation by Phosphofructokinase-1 [PDF]

open access: yes, 2015
V-ATPase is a vacuolar (lysosome-like) ATPase-dependent proton pump necessary for maintaining pH homeostasis in the organelles of the endomembrane system. It also contributes to regulation of the cytosol pH and the extracellular pH. In specialized cells (
Chan, Chun-Yuan
core   +1 more source

The structure and function of the fungal V-ATPase [PDF]

open access: yesJournal of Experimental Biology, 1992
ABSTRACT The fungal vacuole is a prominent organelle that functions as a storage site for amino acids, Ca2+, storage carbohydrates, inorganic phosphate and numerous hydrolases (Fig. 1) (Klionsky et al. 1990). A hallmark of fungal vacuoles is that they are acidic compartments involved in the turnover of cellular macromolecules.
openaire   +2 more sources

Mitf is a master regulator of the v-ATPase forming an Mitf/v-ATPase/TORC1 control module for cellular homeostasis [PDF]

open access: yesJournal of Cell Science, 2015
The v-ATPase is a fundamental eukaryotic enzyme central to cellular homeostasis. Although its impact on key metabolic regulators such as TORC1 is well-documented, our knowledge of mechanisms that regulate v-ATPase activity is limited. Here, we report that the Drosophila transcription factor Mitf is a master regulator of this holoenzyme.
Zhang, T.   +11 more
openaire   +3 more sources

Configuration of the myxobacterial polyketide Archazolid A, a potent inhibitor of vacuolar-type ATPase (V-ATPase).

open access: yes, 2014
Configuration of the myxobacterial polyketide Archazolid A, a potent inhibitor of vacuolar-type ATPase (V-ATPase).
Rainer Wilcken (509958)   +6 more
core   +1 more source

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