Results 31 to 40 of about 547,455 (357)

LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate [PDF]

, 2016
Background Lrrk2, a gene linked to Parkinson\u2019s disease, encodes a large scaffolding protein with kinase and GTPase activities implicated in vesicle and cytoskeletal-related processes.
Arrigoni, Giorgio, Belluzzi, Elisa, Beltramini, Mariano, Bubacco, Luigi, Carrion, Maria Per\ue8z, Cirnaru, Maria Daniela, Civiero, Laura, Cogo, Susanna, Franchin, Cinzia, Gonnelli, Adriano, Greggio, Elisa, Marte, Antonella, Onofri, Franco, Piccoli, Giovanni, Plotegher, Nicoletta, Russo, Isabella   +15 more
core   +5 more sources

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, Hallie S. Rane, Karlett J. Parra   +2 more
doaj   +1 more source

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

, 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, Boersch, Michael, Boettcher, Bettina, Ernst, Stefan, Zarrabi, Nawid   +4 more
core   +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, Chung, Clive Yik-Sham, Ford, Breanna, Nomura, Daniel K, Olzmann, James A, Shin, Hijai R, Ward, Carl C, Zoncu, Roberto   +7 more
core   +1 more source

Chaperones of F1-ATPase [PDF]

Journal of Biological Chemistry, 2009
Mitochondrial F(1)-ATPase contains a hexamer of alternating alpha and beta subunits. The assembly of this structure requires two specialized chaperones, Atp11p and Atp12p, that bind transiently to beta and alpha. In the absence of Atp11p and Atp12p, the hexamer is not formed, and alpha and beta precipitate as large insoluble aggregates.
Ludlam, Anthony, Brunzelle, Joseph, Pribyl, Thomas, Xu, Xingjue, Gatti, Domenico L., Ackerman, Sharon H.   +5 more
openaire   +2 more sources

The parietal cell gastric H, K-ATPase also functions as the Na, K-ATPase and Ca-ATPase in altered states [v2; ref status: indexed, http://f1000r.es/1tc]

F1000Research, 2013
This article offers an explanation for the apparent lack of Na, K-ATPase activity in parietal cells although ouabain has been known to inhibit gastric acid secretion since 1962.
Tushar Ray
doaj   +1 more source

Subunit interactions influence the biochemical and biological properties of Hsp104 [PDF]

, 2001
Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo. In vitro, NBD1 mutations virtually eliminate ATP hydrolysis with little effect on hexamerization; analogous ...
Kowal, Anthony S, Lindquist, Susan L, Queitsch, Christine, Schirmer, Eric, Ware, Danielle M   +4 more
core   +2 more sources

Dynamics of enzymatic activity in primary culture of Syrian hamster adherent leukocytes ex vivo infected with SARS-CoV-2

Журнал микробиологии, эпидемиологии и иммунобиологии
Introduction. The continued epidemic relevance of SARS-CoV-2, even after the end of the associated COVID-19 pandemic in 2023, necessitates further study of the interaction of this virus with the first line of cellular defense, neutrophils.
Svetlana A. Abramova, Irina N. Lyapun, Elena I. Drobot, Natalia V. Krylova, Olga V. Iunikhina, Valeria A. Lubova, Evgeniy K. Merlov, Iurii A. Belov, Larisa M. Somova, Mikhail Yu. Shchelkanov   +9 more
doaj   +1 more source

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

FEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang, Naoki Sunagawa, Toma Kashima, Kiyohiko Igarashi, Akimasa Miyanaga, Shinya Fushinobu   +5 more
wiley   +1 more source

Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex [PDF]

, 2012
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an essential protein translocation machinery. The nature of the conformational changes induced by each stage of the hydrolytic cycle of ATP and how they are coupled to protein ...
Alice Robson, Bauer, Berger, Bessonneau, Breyton, Brundage, Cannon, Dalal, Deville, Ding, Duong, Egea, Erlandson, Erlandson, Gelis, Gold, Gold, Gold, Hizlan, Hunt, Ian Collinson, Karamanou, Lill, Or, Osborne, Osborne, Park, Park, Piggot, Piggot, Richard B. Sessions, Robson, Robson, Robson, Sarah Whitehouse, Tam, Van den Berg, Vicki A.M. Gold, William J. Allen, Wolf, Woodbury, Zimmer, Zimmer   +42 more
core   +2 more sources