Results 41 to 50 of about 697,459 (324)

Conformational Changes in Myosin under ATP Hydrolysis [PDF]

open access: yesEuropean Journal of Biochemistry, 1974
During ATP hydrolysis by spin‐labelled myosin the time‐dependent local conformational changes near S1 thiol groups have been observed. In the steady‐state stage of ATP hydrolysis practically all myosin molecules are in conformationally changed state M̃.
L A, Blumenfeld, L G, Ignatéva
openaire   +2 more sources

In vivo analysis reveals that ATP-hydrolysis couples remodeling to SWI/SNF release from chromatin

open access: yeseLife, 2021
ATP-dependent chromatin remodelers control the accessibility of genomic DNA through nucleosome mobilization. However, the dynamics of genome exploration by remodelers, and the role of ATP hydrolysis in this process remain unclear.
Ben C Tilly   +7 more
doaj   +1 more source

Insights into the cooperative nature of ATP hydrolysis in actin filaments

open access: yesbioRxiv, 2018
Actin filaments continually assemble and disassemble within a cell. Assembled filaments “age” as a bound nucleotide ATP within each actin subunit quickly hydrolyzes, followed by a slower release of the phosphate Pi, leaving behind a bound ADP.
H. Katkar   +6 more
semanticscholar   +1 more source

ATP hydrolysis by UPF1 is required for efficient translation termination at premature stop codons

open access: yesNature Communications, 2016
Nonsense-mediated mRNA decay (NMD) represents a eukaryotic quality control pathway that recognizes and rapidly degrades transcripts harbouring nonsense mutations to limit accumulation of non-functional and potentially toxic truncated polypeptides.
Lucas D. Serdar   +2 more
semanticscholar   +1 more source

ATP binding by an F1Fo ATP synthase ε subunit is pH dependent, suggesting a diversity of ε subunit functional regulation in bacteria

open access: yesFrontiers in Molecular Biosciences, 2023
It is a conjecture that the ε subunit regulates ATP hydrolytic function of the F1Fo ATP synthase in bacteria. This has been proposed by the ε subunit taking an extended conformation, with a terminal helix probing into the central architecture of the ...
Alexander Krah   +8 more
doaj   +1 more source

Regulation of Ecto-5´-Nucleotidase by Docosahexaenoic Acid in Human Endothelial Cells

open access: yesCellular Physiology and Biochemistry, 2013
Background/Aims: Modulation of extracellular adenine nucleotide and adenosine concentrations is one potential mechanism by which docosahexaenoic acid (DHA) may exert beneficial effects in critically ill patients.
Vu Thi Thom   +2 more
doaj   +1 more source

The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity. [PDF]

open access: yesPLoS ONE, 2012
Hsc70 is a conserved ATP-dependent molecular chaperone, which utilizes the energy of ATP hydrolysis to alter the folding state of its client proteins. In contrast to the Hsc70 systems of bacteria, yeast and humans, the Hsc70 system of C. elegans (CeHsc70)
Li Sun   +5 more
doaj   +1 more source

Rate Acceleration of ATP Hydrolysis by F1Fo-ATP Synthase [PDF]

open access: yesJournal of Experimental Biology, 2000
ABSTRACT The rate acceleration of ATP hydrolysis by F1Fo-ATP synthase is of the order of 1011-fold. We present a cyclic enzyme mechanism for the reaction, relate it to known F1 X-ray structure and speculate on the linkage between enzyme reaction intermediates and subunit rotation.
A E, Senior, S, Nadanaciva, J, Weber
openaire   +2 more sources

Energy interconversion by the sarcoplasmic reticulum Ca2+-ATPase: ATP hydrolysis, Ca2+ transport, ATP synthesis and heat production

open access: yesAnais da Academia Brasileira de Ciências, 2000
The sarcoplasmic reticulum of skeletal muscle retains a membrane bound Ca2+-ATPase which is able to interconvert different forms of energy. A part of the chemical energy released during ATP hydrolysis is converted into heat and in the bibliography it is ...
LEOPOLDO DE MEIS
doaj   +1 more source

Phosphorus Chemistry at the Roots of Bioenergetics: Ligand Permutation as the Molecular Basis of the Mechanism of ATP Synthesis/Hydrolysis by FOF1-ATP Synthase

open access: yesMolecules, 2023
The integration of phosphorus chemistry with the mechanism of ATP synthesis/hydrolysis requires dynamical information during ATP turnover and catalysis. Oxygen exchange reactions occurring at β-catalytic sites of the FOF1-ATP synthase/F1-ATPase imprint a
Sunil Nath
doaj   +1 more source

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