Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + actin
ADP + phosphate + actin
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
CTP + H2O + actin
CDP + phosphate + actin
-
-
-
-
?
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
gTP + H2O + actin
GDP + phosphate + actin
-
-
-
-
?
GTP + H2O + myosin bound to actin filament at position n
GDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ITP + H2O + actin
IDP + phosphate + actin
-
-
-
-
?
ITP + H2O + myosin bound to actin filament at position n
IDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
TTP + H2O + actin
TDP + phosphate + actin
-
-
-
-
?
UTP + H2O + actin
UDP + phosphate + actin
-
-
-
-
?
UTP + H2O + myosin bound to actin filament at position n
UDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
additional information
?
-
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
nucleoside triphosphates are hydrolyzed in decreasing order: GTP, ITP, CTP, ATP, UTP
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
nucleoside triphosphates are hydrolyzed in the following order: GTP, ITP, CTP, ATP, UTP
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
ATP binding site of myosin and catalytically active conformation, modeling and analysis of crystal structure, PDB 1VOM
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
P13538; P02609; P02604
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
Delivering of F-actin to the lamella of migrating fibroblasts
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
Lethocerus griseus
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
246975, 246976, 246978, 246983, 246995, 246996, 246997, 247001, 247004, 247005, 733515, 733791, 735020, 749738, 749747, 749819, 749998, 751659 -
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
246977, 246980, 246982, 246988, 246998, 247002, 695471, 697052, 735134, 751816, 751969 -
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
CTP + H2O + myosin bound to actin filament at position n
CDP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
additional information
?
-
during its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP
-
-
?
additional information
?
-
P13538; P02609; P02604
myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain (lever arm) relative to the motor domain during the ATPase cycle. This rotation can be accompanied by an interaction between the motor domain and the C-terminus of the essential light chain associated with the regulatory domain. During rotation, the regulatory domain acts as a semi-rigid lever arm, which amplifies and transmits conformational changes occurring in the motor domain during ATP hydrolysis, the sliding velocity of actin filaments in the in vitro motility assay strongly depends on the length of the lever arm. The essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle
-
-
?
additional information
?
-
-
contraction of free-floating-fibroblast-populated collagen lattice through elongated fibroblasts and rapid myosin ATPase, requiring tyrosine phosphorylation. The mechanism for attached-delayed-released-fibroblast-populated collagen lattice contraction is through cell contraction by sustained myosin ATPase, involving tyrosine dephosphorylation
-
-
?
additional information
?
-
-
kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates. The results are consistent with a dual rate-limitation model in which the rate of force recovery is limited by both NTP cleavage and phosphate release, with their relative contributions and apparent rate constants influenced by an intervening rapid force-generating transition
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
additional information
?
-
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
nucleoside triphosphates are hydrolyzed in the following order: GTP, ITP, CTP, ATP, UTP
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
P13538; P02609; P02604
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
Delivering of F-actin to the lamella of migrating fibroblasts
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
Lethocerus griseus
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
246975, 246976, 246978, 246983, 246995, 246996, 246997, 247001, 247004, 247005, 733515, 733791, 735020, 749738, 749747, 749819, 749998, 751659 -
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
?
ATP + H2O + myosin bound to actin filament at position n
ADP + phosphate + myosin bound to actin filament at position n+1
-
-
-
-
ir
additional information
?
-
during its contraction cycle, the myosin motor catalyzes the hydrolysis of ATP
-
-
?
additional information
?
-
P13538; P02609; P02604
myosin head (myosin subfragment 1, S1) consists of two major structural domains, the motor (or catalytic) domain and the regulatory domain. Functioning of the myosin head as a molecular motor is believed to involve a rotation of the regulatory domain (lever arm) relative to the motor domain during the ATPase cycle. This rotation can be accompanied by an interaction between the motor domain and the C-terminus of the essential light chain associated with the regulatory domain. During rotation, the regulatory domain acts as a semi-rigid lever arm, which amplifies and transmits conformational changes occurring in the motor domain during ATP hydrolysis, the sliding velocity of actin filaments in the in vitro motility assay strongly depends on the length of the lever arm. The essential light chain associated with the regulatory domain may play a crucial role in the motor function of the myosin head, taking part in the overall stabilization of the S1 molecule during the ATPase cycle
-
-
?
additional information
?
-
-
contraction of free-floating-fibroblast-populated collagen lattice through elongated fibroblasts and rapid myosin ATPase, requiring tyrosine phosphorylation. The mechanism for attached-delayed-released-fibroblast-populated collagen lattice contraction is through cell contraction by sustained myosin ATPase, involving tyrosine dephosphorylation
-
-
?
additional information
?
-
-
kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates. The results are consistent with a dual rate-limitation model in which the rate of force recovery is limited by both NTP cleavage and phosphate release, with their relative contributions and apparent rate constants influenced by an intervening rapid force-generating transition
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-(2)-blebbistatin
-
-
-
1-(4-methoxyphenyl)-2-phenyl-1H-pyrrole
-
-
2,3,4-tribromo-5-(2-methoxyphenyl)-1-methyl-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-dibromo-2-hydroxyphenyl)-1-methyl-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
2,3,4-tribromo-5-(3,5-dichloro-2-hydroxyphenyl)-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-dichloro-2-methoxyphenyl)pyrrole
-
-
2,3,4-tribromo-5-(3,5-difluoro-2-hydroxyphenyl)-1H-pyrrole
-
-
2,3,4-tribromo-5-(3,5-difluoro-2-methoxyphenyl)-1H-pyrrole
-
-
2,3,4-trichloro-5-(2-methoxyphenyl)-1H-pyrrole
-
-
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
2,3,4-triiodo-5-(3,5-dichloro-2-methoxyphenyl)pyrrole
-
-
2,3,4-triiodo-5-(3,5-difluoro-2-methoxyphenyl)-1H-pyrrole
-
-
2,4,6-Trinitrobenzene sulfonate
2,4-dibromo-6-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
-
2,4-dibromo-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
-
2,4-dichloro-6-(3,4,5-tribromo-1H-pyrrol-2-yl)phenol
-
2,4-dichloro-6-(3,4,5-trichloro-1H-pyrrol-2-yl)phenol
-
2,4-dichloro-6-(3,4,5-triiodo-1H-pyrrol-2-yl)phenol
-
-
2,4-difluoro-6-(3,4,5-triiodo-1H-pyrrol-2-yl)phenol
-
-
2-(2-hydroxyphenyl)-1-methyl-1H-pyrrole
-
-
2-(2-hydroxyphenyl)-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1-methyl-1H-pyrrole
-
-
2-(2-methoxyphenyl)-1H-pyrrole
-
-
2-(3,4,5-tribromo-1-methyl-1H-pyrrol-2-yl)phenol
-
2-(3,5-dibromo-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-dibromo-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1-(4-methylbenzene-1-sulfonyl)-2,5-dihydro-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1-(p-tolylsulfonyl)-2,3-dihydro-1H-pyrrole
-
-
2-(3,5-difluoro-2-methoxyphenyl)-1H-pyrrole
-
-
2-Methoxybenzaldehyde
-
-
3,5-dibromo-2-methoxybenzaldehyde
-
-
3,5-dichloro-2-methoxybenzaldehyde
-
-
3,5-difluoro-2-methoxybenzaldehyde
-
-
3-morpholinosydnonimine
-
-
4-methoxy-N-[1-phenyl-4-(trimethylsilyl)but-3-yn-1-yl]aniline
-
-
ADP
-
competitive inhibition
AlF4-
-
phosphate analogue
BeFx
-
phosphate analogue
calponin
-
25% inhibition in the presence of actin, calmodulin abolishes inhibitory effect
-
cardiac myosin binding protein-C
-
reduces actin filament velocity in concentration-dependent manner: 200 nM cMYBP-C to around 25%, 400 nM cMYBP-C to almost 0%
-
D2O
-
about 50% inhibition of enzyme, increase in maximum isometric force P0 by about 20%
Fluorescein 5'-isothiocyanate
-
90% of enzyme activity is lost with the incorporation of 2.6 mol of reagent /mol of myosin, fluorescent label is mainly incorporated into the myosin heavy chain
heparin
-
heparins of molecular weights from 1.75 kDa to 11.6 kDa are competitive inhibitors
HgCl2
-
uncompetitive, 50 nM, 15% inhibition, 400 nM, 80% inhibition, DTT or glutathione protect, full activity is restored by 500 nM DTT or glutathione
KF
-
in the presence of fluoride Mg2+ and MgADP- form a stable S1-MgADP-MgFx complex, that traps the active site of S 1, Mg2+ may occupy the gamma-phosphate position in the ATP binding site of S 1
myosin
-
aging results in chemical changes in myosin (probably oxidation of cysteines) that have inhibitory effects on the actin-activated myosin ATPase
-
N-(2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-(3,5-dibromo-2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-(3,5-dichloro-2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-(3,5-difluoro-2-methoxybenzylidene)-4-methylbenzenesulfonamide
-
-
N-benzyl 4-toluene sulfonamide
-
-
N-benzyl-p-toluenesulfonamide
N-ethylmaleimide
-
in the absence of divalent cations and in the presence of K+ ions
N-[1-(2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dibromo-2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-dichloro-2-methoxyphenyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-2-(trimethylsilyl)buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-4-(trimethylsilyl)but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)-but-3-ynyl]-4-methylbenzenesulfonamide
-
-
N-[1-(3,5-difluoro-2-methoxyphenyl)buta-2,3-dien-1-yl]-4-methylbenzene-1-sulfonamide
-
-
N-[1-(methoxyphenyl)-2-(trimethylsilyl)-buta-2,3-dienyl]-4-methylbenzenesulfonamide
-
-
p-mercuribenzoate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
p-Mercuriphenyl sulfonate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
Pb(CH3COO)2
-
100 micromol lead acetate reduces myosin Ca2+ ATPase activity by 25%
phenylmercuric acetate
-
enzyme activity increases until 40% of SH-groups are titrated, complete inhibition when all SH-groups are titrated
ScFx
-
phosphate analogue
-
Troponin
-
troponin together with tropomyosin inhibits the actomyosin ATPase activity in vitro
-
VO43-
-
phosphate analog, binds in solution to myosin and inhibits its ATPase, forming a stable inactive myosin-ADP-VO43- complex (rate constant of ADP and orthovanadate dissociation about 0.00001 s-1)
Zn2+
-
about 60% residual activity at 5 mM Zn2+. Tetrahydroxythiacalix[4]arene-tetrasulfosphonate and tetrahydroxythiacalix[4]arene-tetraphosphonate restore myosin S1 ATPase activity to the control level in the presence of 5 mM Zn2+
2,3,4-tribromo-5-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
-
2,3,4-tribromo-5-(3,5-dibromo-2-methoxyphenyl)-1H-pyrrole
-
-
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
-
2,3,4-trichloro-5-(3,5-dichloro-2-methoxyphenyl)-1H-pyrrole
-
-
2,3-butanedione monoxime
-
reversible
2,3-butanedione monoxime
-
-
2,4,6-Trinitrobenzene sulfonate
-
inhibition of cardiac and skeletal myosin
2,4,6-Trinitrobenzene sulfonate
-
inhibition of cardiac and skeletal myosin
2,4,6-Trinitrobenzene sulfonate
-
inhibition of cardiac and skeletal myosin
2,4,6-Trinitrobenzene sulfonate
-
inhibition of cardiac and skeletal myosin
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
acetone
-
strong inhibition of cardiac myosin at alkaline pH, weak inhibition of skeletal myosin at alkaline pH
blebbistatin
-
100 micromol reduces appearance of new graded polarity (actomyosin) bundles within the lamella 10-fold
caldesmon
-
in the presence of actin
caldesmon
-
the mechanism of smooth muscle caldesmon-tropomyosin inhibition of the elementary steps of the actomyosin ATPase. At a physiological ratio of caldesmon to actin (1 caldesmon/7 actin monomers) actomyosin ATPase is inhibited by about 75%
caldesmon
-
caldesmon molecules are located along the thin filament and inhibit in vitro the actomyosin ATPase activity
N-benzyl-p-toluenesulfonamide
-
-
N-benzyl-p-toluenesulfonamide
-
reduces force in muscle contraction by 84% and prevents consumption of ATP during electrically stimulated contractions
tropomyosin
-
-
tropomyosin
-
tropomyosin together with troponin inhibits the actomyosin ATPase activity in vitro
vanadate
-
-
vanadate
-
decameric, noncompetitive, without actin, 50% inhibition at 0.0125 mM, in presence of 0.001 mM actin, 50% inhibition at 0.0006 mM, one V10 binding site per monomer
additional information
-
not inhibited by 20-100 mM KCl or 0-30 mM PO4 3-
-
additional information
-
Ca2+-dependent ATPase activity and enzyme protein content in muscle are reduced by ultrasonication for 10 min at 20 mHz with 0.5-1.8 mg/ml protein, e.g. loss of 47% Ca2+-dependent enzyme activity of chicken natural actomyosin at 0.5 mg/ml protein
-
additional information
-
a new state of myosin, the super relaxed state, with a very slow ATP turnover rate in skeletal muscle shows inhibition of the myosin ATPase activity caused by binding of the myosin head to the core of the thick filament in a structural motif identified by electron microscopy
-
additional information
-
pentahalogenated 2-arylpyrrole-type alkaloids pentabromopseudilin and pentachloropseudilin represent a class of isoform-specific allosteric inhibitors of myosin ATPase. Application of the silver(I)-catalyzed cycloisomerization of N-(homopropargyl)toluene-sulfonamides to the total syntheses of the natural products and several non-natural analogues. Inhibitory effect of pentahalogenated pseudilins on myosin ATPase activity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Saeiki, K.; Yasunaga, T.; Matsuura, Y.; Wakabayashi, T.
Role of residues 230 and 236 of actin in myosin-ATPase activation by actin-tropomyosin
Biochem. Biophys. Res. Commun.
275
428-433
2000
Oryctolagus cuniculus
brenda
Murphy, C.T.; Spudich, J.A.
The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
Biochemistry
38
3785-3792
1999
Gallus gallus, Oryctolagus cuniculus, Dictyostelium sp.
brenda
Katoch, S.S.; Soni, A.
Changes in myosin ATPase activity in skeletal muscles of rat during cold stress
Indian J. Biochem. Biophys.
36
204-206
1999
Rattus norvegicus
brenda
Park, S.; Ajtai, K.; Burghardt, T.P.
Inhibition of myosin ATPase by metal fluoride complexes
Biochim. Biophys. Acta
1430
127-140
1999
Oryctolagus cuniculus
brenda
Ye, L-H.; Kishi, H.; Nakamura, A.; Okagaki, T.; Tanaka, T.; Oiwa, K.; Kohama, K.
Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain
Proc. Natl. Acad. Sci. USA
96
6666-6671
1999
Gallus gallus
brenda
Degan, P.; Gesser, H.
Ca2+ activated myosin-ATPase in cardiac myofibrils of rainbow trout, freshwater turtle and rat
J. Exp. Zool.
278
381-390
1997
Oncorhynchus mykiss, Trachemys scripta, Rattus norvegicus
brenda
Rayment, I.
The structural basis of the myosin ATPase activity
J. Biol. Chem.
271
15850-15853
1996
Dictyostelium sp.
brenda
Hasson, T.; Mooseker, M.S.
Vertebrate unconventional myosins
J. Biol. Chem.
271
16431-16434
1996
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Wank, V.; Bauer, R.; Punkt, K.; Ziegan, J.
Enzyme activity patterns of myosin ATPase, alpha-glycerophosphate dehydrogenase and succinate dehydrogenase within different muscle fibre types
Acta Histochem.
96
213-218
1994
Oryctolagus cuniculus
brenda
Szymanski, P.T.; Ferguson, D.G.; Paul, R.J.
Polylysine activates smooth muscle myosin ATPase activity via induction of a 10S to 6S transition
Am. J. Physiol.
265
379-386
1993
Gallus gallus
brenda
Lin, Y.; Ye, L.H.; Ishikawa, R.; Fujita, K.; Kohama, K.
Stimulatory effect of calponin on myosin ATPase activity
J. Biochem.
113
643-645
1993
Gallus gallus
brenda
Bolognani, L.; Buttafoco, P.; Ferrari, R.; Venturelli, T.; Volpi, N.
Effects of monocarboxylic and dicarboxylic acids on myosin ATPase activity tested by luminometric procedure
Biochem. Int.
26
231-239
1992
Bos taurus
brenda
Volpi, N.; Bianchini, P.; Bolognani, L.
Competitive inhibition of myosin ATPase activity by different molecular weight heparins
Biochem. Int.
24
243-253
1991
Bos taurus
brenda
Tuxen, A.
Effect of varying the preincubation and incubation temperature on the reaction pattern for myosin ATPase in rat skeletal muscle
Acta Anat. (Basel)
139
161-163
1990
Rattus norvegicus
brenda
Abe, M.; Takahashi, K.; Hiwada, K.
Effect of calponin on actin-activated myosin ATPase activity
J. Biochem.
108
835-838
1990
Gallus gallus
brenda
Srivastava, S.; Sasser, G.; Peterson, D.L.; Driska, S.P.
Characterization of the fluorescein isothiocyanate-reactive site of gizzard myosin ATPase
Biochim. Biophys. Acta
912
230-238
1987
Meleagris gallopavo
brenda
White, D.C.S.; Ricigliano, W.; Webb, M.R.
Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements
J. Muscle Res. Cell Motil.
8
537-540
1987
Lethocerus griseus, Lethocerus indicus
brenda
Lynch, T.J.; Albanesi, J.P.; Korn, E.D.; Robinson, E.A.; Bowerst, B.; Fujisaki, H.
ATPase activities and actin-binding properties of subfragments of Acanthamoeba myosin IA
J. Biol. Chem.
261
17156-17162
1986
Acanthamoeba castellanii
brenda
Kanda, K.; Sobue, K.; Kakiuchi, S.
Phosphorylation of myosin light chain and the actin-activated ATPase activity of adrenal medullary myosin
J. Biochem.
97
961-964
1985
Bos taurus
brenda
Tamura, Y.; Kudo, T.; Sako, H.; Miyakama, S.; Nishimoto, T.; Saijo, Y.; Orino, S.; Mori, H.
Enzymatic properties of myosin ATPase from the conduction system of bovine heart
Tokushima J. Exp. Med.
32
1-8
1985
Bos taurus
brenda
Tanii, I.; Osafune, M.; Arata, T.; Inoue, A.
ATPase characterisics of myosin from nematode Caenorhabditis elegans purified by an improved method. Formation of myosin-phosphate-ADP complex and ATP-induced fluorescence enhancement
J. Biochem.
98
1201-1209
1985
Caenorhabditis elegans, Oryctolagus cuniculus
brenda
Kameyama, S.; Ichikawa, H.; Sunaga, Y.; Nakata, S.; Saito, Y.; Eiki, T.; Watanabe, S.
Biochemical characteristics of cardiac myosin: the pH dependence of Ca-ATPase activity, and that of the absorption spectrum of 2,4,6-trinitrophenyl groups attached to myosin
J. Biochem.
97
625-632
1985
Bos taurus, Gallus gallus, Oryctolagus cuniculus, Sus scrofa
brenda
Bechet, J.J.; Bachouchi, N.; Janmot, C.; d'Albis, A.
Isoenzymes of myosin subfragments. Chromatographic fractionation on carboxymethylcellulose and actin-activated ATPase activity as a function of temperature
Biochim. Biophys. Acta
703
54-61
1982
Oryctolagus cuniculus
brenda
Srivastava, S.; Kanungo, M.S.
Aging modulates some properties of skeletal myosin ATPase of rat
Biochem. Med.
28
266-272
1982
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Korn, E.D.; Collins, J.H.; Maruta, H.
Myosins from Acanthamoeba castellanii
Methods Enzymol.
85
357-363
1982
Acanthamoeba castellanii
brenda
Yamashita, T.; Tanaka, Y.; Matsuzawa, H.
Cytoplasmic and plasma membrane adenosine triphosphatase of polymorphonuclear neutrophils, comparison of their enzymatic properties and attempt for a direct determination of myosin ATPase activity using polymorphonuclear neutrophil extract
Biochim. Biophys. Acta
599
246-253
1980
Cavia porcellus
brenda
Takeuchi, K.
Comparison of kinetic properties of the ATPase reaction of arterial smooth muscle myosin with skeletal muscle myosin
J. Biochem.
88
1693-1702
1980
Bos taurus, Oryctolagus cuniculus
brenda
Pope, B.; Hoh, J.F.Y.; Weeds, A.
The ATPase activities of rat cardiac myosin isoenzymes
FEBS Lett.
118
205-209
1980
Rattus norvegicus
brenda
Shimizu, T.
Bovine platelet myosin. Properties of Mg- and Ca-ATPase
J. Biochem.
84
607-616
1978
Bos taurus
brenda
Trentham, D.R.
The adenosine triphosphatase reactions of myosin and actomyosin and their relation to energy transduction in muscle
Biochem. Soc. Trans.
5
5-22
1977
Oryctolagus cuniculus
brenda
Kielley, W.W.
Myosin adenosine triphosphatase
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
159-168
1961
Canis lupus familiaris, Oryctolagus cuniculus
-
brenda
Tiago, T.; Aureliano, M.; Gutierrez-Merino, C.
Decavanadate binding to a high affinity site near the myosin catalytic centre inhibits F-actin-stimulated myosin ATPase activity
Biochemistry
43
5551-5561
2004
Oryctolagus cuniculus
brenda
Trombetta, G.; Adami, R.; Cintio, O.; Grazi, E.
Differential response of fast and slow myosin ATPase from skeletal muscle to F-actin and to phalloidin F-actin
Biochim. Biophys. Acta
1569
135-138
2002
Oryctolagus cuniculus
brenda
Kobayashi, T.; Saeki, Y.; Chaen, S.; Shirakawa, I.; Sugi, H.
Effect of deuterium oxide on contraction characteristics and ATPase activity in glycerinated single rabbit skeletal muscle fibers
Biochim. Biophys. Acta
1659
46-51
2004
Oryctolagus cuniculus
brenda
Amitani, I.; Sakamoto, T.; Ando, T.
Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor
Biophys. J.
80
379-397
2001
Oryctolagus cuniculus
brenda
Moreira, C.M.; Oliveira, E.M.; Bonan, C.D.; Sarkis, J.J.; Vassallo, D.V.
Effects of mercury on myosin ATPase in the ventricular myocardium of the rat
Comp. Biochem. Physiol. C
135C
269-275
2003
Rattus norvegicus
brenda
Shih, W.M.; Spudich, J.A.
The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle
J. Biol. Chem.
276
19491-19494
2001
Dictyostelium discoideum
brenda
Wang, F.; Kovacs, M.; Hu, A.; Limouze, J.; Harvey, E.V.; Sellers, J.R.
Kinetic mechanism of non-muscle myosin IIB: Functional adaptations for tension generation and maintenance
J. Biol. Chem.
278
27439-27448
2003
Homo sapiens
brenda
Lowe, D.A.; Husom, A.D.; Ferrington, D.A.; Thompson, L.V.
Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats
Mech. Ageing Dev.
125
619-627
2004
Rattus norvegicus
brenda
Okafor, C.; Liao, R.; Perreault-Micale, C.; Li, X.; Ito, T.; Stepanek, A.; Doye, A.; de Tombe, P.; Gwathmey, J.K.
Mg-ATPase and Ca+ activated myosin AtPase activity in ventricular myofibrils from non-failing and diseased human hearts--effects of calcium sensitizing agents MCI-154, DPI 201-106, and caffeine
Mol. Cell. Biochem.
245
77-89
2003
Homo sapiens
brenda
Alahyan, M.; Webb, M.R.; Marston, S.B.; El-Mezgueldi, M.
The mechanism of smooth muscle caldesmon-tropomyosin inhibition of the elementary steps of the actomyosin ATPase
J. Biol. Chem.
281
19433-19448
2006
Oryctolagus cuniculus
brenda
Prochniewicz, E.; Thomas, D.D.; Thompson, L.V.
Age-related decline in actomyosin function
J. Gerontol.
A
425-431
2005
Rattus norvegicus
brenda
Burton, K.; White, H.; Sleep, J.
Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates
J. Physiol.
563
689-711
2005
Oryctolagus cuniculus
brenda
Borlak, J.; Zwadlo, C.
The myosin ATPase inhibitor 2,3-butanedione monoxime dictates transcriptional activation of ion channels and Ca(2+)-handling proteins
Mol. Pharmacol.
66
708-717
2004
Rattus norvegicus
brenda
Paul Ehrlich, H.; Sun, B.; Kainth, K.S.; Kromah, F.
Elucidating the mechanism of wound contraction: rapid versus sustained myosin ATPase activity in attached-delayed-released compared with free-floating fibroblast-populated collagen lattices
Wound Repair Regen.
14
625-632
2006
Homo sapiens
brenda
Zhong, S.; Thompson, L.V.
The roles of myosin ATPase activity and myosin light chain relative content in the slowing of type IIB fibers with hindlimb unweighting in rats
Am. J. Physiol.
293
C723-C728
2007
Rattus norvegicus
brenda
Kulikova, N.; Pronina, O.E.; Dabrowska, R.; Borovikov, Y.S.
Caldesmon restricts the movement of both C- and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle
Biochem. Biophys. Res. Commun.
345
280-286
2006
Oryctolagus cuniculus
brenda
Tiago, T.; Simao, S.; Aureliano, M.; Martin-Romero, F.J.; Gutierrez-Merino, C.
Inhibition of skeletal muscle S1-myosin ATPase by peroxynitrite
Biochemistry
45
3794-3804
2006
Oryctolagus cuniculus
brenda
Lieto-Trivedi, A.; Dash, S.; Coluccio, L.M.
Myosin surface loop 4 modulates inhibition of actomyosin 1b ATPase activity by tropomyosin
Biochemistry
46
2779-2786
2007
Mammalia
brenda
Borovikov, Y.S.; Kulikova, N.; Pronina, O.E.; Khaimina, S.S.; Wrzosek, A.; Dabrowska, R.
Caldesmon freezes the structure of actin filaments during the actomyosin ATPase cycle
Biochim. Biophys. Acta
1764
1054-1062
2006
Oryctolagus cuniculus
brenda
Tiago, T.; Martel, P.; Gutierrez-Merino, C.; Aureliano, M.
Binding modes of decavanadate to myosin and inhibition of the actomyosin ATPase activity
Biochim. Biophys. Acta
1774
474-480
2007
Dictyostelium discoideum
brenda
Padilha, A.S.; Moreira, C.M.; Meira, E.F.; Siman, F.D.; Stefanon, I.; Vassallo, D.V.
Chronic ouabain treatment enhances cardiac myosin ATPase activity in rats
Clin. Exp. Pharmacol. Physiol.
35
801-806
2008
Rattus norvegicus
brenda
Haagensen, L.; Jensen, D.H.; Gesser, H.
Dependence of myosin-ATPase on structure bound creatine kinase in cardiac myfibrils from rainbow trout and freshwater turtle
Comp. Biochem. Physiol. A
150
404-409
2008
Oncorhynchus mykiss, Trachemys scripta
brenda
Onishi, H.; Mikhailenko, S.V.; Morales, M.F.
Toward understanding actin activation of myosin ATPase: the role of myosin surface loops
Proc. Natl. Acad. Sci. USA
103
6136-6141
2006
Gallus gallus
brenda
Blair, D.R.; Funai, K.; Schweitzer, G.G.; Cartee, G.D.
A myosin II ATPase inhibitor reduces force production, glucose transport, and phosphorylation of AMPK and TBC1D1 in electrically stimulated rat skeletal muscle
Am. J. Physiol. Endocrinol. Metab.
296
E993-E1002
2009
Rattus norvegicus
brenda
Vassallo, D.V.; Lebarch, E.C.; Moreira, C.M.; Wiggers, G.A.; Stefanon, I.
Lead reduces tension development and the myosin ATPase activity of the rat right ventricular myocardium
Braz. J. Med. Biol. Res.
41
789-795
2008
Rattus norvegicus
brenda
Kronert, W.A.; Dambacher, C.M.; Knowles, A.F.; Swank, D.M.; Bernstein, S.I.
Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function
J. Mol. Biol.
379
443-456
2008
Drosophila melanogaster
brenda
Saber, W.; Begin, K.J.; Warshaw, D.M.; VanBuren, P.
Cardiac myosin binding protein-C modulates actomyosin binding and kinetics in the in vitro motility assay
J. Mol. Cell. Cardiol.
44
1053-1061
2008
Gallus gallus
brenda
Joubert, F.; Wilding, J.R.; Fortin, D.; Domergue-Dupont, V.; Novotova, M.; Ventura-Clapier, R.; Veksler, V.
Local energetic regulation of sarcoplasmic and myosin ATPase is differently impaired in rats with heart failure
J. Physiol.
586
5181-5192
2008
Rattus norvegicus
brenda
Anderson, T.W.; Vaughan, A.N.; Cramer, L.P.
Retrograde flow and myosin II activity within the leading cell edge deliver F-actin to the lamella to seed the formation of graded polarity actomyosin II filament bundles in migrating fibroblasts
Mol. Biol. Cell
19
5006-5018
2008
Gallus gallus
brenda
Katayama, T.; Watanabe, M.; Tanaka, H.; Hino, M.; Miyakawa, T.; Ohki, T.; Ye, L.; Xie, C.; Yoshiyama, S.; Nakamura, A.; Ishikawa, R.; Tanokura, M.; Oiwa, K.; Kohama, K.
Stimulatory effects of arachidonic acid on myosin ATPase activity and contraction of smooth muscle via myosin motor domain
Am. J. Physiol. Heart Circ. Physiol.
298
H505-H514
2010
Gallus gallus
brenda
Caremani, M.; Lehman, S.; Lombardi, V.; Linari, M.
Orthovanadate and orthophosphate inhibit muscle force via two different pathways of the myosin ATPase cycle
Biophys. J.
100
665-674
2011
Oryctolagus cuniculus
brenda
Cooke, R.
The role of the myosin ATPase activity in adaptive thermogenesis by skeletal muscle
Biophys. Rev.
3
33-45
2011
Oryctolagus cuniculus
brenda
Preller, M.; Chinthalapudi, K.; Martin, R.; Knolker, H.J.; Manstein, D.J.
Inhibition of myosin ATPase activity by halogenated pseudilins: a structure-activity study
J. Med. Chem.
54
3675-3685
2011
Dictyostelium discoideum (P08799)
brenda
Ahmad, R.; Hasnain, A.
Ultrasonication of chicken natural actomyosin: effect on ATPase activity, turbidity and SDS-PAGE profiles at different protein concentrations
Am. J. Biochem. Mol. Biol.
3
240-247
2013
Gallus gallus
-
brenda
Sato, M.K.; Ishihara, T.; Tanaka, H.; Ishijima, A.; Inoue, Y.
Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis
Biophys. J.
103
711-718
2012
Oryctolagus cuniculus
brenda
Kiani, F.A.; Fischer, S.
Advances in quantum simulations of ATPase catalysis in the myosin motor
Curr. Opin. Struct. Biol.
31
115-123
2015
Dictyostelium discoideum (P08799)
brenda
Martin, R.; Risacher, C.; Barthel, A.; Jaeger, A.; Schmidt, A.; Richter, S.; Boehl, M.; Preller, M.; Chinthalapudi, K.; Manstein, D.; Gutzeit, H.; Knoelker, H.
Silver(I)-catalyzed route to pyrroles: synthesis of halogenated pseudilins as allosteric inhibitors for myosin ATPase and x-ray crystal structures of the protein-inhibitor complexes
Eur. J. Org. Chem.
2014
4487-4505
2014
Oryctolagus cuniculus
-
brenda
Heissler, S.M.; Liu, X.; Korn, E.D.; Sellers, J.R.
Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2
J. Biol. Chem.
288
26709-26720
2013
Acanthamoeba castellanii (P05659), Acanthamoeba castellanii
brenda
Yamada, A.; Yoshio, M.; Oiwa, K.
Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro
J. Muscle Res. Cell Motil.
34
115-123
2013
Mytilus galloprovincialis
brenda
Matusovsky, O.S.; Shevchenko, U.V.; Matusovskaya, G.G.; Sobieszek, A.; Dobrzhanskaya, A.V.; Sheludko, N.S.
Catch muscle myorod modulates ATPase activity of myosin in a phosphorylation-dependent way
PLoS ONE
10
e0125379
2015
Oryctolagus cuniculus, Crenomytilus grayanus
brenda
Logvinova, D.S.; Markov, D.I.; Nikolaeva, O.P.; Sluchanko, N.N.; Ushakov, D.S.; Levitsky, D.I.
Does interaction between the motor and regulatory domains of the myosin head occur during ATPase cycle? Evidence from thermal unfolding studies on myosin subfragment 1
PLoS ONE
10
e0137517
2015
Gallus gallus (P13538 and P02609 and P02604)
brenda
Mizui, T.; Sekino, Y.; Yamazaki, H.; Ishizuka, Y.; Takahashi, H.; Kojima, N.; Kojima, M.; Shirao, T.
Myosin II ATPase activity mediates the long-term potentiation-induced exodus of stable F-actin bound by drebrin A from dendritic spines
PLoS ONE
9
e85367
2014
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Borovikov, Y.S.; Avrova, S.V.; Rysev, N.A.; Sirenko, V.V.; Simonyan, A.O.; Chernev, A.A.; Karpicheva, O.E.; Piers, A.; Redwood, C.S.
Aberrant movement of beta-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle
Arch. Biochem. Biophys.
577-578
11-23
2015
Oryctolagus cuniculus
brenda
Kobayashi, M.; Ramirez, B.E.; Warren, C.M.
Interplay of actin, ADP and Mg2+ interactions with striated muscle myosin Implications of their roles in ATPase
Arch. Biochem. Biophys.
662
101-110
2019
Oryctolagus cuniculus
brenda
Borovikov, Y.; Simonyan, A.; Karpicheva, O.; Avrova, S.; Rysev, N.; Sirenko, V.; Piers, A.; Redwood, C.
The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle
Biochem. Biophys. Res. Commun.
494
681-686
2017
Oryctolagus cuniculus
brenda
Ghashghaee, N.; Li, K.; Dong, W.
Direct interaction between troponin and myosin enhances the ATPase activity of heavy meromyosin
Biologia (Poland)
72
702-708
2017
Oryctolagus cuniculus
-
brenda
Kiani, F.; Fischer, S.
ATP-dependent interplay between local and global conformational changes in the myosin motor
Cytoskeleton (Hoboken)
73
643-651
2016
Homo sapiens
brenda
Li, J.; Lu, Z.; He, J.; Chen, Q.; Wang, X.; Kang, L.; Li, X.D.
Alternative exon-encoding regions of Locusta migratoria muscle myosin modulate the pH dependence of ATPase activity
Insect Mol. Biol.
25
689-700
2016
Locusta migratoria
brenda
Labyntseva, R.; Yavorovska, V.; Bevza, O.; Drapaylo, A.; Kalchenko, V.; Kosterin, S.
Thiacalix[4]arenes remove the inhibitory effects of Zn cations on the myosin ATPase activity
Nanoscale Res. Lett.
13
224
2018
Sus scrofa
brenda
Fujii, T.; Namba, K.
Structure of actomyosin rigour complex at 5.2 A resolution and insights into the ATPase cycle mechanism
Nat. Commun.
8
13969
2017
Oryctolagus cuniculus
brenda
Chung, C.S.; Mechas, C.; Campbell, K.S.
Myocyte contractility can be maintained by storing cells with the myosin ATPase inhibitor 2,3 butanedione monoxime
Physiol. Rep.
3
e12445
2015
Rattus norvegicus
brenda
Szatmari, D.; Bugyi, B.; Ujfalusi, Z.; Grama, L.; Dudas, R.; Nyitrai, M.
Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin
PLoS ONE
12
e0186288
2017
Rattus norvegicus
brenda