[HTML][HTML] Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature communications, 2017 - nature.com
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature Communications, 2017 - ui.adsabs.harvard.edu
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature Communications, 2017 - econpapers.repec.org
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature communications, 2017 - pubmed.ncbi.nlm.nih.gov
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature Communications, 2017 - ideas.repec.org
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism.

T Fujii, K Namba - Nature Communications, 2017 - europepmc.org
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

[PDF][PDF] Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - NATURE COMMUNICATIONS - cyberleninka.org
Results CryoEM data collection and helical image analysis. For sample preparation of the
actomyosin rigour complex, we used apyrase to completely remove residual ATP in solution …

[HTML][HTML] Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature Communications, 2017 - ncbi.nlm.nih.gov
Muscle contraction is driven by cyclic association and dissociation of myosin head of the
thick filament with thin actin filament coupled with ATP binding and hydrolysis by myosin …

Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature Communications, 2017 - cir.nii.ac.jp
抄録< jats: title> Abstract</jats: title>< jats: p> Muscle contraction is driven by cyclic
association and dissociation of myosin head of the thick filament with thin actin filament …

[引用][C] Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism

T Fujii, K Namba - Nature Communications, 2017 - Nature Publishing Group