scholarly article | Q13442814 |
P356 | DOI | 10.1021/BI00849A022 |
P698 | PubMed publication ID | 4234754 |
P2093 | author name string | E Eisenberg | |
C R Zobel | |||
C Moos | |||
P433 | issue | 9 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 3186-3194 | |
P577 | publication date | 1968-09-01 | |
P1433 | published in | Biochemistry | Q764876 |
P1476 | title | Subfragment 1 of myosin: adenosine triphophatase activation by actin | |
P478 | volume | 7 |
Q39845505 | A cross-bridge model of muscle contraction |
Q43427437 | Actin activation of the myosin ATPase: a kinetic analysis |
Q72527806 | Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase |
Q33953466 | Formation of a ternary complex: Actin, 5′-adenylyl imidodiphosphate, and the subfragments of myosin |
Q54620913 | Interaction of SH 1 -blocked HMM with actin and ATP. |
Q36594148 | Interaction of myosin filaments and minifilaments with actin: a comparative study |
Q39876673 | Kinetics and regulation of the myofibrillar adenosine triphosphatase |
Q39798671 | Mechanism of oxygen exchange in actin-activated hydrolysis of adenosine triphosphate by myosin subfragment 1 |
Q34258915 | Possible role of helix-coil transitions in the microscopic mechanism of muscle contraction |
Q59095850 | Role of myosin light chains in calcium regulation |
Q39106795 | Steady-state studies of the actin-activated adenosine triphosphatase activity of myosin |
Q40218299 | Structural aspects of actomyosin interaction |
Q72393860 | Structural changes in myosin B during the process of superprecipitation |
Q37688107 | Structure of the actin-myosin complex in the presence of ATP. |
Q77914414 | Subfragment 1 of cow carotid myosin |
Q42048193 | The enzymic properties of a modified ox heart myosin adenosine triphosphatase on covalent binding to an insoluble cellulose matrix |
Q39880206 | The mechanism of the skeletal muscle myosin ATPase. I. Identity of the myosin active sites |
Q38188550 | The modeling of the actomyosin subfragment-1 ATPase activity |
Search more.