[PDF][PDF] Multiple-and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: unitary steps and forces
We have developed a new technique for measurements of piconewton forces and
nanometer displacements in the millisecond time range caused by actin-myosin interaction …
nanometer displacements in the millisecond time range caused by actin-myosin interaction …
Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy.
I Rayment, HM Holden, JR Sellers… - Proceedings of the …, 1995 - National Acad Sciences
In 10-30% of hypertrophic cardiomyopathy kindreds, the disease is caused by> 29 missense
mutations in the cardiac beta-myosin heavy chain (MYH7) gene. The amino acid sequence …
mutations in the cardiac beta-myosin heavy chain (MYH7) gene. The amino acid sequence …
A potential catalytic site revealed by the 1.7-Å crystal structure of the amino-terminal signalling domain of Sonic hedgehog
WITHIN the past few years, members of the hedgehog (hh) family of secreted signalling
proteins have emerged as the primary signals generated by certain embryonic patterning …
proteins have emerged as the primary signals generated by certain embryonic patterning …
Molecular model of muscle contraction
TAJ Duke - Proceedings of the National Academy of …, 1999 - National Acad Sciences
A quantitative stochastic model of the mechanochemical cycle of myosin, the protein that
drives muscle contraction, is proposed. It is based on three premises:(i) the myosin head …
drives muscle contraction, is proposed. It is based on three premises:(i) the myosin head …
Fifty years of muscle and the sliding filament hypothesis
HE Huxley - European journal of biochemistry, 2004 - Wiley Online Library
This review describes the early beginnings of X‐ray diffraction work on muscle structure and
the contraction mechanism in the MRC Unit in the Cavendish Laboratory, Cambridge, and …
the contraction mechanism in the MRC Unit in the Cavendish Laboratory, Cambridge, and …
Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin
M Capitanio, M Canepari… - Proceedings of the …, 2006 - National Acad Sciences
During skeletal muscle contraction, regular arrays of actin and myosin filaments slide past
each other driven by the cyclic ATP-dependent interaction of the motor protein myosin II (the …
each other driven by the cyclic ATP-dependent interaction of the motor protein myosin II (the …
Blebbistatin, a myosin II inhibitor, is photoinactivated by blue light
T Sakamoto, J Limouze, CA Combs, AF Straight… - Biochemistry, 2005 - ACS Publications
Blebbistatin is a small molecule inhibitor discovered in a screen for inhibitors of nonmuscle
myosin IIA. Blebbistatin inhibits the actin-activated MgATPase activity and in vitro motility of …
myosin IIA. Blebbistatin inhibits the actin-activated MgATPase activity and in vitro motility of …
The DExH protein NPH-II is a processive and directional motor for unwinding RNA
E Jankowsky, CH Gross, S Shuman, AM Pyle - Nature, 2000 - nature.com
All aspects of cellular RNA metabolism and processing involve DExH/D proteins, which are
a family of enzymes that unwind or manipulate RNA in an ATP-dependent fashion. DExH/D …
a family of enzymes that unwind or manipulate RNA in an ATP-dependent fashion. DExH/D …
Identification of globular mechanochemical heads of kinesin
JM Scholey, J Heuser, JT Yang, LSB Goldstein - Nature, 1989 - nature.com
KINESIN is a mechanoenzyme which uses energy liberated from ATP hydrolysis to transport
particles towards the'plus ends' of microtubules1–6. The enzyme consists of two polypeptide …
particles towards the'plus ends' of microtubules1–6. The enzyme consists of two polypeptide …
X-ray Structures of the MgADP, MgATPγS, and MgAMPPNP Complexes of the Dictyostelium discoideum Myosin Motor Domain,
The three-dimensional structures of the truncated myosin head from Dictyostelium
discoideum myosin II (S1dC) complexed with MgAMPPNP, MgATPγS, and MgADP are …
discoideum myosin II (S1dC) complexed with MgAMPPNP, MgATPγS, and MgADP are …