Akter L, Flechsig H, Marchesi A, Franz C
Int J Mol Sci. 2024; 25(4).
PMID: 38396630
PMC: 10888245.
DOI: 10.3390/ijms25041951.
Rockenfeller R, Gunther M, Hooper S
Biophys J. 2022; 121(10):1823-1855.
PMID: 35450825
PMC: 9199101.
DOI: 10.1016/j.bpj.2022.04.019.
Brizendine R, Anuganti M, Cremo C
J Gen Physiol. 2021; 153(3).
PMID: 33439241
PMC: 7809879.
DOI: 10.1085/jgp.202012751.
Bennett P, Knight P, Ranatunga K
J Muscle Res Cell Motil. 2019; 40(3-4):275-278.
PMID: 31643007
DOI: 10.1007/s10974-019-09561-7.
Craig R
Appl Microsc. 2018; 47(4):226-232.
PMID: 29682492
PMC: 5909410.
DOI: 10.9729/am.2017.47.4.226.
Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.
Lee K, Sulbaran G, Yang S, Mun J, Alamo L, Pinto A
Proc Natl Acad Sci U S A. 2018; 115(9):E1991-E2000.
PMID: 29444861
PMC: 5834683.
DOI: 10.1073/pnas.1715247115.
Estimation of actomyosin active force maintained by tropomyosin and troponin complex under vertical forces in the in vitro motility assay system.
Ishii S, Kawai M, Ishiwata S, Suzuki M
PLoS One. 2018; 13(2):e0192558.
PMID: 29420610
PMC: 5805308.
DOI: 10.1371/journal.pone.0192558.
Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.
Alamo L, Koubassova N, Pinto A, Gillilan R, Tsaturyan A, Padron R
Biophys Rev. 2017; 9(5):461-480.
PMID: 28871556
PMC: 5662037.
DOI: 10.1007/s12551-017-0295-1.
Myosin II sequences for Lethocerus indicus.
Fee L, Lin W, Qiu F, Edwards R
J Muscle Res Cell Motil. 2017; 38(2):193-200.
PMID: 28707142
PMC: 5660136.
DOI: 10.1007/s10974-017-9476-6.
An approach to improve the resolution of helical filaments with a large axial rise and flexible subunits.
Yang S, Woodhead J, Zhao F, Sulbaran G, Craig R
J Struct Biol. 2015; 193(1):45-54.
PMID: 26592473
PMC: 4696882.
DOI: 10.1016/j.jsb.2015.11.007.
Orientation of the N- and C-terminal lobes of the myosin regulatory light chain in cardiac muscle.
Kampourakis T, Sun Y, Irving M
Biophys J. 2015; 108(2):304-14.
PMID: 25606679
PMC: 4302210.
DOI: 10.1016/j.bpj.2014.11.049.
Flexibility within the heads of muscle myosin-2 molecules.
Billington N, Revill D, Burgess S, Chantler P, Knight P
J Mol Biol. 2013; 426(4):894-907.
PMID: 24333017
PMC: 3919154.
DOI: 10.1016/j.jmb.2013.11.028.
Geometrical conditions indispensable for muscle contraction.
Skubiszak L
Int J Mol Sci. 2011; 12(4):2138-57.
PMID: 21731432
PMC: 3127108.
DOI: 10.3390/ijms12042138.
RECENT IMPROVEMENTS IN SMALL ANGLE X-RAY DIFFRACTION FOR THE STUDY OF MUSCLE PHYSIOLOGY.
Reconditi M
Rep Prog Phys. 2009; 69(10):2709-2759.
PMID: 19946470
PMC: 2783642.
DOI: 10.1088/0034-4885/69/10/R01.
Remarks on muscle contraction mechanism.
Mitsui T, Ohshima H
Int J Mol Sci. 2009; 9(5):872-904.
PMID: 19325791
PMC: 2635709.
DOI: 10.3390/ijms9050872.
Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments.
Zhao F, Craig R, Woodhead J
J Mol Biol. 2008; 385(2):423-31.
PMID: 18976661
PMC: 4266557.
DOI: 10.1016/j.jmb.2008.10.038.
Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length.
Suggs J, Cammarato A, Kronert W, Nikkhoy M, Dambacher C, Megighian A
J Mol Biol. 2007; 367(5):1312-29.
PMID: 17316684
PMC: 1965590.
DOI: 10.1016/j.jmb.2007.01.045.
Mechanical properties of single myosin molecules probed with the photonic force microscope.
Scholz T, Altmann S, Antognozzi M, Tischer C, Horber J, Brenner B
Biophys J. 2004; 88(1):360-71.
PMID: 15489300
PMC: 1305012.
DOI: 10.1529/biophysj.104.047795.
Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization.
Hase M, Kuznetsov N, CORDES V
Mol Biol Cell. 2001; 12(8):2433-52.
PMID: 11514627
PMC: 58605.
DOI: 10.1091/mbc.12.8.2433.
The M.ADP.Pi state is required for helical order in the thick filaments of skeletal muscle.
Xu S, Gu J, Rhodes T, Belknap B, Rosenbaum G, Offer G
Biophys J. 1999; 77(5):2665-76.
PMID: 10545367
PMC: 1300541.
DOI: 10.1016/s0006-3495(99)77101-8.
