Zobrazeno 1 - 10
of 104
pro vyhledávání: '"Enrico Grazi"'
Autor:
Enrico Grazi
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 6, Pp 12064-12075 (2015)
Force and length steps, applied to a muscle fiber in the isometric state, are believed to synchronize attached cross-bridges. This alleged synchronization facilitates the interpretation of the experiments. A rapid force step elicits an elastic respon
Externí odkaz:
https://doaj.org/article/a226d5b93aa9424285b7e311fac9cf0a
Autor:
Sara Pozzati, Enrico Grazi
Publikováno v:
International Journal of Molecular Sciences, Vol 10, Iss 3, Pp 942-953 (2009)
We have considered the Huxley-Simmons manoeuvre. On the assumption that the quick release is an elastic process and on the basis of the isometric tension and of the stiffness of the muscle fibre we calculated that the spontaneous release of the fibre
Externí odkaz:
https://doaj.org/article/de2d055847654494a9bf4e9c6ead9a3a
Autor:
Enrico Grazi
Publikováno v:
International Journal of Molecular Sciences, Vol 9, Iss 8, Pp 1435-1452 (2008)
The interaction between water and the protein of the contractile machinery as well as the tendency of these proteins to form geometrically ordered structures provide a link between water and muscle contraction. Protein osmotic pressure is strictly re
Externí odkaz:
https://doaj.org/article/aaf64a8adb36436eb70346cbcf6ea03d
Autor:
Enrico Grazi
Publikováno v:
Archives of Biochemistry and Biophysics. 533:42-46
The anisotropy decay of the spin-labelled myosin subfragment-1, takes place with different rates depending on the physiological state of muscle: relaxation, isometric contraction and rigor. The decay is mostly explained by the rotation of myosin subf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e6ee0ca6cf54a8bf6f8dee0bf62db42
https://doi.org/10.1016/j.abb.2013.02.016
https://doi.org/10.1016/j.abb.2013.02.016
Autor:
Enrico Grazi
Publikováno v:
Archives of Biochemistry and Biophysics. 522:121-124
The analysis of the quick release is usually made by fitting a straight line to the first few experimental points of the tension–length curve. The line is then extrapolated to zero force. The fact that the tension–length curve can be represented
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70a51cb082786b47f26b4cf5873191d2
https://doi.org/10.1016/j.abb.2012.04.008
https://doi.org/10.1016/j.abb.2012.04.008
Autor:
Enrico Grazi, Barbara Viviani, Marco Binaglia, Mariaserena Boraso, Stefano Bartesaghi, Corrado L. Galli, Emanuela Corsini, Marina Marinovich
Publikováno v:
Toxicology Letters. 182:63-68
Neurological complications as well as movement disorders are relevant symptoms in animals and humans chronically exposed to dithiocarbamates. Using rat pheochromocytoma cells differentiated by NGF (PC12), we investigated whether propineb affects acet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faafc2fbf4b43105fdc39139576fecfd
https://doi.org/10.1016/j.toxlet.2008.08.016
https://doi.org/10.1016/j.toxlet.2008.08.016
Autor:
Cristina Di Bona, Enrico Grazi
Publikováno v:
Journal of Theoretical Biology. 242:853-861
A simple model is presented where, by an iterative procedure, the forces delivered by the power strokes are summed up to overcome the load. The system is moderated by the viscous hindrance. The model reproduces the features of muscle contraction as d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81117a63800a27ac31c457955cae2cf0
https://doi.org/10.1016/j.jtbi.2006.05.021
https://doi.org/10.1016/j.jtbi.2006.05.021
Autor:
Cristina Di Bona, Enrico Grazi
Publikováno v:
Biophysical Chemistry. 118:113-117
We present a model of muscle contraction based on purely physical grounds and modulated by a parameter, k, related to the visco-elastic hindrances of the contractile apparatus. The model predicts a strong cooperation among sarcomere units and propose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ffdef9831792646f9e45aa1f912e085
https://doi.org/10.1016/j.bpc.2005.07.005
https://doi.org/10.1016/j.bpc.2005.07.005
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1569:135-138
Fast muscle myosin responds in similar way to F-actin and to phalloidin F-actin. It is activated 7.5 fold at infinite F-actin concentration and 6.8 fold at infinite phalloidin F-actin. The actomyosin dissociation constants are 0.89 +/- 0.34 microM wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd2636007f0b410c24391bb27a5300ce
https://doi.org/10.1016/s0304-4165(01)00243-4
https://doi.org/10.1016/s0304-4165(01)00243-4
Publikováno v:
Biophysical Chemistry. 92:201-207
(Iodoacetamido)tetramethylrhodamine disrupts F-actin. At the 1:1 fluorophore to actin (as monomer) ratio approximately 80% of the protein becomes non-sedimentable. The fluorescent, non-sedimentable actin copolymerizes with G-actin to yield fluorescen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c92dca073c6283b97c3f4ebcd1755114
https://doi.org/10.1016/s0301-4622(01)00198-3
https://doi.org/10.1016/s0301-4622(01)00198-3