Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Manuela, Maffei"'
Ultra-fast force-clamp spectroscopy data on the interaction between skeletal muscle myosin and actin
Autor:
Manuela Maffei, Diego Beneventi, Monica Canepari, Roberto Bottinelli, Francesco Saverio Pavone, Marco Capitanio
Publikováno v:
Data in Brief, Vol 25, Iss , Pp - (2019)
Ultrafast force-clamp spectroscopy is a single molecule technique based on laser tweezers with sub-millisecond and sub-nanometer resolution. The technique has been successfully applied to investigate the rapid conformational changes that occur when a
Externí odkaz:
https://doaj.org/article/57d584d2b5de42639e9bbdac391bfcd3
Autor:
Silvia Carnio, Francesca LoVerso, Martin Andres Baraibar, Emanuela Longa, Muzamil Majid Khan, Manuela Maffei, Markus Reischl, Monica Canepari, Stefan Loefler, Helmut Kern, Bert Blaauw, Bertrand Friguet, Roberto Bottinelli, Rüdiger Rudolf, Marco Sandri
Publikováno v:
Cell Reports, Vol 8, Iss 5, Pp 1509-1521 (2014)
The cellular basis of age-related tissue deterioration remains largely obscure. The ability to activate compensatory mechanisms in response to environmental stress is an important factor for survival and maintenance of cellular functions. Autophagy i
Externí odkaz:
https://doaj.org/article/d78aec26017e4e48b4432c3199f814e4
Publikováno v:
European Biophysics Journal. 46:195-202
In vitro motility assay (IVMA) experiments were performed to analyze the movement of actin filaments sliding on a pavement of myosin molecules at different [ATP] and [ADP]. In standard experimental conditions at [ATP] = 2 mM, about 80% of the actin f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de3be2b8a9f94a2cccad3666d55923e5
https://doi.org/10.1007/s00249-016-1194-2
https://doi.org/10.1007/s00249-016-1194-2
Autor:
J. F. Desaphy, Emanuela Longa, Rizwan Qaisar, Monica Canepari, Valentina Agoni, Roberto Bottinelli, D. Conte Camerino, Manuela Maffei
Publikováno v:
Acta Physiologica. 212:316-329
Aim Notwithstanding the widely accepted idea that following disuse skeletal muscles become faster, an increase in shortening velocity was previously observed mostly in fibres containing type 1 myosin, whereas a decrease was generally found in fibres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::466a1ece9b1880fef0245c2b45d3143f
https://doi.org/10.1111/apha.12320
https://doi.org/10.1111/apha.12320
Publikováno v:
Experimental Physiology. 97:873-881
An in vitro motility assay approach was used to investigate the mechanisms of the functional differences between myosin isoforms, by studying the effect of MgATP and MgADP on actin sliding velocity (Vf) of pure slow and fast rat skeletal myosin at di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8c388a1a94f6620b0af2940f627aec6
https://doi.org/10.1113/expphysiol.2012.064576
https://doi.org/10.1113/expphysiol.2012.064576
Publikováno v:
Muscle & Nerve. 40:249-256
Duchenne muscular dystrophy (DMD) is a genetic disease characterized by skeletal muscle wasting and atrophy. Recent evidence suggests that the impaired skeletal muscle performance in DMD is not solely dependent on a loss of contractile muscle mass. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e3a86ee0a59030fa3306c44eb3d5b010
https://doi.org/10.1002/mus.21302
https://doi.org/10.1002/mus.21302
Publikováno v:
Journal of Applied Physiology. 99:2239-2245
It was shown that the temperature sensitivity of shortening velocity of skeletal muscles is higher at temperatures below physiological (10-25 degrees C) than at temperatures closer to physiological (25-35 degrees C) and is higher in slow than fast mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dda0e3972cb9db6a316f4121133cab86
https://doi.org/10.1152/japplphysiol.00543.2005
https://doi.org/10.1152/japplphysiol.00543.2005
Autor:
Janine Lossie, Walter Steffen, Vera Regitz-Zagrosek, Oriane Larchevêque, Ingo Morano, Roberto Bottinelli, Monica Canepari, Shokoufeh Mahmoodzadeh, Philipp Baumert, Hannelore Haase, Manuela Maffei, Martin Taube, Clemens Köhncke
Publikováno v:
Biochemical and biophysical research communications. 450(1)
The essential myosin light chain (ELC) is involved in modulation of force generation of myosin motors and cardiac contraction, while its mechanism of action remains elusive. We hypothesized that ELC could modulate myosin stiffness which subsequently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1309efe98696782d68fc0e975437068a
https://pubmed.ncbi.nlm.nih.gov/24911555
https://pubmed.ncbi.nlm.nih.gov/24911555
Autor:
Monica Canepari, Diego Beneventi, Roberto Bottinelli, Francesco S. Pavone, Carina Monico, Manuela Maffei, Francesco Vanzi, Marco Capitanio
Publikováno v:
Nature Methods
Nature methods 9 (2012): 1013–1019. doi:10.1038/NMETH.2152
info:cnr-pdr/source/autori:Capitanio Marco [ 1,2 ] ; Canepari Monica [ 3 ] ; Maffei Manuela [ 3 ] ; Beneventi Diego [ 1 ] ; Monico Carina [ 1 ] ; Vanzi Francesco [ 1,4 ] ; Bottinelli Roberto [ 3,5 ] ; Pavone Francesco Saverio [ 1,2,6,7 ]/titolo:Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke/doi:10.1038%2FNMETH.2152/rivista:Nature methods/anno:2012/pagina_da:1013/pagina_a:1019/intervallo_pagine:1013–1019/volume:9
Nature Methods; Vol 9
Nature methods 9 (2012): 1013–1019. doi:10.1038/NMETH.2152
info:cnr-pdr/source/autori:Capitanio Marco [ 1,2 ] ; Canepari Monica [ 3 ] ; Maffei Manuela [ 3 ] ; Beneventi Diego [ 1 ] ; Monico Carina [ 1 ] ; Vanzi Francesco [ 1,4 ] ; Bottinelli Roberto [ 3,5 ] ; Pavone Francesco Saverio [ 1,2,6,7 ]/titolo:Ultrafast force-clamp spectroscopy of single molecules reveals load dependence of myosin working stroke/doi:10.1038%2FNMETH.2152/rivista:Nature methods/anno:2012/pagina_da:1013/pagina_a:1019/intervallo_pagine:1013–1019/volume:9
Nature Methods; Vol 9
A dual-trap force-clamp configuration is used to apply a constant load between a binding protein and a single intermittently interacting biological polymer. This allows high-resolution measurements of short-lived molecular complexes and reveals previ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::931a5842ca31e591ab06b8de87826bda
https://pubmed.ncbi.nlm.nih.gov/22941363
https://pubmed.ncbi.nlm.nih.gov/22941363
Autor:
Giulia Falorsi, Pasquale Bianco, Luca Melli, Manuela Maffei, Luca Salvi, Vincenzo Lombardi, Giovanna Coceano, Dan Cojoc
Publikováno v:
Biophysical Journal. 106:453a-454a
We report the progress toward the realization of a synthetic sarcomere-like machine consisting of an array of motor proteins, regularly distributed on an inorganic nano-structured surface, interacting with a single actin filament. The mechanical outp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3cb1ce9addc882cc25c724c517c50a1
https://doi.org/10.1016/j.bpj.2013.11.2569
https://doi.org/10.1016/j.bpj.2013.11.2569