A kinetic model that explains the effect of inorganic phosphate on the mechanics and energetics of isometric contraction of fast skeletal muscle

Por Linari, Marco, Caremani, Marco, Lombardi, Vincenzo
Publicado em 2010

Orthovanadate and Orthophosphate Inhibit Muscle Force via Two Different Pathways of the Myosin ATPase Cycle

Por Caremani, Marco, Lehman, Steve, Lombardi, Vincenzo, Linari, Marco
Publicado em 2011

Stiffness and Fraction of Myosin Motors Responsible for Active Force in Permeabilized Muscle Fibers from Rabbit Psoas

Por Linari, Marco, Caremani, Marco, Piperio, Claudia, Brandt, Philip, Lombardi, Vincenzo
Publicado em 2007

The working stroke of the myosin II motor in muscle is not tightly coupled to release of orthophosphate from its active site

Por Caremani, Marco, Melli, Luca, Dolfi, Mario, Lombardi, Vincenzo, Linari, Marco
Publicado em 2013

Force and number of myosin motors during muscle shortening and the coupling with the release of the ATP hydrolysis products

Por Caremani, Marco, Melli, Luca, Dolfi, Mario, Lombardi, Vincenzo, Linari, Marco
Publicado no J Physiol (2015)

Thick Filament Mechano-Sensing in Skeletal and Cardiac Muscles: A Common Mechanism Able to Adapt the Energetic Cost of the Contraction to the Task

Por Piazzesi, Gabriella, Caremani, Marco, Linari, Marco, Reconditi, Massimo, Lombardi, Vincenzo
Publicado no Front Physiol (2018)

Effect of Inorganic Phosphate on the Force and Number of Myosin Cross-Bridges During the Isometric Contraction of Permeabilized Muscle Fibers from Rabbit Psoas

Por Caremani, Marco, Dantzig, Jody, Goldman, Yale E., Lombardi, Vincenzo, Linari, Marco
Publicado em 2008

Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit

Por Percario, Valentina, Boncompagni, Simona, Protasi, Feliciano, Pertici, Irene, Pinzauti, Francesca, Caremani, Marco
Publicado no J Physiol (2018)

Size and speed of the working stroke of cardiac myosin in situ

Por Caremani, Marco, Pinzauti, Francesca, Reconditi, Massimo, Piazzesi, Gabriella, Stienen, Ger J. M., Lombardi, Vincenzo, Linari, Marco
Publicado no Proc Natl Acad Sci U S A (2016)

Nebulin plays a direct role in promoting strong actin-myosin interactions

Por Bang, Marie-Louise, Caremani, Marco, Brunello, Elisabetta, Littlefield, Ryan, Lieber, Richard L., Chen, Ju, Lombardi, Vincenzo, Linari, Marco
Publicado em 2009

Minimum number of myosin motors accounting for shortening velocity under zero load in skeletal muscle

Por Fusi, Luca, Percario, Valentina, Brunello, Elisabetta, Caremani, Marco, Bianco, Pasquale, Powers, Joseph D., Reconditi, Massimo, Lombardi, Vincenzo, Piazzesi, Gabriella
Publicado no J Physiol (2016)

The force and stiffness of myosin motors in the isometric twitch of a cardiac trabecula and the effect of the extracellular calcium concentration

Por Pinzauti, Francesca, Pertici, Irene, Reconditi, Massimo, Narayanan, Theyencheri, Stienen, Ger J. M., Piazzesi, Gabriella, Lombardi, Vincenzo, Linari, Marco, Caremani, Marco
Publicado no J Physiol (2018)

Muscle Thixotropy: More than Just Cross-Bridges? Response to Comment by Campbell and Lakie

Por Kellermayer, Miklós S. Z., Bianco, Pasquale, Mártonfalvi, Zsolt, Nagy, Attila, Kengyel, András, Szatmári, Dávid, Huber, Tamás, Linari, Marco, Caremani, Marco, Lombardi, Vincenzo
Publicado em 2008

The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle

Por Brunello, Elisabetta, Caremani, Marco, Melli, Luca, Linari, Marco, Fernandez-Martinez, Manuel, Narayanan, Theyencheri, Irving, Malcolm, Piazzesi, Gabriella, Lombardi, Vincenzo, Reconditi, Massimo
Publicado em 2014

Myosin filament activation in the heart is tuned to the mechanical task

Por Reconditi, Massimo, Caremani, Marco, Pinzauti, Francesca, Powers, Joseph D., Narayanan, Theyencheri, Stienen, Ger J. M., Linari, Marco, Lombardi, Vincenzo, Piazzesi, Gabriella
Publicado no Proc Natl Acad Sci U S A (2017)