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1. Full Text Residual force enhancement in myofibrils and sarcomeres
by V Joumaa and T.R Leonard and W Herzog
Proceedings of the Royal Society B: Biological Sciences, ISSN 0962-8452, 06/2008, Volume 275, Issue 1641, pp. 1411 - 1419
=18) that, owing to the strict in series arrangement, allowed for evaluation of this property in individual sarcomeres ( 
Protein isoforms | Microfilaments | Contractile proteins | Muscles | Actins | Stiffness | Muscle contraction | Sarcomeres | Myofibrils | Skeletal muscle | Mechanism of contraction | Cross-bridge theory | Sarcomere length instability | Sliding filament theory | SINGLE MYOFIBRILS | sarcomere length instability | HUMAN ADDUCTOR POLLICIS | STRETCH | RAT MUSCLE | TENSION | sliding filament theory | EVOLUTIONARY BIOLOGY | ISOMETRIC FORCE | STIFFNESS | cross-bridge theory | BIOLOGY | SKELETAL-MUSCLE FIBERS | ECOLOGY | mechanism of contraction | TITIN ISOFORMS | skeletal muscle | STRIATED-MUSCLE | Rabbits | Biomechanical Phenomena | Animals | Muscle Contraction - physiology | Muscle, Skeletal - physiology | Sarcomeres - physiology | In Vitro Techniques | Myofibrils - physiology | Isometric Contraction - physiology
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2. Full Text The Relaxation Properties of Myofibrils Are Compromised by Amino Acids that Stabilize α-Tropomyosin
by Scellini, Beatrice and Piroddi, Nicoletta and Matyushenko, Alexander M and Levitsky, Dmitrii I and Poggesi, Corrado and Lehrer, Sherwin S and Tesi, Chiara
Biophysical Journal, ISSN 0006-3495, 01/2017, Volume 112, Issue 2, pp. 376 - 387
We investigated the functional impact of -tropomyosin (Tm) substituted with one (D137L) or two (D137L/G126R) stabilizing amino acid substitutions on the... 
SINGLE MYOFIBRILS | HYPERTROPHIC CARDIOMYOPATHY MUTATIONS | BIOPHYSICS | CONSERVED ASP-137 | FORCE GENERATION | MIDDLE PART | MUSCLE THIN FILAMENT | INORGANIC-PHOSPHATE | STRIATED-MUSCLE | FAST SKELETAL-MUSCLE | CARDIAC TROPONIN-I | Myofibrils - drug effects | Rabbits | Sequence Deletion | Tropomyosin - genetics | Psoas Muscles - cytology | Calcium - metabolism | Humans | Myofibrils - physiology | Tropomyosin - pharmacology | Animals | Troponin I - genetics | Myofibrils - metabolism | Muscle Relaxation - drug effects | Protein Stability | Tropomyosin - chemistry | Troponin I - metabolism | Psoas Muscles - physiology | Tropomyosin - metabolism | Amino Acid Substitution | Molecular Machines, Motors, and Nanoscale Biophysics
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3. Full Text PKA Phosphorylation of Cardiac Troponin I Modulates Activation and Relaxation Kinetics of Ventricular Myofibrils
by Rao, Vijay and Cheng, Yuanhua and Lindert, Steffen and Wang, Dan and Oxenford, Lucas and McCulloch, Andrew D and McCammon, J. Andrew and Regnier, Michael
Biophysical Journal, ISSN 0006-3495, 09/2014, Volume 107, Issue 5, pp. 1196 - 1204
Protein kinase A (PKA) phosphorylation of myofibril proteins constitutes an important pathway for -adrenergic modulation of cardiac contractility and... 
REDEVELOPMENT KINETICS | SINGLE MYOFIBRILS | BIOPHYSICS | RABBIT SKELETAL-MUSCLE | CALCIUM-BINDING | TENSION | FORCE DEVELOPMENT | REGULATORY UNIT INTERACTIONS | STRIATED-MUSCLE | CROSS-BRIDGE | FUNCTIONAL CONSEQUENCES | Cyclic AMP-Dependent Protein Kinases - metabolism | Recombinant Proteins - metabolism | Phosphorylation | Calcium - metabolism | Myocardial Contraction - physiology | Cells, Cultured | Rats | Ions - metabolism | Myofibrils - physiology | Troponin C - metabolism | Animals | Kinetics | Mutation | Troponin I - metabolism | Protein C | Myosin | Protein binding | Resveratrol | Proteins and Nucleic Acids
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4. Full Text Sarcomere Stiffness during Stretching and Shortening of Rigor Skeletal Myofibrils
by Shalabi, Nabil and Persson, Malin and Månsson, Alf and Vengallatore, Srikar and Rassier, Dilson E and Linnéuniversitetet and Institutionen för kemi och biomedicin (KOB) and Fakulteten för Hälso- och livsvetenskap (FHL)
Biophysical Journal, ISSN 0006-3495, 12/2017, Volume 113, Issue 12, pp. 2768 - 2776
In this study, we measured the stiffness of skeletal muscle myofibrils in rigor. Using a custom-built atomic force microscope, myofibrils were first placed in... 
ACTIVE FORCE | FRACTION | WORKING STROKE | BIOPHYSICS | CONTRACTION | MECHANISM | SINGLE-MYOSIN MOLECULES | MUSCLE-FIBERS | NONLINEAR ELASTICITY | CROSS-BRIDGE | Rabbits | Biomechanical Phenomena | Animals | Sarcomeres - metabolism | Microscopy, Atomic Force | Cytoskeletal Proteins - metabolism | Female | Mechanical Phenomena | Muscles | Mechanical engineering | Molecular Machines, Motors, and Nanoscale Biophysics | Biological Sciences | Biofysik | Naturvetenskap | Biologiska vetenskaper | Biokemi | Biochemistry | Natural Sciences | Biophysics
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5. Full Text Does partial titin degradation affect sarcomere length nonuniformities and force in active and passive myofibrils?
by Joumaa, V and Bertrand, F and Liu, S and Poscente, S and Herzog, W
American Journal of Physiology - Cell Physiology, ISSN 0363-6143, 09/2018, Volume 315, Issue 3, pp. C310 - C318
The aim of this study was to determine the role of titin in preventing the development of sarcomere length nonuniformities following activation and after... 
Passive stretch | Sarcomere stability | Z-disk | Active stretch | Force regulation | SINGLE MYOFIBRILS | PHYSIOLOGY | force regulation | CONTRACTILE PROPERTIES | CARDIAC-MUSCLE | CALCIUM SENSITIVITY | CELL BIOLOGY | SKELETAL-MUSCLE | SKINNED FIBERS | sarcomere stability | FRANK-STARLING MECHANISM | GIANT PROTEIN TITIN | PHYSIOLOGICAL-ROLE | active stretch | passive stretch | STRIATED-MUSCLES | Proteins | Physiological aspects | Muscle cells
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6. Full Text The familial hypertrophic cardiomyopathy-associated myosin mutation R403Q accelerates tension generation and relaxation of human cardiac myofibrils
by Alexandra Belus and Nicoletta Piroddi and Beatrice Scellini and Chiara Tesi and Giulia D Amati and Francesca Girolami and Magdi Yacoub and Franco Cecchi and Iacopo Olivotto and Corrado Poggesi
The Journal of Physiology, ISSN 0022-3751, 08/2008, Volume 586, Issue 15, pp. 3639 - 3644
The R403Q mutation in β-myosin heavy chain was the first mutation to be identified as responsible for familial hypertrophic cardiomyopathy (FHC). In spite of... 
GENE-MUTATIONS | MYOCARDIUM | SINGLE MYOFIBRILS | HEAVY-CHAIN | PHYSIOLOGY | CONTRACTION | KINETICS | MOUSE MODEL | ENERGETICS | BETA-MYOSIN | STRIATED-MUSCLE | NEUROSCIENCES | Calcium - metabolism | Cardiomyopathy, Hypertrophic, Familial - genetics | Tissue Culture Techniques | Humans | Myocardial Contraction - physiology | Gene Expression Regulation | Male | Myofibrils - genetics | Myofibrils - physiology | Myocardial Contraction - genetics | Ventricular Myosins - metabolism | Adult | Female | Mutation | Ventricular Myosins - genetics | Muscle proteins | Genetic aspects | Myosin | Cardiovascular
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7. Full Text Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation
by Nixon, Benjamin R and Liu, Bin and Scellini, Beatrice and Tesi, Chiara and Piroddi, Nicoletta and Ogut, Ozgur and John Solaro, R and Ziolo, Mark T and Janssen, Paul M.L and Davis, Jonathan P and Poggesi, Corrado and Biesiadecki, Brandon J
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 07/2013, Volume 535, Issue 1, pp. 30 - 38
► Sf9 insect cell expressed and purified αTm is N-terminal acetylated. ► Pseudo-phosphorylated αTm S283D regulates filaments like phosphorylated muscle αTm. ►... 
Human | Relaxation | Phosphorylation | Myofibril | Calcium | Tropomyosin | SINGLE MYOFIBRILS | THIN FILAMENT | BIOCHEMISTRY & MOLECULAR BIOLOGY | RABBIT SKELETAL-MUSCLE | ALPHA-ALPHA-TROPOMYOSIN | MYOFILAMENT CALCIUM SENSITIVITY | MYOCARDIAL-CONTRACTION | BIOPHYSICS | CARBOXYL-TERMINUS | STRIATED-MUSCLE | CARDIAC TROPONIN-I | COOPERATIVE BINDING | Tropomyosin - genetics | Baculoviridae - metabolism | Calcium - metabolism | Baculoviridae - genetics | Myofibrils - genetics | Sf9 Cells | Cloning, Molecular | Acetylation | Muscle, Striated - cytology | Tropomyosin - metabolism | Recombinant Proteins - metabolism | Rabbits | Actin Cytoskeleton - metabolism | Mutagenesis, Site-Directed | Myosin Subfragments - metabolism | Recombinant Proteins - genetics | Muscle Relaxation | Myofibrils - physiology | Serine - metabolism | Actin Cytoskeleton - physiology | Biomechanical Phenomena | Animals | Protein Binding | Mice | Myofibrils - metabolism | Enzyme Activation | Muscle, Striated - metabolism | Muscle proteins | Cells | Index Medicus | myofibril | calcium | phosphorylation | human | relaxation
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8. Full Text The effects of fatigue and oxidation on contractile function of intact muscle fibers and myofibrils isolated from the mouse diaphragm
by Bagni, M. Angela and Colombini, Barbara and Nocella, Marta and Pregno, Claudio and S. Cornachione, Anabelle and Rassier, Dilson E
Scientific Reports, ISSN 2045-2322, 12/2019, Volume 9, Issue 1, pp. 4422 - 11
The goal of this study was to investigate the effects of repetitive stimulation and the oxidant H2O2 on fatigue of diaphragm intact fibers and in myofibrils... 
SKELETAL-MUSCLE | REACTIVE OXYGEN | STRETCH | CA2+ RELEASE | MULTIDISCIPLINARY SCIENCES | N-ACETYLCYSTEINE | DYSFUNCTION | FORCE ENHANCEMENT | CROSS-BRIDGE | FREE-RADICALS | SINGLE FIBERS | Hydrogen peroxide | Calcium | Contractility | Acetylcysteine | Fatigue | Oxidation | Diaphragm | Muscle contraction | Myofibrils | Fibers
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9. Full Text Isolation and Mechanical Measurements of Myofibrils from Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes
by Pioner, Josè Manuel and Racca, Alice W and Klaiman, Jordan M and Yang, Kai-Chun and Guan, Xuan and Pabon, Lil and Muskheli, Veronica and Zaunbrecher, Rebecca and Macadangdang, Jesse and Jeong, Mark Y and Mack, David L and Childers, Martin K and Kim, Deok-Ho and Tesi, Chiara and Poggesi, Corrado and Murry, Charles E and Regnier, Michael
Stem Cell Reports, ISSN 2213-6711, 06/2016, Volume 6, Issue 6, pp. 885 - 896
Tension production and contractile properties are poorly characterized aspects of excitation-contraction coupling of human induced pluripotent stem... 
SINGLE MYOFIBRILS | ACTIVATION | HYPERTROPHIC CARDIOMYOPATHY | FUNCTIONAL MATURATION | TENSION GENERATION | CONTRACTION | FORCE GENERATION | HUMAN ATRIAL | RELAXATION | CAVEOLIN-3 | CELL & TISSUE ENGINEERING | CELL BIOLOGY | Excitation Contraction Coupling - physiology | Cell Line | Gene Expression | Induced Pluripotent Stem Cells - physiology | Myocytes, Cardiac - cytology | Cardiac Myosins - genetics | Humans | Myosin Heavy Chains - genetics | Myofibrils - physiology | Cardiomyopathies - genetics | Biomechanical Phenomena | Cardiomyopathies - physiopathology | Myofibrils - ultrastructure | Myocytes, Cardiac - physiology | Nanostructures - chemistry | Cell Differentiation | Kinetics | Mutation | Primary Cell Culture | Induced Pluripotent Stem Cells - cytology
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10. Full Text MgADP activation contributes to force enhancement during fast stretch of isolated skeletal myofibrils
by Minozzo, Fábio C and Altman, David and Rassier, Dilson E
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 08/2015, Volume 463, Issue 4, pp. 1129 - 1134
When an activated muscle is rapidly stretched, force rises and peaks while muscle lengthens. The peak force is normally called critical-force (P ). The... 
AFM | Myofibril | Force enhancement | Crossbridges | MgADP | SINGLE MYOFIBRILS | MYOSIN | FROG-MUSCLE FIBERS | NON-CROSSBRIDGE CONTRIBUTIONS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOTOR DOMAIN | TENSION | LENGTH RELATIONSHIP | BIOPHYSICS | CROSS-BRIDGE KINETICS | STRIATED-MUSCLE | POWER STROKE | Rabbits | Animals | Calcium - metabolism | Muscle, Skeletal - metabolism | Myofibrils - metabolism | Adenosine Diphosphate - metabolism | Muscle, Skeletal - physiology | Myofibrils - physiology
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11. Full Text ATP binding and cross‐bridge detachment steps during full Ca2+ activation: comparison of myofibril and muscle fibre mechanics by sinusoidal analysis
by Iorga, Bogdan and Wang, Li and Stehle, Robert and Pfitzer, Gabriele and Kawai, Masataka
The Journal of Physiology, ISSN 0022-3751, 07/2012, Volume 590, Issue 14, pp. 3361 - 3373
Key points •  Sinusoidal length change was employed to study the single myofibril mechanics during full Ca2+ activation for the first time, and the tension... 
SINGLE MYOFIBRILS | MUSCULAR-CONTRACTION | PHYSIOLOGY | FORCE GENERATION | INORGANIC-PHOSPHATE | RABBIT PSOAS MUSCLE | INDIVIDUAL SARCOMERES | STRIATED-MUSCLE | CROSSBRIDGE KINETICS | FAST SKELETAL-MUSCLE | NEUROSCIENCES | ELEMENTARY STEPS | Rabbits | Animals | Muscle Contraction | Calcium - metabolism | Adenosine Triphosphate - metabolism | Myofibrils - metabolism | Kinetics | Muscle Fibers, Skeletal - metabolism | Muscle Tonus | Psoas Muscles - physiology | Skeletal Muscle and Exercise
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12. Full Text Effects of Chronic Atrial Fibrillation on Active and Passive Force Generation in Human Atrial Myofibrils
by Belus, A and Piroddi, N and Ferrantini, C and Tesi, C and Cazorla, O and Toniolo, L and st, M and Mearini, G and Carrier, L and Rossi, A and Mugelli, A and Cerbai, E and van der Velden, J and Poggesi, C
Circulation Research, ISSN 0009-7330, 2010, Volume 107, Issue 1, pp. 144 - 152
RATIONALE:Chronic atrial fibrillation (cAF) is associated with atrial contractile dysfunction. Sarcomere remodeling may contribute to this contractile... 
Cardiac troponin | Cardiac MyBP-C | Titin | Atrial light chain-2 | Myosin | SINGLE MYOFIBRILS | HUMAN MYOCARDIUM | CARDIAC & CARDIOVASCULAR SYSTEMS | TENSION GENERATION | cardiac troponin | cardiac MyBP-C | myosin | CARDIAC-MUSCLE | BINDING PROTEIN-C | TROPONIN-I | SKELETAL-MUSCLE | I ISOFORM EXPRESSION | STRUCTURAL-CHANGES | atrial light chain-2 | PERIPHERAL VASCULAR DISEASE | HEMATOLOGY | HUMAN HEART | Myofibrils - pathology | Humans | Middle Aged | Myocardial Contraction - physiology | Male | Myocardium - pathology | Atrial Fibrillation - physiopathology | Myofibrils - physiology | Myocytes, Cardiac - pathology | Myocytes, Cardiac - physiology | Female | Aged | Heart Atria - physiopathology | In Vitro Techniques | Chronic Disease | Life Sciences | Human health and pathology | Santé publique et épidémiologie | Cardiology and cardiovascular system
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13. Titin (visco-) elasticity in skeletal muscle myofibrils
by Herzog, J.A and Leonard, T.R and Jinha, A and Herzog, W
MCB Molecular and Cellular Biomechanics, ISSN 1556-5297, 2014, Volume 11, Issue 1, pp. 1 - 17
Titin is the third most abundant protein in sarcomeres and fulfills a number of mechanical and signaling functions. Specifically, titin is responsible for most... 
Cross-bridge theory | Visco-elastic | Passive properties | Skeletal muscle | Stretch-shortening cycles | Energy loss | Elastic | Actin | Sarcomere mechanics | Titin | Myosin | Muscle properties | Stiffness | Sarcomere | Sliding filament theory | Hysteresis | sarcomere mechanics | PASSIVE FORCE ENHANCEMENT | visco-elastic | TENSION | CONNECTIN/TITIN | stretch-shortening cycles | sliding filament theory | sarcomere | hysteresis | CELL BIOLOGY | titin | passive properties | muscle properties | cross-bridge theory | PROTEIN TITIN | CALCIUM | energy loss | skeletal muscle | SINGLE MYOFIBRILS | ENGINEERING, BIOMEDICAL | myosin | ACTIN-BINDING | stiffness | actin | FILAMENTS | RAT CARDIAC MYOCYTES | elastic | PEVK DOMAIN | Protein Structure, Tertiary | Rabbits | Animals | Connectin | Protein Unfolding | Sarcomeres - metabolism | Muscle Contraction - physiology | Protein Refolding | Elasticity | Sarcomeres - chemistry | Kinetics
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14. Full Text The Dilated Cardiomyopathy-Causing Mutation ACTC E361G in Cardiac Muscle Myofibrils Specifically Abolishes Modulation of Ca2+ Regulation by Phosphorylation of Troponin I
by Vikhorev, Petr G and Song, Weihua and Wilkinson, Ross and Copeland, O’Neal and Messer, Andrew E and Ferenczi, Michael A and Marston, Steven B
Biophysical Journal, ISSN 0006-3495, 11/2014, Volume 107, Issue 10, pp. 2369 - 2380
Phosphorylation of troponin I by protein kinase A (PKA) reduces Ca sensitivity and increases the rate of Ca release from troponin C and the rate of relaxation... 
SINGLE MYOFIBRILS | HYPERTROPHIC CARDIOMYOPATHY | BIOPHYSICS | LENGTH-DEPENDENT ACTIVATION | MOUSE MODEL | RELAXATION KINETICS | G159D MUTATION | CALCIUM SENSITIVITY | STRIATED-MUSCLE | VENTRICULAR MUSCLE | SER23/24 PHOSPHORYLATION | Molecular Machines, Motors and Nanoscale Biophysics
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