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28 results for “titin”
Data from: Effects of a titin mutation on force enhancement and force depression in mouse soleus muscles
The force produced by muscles varies with muscle length. Compared to isometric contractions at the same final length, force increases after lengthening, known as force enhancement, and decreases after shortening, known as force depression. The mechanisms of force enhancement remain unexplained by the sliding-filament and cross-bridge theories of muscle contraction. Although cross-bridge mechanisms have been proposed to account for force depression, so too have other mechanisms. In addition to cross bridges, titin has been suggested to contribute to both force enhancement and depression. Although titin is too compliant in passive muscles to contribute to active stiffness, recent evidence suggests that calcium activation increases titin stiffness. To test the hypothesis that titin plays a role in force enhancement and depression, we investigated muscle force in active and passive wild type and mdm soleus muscles after isovelocity stretching and shortening at three activation levels. Muscles from mdm mice (muscular dystrophy with myositis) have a predicted 83 amino acid deletion in the N2A region of titin and show no increase in stiffness when activated. We found that: 1) force enhancement and depression were reduced in mdm soleus compared to wild type muscles; 2) force enhancement increased with the amplitude of stretch across all activation levels in wild type and mdm muscles, while force depression increased with amplitude in wild type but not in mdm muscles; and 3) maximal shortening velocity of wild type and mdm muscles was similar, although active stress was reduced in mdm compared to wild type muscles. The results of this study suggest a role for titin in force enhancement and depression, which contribute importantly to regulation of muscle force during natural movements.
Data from: Effects of a titin mutation on force enhancement and force depression in mouse soleus muscles
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Images for pdb entry 8BXR Titin FnIII-domain I109-I111 (I/A4-A/A6) from the MIR region
<p>Structure for 8BXR Titin FnIII-domain I109-I111 (I/A4-A/A6) from the MIR region calculated from these two merged data sets. </p>
Images for 8BVO Titin I110-I111 FnIII tandem from the MIR region (I/A5-I/A6)
<p>Images for 8BVO Titin I110-I111 FnIII tandem from the MIR region (I/A5-I/A6)</p>
Images for 8BW6 Titin FnIII-domain I110 (I/A6) from the MIR region 1
<p><br> Images from 8BW6 Titin FnIII-domain I110 (I/A6) from the MIR region 1</p>
The Skeletal Muscle Molecular Clock Regulates Sarcomere Length Through Titin Splicing [2]
GEO Series GSE189863. Mus musculus. 6 samples. Type: Expression profiling by high throughput sequencing.
Regulation of sarcomere formation and function in the healthy heart requires a titin intronic enhancer [RNA-seq]
GEO Series GSE282670. Mus musculus. 10 samples. Type: Expression profiling by high throughput sequencing.
The Skeletal Muscle Molecular Clock Regulates Sarcomere Length Through Titin Splicing [1]
GEO Series GSE172067. Mus musculus. 6 samples. Type: Expression profiling by high throughput sequencing.
Titin truncating variant associated with atrial fibrillation leads to cell type-specific effects in atrial and ventricular patient hiPSC-CM models
GEO Series GSE234141. Homo sapiens. 24 samples. Type: Expression profiling by high throughput sequencing.
Regulation of sarcomere formation and function in the healthy heart requires a titin intronic enhancer [scRNA-Seq]
GEO Series GSE282693. Homo sapiens. 8 samples. Type: Expression profiling by high throughput sequencing.
Regulation of sarcomere formation and function in the healthy heart requires a titin intronic enhancer.
GEO Series GSE283867. Homo sapiens; Mus musculus. 32 samples. Type: Expression profiling by high throughput sequencing; Genome binding/occupancy profiling by high throughput sequencing.
RNA sequencing of wildtype and homozygous titin A178D mouse left ventricle samples
GEO Series GSE154504. Mus musculus. 7 samples. Type: Expression profiling by high throughput sequencing.
Titin truncating variantsin hiPSC-cardiomyocytes inducepathogenic proteinopathy, sarcomeredefect and contractile dysfunction independent of the core contractilemachinery [bulk RNA-seq]
GEO Series GSE183216. Homo sapiens. 18 samples. Type: Expression profiling by high throughput sequencing.
Titin truncating variantsin hiPSC-cardiomyocytes inducepathogenic proteinopathy, sarcomeredefect and contractile dysfunction independent of the core contractilemachinery [scRNA-seq]
GEO Series GSE183217. Homo sapiens. 7 samples. Type: Expression profiling by high throughput sequencing.
A Titin Missense Variant Causes Atrial Fibrillation
GEO Series GSE312917. Homo sapiens. 6 samples. Type: Expression profiling by high throughput sequencing.
Dataset: Titin activates myosin filaments in skeletal muscle by switching from an extensible spring to a mechanical rectifier
<p>Experimental dataset for publication on PNAS (2219346120)</p>
Urinary Titin Biomarker in DMD
ClinicalTrials.gov study NCT07332013. IPD Sharing: NO. Countries: 1. Publications: 0.
The Validity of Urinary Titin and Skeletal Muscle Index as Predictor of Muscle Weakness in Critically Ill Patients. A Prospective Cohort Study
ClinicalTrials.gov study NCT06487728. IPD Sharing: YES. Countries: 1. Publications: 0.
Titin truncating variantsin hiPSC-cardiomyocytes inducepathogenic proteinopathy, sarcomeredefect and contractile dysfunction independent of the core contractilemachinery
GEO Series GSE183218. Homo sapiens. 25 samples. Type: Expression profiling by high throughput sequencing.
Comparative transcriptomic studies to determine the molecular effects of titin mechanical knock-out in skeletal muscles
GEO Series GSE271916. Mus musculus. 56 samples. Type: Expression profiling by high throughput sequencing.
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