Results 11 to 20 of about 26,024 (216)
Effect of titin phosphorylation on degradation of titin from skeletal muscles
The degradation of titin could make the myofibrillar fragmentation to improve meat tenderization during postmortem. This study aimed to investigate effect of phosphorylation on titin degradation.
Ying Wang +5 more
doaj +2 more sources
Individual globular domains and domain unfolding visualized in overstretched titin molecules with atomic force microscopy. [PDF]
Titin is a giant elastomeric protein responsible for the generation of passive muscle force. Mechanical force unfolds titin's globular domains, but the exact structure of the overstretched titin molecule is not known.
Zsolt Mártonfalvi, Miklós Kellermayer
doaj +3 more sources
Titin‐based mechanosensing modulates muscle hypertrophy
Background Titin is an elastic sarcomeric filament that has been proposed to play a key role in mechanosensing and trophicity of muscle. However, evidence for this proposal is scarce due to the lack of appropriate experimental models to directly test the
Robbert van derPijl +6 more
doaj +2 more sources
C-type natriuretic peptide moderates titin-based cardiomyocyte stiffness
Heart failure is often accompanied by titin-dependent myocardial stiffness. Phosphorylation of titin by cGMP-dependent protein kinase I (PKGI) increases cardiomyocyte distensibility.
Konstanze Michel +11 more
doaj +2 more sources
Urinary Titin Is Increased in Patients After Cardiac Surgery [PDF]
Background: Few non-invasive biomarkers have been used to detect myocardial injury in patients with heart diseases. Recently, the N-terminal fragment (N-titin) of titin, a giant sarcomeric protein, which is involved in muscular passive tension and ...
Jun Tanihata +5 more
doaj +2 more sources
Force generation by titin folding [PDF]
AbstractTitin is a giant protein that provides elasticity to muscle. As the sarcomere is stretched, titin extends hierarchically according to the mechanics of its segments. Whether titin's globular domains unfold during this process and how such unfolded domains might contribute to muscle contractility are strongly debated.
Mártonfalvi, Zsolt +4 more
openaire +6 more sources
The giant muscle protein titin is a major contributor to passive force; however, its role in active force generation is unresolved. Here, we use a novel titin-cleavage (TC) mouse model that allows specific and rapid cutting of elastic titin to quantify ...
Yong Li +7 more
doaj +1 more source
This study aimed to examine the validity of urinary N-terminal titin fragment/creatinine (urinary N-titin/Cr) reflecting muscle damage biomarker in patients with interstitial lung disease. This retrospective study enrolled patients with interstitial lung
Masatoshi Hanada +12 more
doaj +1 more source
Mechanoenzymatics of titin kinase [PDF]
Biological responses to mechanical stress require strain-sensing molecules, whose mechanically induced conformational changes are relayed to signaling cascades mediating changes in cell and tissue properties. In vertebrate muscle, the giant elastic protein titin is involved in strain sensing via its C-terminal kinase domain (TK) at the sarcomeric M ...
Puchner, E M +9 more
openaire +6 more sources
Computing Average Passive Forces in Sarcomeres in Length-Ramp Simulations. [PDF]
Passive forces in sarcomeres are mainly related to the giant protein titin. Titin's extensible region consists of spring-like elements acting in series.
Gudrun Schappacher-Tilp +3 more
doaj +1 more source

