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The tendency of smooth muscle tropomyosin to form semi-rigid polymers with continuous and undampened rigidity may compensate for the lack of troponin-based structural support in smooth muscles.
Deletion of regions 2-3 in tropomyosin (show TPM2 Proteins) alpha resulted in an 60 % decrease in both isometric tension and stiffness of tropomyosin (show TPM2 Proteins)-reconstituted myocardium.
Tropomyosin (show TPM2 Proteins) is primarily responsible for the change in the kinetic constants of the elementary steps of the cross bridge cycle.
Tm affects the conformation of actin so as to increase the area of hydrophobic interaction between actin and myosin molecules
Stress fibre formation and up-regulation of alpha-smooth muscle actin (show ACTG2 Proteins) (alphaSMA (show ACTA2 Proteins)) induced by TGFbeta2 could be reversed by Tpm1/2 knock-down by siRNA.
The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin (show TPM2 Proteins) position.
three-dimensional structure of F-actin at a resolution of 3.7 A in complex with tropomyosin (show TPM2 Proteins) at a resolution of 6.5 A, determined by electron cryomicroscopy
data also identify a novel alphaTM1/Tmod1-based pathway stabilizing F-actin at cell-cell junctions, which may be required for maintenance of cell shapes during embryonic cardiac morphogenesis.
This is the first study to demonstrate that decreasing phosphorylation of tropomyosin (show TPM2 Proteins) can rescue a hypertrophic cardiomyopathic phenotype.
Tropomyosin (show TPM2 Proteins) dephosphorylation results in myocyte hypertrophy with increases in SERCA2a (show ATP2A2 Proteins) expression.
The results identify a novel mode of myofilament desensitization to Ca(2 (show CA2 Proteins)+) associated with a DCM linked switch in TPM1-kappa.
signaling by alpha-tropomyosin may have a role in familial hypertrophic cardiomyopathy
A point mutation in alpha-TM causes a disease similar to familial hypertophic cardiomyopahy.
PTB (show PTBP1 Proteins) interacting protein raver1 (show RAVER1 Proteins) regulates alpha-tropomyosin alternative splicing.
The impact of tropomyosins on actin filament assembly is isoform specific.
TPM1 is the second gene linked to EA with LVNC in humans, implicating overlap in the molecular basis of structural and myopathic heart disease.
data demonstrate that the K15N mutation alters pointed end dynamics by affecting molecular interactions between Tpm1.1, Lmod2 (show LMOD2 Proteins) and Tmod1 (show TMOD1 Proteins).
Results report evidence for the existence of variants in LHFPL2 (show LHFPL2 Proteins) and TPM1 with low allele frequencies and large effects on age-at-onset of familial Parkinson's disease.
In diabetes, expression of high molecular weight (HMW) isoforms from tropomyosin 1 (TPM1) were markedly decreased but HMW isoforms from tropomyosin 4 (TPM4 (show TPM4 Proteins)) were not significantly different.
results suggest that TPM1 can suppress tumors in oral squamous cell carcinoma, and the TPM1 expression level is related to oral squamous cell carcinoma patient prognosis
Data suggest that the tropomyosin (show TPM2 Proteins) overlap region structure and function are affected differentially by a point mutation in cardiac tropomyosin (TPM1, D230N) that is associated with dilated cardiomyopathy as compared to a point mutation in cardiac troponin T (TNNT2 (show TNNT2 Proteins), R92L) that is associated with hypertrophic cardiomyopathy.
Data indicate that various hypertrophic cardiomyopathy (HCM) mutations can differently affect the structural and functional properties of tropomyosin (show TPM2 Proteins) (Tpm (show TPMT Proteins)) and cause HCM by different molecular mechanisms.
Promoter variants in HOXA9 (show HOXA9 Proteins), TPM1, and TPM2 (show TPM2 Proteins), alter promoter expression suggesting that they have a functional role in clubfoot.
We show that the phosphorylation of cTnI and alphaTm vary in the different chambers of the heart, whereas the phosphorylation of MLC2 and cTnT does not.
The results indicate that cross-linking significantly affects properties of Tpm (show TPMT Proteins) and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm (show TPMT Proteins) in human heart diseases.
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions
analysis of the thin filament associated with the R167H and K168E substitutions in tropomyosin (show TPM2 Proteins) Tpm1.1
We propose that TR100 acts to compromise the integrity of Tpm cables rather than prevent overlap complex formation. Our data suggests that TR100 is incorporated into the growing actin-Tpm co-polymer given that its effects cannot be observed on pre-formed Tpm3.1/actin filaments
Maximal Ca(2 (show CA2 Proteins)+) activated force was the same in alphaalphaTm versus betabetaTm myofibrils, but betabetaTm myofibrils showed a marked slowing of relaxation and an impairment of regulation under resting conditions
Tmod1 (show TMOD1 Proteins) and Tmod3 (show TMOD3 Proteins) showed somewhat different tropomyosin (show TPM2 Proteins)-binding site utilization.
Thermal denaturation of rabbit cardiac alpha,alpha-tropomyosin is monitored at neutral pH and compared to shark tropomyosin (show TPM2 Proteins), showing that amino acid substitutions predicted to be unfavorable in one temperature regime are desirable in another.
The rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin (show TPM2 Proteins), was measured.
a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed.
This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy.
, alpha-tropomyosin 2
, alpha-tropomyosin of skeletal fast muscle
, tropomyosin (CTm4)
, tropomyosin (CTm7)
, tropomyosin alpha-1 chain
, Tropomyosin-1 alpha chain
, tropomyosin 1 alpha chain
, alpha tropomyosin
, hepatoma alpha tropomyosin
, smooth muscle alpha-tropomyosin
, striated muscle alpha-tropomyosin
, tropomyosin 3 alpha
, alpha-skeletal tropomyosin
, cardiomyopathy, hypertrophic 3
, sarcomeric tropomyosin kappa
, tropomyosin 1 (alpha) isoform 1
, tropomyosin 1 (alpha) isoform 2
, tropomyosin 1 (alpha) isoform 3
, tropomyosin 1 (alpha) isoform 4
, tropomyosin 1 (alpha) isoform 5
, tropomyosin 1 (alpha) isoform 6
, tropomyosin 1 (alpha) isoform 7