TPM1 Antibody

1. The results indicate that cross-linking significantly affects properties of Tpm and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm in human heart diseases. PMID: 27856252
2. altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions PMID: 27480605
3. analysis of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1 PMID: 27956029
4. 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 PMID: 26804624
5. Maximal Ca(2+) 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 PMID: 25380572
6. Tmod1 and Tmod3 showed somewhat different tropomyosin-binding site utilization. PMID: 24922351
7. Thermal denaturation of rabbit cardiac alpha,alpha-tropomyosin is monitored at neutral pH and compared to shark tropomyosin, showing that amino acid substitutions predicted to be unfavorable in one temperature regime are desirable in another. PMID: 21707054
8. The rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin, was measured. PMID: 21575577
9. a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed. PMID: 21320445

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KEGG: ocu:100125989

UniGene: Ocu.3324