anti-Tropomodulin 1 (TMOD1) Antikörper

Human Tropomodulin 1 (TMOD1) Interaktionspartner

1. Tmod1 function in mouse and human erythroblasts, was investigated.

2. The mutation reduced binding affinity for both Lmod2 (zeige LMOD2 Antikörper) and Tmod1. The effect of the K15N mutation on Tpm1.1 binding to Lmod2 (zeige LMOD2 Antikörper) and Tmod1 provides a molecular rationale for the development of familial dilated cardiomyopathies .

3. Study highlighted a novel TMOD1-mediated link between NF-kappaB (zeige NFKB1 Antikörper) activation and MMP13 (zeige MMP13 Antikörper) induction, which accounts in part for the NF-kappaB (zeige NFKB1 Antikörper)-dependent malignant phenotype of TNBC.

4. Tmod1 and Tmod3 (zeige TMOD3 Antikörper) showed somewhat different tropomyosin (zeige TPM2 Antikörper)-binding site utilization.

5. The structures and biochemical analysis of structure-inspired mutants showed that one Tmod molecule interacts with three actin subunits at the pointed end, while also contacting two tropomyosin (zeige TPM2 Antikörper) molecules on each side of the filament.

6. Tropomyosin (zeige TPM2 Antikörper) requires an intact N-terminal coiled coil to interact with this protein

7. levels of TM1 (zeige TPM2 Antikörper), TM2 (zeige TPM2 Antikörper) and TM3 (zeige TPM1 Antikörper) are reduced in human transitional cell carcinoma cells, but significantly upregulated by inhibition of the mitogen-activated protein kinase (zeige MAPK1 Antikörper)-signaling pathway

8. The N-terminal "KRK ring" may participate in balancing electrostatic force with hydrophobic interaction in dimerization of TM and its binding to E-Tmod.

9. study identifies several amino acid residues on Tmod-1 that are important for its interaction with TM5 (a nonmuscle TM isoform)

Mouse (Murine) Tropomodulin 1 (TMOD1) Interaktionspartner

1. Tmod1 function in mouse and human erythroblasts, was investigated.

2. distinct F-actin organizations are present in small protrusions versus large paddles. Formation and/or maintenance of large paddle domains depends on a beta2-spectrin-actin network stabilized by Tmod1. alpha-Actinin (zeige ACTN1 Antikörper)-crosslinked F-actin bundles are enhanced in absence of Tmod1, indicating altered cytoskeleton organization.

3. TMOD1 expression was upregulated significantly (p<0.05) in OSCC.

4. RNAi depletion of Tmod1 from either wild-type or Tmod4 (zeige TMOD4 Antikörper)(-/-) muscle fibers leads to thin filament elongation by approximately 15%.

5. The C-terminal extension of Lmod2 (zeige LMOD2 Antikörper) and C terminal of Tmod1 are sufficient to produce a filament nucleator.

6. Calpain-mediated proteolysis of tropomodulin isoforms TMOD1 and TMOD4 (zeige TMOD4 Antikörper) leads to thin filament elongation in dystrophic skeletal muscle.

7. Role of Tmod1 protein's leucine rich repeat domain in the formation of neurite-like processes

8. Tmod1 is involved in a functional synergy critical for regulating lens fiber cell geometry, transparency, and mechanical stiffness.

9. Tropomodulin 1 constrains fiber cell geometry during elongation and maturation in the lens cortex.

10. The Tmod1 deletion caused Tmod3 to leave its SR compartment, leading to mislocalization and destabilization of the Tmod3-gamma(cyto)-actin-sAnk1.5 complex.