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TPM3 encodes a member of the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Zusätzlich bieten wir Ihnen TPM3 Antikörper (35) und TPM3 Proteine (16) und viele weitere Produktgruppen zu diesem Protein an.
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This work uncovers a Quaking/Tpm3 pathway controlling de novo myofibril assembly.
Analysis of the residual, resected tumor identified a chromoplectic TPM3-ALK (zeige ALK ELISA Kits) rearrangement that involved many other known oncogenes and was confirmed by rtPCR.
expression levels of tropomyosin 3 (TPM3) were higher in stage III ESCC tissue compared with stage I (P<0.05). The findings of the present study identified twelve proteins, which are closely associated with ESCC invasion and metastasis, apoptosis and cell signal transduction.
Dominant mutations in TPM3, encoding alpha-tropomyosinslow, cause a congenital myopathy characterized by generalized muscle weakness. Here, we used a multidisciplinary approach to investigate the mechanism of muscle dysfunction in 12 TPM3-myopathy patients.
This work expands the phenotypic spectrum of TPM3-related disease and provides insights into the pathophysiological mechanisms of the actin-tropomyosin (zeige TPM2 ELISA Kits) complex
Western blot showed phosphorylation of ALK (zeige ALK ELISA Kits), ERK1/2 (zeige MAPK1/3 ELISA Kits), and STAT3 (zeige STAT3 ELISA Kits) in cells transfected with TPM3-ALK (zeige ALK ELISA Kits). Coiled-coil structure of TPM3 contributes to the transforming ability of the TPM3-ALK (zeige ALK ELISA Kits) fusion protein, and longer TPM3 region leads to higher dimer formation.
Patients with TPM2 (zeige TPM2 ELISA Kits) mutations tended to present with milder symptoms than those with TPM3 mutations, DA being present only in the TPM2 (zeige TPM2 ELISA Kits) group.
in a cohort of 94 patients with congenital myopathy, 2 related female patients and 2 sporadic male patients were found to carry mutations in TPM2 (zeige TPM2 ELISA Kits) and TPM3 genes respectively; clinical presentation and muscle morphological findings differed in the patients
DATA show that tropomyosin 3 protein (TPM3) plays a critical role in the progression of gliomas.
study reports on a three-generation family with cap myopathy caused by a novel heterozygous mutation in TPM3
In addition to CLIC1 (zeige CLIC1 ELISA Kits) and TPM1 (zeige TPM1 ELISA Kits), which were the proteins initially discovered in a xenograft mouse model, CLIC4 (zeige CLIC4 ELISA Kits), TPM2 (zeige TPM2 ELISA Kits), TPM3, and TPM4 (zeige TPM4 ELISA Kits) were present in ovarian cancer patient sera at significantly elevated levels compared with controls.
Tpm3 plays crucial roles in maintaining cortical actin integrity and asymmetric cell division during oocyte maturation, and that dynamic regulation of cortical actin by Tpm3 is critical to ensure proper polar body protrusion.
TMBr-3 and TM5NM1 modestly affected actin assembly kinetics, in an opposite manner.
Tropomyosin (zeige TPM2 ELISA Kits) regulates cell migration during skin wound healing.
Data conclude that exon 9d-containing isoforms are not essential for survival of neuronal cells and that isoform choice from the gamma-Tm gene is flexible in the brain
Reduced expression of Tpm3, sarcomere genes and Lrtm1 in the diaphragm of mice with diaphragmatic defects.
Tropomyosin 3 expression leads to hypercontractility and attenuates myofilament length-dependent Ca(2 (zeige CA2 ELISA Kits)+) activation.
tropomyosin (zeige TPM2 ELISA Kits) isoforms regulate neuronal size and shape
results indicate that a Tm5NM1-defined actin cytoskeleton is required for the normal excitation-contraction coupling in skeletal muscle
This gene encodes a member of the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins that polymerize end-to-end along the major groove in most actin filaments. They provide stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, they regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in this gene result in autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are associated with cancer. Multiple transcript variants encoding different isoforms have been found for this gene.
, tropomyosin alpha-3 chain
, alpha-tropomyosin, slow skeletal
, cytoskeletal tropomyosin TM30
, heat-stable cytoskeletal protein 30 kDa
, tropomyosin gamma
, nonmuscle tropomyosin 5
, tropomyosin 3, gamma
, tropomyosin non-muscle
, tropomyosin 5