INT43484
From wiki-pain
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Sentences Mentioned In
Key: | Protein | Mutation | Event | Anatomy | Negation | Speculation | Pain term | Disease term |
Alteration of BMP-4 and Runx2 expression patterns in mouse temporomandibular joint after ovariectomy. | |||||||||||||||
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Napierala et al. 2005 reported two patients with promoter sequence variants and hypothesized that promoter mutations affecting binding of transcription factors critical for RUNX2 expression might change the transcriptional activity of the gene. | |||||||||||||||
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Extensive deletion analysis [4], [6], [8] coupled with in vitro assays have established that amino acids (aa) 1660 is sufficient to interact with MEF2, Runx2, HDAC1, 14-3-3, and also for phosphorylation and nuclear export [3], [12], [13], [16][19]. | |||||||||||||||
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Therefore it is highly likely that the expressed HDAC4 1-747 retains its binding to and repression of MEF2C and Runx2 in vivo, explaining the lack of chondrocyte hypertrophy in our mutant mice. | |||||||||||||||
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2; Runx2: Runt related transcription factor 2; Th17: T helper 17; TRAP: telomeric repeat amplification protocol; Tregs: regulatory T cells; TUNEL: Terminal deoxynucleotidyl transferase-mediated dUTP-biotin nick end labeling; SHED: Stem cells from human exfoliated deciduous teeth; SLE: systemic lupus erythematosus; sRANKL: soluble receptor activator for nuclear factor ? | |||||||||||||||
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2; Runx2: Runt related transcription factor 2; Th17: T helper 17; TRAP: telomeric repeat amplification protocol; Tregs: regulatory T cells; TUNEL: Terminal deoxynucleotidyl transferase-mediated dUTP-biotin nick end labeling; SHED: Stem cells from human exfoliated deciduous teeth; SLE: systemic lupus erythematosus; sRANKL: soluble receptor activator for nuclear factor ? | |||||||||||||||
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Signaling via Smad1 cooperates with the transcription factor Runx2 (CBFA1) to induce chondrocyte terminal differentiation. | |||||||||||||||
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Signaling via Smad1 cooperates with the transcription factor Runx2 (CBFA1) to induce chondrocyte terminal differentiation. | |||||||||||||||
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By comparison, alpha 2 receptors may exist in multiple-affinity states reflecting the ability of the alpha 2 binding site protein to complex to additional membrane proteins which themselves are receptors for the physiological substrates GTP, Na+, Mg2+, and possibly Ca2+-calmodulin. | |||||||||||||||
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General Comments
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