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We demonstrate that promoter binding by TRF2 mediates PCGF3 (zeige PCGF3 Proteine) promoter activity, and both the N-terminal and C-terminal domains of TRF2 are necessary for promoter activity
The reports the crystal structure of the N-terminal domain of TIN2 (zeige TINF2 Proteine) in complex with TIN2 (zeige TINF2 Proteine)-binding motifs from TPP1 (zeige TPP1 Proteine) and TRF2, revealing how TIN2 (zeige TINF2 Proteine) interacts cooperatively with TPP1 (zeige TPP1 Proteine) and TRF2.
Both TRF1 (zeige TERF1 Proteine) and TRF2 were overexpressed in prostate cancer. There was no specificity of TRF2 in prostate cancer, while TRF1 (zeige TERF1 Proteine) may be associated with prostate cancer progression.
the excessive HULC plus MALAT1 reduced the methylation of the TERC promoter dependent on TRF2, increasing the TERC expression that causes the increase of interplay between TRET and TERC.
TERF2 knockdown by RNA interference had no effect on cell proliferation, migration, senescence and apoptosis. Instead, TERF2 knockdown increased the expression of cytokines implicated in inflammation and angiogenesis, except for vascular endothelial growth factor (zeige VEGF Proteine).
the telomere stability is under direct control of one of the major pro-oncogenic signaling pathways (RAS/RAF (zeige RAF1 Proteine)/MEK (zeige MAP2K1 Proteine)/ERK (zeige EPHB2 Proteine)) via TRF2 phosphorylation.
the B-domain improves TRF2's interaction with DNA via enhanced long-range electrostatic interactions.
our findings describe TRF2 as a novel SIRT6 (zeige SIRT6 Proteine) substrate and demonstrate that acetylation of TRF2 plays a crucial role in the regulation of TRF2 protein stability, thus providing a new route for modulating its expression level during oncogenesis and damage response.
The results suggest that dimerized TRF2 recruits origin recognition complex and stimulates pre-replication complex formation at telomeres through the TRFH domain.
Studied the disruption pattern of of 3D telomere-TRF2 interaction in the progression from mononuclear Hodgkin cells (H) to multinucleated Reed-Sternberg cells (RS).
It plays a role in hematopoietic stem cell regulation and in the maintenance of the HSC (zeige FUT1 Proteine) pool and the development of hematological disorders.
Selective inactivation of Terf2 in neural progenitors induced apoptosis, resulting in a complete loss of the brain structure.
The authors propose that TRF2 masks and stabilizes the t-loop three-way junction, thereby protecting telomeres from detrimental deletions and PARP1 (zeige PARP1 Proteine) activation.
TRF2, a component of shelterin, binds to core histones to protect chromosome ends from inappropriate DNA damage response and loss of telomeric DNA. The N-terminal Gly/Arg-rich domain (GAR domain) of TRF2 directly binds to the globular domain of core histones.
Overexpressing TRF2-S and silencing FMRP (zeige FMR1 Proteine) promotes mRNA entry to axons and enhances axonal outgrowth and neurotransmitter release from presynaptic terminals.
TRF2 binds and transactivates the promoter of the angiogenic tyrosine kinase (zeige TYRO3 Proteine) platelet-derived growth factor receptor beta (zeige PDGFRB Proteine) (PDGFRbeta).
role of TRF2 in skin homeostasis, is reported.
shelterin protein TIN2 (zeige TINF2 Proteine) can protect chromosome ends as a TRF2-tethered TIN2 (zeige TINF2 Proteine)/TPP1 (zeige TPP1 Proteine)/POT1 (zeige POT1 Proteine) complex that lacks a physical connection to TRF1 (zeige TERF1 Proteine)
We concluded that genomic instability resulting from loss of TRF2 expression provides biological advantages to the cancer stem cell population
Conditional deletion of individual components of shelterin showed that TRF2 was required for the formation and/or maintenance of t-loops, whereas deletion of TRF1 (zeige TERF1 Proteine), Rap1 (zeige TERF2IP Proteine), or the POT1 (zeige POT1 Proteine) proteins (POT1a (zeige POT1 Proteine) and POT1b) had no effect on the frequency of t-loop occurrence.
This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic.
telomeric repeat binding factor 2
, TTAGGG repeat-binding factor 2
, telomeric DNA-binding protein
, telomeric repeat binding protein 2
, telomeric repeat-binding factor 2
, TTAGGG-repeat binding factor 2 TRF2
, telomeric repeat binding factor a
, TTAGGG repeat binding factor 2