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TERF1 is a multifunctional ERF protein that can integrate different stress signal pathways
AUX1 and PIN2 protect lateral root (LR) formation in Arabidopsis during the early stages of iron (Fe) stress.
Data show that ROTUNDA3 (RON3; At4g24500) protein as a regulator of the protein phosphatase 2A-driven PIN (show DYNLL1 Proteins)-FORMED (PIN (show DYNLL1 Proteins)) auxin transport recycling and its importance in auxin transport-related plant developmental programs.
Brief treatment with indole-3-carbinol led to a reduction in the amount of PIN1 and to mislocalization of PIN2.
PIN2 auxin efflux carriers are differentially controlled in tricho- and atrichoblast cells. PIN2 proteins show lower abundance at the plasma membrane of trichoblast cells, despite showing higher rates of intracellular trafficking in these cells.
under low-B conditions PIN1 is down-regulated and PIN2 plays an important role in root meristem maintenance.
Reduction in PIN2 intensity, polarization, and endocytosis under low phosphate conditions is MAX2 dependent.
Functional interplay between protein kinase CK2 (show CSNK2A1 Proteins) and salicylic acid sustains PIN2 transcriptional expression.
High temperature selectively promotes the retrieval of PIN2 from late endosomes and sorts them to the plasma membrane through an endosomal trafficking pathway dependent on SORTING NEXIN1.
By using solubilized membrane protein immunoprecipitation assays, we established quantitative approaches, suitable for analysis of PIN2 ubiquitylation and variations therein
Strigolactones (SLs) increase PIN2 polar localization, PIN2 endocytosis, endosomal trafficking, actin debundling and actin dynamics in a MAX2-dependent fashion.
TRF1 tethers SA1 (show STAG1 Proteins) within telomeric regions that SA1 (show STAG1 Proteins) transiently interacts with. SA1 (show STAG1 Proteins) and TRF1 together form longer DNA-DNA pairing tracts than with TRF1 alone, as revealed by atomic force microscopy imaging
data suggest that NUB1 participates in telomere maintenance by regulating the levels of TRF1 at telomeres through both NEDD8 (show NEDD8 Proteins)-dependent and NEDD8 (show NEDD8 Proteins)-independent pathways.
Data indicate that overexpression of telomeric repeat binding factor 1 (TRF1) in aging endothelial cells (EC) reduced telomere-associated DNA damage foci.
we provide mechanistic insight into the role of TRF1 in liver regeneration and provide a mouse model recapitulating the clinical features of LLCC.
TRF1 links TopoIIalpha and SAC (show ADCY10 Proteins) proteins in a pathway that ensures correct telomere replication and mitotic segregation, unveiling how TRF1 protects from telomere fragility and mitotic defects.
ZSCAN4 (show ZSCAN4 Proteins) indirectly interacts with TRF1 in cancer cells. We show that ZSCAN4 (show ZSCAN4 Proteins) plays an important role independent of telomere maintenance pathways (telomerase positive and alternative pathway) or cell lineage.
analysis of human telomere repeat binding factor 1 (hTRF1) in complex with Escherichia coli Hsp70 (show HSP70 Proteins) (DnaK)
Results showed significant interaction between variants at TERF1 and AFAP1L2 (show AFAP1L2 Proteins) loci. Given the key role of TERF1 in telomere biology and its physical interaction with AFAP1L2 (show AFAP1L2 Proteins), these results support a role for telomere dysfunction in melanoma development.
Modulating miR (show MLXIP Proteins)-155 expression in cells altered TRF1 levels and TRF1 abundance at telomeres. Compromising TRF1 expression by elevating miR (show MLXIP Proteins)-155 increased telomere fragility and altered the structure of metaphase chromosomes.
TAP68 functions in mediating TRF1-tankyrase 1 (show TNKS Proteins) localization to the centrosome and in mitotic regulation
full-length TRF1 presents a molecular architecture that assists its interaction with telometic DNA and at the same time makes TRFH domains accessible to other TRF1 binding partners.
Gene dosage reductions of Trf1 and/or Tin2 (show TINF2 Proteins) induce telomere DNA damage and lymphoma formation in aging mice.
TRF1 is exclusively located at telomeres under normal conditions and under extreme telomere shortening.
Telomeric repeat-binding factor 1, a core component of the telomere protein complex, is a mediator of telomere associations in mammalian cells.
TRF1 binds BLM to facilitate lagging but not leading strand telomeric DNA synthesis
TRF1 is necessary for both induction and maintenance of pluripotency.
Loss of TRF1 leads to bone marrow failure and recapitulates clinical features of dyskeratosis congenita.
Identification of a tankyrase-binding motif shared by IRAP (show IL1RN Proteins), TAB182, and human TRF1 but not mouse protein.
Here we show that targeted deletion of exon 1 of the mouse gene encoding Trf1 causes early (day 5 to 6 postcoitus) embryonic lethality.These data suggest that murine Trf1 has an essential function that is independent of telomere length regulation
TRF1 interacts with other telomere-binding molecules and integrates into the functional telomere structure
This gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products.
telomeric repeat binding factor 1
, telomeric repeat binding factor (NIMA-interacting) 1
, telomeric repeat-binding factor 1
, ethylene-responsive factor 1
, ethylene response factor
, telomeric repeat-binding factor 1-like
, NIMA-interacting protein 2
, TTAGGG repeat-binding factor 1
, telomeric protein Pin2/TRF1
, Telomeric repeat-binding factor 1