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anti-Human CDT1 Antibodies:
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Human Polyclonal CDT1 Primary Antibody for ICC, IF - ABIN251007
Pos, Wiener, Pocza, Racz, Toth, Darvas, Molnar, Hegyesi, Falus: Histamine suppresses fibulin-5 and insulin-like growth factor-II receptor expression in melanoma. in Cancer research 2008
Show all 4 Pubmed References
Human Polyclonal CDT1 Primary Antibody for ELISA, WB - ABIN546917
Whittaker, Royzman, Orr-Weaver et al.: Drosophila double parked: a conserved, essential replication protein that colocalizes with the origin recognition complex and links DNA replication with mitosis and the down-regulation of S phase ... in Genes & development 2000
Human Monoclonal CDT1 Primary Antibody for WB - ABIN2668790
Arentson, Faloon, Seo, Moon, Studts, Fremont, Choi: Oncogenic potential of the DNA replication licensing protein CDT1. in Oncogene 2002
DTL promotes genomic stability through two distinct mechanisms. First, it is an essential component of the CUL4-DDB1 complex that controls CDT1 levels, thereby preventing rereplication. Second, it is required for the early G2/M checkpoint.
Results show that both Cdc6 and Cdt1, when expressed in a high level, alone or in combination, were significantly associated with poorer survival in the breast cancer patient cohort. In line with this finding, the expression of Cdc6 and Cdt1 was upregulated in breast cancer cells compared to normal breast epithelial cells. Expression of Cdc6 and Cdt1 was significantly higher in ER negative breast cancer.
CDT1, MCM7, and NUDT1 were shown to be up-regulated in hepatocellular carcinoma tissues and provide a more accurate diagnosis than alpha-fetal protein alone.
PPP2R3B codes for the PR70 protein, a regulatory substrate-recognizing subunit of protein phosphatase 2A. PR70 decreased melanoma growth by negatively interfering with DNA replication and cell cycle progression through its role in stabilizing CDC6-chromatin licensing and CDT1 interaction
USP37 interacts with Cdt1 and is able to de-ubiquitinate Cdt1 in vivo and, USP37 is able to regulate the loading of MCM complexes onto the chromatin.
mismatch repair (MMR) proteins are also involved in the degradation of Cdt1 after ultraviolet irradiation in the G1 phase
Cdt1-binding protein GRWD1 promotes chromatin fluidity by influencing nucleosome structures, e.g., by transient eviction of H2A-H2B, and thereby promotes efficient MCM loading at replication origins.
ATM silencing induced partial reduction in levels of Skp2, a component of SCF(Skp2) ubiquitin ligase that controls Cdt1 degradation.
FBXO31 interacts with Cdt1 and regulates the degradation of Cdt1 in G2 phase.
Protein levels of Geminin and Cdt1 are tightly regulated through the cell cycle, and the Cdt1-Geminin complex likely acts as a molecular switch that can enable or disable the firing of each origin of replication.
These results demonstrate an important role for Cdt1 in human papillomavirus E7-induced rereplication and shed light on mechanisms by which human papillomavirus induces genomic instability.
ATR, activated after DNA damage, phosphorylates Cdt2 and promotes the rapid degradation of Cdt1 after UV irradiation in the G1 phase of the cell cycle.
A lethal phenotype was seen in four individuals with compound heterozygous CDT1 mutations
results support the conclusion that Cdt1 binding to Hec1 is essential for an extended Ndc80 configuration and stable kinetochore-microtubule attachment
Genes in the erythroid differentiation and cell cycle regulation pathways influence interindividual variation in RBC indices. Our results provide insights into the molecular basis underlying variation in RBC traits.
FOXO3 is a binding partner of Cdt1.
The over-expression of geminin and cdt1 may play an important role in pathogenesis of acute leukemia.
Cdt1- and SNF2H-mediated promotion of MCM loading may be biologically relevant for the regulation of DNA replication.
JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone acetylase and blocks replication licensing in response to stress
findings support a model in which MAP kinase activity in G(2) promotes reaccumulation of a low-activity Cdt1 isoform after replication is complete.
p97 is an essential regulator of DNA damage-dependent CDT1 destruction
conserved arginine residues play critical roles in interaction with Geminin and Mcm that are crucial for proper conformation of the complexes and its licensing activity.
Study shows that ablation of Geminin induces massive rereplication as a result of unrestrained Cdt1 activity in embryonic stem cells, whereas it has no such effect in embryonic fibroblasts in which alternative regulation of Cdt1 activity is intact.
This study reveals a conserved new regulatory Cdt1 domain crucial for proper DNA licensing activity.
Structure and mutagenesis studies of the C-terminal region of licensing factor Cdt1 enable the identification of key residues for binding to replicative helicase Mcm proteins.
Determined the structures of mCdt1CS (mCdt1C_small; residues 452 to 557) and mCdt1CL (mCdt1C_large; residues 420 to 557) using X-ray crystallography and NMR. This study reveals that Cdt1 is formed with a tandem repeat of the winged helix domain.
Cdt1 function is negatively regulated by the Cdk phosphorylation independent of geminin binding
crystal structure of the mouse geminin-Cdt1 complex using tGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368, truncated Cdt1)
In situ hybridization and immunohistochemistry localize Cdt1 as well as geminin to the proliferative compartment of the developing mouse gut epithelium
Cdt1 expression characterizes progenitor cells in G1 phase
hCdt1 and hCdc6 expression promote malignant behavior
These results suggested that, at least in vitro, oleic acid-containing cell membranes of the lipid bilayer inhibit Cdt1-geminin complex formation by binding to Cdt1 and thereby liberating Cdt1 from inhibition by geminin.
DNA binding and helicase activities of Mcm4/6/7 are significantly stimulated by Cdt1
PcG complex 1, involving Rae28 and Cdt1, supports the activity of hematopoietic stem cells by enhancing cycling capability and hematopoietic activity through direct regulation of Geminin
Hepatitis B virus X protein increases the Cdt1-to-geminin ratio inducing DNA re-replication and polyploidy
The results showed that the Cdt1 region spanning amino acids (a. a.) 255-620 is required for efficient inhibition of DNA replication, and that, within this region, a. a. 255-289 have a critical role in inhibition.
These findings suggested that excess Cdt1 suppressed the progression of replication forks.
Dynamic interactions of high Cdt1 and geminin levels regulate S phase in early Xenopus embryos.
CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication
Loading of geminin onto chromatin requires Cdt1, suggesting that geminin is targeted at replication origins.
results allow us to build a comprehensive model of how re-replication of DNA is prevented in Xenopus, with Cdt1 regulation being the key feature
Removal of Cdt1 from chromatin and its nuclear exclusion in G2 is critical in regulating licensing and limiting DNA replication in S phase to only one round.
Cdt1 and DDB1 interact in extracts, and DDB1 chromatin loading is dependent on the binding of Cdt1 to PCNA, which indicates that PCNA docking activates the pre-formed Cdt1-Cul4(DDB1) ligase complex.
These results suggest a model in which the MCM2-7 helicase is loaded onto chromatin by a Cdt1-geminin complex, which is inactivated upon origin firing by binding additional geminin.
Cdt1, with its two opposing regulatory binding factors MCM9 and geminin, appears to be a major platform on the pre-replication complexes to integrate cell-cycle signals.
Cdt1 blocks nascent chain elongation after detecting illegitimate activation of the licensing system.
during meiosis Geminin functions as a stabilizer of Cdt1 promoting its accumulation for the early division cycles of the embryo
The protein encoded by this gene is involved in the formation of the pre-replication complex that is necessary for DNA replication. The encoded protein can bind geminin, which prevents replication and may function to prevent this protein from initiating replication at inappropriate origins. Phosphorylation of this protein by cyclin A-dependent kinases results in degradation of the protein.
chromatin licensing and DNA replication factor 1
, DNA replication factor Cdt1-like
, DNA replication factor Cdt1
, Double parked, Drosophila, homolog of
, double parked homolog
, retroviral insertion site 2 protein
, retroviral integration site 1
, retroviral integration site 2
, DNA replication factor