ACD Antibody, FITC conjugated

1. A defective POT1-TPP1 complex leads to longer and fragile telomeres, which in turn promotes genomic instability and cancer. PMID:28393830
2. several missense mutations in human cancers that disrupt the POT1C-TPP1 interaction, resulting in POT1 instability, were identified. PMID:28393832
3. the human POT1-TPP1 complex is a processivity factor for telomerase PMID:21461822
4. UPF1 interacts with TPP1 and telomerase and sustains telomere leading-strand replication PMID:21829167
5. Altered expression of TPP1 might contribute to persistent proliferation of fibroblast-like synovial cells in rheumatoid arthritis. PMID:21833529
6. seven separation-of-function mutations map to a patch of amino acids on the surface of TPP1, the TEL patch, that both recruits telomerase to telomeres and promotes high-processivity DNA synthesis PMID:23103865
7. Blocking TPP1 S111 phosphorylation by mutating residue S111 led to reduced telomerase association and telomere shortening. PMID:23509301
8. Telomere damage and reduced TPP1 dimerization as a result of Akt inhibition was also accompanied by diminished recruitment of TPP1 and POT1 to the telomeres. PMID:23862686
9. Elevated expression of TPP1 in human colorectal cancer cells could protect telomere from DNA damage and confer radioresistance. PMID:24260532
10. Down-regulation of TPP1 induced cell apoptosis in telomerase-negative osteosarcoma cell line. PMID:24513288
11. G-quadruplex formation of telomeres significantly enhances the ability of POT1/TPP1 to block RPA's access to telomeres. PMID:24516170
12. TPP1 has recently emerged as a primary contributor in protecting telomere DNA and in recruiting telomerase to the telomere ends. (Review) PMID:24780581
13. TPP1 provides an essential step of telomerase activation as well as feedback regulation of telomerase by telomere length, which is necessary to determine the appropriate telomere length set point in human embryonic stem cells PMID:25128433
14. TPP1 is a binding partner and substrate for the deubiquitinating enzyme USP7. PMID:25172512
15. these data provide a molecular basis by which POT1-TPP1 increases the processivity of telomerase15. Further, we show that this increased processivity may arise from the dynamic sliding of POT1-TPP1 that induces fast translocation of telomerase. PMID:25263700
16. Mutations have been identified in the TEN-domain of TERT that disrupt the interaction of telomerase with TPP1 in vivo and in vitro but have very little effect on the catalytic activity of telomerase. PMID:25271372
17. The conservation between fission yeast Tpz1-Pot1 and human TPP1-POT1 interactions resulted in mapping a human melanoma-associated POT1 mutation (A532P) to the TPP1-POT1 interface. PMID:26365187
18. that the insertion in fingers domain can mediate enzyme processivity and telomerase recruitment to telomeres in a TPP1-dependent manner PMID:26503784
19. Binding of POT1-TPP1 unfolds telomere secondary structure to assist loading of additional heterodimers. PMID:27173378
20. Together, these functional data combined with biophysical analyses and homology modeling provide a molecular understanding of the diverse contributions of TPP1 in telomere maintenance. PMID:27655633
21. We found that NEK6-mediated phosphorylation of TPP1 Ser255 in G2/M phase regulates the association between telomerase activity and TPP1. Furthermore, we found evidence that POT1 negatively regulates TPP1 phosphorylation because the level of Ser255 phosphorylation was elevated when telomeres were elongated by a POT1 mutant lacking its OB-fold domains PMID:27396482
22. We report the crystal structure of a mutant TPP1 implicated in dyskeratosis congenita (DC) to reveal how the mutation disrupts a region of the protein essential for telomerase function. Furthermore, we demonstrated that this mutation, when introduced into a human cell line, is sufficient to cause the cellular underpinnings of DC. PMID:27807141
23. a novel ACD mutation(p.G223V)is detected; ACD is a novel gene involved in childhood pre-B acute lymphoblastic leukemia and may play a functional role in enhancing leukemia cell survival PMID:26345285
24. The data support a causal relationship between a TPP1 mutation and bone marrow disorders in a family. PMID:25205116
25. Clustering of novel mutations in the POT1 binding domain of ACD was statistically higher (P = .005) in melanoma probands compared with population control individuals (n = 6785). PMID:25505254
26. Shelterin protein TPP 1 interacts with hTERT and recruits hTERT onto the telomeres, suggesting that TPP 1 might be involved in regulation of telomere shortening. PMID:24721976
27. POT1-TPP1 binds telomeric DNA in a coordinated manner to facilitate assembly of the nucleoprotein complexes into a state that is more accessible to enzymatic activity. PMID:23616058
28. Study shows that the OB-fold domain of the telomere-binding protein TPP1 recruits telomerase to telomeres through an association with the telomerase reverse transcriptase TERT; data define a potential interface for telomerase-TPP1 interaction required for telomere maintenance and implicate defective telomerase recruitment in telomerase-related disease. PMID:22863003
29. a paper that firstly reported cloning of human TTP1 (PTOP) and its biological function at telomere. TPP1 interacts with both POT1 and TIN2, heterodimerizes with POT1 and regulates POT1 telomeric recruitment and telomere length. PMID:15181449
30. The presence of dysfunctional telomeres in chronic lymphocytic leukemia did not correlate with telomere shortening or chromatin marks deregulation but with a down-regulation of 2 shelterin genes: ACD and TINF2. PMID:21355086
31. Results support a model in which POT1-TPP1 enhances telomerase processivity in a manner markedly different from the sliding clamps used by DNA polymerases. PMID:20094033
32. TIN2-anchored TPP1 plays a major role in the recruitment of telomerase to telomeres in human cells. PMID:20404094
33. TINT1 localized to telomeres via TIN2, where it functions as a negative regulator of telomerase-mediated telomere elongation. PMID:15380063
34. Sequencing of ACD in 15 patients with clinical features of IMAGe syndrome, adrenal hypoplasia congenita, or congenital adrenal insufficiency revealed no coding mutations, but three novel SNPs were identified PMID:16504561
35. coordinated interactions among TPP1, TIN2, TRF1, and TRF2 may ensure robust assembly of the telosome, telomere targeting of its subunits, and, ultimately, regulated telomere maintenance PMID:16880378
36. findings highlight the critical role of TPP1 in telomere maintenance, and support a yin-yang model in which TPP1 and POT1 function as a unit to protect human telomeres, by both positively and negatively regulating telomerase access to telomere DNA PMID:17237767
37. crystal structure of human TPP1 reveals an oligonucleotide/oligosaccharide-binding fold that is structurally similar to the beta-subunit of the telomere end-binding protein of a ciliated protozoan; TPP1 is the missing beta-subunit of human POT1 PMID:17237768
38. REVIEW:TPP1 as a critical mediator of control of telomerase activity PMID:17373762
39. No mutations were identified in ACD in this collection of patients with ACTH resistance phenotypes. However, the newly identified SNPs in ACD should be more closely examined for possible links to disease. PMID:17466001
40. Tpp1 is required for the protective function of Pot1 proteins. PMID:17632522
41. Increased expression of TPP1 correlates with resistance to radiation in human laryngeal cancer cell lines. PMID:19424630
42. Studies indicate that TPP1 and POT1can form heterodimers that bind to the telomeric single-stranded DNA, an activity that is central for telomere end capping. PMID:19648609

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HGNC: 25070

UNIGENE: Hs.78019

KEGG: hsa:65057

STRING: 9606.ENSP00000377496

OMIM: 609377