| Study identifies CTDP1 as an autoantigen specific for Behcet Disease. | Identification of Novel Biomarkers for Behcet Disease Diagnosis Using Human Proteome Microarray Approach.
Hu CJ, Pan JB, Song G, Wen XT, Wu ZY, Chen S, Mo WX, Zhang FC, Qian J, Zhu H, Li YZ., Free PMC Article | 06/24/2017 |
| results demonstrated that CTDP1 was upregulated in human lung cancer tissues. In addition, it implied that CTDP1 played an important role in cell proliferation and may be a useful therapeutic target in human lung cancer. | Lentivirus-mediated knockdown of CTDP1 inhibits lung cancer cell growth in vitro.
Zhong R, Ge X, Chu T, Teng J, Yan B, Pei J, Jiang L, Zhong H, Han B. | 07/30/2016 |
| Data propose that Fcp1 has a crucial role in the liaison between dephosphorylation and ubiquitination that drives mitosis exit. | Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit.
Visconti R, Palazzo L, Della Monica R, Grieco D., Free PMC Article | 09/22/2012 |
| although FCP1 is intrinsically disordered, the above 16 residues composing the RAP74 binding surface form nascent alpha-helical structure in the unbound state. | The disordered C-terminus of the RNA polymerase II phosphatase FCP1 is partially helical in the unbound state.
Lawrence CW, Bonny A, Showalter SA. | 09/17/2011 |
| NMR assignments for C terminal region | NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state.
Showalter SA. | 01/25/2010 |
| NMR and thermodynamic studies further elucidate the complex molecular mechanism by which TFIIF and FCP1 cooperate for RNAPII recycling. | NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 phosphatase.
Yang A, Abbott KL, Desjardins A, Di Lello P, Omichinski JG, Legault P. | 01/21/2010 |
| These data suggest that icariin exerts its potent osteogenic effect through induction of Runx2 expression, production of BMP-4 and activation of BMP signaling. | Human phosphorylated CTD-interacting protein, PCIF1, negatively modulates gene expression by RNA polymerase II.
Hirose Y, Iwamoto Y, Sakuraba K, Yunokuchi I, Harada F, Ohkuma Y. | 01/21/2010 |
| FCP1 augments tat transactivation of the HIV-1 long-terminal repeat | A protein phosphatase from human T cells augments tat transactivation of the human immunodeficiency virus type 1 long-terminal repeat.
Bharucha DC, Zhou M, Nekhai S, Brady JN, Shukla RR, Kumar A. | 01/21/2010 |
| cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 | Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF.
Kamada K, Roeder RG, Burley SK., Free PMC Article | 01/21/2010 |
| FCP1 kinase from HeLa cells is phosphorylated and affects transcription elongation | The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation.
Friedl EM, Lane WS, Erdjument-Bromage H, Tempst P, Reinberg D., Free PMC Article | 01/21/2010 |
| Enhanced binding to RAP74 following phosphorylation. | Interactions of the HIV-1 Tat and RAP74 proteins with the RNA polymerase II CTD phosphatase FCP1.
Abbott KL, Archambault J, Xiao H, Nguyen BD, Roeder RG, Greenblatt J, Omichinski JG, Legault P. | 01/21/2010 |
| FCP1 is important for transcription elongation along with TFIIF | FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation.
Mandal SS, Cho H, Kim S, Cabane K, Reinberg D., Free PMC Article | 01/21/2010 |
| found that FCP1 is a genuine substrate of PRMT5-methylation both in vivo and in vitro, and FCP1-associated PRMT5 can methylate histones H4 in vitro | Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation.
Amente S, Napolitano G, Licciardo P, Monti M, Pucci P, Lania L, Majello B. | 01/21/2010 |
| high-resolution solution structure of a cterRAP74cterFCP complex by NMR spectroscopy | NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.
Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG., Free PMC Article | 01/21/2010 |
| Congenital cataracts facial dysmorphism neuropathy is caused by a single-nucleotide substitution in an antisense Alu element in intron 6 of CTDP1, resulting in a rare mechanism of aberrant splicing and an Alu insertion in the processed mRNA | Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome.
Varon R, Gooding R, Steglich C, Marns L, Tang H, Angelicheva D, Yong KK, Ambrugger P, Reinhold A, Morar B, Baas F, Kwa M, Tournev I, Guerguelcheva V, Kremensky I, Lochmüller H, Müllner-Eidenböck A, Merlini L, Neumann L, Bürger J, Walter M, Swoboda K, Thomas PK, von Moers A, Risch N, Kalaydjieva L. | 01/21/2010 |
| FCP1 binds to a groove of RAP74 between alpha-helices H2 and H3, without affecting the secondary structure of RAP74 C-terminal domain; FCP1 binds also to a groove of TFIIB core domain beween alpha helices D1 and E1 in the first cyclin repeat. | Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG. | 01/21/2010 |