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    NELFCD negative elongation factor complex member C/D [ Homo sapiens (human) ]

    Gene ID: 51497, updated on 27-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    TH1L involvement in colorectal cancer pathogenesis by regulation of CCL20 through the NF-kappaB signalling pathway.

    TH1L involvement in colorectal cancer pathogenesis by regulation of CCL20 through the NF-κB signalling pathway.
    Wang S, Sun Y, Li C, Chong Y, Ai M, Wang Y, Shi H, Shang Y., Free PMC Article

    06/5/2024
    Structural basis of the human negative elongation factor NELF-B/C/E ternary complex.

    Structural basis of the human negative elongation factor NELF-B/C/E ternary complex.
    Cao Y, Qin Y, Zhang W, Tian W, Ren Y, Ren J, Wang J, Wang M, Jiang J, Wang Z.

    09/11/2023
    NELFCD polymorphisms are associated with jaundice-stage progression in primary biliary cholangitis.

    NELFCD and CTSZ loci are associated with jaundice-stage progression in primary biliary cholangitis in the Japanese population.
    Nishida N, Aiba Y, Hitomi Y, Kawashima M, Kojima K, Kawai Y, Ueno K, Nakamura H, Yamashiki N, Tanaka T, Tamura S, Mori A, Yagi S, Soejima Y, Yoshizumi T, Takatsuki M, Tanaka A, Harada K, Shimoda S, Komori A, Eguchi S, Maehara Y, Uemoto S, Kokudo N, Nagasaki M, Tokunaga K, Nakamura M., Free PMC Article

    11/30/2019
    A positively charged face of NELF-AC is involved in RNA binding, whereas the opposite face of the NELF-AC subcomplex binds NELF-B. NELF-B is predicted to form a HEAT repeat fold, also binds RNA in vivo, and anchors the subunit NELF-E, which is confirmed to bind RNA in vivo.

    Architecture and RNA binding of the human negative elongation factor.
    Vos SM, Pöllmann D, Caizzi L, Hofmann KB, Rombaut P, Zimniak T, Herzog F, Cramer P., Free PMC Article

    11/25/2017
    data show that NELF subunits exhibit highly specific subcellular localizations, such as in NELF bodies or in midbodies, and some shuttle actively between the nucleus and cytoplasm; loss of NELF from cells can lead to enlarged and/or multiple nuclei

    Cellular dynamics of the negative transcription elongation factor NELF.
    Yung TM, Narita T, Komori T, Yamaguchi Y, Handa H.

    11/17/2012
    Trihydrophobin 1 phosphorylation by c-Src regulates MAPK/ERK signaling and cell migration.

    Trihydrophobin 1 phosphorylation by c-Src regulates MAPK/ERK signaling and cell migration.
    Wu W, Sun Z, Wu J, Peng X, Gan H, Zhang C, Ji L, Xie J, Zhu H, Ren S, Gu J, Zhang S., Free PMC Article

    05/19/2012
    TH1 might play an important role in regulation of proliferation and invasion in human breast cancer.

    Negative role of trihydrophobin 1 in breast cancer growth and migration.
    Zou W, Yang Y, Wu Y, Sun L, Chi Y, Wu W, Yun X, Xie J, Gu J., Free PMC Article

    10/23/2010
    These results indicate that TH1 is a novel regulator to control the duration and magnitude of androgen signal transduction and might be directly involved in androgen-related developmental, physiological, and pathological processes.

    Trihydrophobin 1 attenuates androgen signal transduction through promoting androgen receptor degradation.
    Yang Y, Zou W, Kong X, Wang H, Zong H, Jiang J, Wang Y, Hong Y, Chi Y, Xie J, Gu J.

    06/28/2010
    diverse transcriptional consequence of NELF-mediated RNAPII pausing in the human genome

    Human negative elongation factor activates transcription and regulates alternative transcription initiation.
    Sun J, Li R., Free PMC Article

    03/29/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Association of tagging single nucleotide polymorphisms on 8 candidate genes in dopaminergic pathway with schizophrenia in Croatian population.
    Pal P, Mihanović M, Molnar S, Xi H, Sun G, Guha S, Jeran N, Tomljenović A, Malnar A, Missoni S, Deka R, Rudan P., Free PMC Article

    09/16/2009
    TH1 interacts with PAK1 and specifically restricts the activation of MAPK modules through the upstream region of the MAPK pathway, thereby influencing cell migration.

    Trihydrophobin 1 Interacts with PAK1 and Regulates ERK/MAPK Activation and Cell Migration.
    Cheng C, Kong X, Wang H, Gan H, Hao Y, Zou W, Wu J, Chi Y, Yang J, Hong Y, Chen K, Gu J., Free PMC Article

    01/21/2010
    Maternal serum Th1 cytokines concentrations increase in preterm and term delivery.

    [Maternal serum Th1 and Th2 cytokines in preterm and term delivery].
    Jarocki S, Redźko S, Przepieść J, Urban J.

    01/21/2010
    Trihydrophobin 1 negatively regulates A-Raf kinase

    Trihydrophobin 1 is a new negative regulator of A-Raf kinase.
    Liu W, Shen X, Yang Y, Yin X, Xie J, Yan J, Jiang J, Liu W, Wang H, Sun M, Zheng Y, Gu J.

    01/21/2010
    Negative elongation factor (NELF) is a four subunit transcription factor. Our results point to a surprising role of NELF in the 3' end processing of histone mRNAs and suggest that NELF is a new factor that coordinates mRNA processing in transcription.

    NELF interacts with CBC and participates in 3' end processing of replication-dependent histone mRNAs.
    Narita T, Yung TM, Yamamoto J, Tsuboi Y, Tanabe H, Tanaka K, Yamaguchi Y, Handa H.

    01/21/2010
    In a two-hybrid screen of human fetal liver cDNA library, TH1 was detected as a new interaction partner of A-Raf; this specific interaction may have played a critical role in the activation of A-Raf.

    Identification of TH1 as an interaction partner of A-Raf kinase.
    Yin XL, Chen S, Gu JX.

    01/21/2010
    A study was done of ubiquitin-dependent proeolysis of TH1L protein by E6-AP.

    Ubiquitin-dependent proteolysis of trihydrophobin 1 (TH1) by the human papilloma virus E6-associated protein (E6-AP).
    Yang Y, Liu W, Zou W, Wang H, Zong H, Jiang J, Wang Y, Gu J.

    01/21/2010
    NELF-C and NELF-D are highly related or identical to the protein called TH1, of unknown function. NELF-B and NELF-C or NELF-D are integral subunits that bring NELF-A and NELF-E together. [NELF-B] [NELF-C]

    Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex.
    Narita T, Yamaguchi Y, Yano K, Sugimoto S, Chanarat S, Wada T, Kim DK, Hasegawa J, Omori M, Inukai N, Endoh M, Yamada T, Handa H., Free PMC Article

    01/21/2010
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