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    DNAJC7 DnaJ heat shock protein family (Hsp40) member C7 [ Homo sapiens (human) ]

    Gene ID: 7266, updated on 5-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Rare DNAJC7 Variants May Play a Minor Role in Chinese Patients with ALS.

    Rare DNAJC7 Variants May Play a Minor Role in Chinese Patients with ALS.
    Wang S, Zheng X, Wei Q, Lin J, Yang T, Xiao Y, Jiang Q, Li C, Shang H.

    04/1/2024
    DnaJC7 in Amyotrophic Lateral Sclerosis.

    DnaJC7 in Amyotrophic Lateral Sclerosis.
    Dilliott AA, Andary CM, Stoltz M, Petropavlovskiy AA, Farhan SMK, Duennwald ML., Free PMC Article

    04/30/2022
    Mutation screening of the DNAJC7 gene in Japanese patients with sporadic amyotrophic lateral sclerosis.

    Mutation screening of the DNAJC7 gene in Japanese patients with sporadic amyotrophic lateral sclerosis.
    Tohnai G, Nakamura R, Atsuta N, Nakatochi M, Hayashi N, Ito D, Watanabe H, Watanabe H, Katsuno M, Izumi Y, Taniguchi A, Kanai K, Morita M, Kano O, Kuwabara S, Oda M, Abe K, Aoki M, Aiba I, Okamoto K, Mizoguchi K, Ishihara T, Kawata A, Yokota T, Hasegawa K, Nagano I, Yabe I, Tanaka F, Kuru S, Hattori N, Nakashima K, Kaji R, Sobue G, Japanese Consortium for Amyotrophic Lateral Sclerosis Research (JaCALS).

    04/30/2022
    Validation of the pathogenic role of rare DNAJC7 variants in Chinese patients with amyotrophic lateral sclerosis.

    Validation of the pathogenic role of rare DNAJC7 variants in Chinese patients with amyotrophic lateral sclerosis.
    He J, Ma X, Yu W, Tang L, Fu J, Liu X, Ye S, Wan M, Fan D.

    01/1/2022
    Mutations of DNAJC7 are rare in Chinese amyotrophic lateral sclerosis patients.

    Mutations of DNAJC7 are rare in Chinese amyotrophic lateral sclerosis patients.
    Sun X, Zhao X, Liu Q, Zhang K, Liu S, Wang Z, Yang X, Shang L, Cui L, Zhang X.

    11/22/2021
    results highlight DNAJC7 as a novel gene for ALS.

    Exome sequencing in amyotrophic lateral sclerosis implicates a novel gene, DNAJC7, encoding a heat-shock protein.
    Farhan SMK, Howrigan DP, Abbott LE, Klim JR, Topp SD, Byrnes AE, Churchhouse C, Phatnani H, Smith BN, Rampersaud E, Wu G, Wuu J, Shatunov A, Iacoangeli A, Al Khleifat A, Mordes DA, Ghosh S, ALSGENS Consortium, FALS Consortium, Project MinE Consortium, CReATe Consortium, Eggan K, Rademakers R, McCauley JL, Schüle R, Züchner S, Benatar M, Taylor JP, Nalls M, Gotkine M, Shaw PJ, Morrison KE, Al-Chalabi A, Traynor B, Shaw CE, Goldstein DB, Harms MB, Daly MJ, Neale BM., Free PMC Article

    02/1/2020
    The data from the current study for the first time demonstrated increased serum polyglutamylated DNAJC7 as a potential biomarker for renal cell carcinoma early detection

    Reduced cytosolic carboxypeptidase 6 (CCP6) level leads to accumulation of serum polyglutamylated DNAJC7 protein: A potential biomarker for renal cell carcinoma early detection.
    Li C, Wang J, Hao J, Dong B, Li Y, Zhu X, Ding J, Ren S, Zhao H, Wu S, Tian Y, Wang GQ., Free PMC Article

    12/9/2017
    ubiquitin-proteasomal regulation of CCRP and HSP70 are important contributors to the regulation of cytoplasmic CAR levels, and hence the ability of CAR to respond to PB or PB-like inducers

    Coordinated regulation of nuclear receptor CAR by CCRP/DNAJC7, HSP70 and the ubiquitin-proteasome system.
    Timsit YE, Negishi M., Free PMC Article

    12/27/2014
    these findings strongly suggest that DnaJC7 participates in p53/MDM2 negative feedback regulatory pathway, and thereby enhancing the stability and activity of p53.

    Co-chaperon DnaJC7/TPR2 enhances p53 stability and activity through blocking the complex formation between p53 and MDM2.
    Kubo N, Wu D, Yoshihara Y, Sang M, Nakagawara A, Ozaki T.

    07/27/2013
    TPR2 exhibited strong interaction with glucocorticoid receptor and progesterone receptors.

    Differential impact of tetratricopeptide repeat proteins on the steroid hormone receptors.
    Schülke JP, Wochnik GM, Lang-Rollin I, Gassen NC, Knapp RT, Berning B, Yassouridis A, Rein T., Free PMC Article

    10/30/2010
    Data show that Tpr2 associates with Hsp90 and Hsp70 complexes, promoted the accumulation of Hsp70 in PR heterocomplexes in the presence of Hsp90. Thus, Tpr2 has the potential to regulate PR chaperoning.

    Role of the cochaperone Tpr2 in Hsp90 chaperoning.
    Moffatt NS, Bruinsma E, Uhl C, Obermann WM, Toft D.

    01/21/2010
    TPR2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.

    Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
    Brychzy A, Rein T, Winklhofer KF, Hartl FU, Young JC, Obermann WM., Free PMC Article

    01/21/2010
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