| Oculopharyngeal muscular dystrophy mutations link the RNA-binding protein HNRNPQ to autophagosome biogenesis. | Oculopharyngeal muscular dystrophy mutations link the RNA-binding protein HNRNPQ to autophagosome biogenesis.
Ishtayeh H, Galves M, Barnatan TT, Berdichevsky Y, Amer-Sarsour F, Pasmanik-Chor M, Braverman I, Blumen SC, Ashkenazi A., Free PMC Article | 10/28/2023 |
| Further evidence for de novo variants in SYNCRIP as the cause of a neurodevelopmental disorder. | Further evidence for de novo variants in SYNCRIP as the cause of a neurodevelopmental disorder.
Semino F, Schröter J, Willemsen MH, Bast T, Biskup S, Beck-Woedl S, Brennenstuhl H, Schaaf CP, Kölker S, Hoffmann GF, Haack TB, Syrbe S. | 04/9/2022 |
| A novel antisense lncRNA NT5E promotes progression by modulating the expression of SYNCRIP and predicts a poor prognosis in pancreatic cancer. | A novel antisense lncRNA NT5E promotes progression by modulating the expression of SYNCRIP and predicts a poor prognosis in pancreatic cancer.
Zhang P, Cao M, Zhang Y, Xu L, Meng F, Wu X, Xia T, Chen Q, Shi G, Wu P, Chen L, Lu Z, Yin J, Cai B, Cao S, Miao Y, Jiang K., Free PMC Article | 06/5/2021 |
| ATP binds nucleic-acid-binding domains beyond RRM fold. | ATP binds nucleic-acid-binding domains beyond RRM fold.
He Y, Kang J, Lim L, Song J. | 09/5/2020 |
| the terminal loop of pri-let-7a was shown to be the main contributor for its interaction with SYNCRIP. Functional studies demonstrated that the SYNCRIP RRM2-3 domain can promote the processing of pri-let-7a | SYNCRIP, a new player in pri-let-7a processing.
Chen Y, Chan J, Chen W, Li J, Sun M, Kannan GS, Mok YK, Yuan YA, Jobichen C., Free PMC Article | 06/20/2020 |
| Identification of the frequent presence of hnRNP R and hnRNP Q in frontotemporal lobar degeneration (FTLD)-FUS inclusions suggests a potential role for these hnRNPs in FTLD-FUS pathogenesis and supports the role of dysfunctional RNA metabolism in FTLD. | Heterogeneous nuclear ribonucleoproteins R and Q accumulate in pathological inclusions in FTLD-FUS.
Gittings LM, Foti SC, Benson BC, Gami-Patel P, Isaacs AM, Lashley T., Free PMC Article | 04/4/2020 |
| Results indentified two candidate haploinsufficient genes contiguous at 6q14 SYNCRIP (encoding hnRNP-Q) and SNHG5 (that hosts snoRNAs), both involved in regulating RNA maturation and translation inT-cell acute lymphoblastic leukemia (T-ALL). | Deletion 6q Drives T-cell Leukemia Progression by Ribosome Modulation.
Gachet S, El-Chaar T, Avran D, Genesca E, Catez F, Quentin S, Delord M, Thérizols G, Briot D, Meunier G, Hernandez L, Pla M, Smits WK, Buijs-Gladdines JG, Van Loocke W, Menschaert G, André-Schmutz I, Taghon T, Van Vlierberghe P, Meijerink JP, Baruchel A, Dombret H, Clappier E, Diaz JJ, Gazin C, de Thé H, Sigaux F, Soulier J. | 12/28/2019 |
| The EGF/hnRNP Q1-induced translation of Aurora-A mRNA is mediated by the mTOR and ERK pathways. | The EGF/hnRNP Q1 axis is involved in tumorigenesis via the regulation of cell cycle-related genes.
Wang YC, Chang KC, Lin BW, Lee JC, Lai CH, Lin LJ, Yen Y, Lin CS, Yang SJ, Lin PC, Lee CT, Hung LY., Free PMC Article | 03/30/2019 |
| A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets. | A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets.
Hobor F, Dallmann A, Ball NJ, Cicchini C, Battistelli C, Ogrodowicz RW, Christodoulou E, Martin SR, Castello A, Tripodi M, Taylor IA, Ramos A., Free PMC Article | 11/24/2018 |
| our data indicate that hnRNP Q1 is a novel trans-acting factor that binds to Aurora-A mRNA 5'-UTRs and regulates its translation, which increases cell proliferation and contributes to tumorigenesis in colorectal cancer | Translational upregulation of Aurora-A by hnRNP Q1 contributes to cell proliferation and tumorigenesis in colorectal cancer.
Lai CH, Huang YC, Lee JC, Tseng JT, Chang KC, Chen YJ, Ding NJ, Huang PH, Chang WC, Lin BW, Chen RY, Wang YC, Lai YC, Hung LY., Free PMC Article | 10/28/2017 |
| SYNCRIP is required for survival of leukemia cells. SYNCRIP controls the myeloid leukemia stem cell program. | Functional screen of MSI2 interactors identifies an essential role for SYNCRIP in myeloid leukemia stem cells.
Vu LP, Prieto C, Amin EM, Chhangawala S, Krivtsov A, Calvo-Vidal MN, Chou T, Chow A, Minuesa G, Park SM, Barlowe TS, Taggart J, Tivnan P, Deering RP, Chu LP, Kwon JA, Meydan C, Perales-Paton J, Arshi A, Gönen M, Famulare C, Patel M, Paietta E, Tallman MS, Lu Y, Glass J, Garret-Bakelman FE, Melnick A, Levine R, Al-Shahrour F, Järås M, Hacohen N, Hwang A, Garippa R, Lengner CJ, Armstrong SA, Cerchietti L, Cowley GS, Root D, Doench J, Leslie C, Ebert BL, Kharas MG., Free PMC Article | 09/16/2017 |
| The acidic domain is a unique structural feature of the splicing factor SYNCRIP. | The acidic domain is a unique structural feature of the splicing factor SYNCRIP.
Beuck C, Williamson JR, Wüthrich K, Serrano P., Free PMC Article | 04/22/2017 |
| hnRNPQ6 is required for APOBEC1-enhanced IL8 production. | The RNA-editing enzyme APOBEC1 requires heterogeneous nuclear ribonucleoprotein Q isoform 6 for efficient interaction with interleukin-8 mRNA.
Shimizu Y, Nishitsuji H, Marusawa H, Ujino S, Takaku H, Shimotohno K., Free PMC Article | 02/7/2015 |
| The hnRNP Q is a novel substrate of SHP2 and the SHP2 activity may be also involved in RNA metabolisms via dephosphorylation of hnRNP Q. | Heterogeneous nuclear ribonucleoprotein Q is a novel substrate of SH2 domain-containing phosphatase-2.
Watanabe N, Kato T, Fujita H, Kitagawa S. | 12/27/2014 |
| The inhibitory effect of hnRNP Q on YB-1 mRNA translation can be explained by its ability to pro-mote YB-1 binding to the regulatory element within the YB-1 mRNA 3' UTR. | Identification of proteins specifically interacting with YB-1 mRNA 3' UTR and the effect of hnRNP Q on YB-1 mRNA translation.
Lyabin DN, Nigmatullina LF, Doronin AN, Eliseeva IA, Ovchinnikov LP. | 04/21/2014 |
| These data indicate that hnRNP Q can stimulate the protein production of HIV-1 Rev-dependent mRNAs without changing mRNA levels and mRNA export, respectively. | Heterogenous nuclear ribonucleoprotein Q increases protein expression from HIV-1 Rev-dependent transcripts.
Vincendeau M, Nagel D, Brenke JK, Brack-Werner R, Hadian K., Free PMC Article | 01/25/2014 |
| Data demonstrate that expression levels of hnRNP A1, Q, K, R, and U influence HIV-1 production by persistently infected | Identification of a heterogeneous nuclear ribonucleoprotein-recognition region in the HIV Rev protein.
Hadian K, Vincendeau M, Mäusbacher N, Nagel D, Hauck SM, Ueffing M, Loyter A, Werner T, Wolff H, Brack-Werner R., Free PMC Article | 01/25/2010 |
| SYNCRIP participates in both RNA replication and translation in HCV life cycle. | SYNCRIP (synaptotagmin-binding, cytoplasmic RNA-interacting protein) is a host factor involved in hepatitis C virus RNA replication.
Liu HM, Aizaki H, Choi KS, Machida K, Ou JJ, Lai MM., Free PMC Article | 01/21/2010 |
| Results demonstrate that galectin-3 stabilizes hnRNP Q via complex formation, and reduction in the hnRNP Q level leads to slow proliferation and less susceptibility to 5-FU. | Galectin-3 stabilizes heterogeneous nuclear ribonucleoprotein Q to maintain proliferation of human colon cancer cells.
Yoo BC, Hong SH, Ku JL, Kim YH, Shin YK, Jang SG, Kim IJ, Jeong SY, Park JG., Free PMC Article | 01/21/2010 |
| Data demonstrate that hnRNP Q is a splicing modulator of SMN2, further underscoring the potential of hnRNP Q as a therapeutic target for spinal muscular atrophy. | The RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) gene.
Chen HH, Chang JG, Lu RM, Peng TY, Tarn WY., Free PMC Article | 01/21/2010 |
| SYNCRIP is transported within the dendrite as a component of mRNA granules | An RNA-interacting protein, SYNCRIP (heterogeneous nuclear ribonuclear protein Q1/NSAP1) is a component of mRNA granule transported with inositol 1,4,5-trisphosphate receptor type 1 mRNA in neuronal dendrites.
Bannai H, Fukatsu K, Mizutani A, Natsume T, Iemura S, Ikegami T, Inoue T, Mikoshiba K. | 01/21/2010 |
| The overexpression of NSAP1 specifically enhanced HCV IRES-dependent translation, and knockdown of NSAP1 by use of a small interfering RNA specifically inhibited the translation of HCV mRNA. | A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon.
Kim JH, Paek KY, Ha SH, Cho S, Choi K, Kim CS, Ryu SH, Jang SK., Free PMC Article | 01/21/2010 |
| Results suggest hnRNPQ interacts via its acidic domain (AcD) with Apobec1 and that this interaction is regulated by AcD phosphorylation. | The acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1.
Quaresma AJ, Oyama S Jr, Barbosa JA, Kobarg J. | 01/21/2010 |
| methylation of hnRNPQ is important for its nuclear localization | The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization.
Passos DO, Quaresma AJ, Kobarg J. | 01/21/2010 |