STAU1 Antibody, HRP conjugated

1. recruited to mutant ATXN2 aggregates in spinocerebellar ataxia type 2 fibroblasts PMID: 30194296
2. Staufen1 has differential roles in embryonal versus alveolar rhabdomyosarcoma through the control of proliferative and apoptotic pathways, respectively. PMID: 28211476
3. Mechanistically, we suggest that SNHG5 stabilizes the target transcripts by blocking their degradation by STAU1. Accordingly, depletion of STAU1 rescues the apoptosis induced after SNHG5 knockdown. Hence, we characterize SNHG5 as a lncRNA promoting tumour cell survival in colorectal cancer. PMID: 28004750
4. E2F1 induces TINCR transcriptional activity and accelerates gastric cancer progression via activation of TINCR/STAU1/CDKN2B signaling axis. PMID: 28569791
5. ADAR1p110 isoform competitively inhibits binding of Staufen1 to the 3'-untranslated-region dsRNAs and antagonizes Staufen1-mediated mRNA decay. PMID: 28436945
6. Stau1 is a stress response gene that remains efficiently translated during hypoxia and ER stress despite the substantial global inhibition of cap-dependent protein translation, promoting cell recovery following stress PMID: 27644878
7. Our findings suggest that HCV may appropriate Stau1 to its advantage to prevent PKR-mediated inhibition of eIF2alpha, which is required for the synthesis of HCV proteins for translocation of viral RNA genome to the polysomes for efficient translation and replication. PMID: 27106056
8. together, these data highlight the broad impact of Stau1 as a splicing regulator and suggest that Stau1 may act as a disease modifier in DM1. PMID: 26824521
9. expression of human Staufen1 is essential for proper dendritic arborisation during neuroblastoma cell differentiation, yet it is not necessary for maintenance of differentiated state, and suggest potential human Stauf1 mRNA targets involved in the process PMID: 25423178
10. The changing pattern of STAU distribution during meiotic maturation of human oocytes implicates a novel mechanism for the regulation of protein synthesis based on mRNA localization PMID: 25620022
11. in vivo atlas of mRNA secondary structures recognized by Staufen 1 PMID: 25799984
12. TINCR, together with Staufen1, seems to stabilize a subset of mRNAs required for epidermal differentiation. PMID: 24019000
13. A common sequence signature consisting of two opposite-polarity Alu motifs was present in the hStau1-associated mRNAs and was shown to be sufficient for binding to hStau1 and hStau1-dependent stimulation of protein expression. PMID: 24470147
14. Staufen1 is an important factor in HCV replication and it might play a role early in the HCV replication cycle, rather than virion morphogenesis. PMID: 23907398
15. STAU1 binding to a 3'-UTR SBS was previously shown to trigger STAU1-mediated mRNA decay (SMD) by directly recruiting the ATP-dependent RNA helicase UPF1 PMID: 24056942
16. These results suggest a new role for Staufen-1 as a cellular Rec and human endogenous retrovirus family HERV-K Gag cofactor. PMID: 23926355
17. this study reports the identification of two new hGIP-interacting partners, DTX1 and STAU1. PMID: 23395680
18. The regulation of STAU1 mediated mRNA decay efficiency by NS1 may contribute to building a more favorable cellular environment for viral replication. PMID: 23722113
19. STAU1 binding to 3' UTR IRAlus functions along with 3' UTR IRAlus-mediated nuclear retention to suppress the shutdown of cellular translation triggered by PKR binding to endogenous cytoplasmic dsRNAs PMID: 23824540
20. SSM-mediated hSTAU1 dimerization increases the efficiency of SMD by augmenting hSTAU1 binding to the ATP-dependent RNA helicase hUPF1 PMID: 23524536
21. TDP-43 is physically associated with fragile X mental retardation protein (FMRP) and Staufen (STAU1) to form a functional complex. PMID: 22584570
22. For Stau1-mediated mRNA decay, Stau1 binds to the 3' untranslated region of target mRNA and recruits Upf1 to elicit rapid mRNA degradation. PMID: 22503102
23. our results unravel a novel function for Staufen1 in splicing regulation and indicate that it may positively modulate the complex DM1 phenotype PMID: 22431750
24. the specific region responsible for the interaction between Stau1 and influenza A Virus NS1 was identified. PMID: 21945618
25. findings that the binding of STAU1 to mRNAs can be transactivated by long non-coding RNAs uncovers an unexpected strategy that cells use to recruit proteins to mRNAs and mediate the decay of these mRNAs PMID: 21307942
26. Gag specifically recruited Staufen1 to the detergent insoluble membranes supporting a key function for this host factor during virus assembly. PMID: 20459747
27. These results indicate a role for hStau1 in late events of the influenza virus infection, possibly during virus morphogenesis. PMID: 20504931
28. Work provides new evidence that Staufen1-containing HIV-1 RNPs preferentially form over other cellular silencing foci and are involved in assembly, localization and encapsidation of vRNA. PMID: 20053637
29. The oligomeric composition of Stau1-containing complexes and the presence of specific mRNAs have been confirmed by biochemical approaches involving two successive immunoprecipitations of Stau1-tagged molecules followed by qRT-PCR amplification. PMID: 20075165
30. Data show that the Staufen isoform Stau(55)co-fractionates with ribosomes, suggesting that it plays some role in translation. PMID: 12133005
31. These data show that Staufen, pr55(Gag), and genomic RNA are part of the same intracellular complex and support a role for Staufen in pr55(Gag) function in viral assembly, genomic RNA encapsidation, and the generation of infectious viral particles. PMID: 15024055
32. The identity of proteins present in staufen complexes from RNA granules indicates that staufen has a role in transport and translation of messenger RNAs. PMID: 15121898
33. Stau1 influences HIV-1 assembly by modulating pr55Gag-pr55Gag interactions, as shown in a live cell interaction assay PMID: 17428849
34. Stau1 influences the expression of a wide variety of physiologic transcripts and metabolic pathways. PMID: 17510634
35. Stau1- and Stau2-mRNPs associate with distinct but overlapping sets of cellular mRNAs. PMID: 18094122
36. 12 amino acids at the N-terminal end of Stau1 is necessary to increase Pr55Gag multimerization and particle release. PMID: 18498651
37. isolated a novel transcript of STAU1, coding a novel isoform that has six amino acids more (SFPLKQ) than isoform a PMID: 18806890

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HGNC: 11370

OMIM: 601716

KEGG: hsa:6780

STRING: 9606.ENSP00000360922

UniGene: Hs.596704