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Subsequent analysis of 844 index cases did not reveal further pathogenic chances in ARL2BP indicating that mutations in ARL2B are a rare cause of arRCD (about 0.1%) in a large cohort of French patients.
Alteration of EBV encoded miR-BART1 expression results in an increase in migration and invasion of nasopharyngeal carcinoma in vitro and causes metastasis in vivo. EBV-miR-BART1 directly targets the cellular tumour suppressor PTEN.
EBV also downregulates two immediate early (显示 JUN 蛋白) genes by miR (显示 MLXIP 蛋白)-BART20-5p.
Mutations in ARL2BP cause autosomal-recessive retinitis pigmentosa.
EBV-miR (显示 MLXIP 蛋白)-BART1 could influence the expression of metabolism-associated genes and might be involved in cancer metabolism in nasopharyngeal carcinoma
Our results imply that BART regulates actin-cytoskeleton rearrangements at membrane ruffles through modulation of the activity of Rac1, which, in turn, inhibits pancreatic cancer cell invasion.
These results imply that BART (显示 BSND 蛋白) contributes to regulating PKCalpha (显示 PKCa 蛋白) activity through binding to ANX7 (显示 ANXA7 蛋白), thereby affecting the invasiveness of pancreatic cancer cells.
We identify a subset of BART (显示 BSND 蛋白) miRNAs that are restricted to Latency III in normal infection but are up regulated in tumors that express Latency I and II.
Our results imply that BART (显示 BSND 蛋白) increases active RhoA (显示 RHOA 蛋白) by inhibiting ARL2 (显示 ARL2 蛋白) function, which in turn inhibits invasiveness of cancer cells.
overexpression of the amino (N)-terminal region of G3BP (显示 G3BP1 蛋白), including the binding region for BART (显示 BSND 蛋白) mRNA, dominant-negatively inhibits formation of the complex between endogenous G3BP (显示 G3BP1 蛋白) and BART (显示 BSND 蛋白) mRNA, and increases the expression of BART (显示 BSND 蛋白).
BART is essential for the transcriptional activity and nuclear retention of STAT3 (显示 STAT3 蛋白)
ADP-ribosylation factor (ARF)-like proteins (ARLs) comprise a functionally distinct group of the ARF family of RAS-related GTPases. The protein encoded by this gene binds to ARL2.GTP with high affinity but does not interact with ARL2.GDP, activated ARF, or RHO proteins. The lack of detectable membrane association of this protein or ARL2 upon activation of ARL2 is suggestive of actions distinct from those of the ARFs. This protein is considered to be the first ARL2-specific effector identified, due to its interaction with ARL2.GTP but lack of ARL2 GTPase-activating protein activity.
ADP-ribosylation factor-like protein 2-binding protein
, ARF-like 2-binding protein
, ADP-ribosylation factor-like 2 binding protein
, Arf-like 2 binding protein BART1
, binder of ARF2 protein 1
, binder of Arl Two
, binder of Arl2
, ADP-ribosylation-like 2 binding protein