| Elevated EVL Methylation Level in the Normal Colon Mucosa Is a Potential Risk Biomarker for Developing Recurrent Adenomas. | Elevated EVL Methylation Level in the Normal Colon Mucosa Is a Potential Risk Biomarker for Developing Recurrent Adenomas.
Yu M, Carter KT, Baker KK, Redman MW, Wang T, Vickers K, Li CI, Cohen SA, Krane M, Ose J, Gigic B, Figueiredo JC, Toriola AT, Siegel EM, Shibata D, Schneider M, Ulrich CM, Dzubinski LA, Schoen RE, Grady WM., Free PMC Article | 09/6/2023 |
| Exercise effects on DNA methylation in EVL, CDKN2A (p14, ARF), and ESR1 in colon tissue from healthy men and women. | Exercise effects on DNA methylation in EVL, CDKN2A (p14, ARF), and ESR1 in colon tissue from healthy men and women.
Duggan C, Yu M, Willbanks AR, Tapsoba JD, Wang CY, Grady WM, McTiernan A., Free PMC Article | 10/15/2022 |
| EVL/miR-342 methylation was preferentially detected in IgD multiple myeloma | Epigenetic silencing of EVL/miR-342 in multiple myeloma.
Li Z, Wong KY, Chan GC, Chng WJ, Chim CS. | 08/4/2018 |
| Identify CRMP-1 as a novel regulator of actin filament elongation and reveal a surprisingly important role for CRMP-1, EVL, and actin polymerization in maintaining the structural integrity of epithelial sheets. | CRMP-1 enhances EVL-mediated actin elongation to build lamellipodia and the actin cortex.
Yu-Kemp HC, Kemp JP Jr, Brieher WM., Free PMC Article | 09/30/2017 |
| ENA/VASP-family proteins are functionally redundant in homologous recombination, and MENA, VASP and EVL may be involved in the DSB repair pathway in humans | Biochemical analysis of the human ENA/VASP-family proteins, MENA, VASP and EVL, in homologous recombination.
Takaku M, Ueno H, Kurumizaka H. | 02/4/2012 |
| EVL, with either E. coli topoisomerase I or human topoisomerase IIIalpha, catalyzed ssDNA catenation. | Single-stranded DNA catenation mediated by human EVL and a type I topoisomerase.
Takaku M, Takahashi D, Machida S, Ueno H, Hosoya N, Ikawa S, Miyagawa K, Shibata T, Kurumizaka H., Free PMC Article | 01/15/2011 |
| Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator) | Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article | 06/30/2010 |
| EVH2 domain, which is highly conserved among the ENA/VASP family proteins, may be responsible for the recombination function of EVL. | Biochemical analysis of the human EVL domains in homologous recombination.
Takaku M, Machida S, Nakayama S, Takahashi D, Kurumizaka H. | 01/21/2010 |
| EVL protein is a novel recombination factor that may be required for repairing specific DNA lesions, and that may cause tumor malignancy by its inappropriate expression. | Recombination activator function of the novel RAD51- and RAD51B-binding protein, human EVL.
Takaku M, Machida S, Hosoya N, Nakayama S, Takizawa Y, Sakane I, Shibata T, Miyagawa K, Kurumizaka H., Free PMC Article | 01/21/2010 |
| A microRNA encoded in an intron of the gene EVL, is commonly suppressed in human colorectal cancer. | Epigenetic silencing of the intronic microRNA hsa-miR-342 and its host gene EVL in colorectal cancer.
Grady WM, Parkin RK, Mitchell PS, Lee JH, Kim YH, Tsuchiya KD, Washington MK, Paraskeva C, Willson JK, Kaz AM, Kroh EM, Allen A, Fritz BR, Markowitz SD, Tewari M. | 01/21/2010 |
| EVL may be implicated in invasion and/or metastasis of human breast cancer. | EVL (Ena/VASP-like) expression is up-regulated in human breast cancer and its relative expression level is correlated with clinical stages.
Hu LD, Zou HF, Zhan SX, Cao KM. | 01/21/2010 |
| EVL is required for endothelial barrier function in vivo. | Ena/VASP is required for endothelial barrier function in vivo.
Furman C, Sieminski AL, Kwiatkowski AV, Rubinson DA, Vasile E, Bronson RT, Fässler R, Gertler FB., Free PMC Article | 01/21/2010 |
| the interaction of the alphaII-spectrin SH3 domain with EVL | Spectrin interacts with EVL (Enabled/vasodilator-stimulated phosphoprotein-like protein), a protein involved in actin polymerization.
Bournier O, Kroviarski Y, Rotter B, Nicolas G, Lecomte MC, Dhermy D. | 01/21/2010 |
| Ena/VASP proteins regulate actin polymerization at actin filament barbed ends in vitro in the presence and absence of barbed end capping proteins. | Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins.
Barzik M, Kotova TI, Higgs HN, Hazelwood L, Hanein D, Gertler FB, Schafer DA., Free PMC Article | 01/21/2010 |
| Data suggest that ena/VASP binding to F-actin allows for gephyrin recruitment to the leading edge of uncapped actin filaments. | The state of the actin cytoskeleton determines its association with gephyrin: role of ena/VASP family members.
Bausen M, Fuhrmann JC, Betz H, O'sullivan GA. | 01/21/2010 |