| Genetic architecture of the inflammatory bowel diseases across East Asian and European ancestries. | Genetic architecture of the inflammatory bowel diseases across East Asian and European ancestries.
Liu Z, Liu R, Gao H, Jung S, Gao X, Sun R, Liu X, Kim Y, Lee HS, Kawai Y, Nagasaki M, Umeno J, Tokunaga K, Kinouchi Y, Masamune A, Shi W, Shen C, Guo Z, Yuan K, FinnGen, International Inflammatory Bowel Disease Genetics Consortium, Chinese Inflammatory Bowel Disease Genetics Consortium, Zhu S, Li D, Liu J, Ge T, Cho J, Daly MJ, McGovern DPB, Ye BD, Song K, Kakuta Y, Li M, Huang H., Free PMC Article | 05/24/2023 |
| Oncogenic fusion transcript analysis identified ADAP1-NOC4L, potentially associated with metastatic colorectal cancer. | Oncogenic fusion transcript analysis identified ADAP1-NOC4L, potentially associated with metastatic colorectal cancer.
Talebi A, Shahidsales S, Aliakbarian M, Pezeshki Rad M, Kerachian MA., Free PMC Article | 01/28/2023 |
| ADAP1 promotes latent HIV-1 reactivation by selectively tuning KRAS-ERK-AP-1 T cell signaling-transcriptional axis. | ADAP1 promotes latent HIV-1 reactivation by selectively tuning KRAS-ERK-AP-1 T cell signaling-transcriptional axis.
Ramirez NP, Lee J, Zheng Y, Li L, Dennis B, Chen D, Challa A, Planelles V, Westover KD, Alto NM, D'Orso I., Free PMC Article | 04/23/2022 |
| In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1. | In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1.
Duellberg C, Auer A, Canigova N, Loibl K, Loose M., Free PMC Article | 05/8/2021 |
| Adap1 deletion in tumor cells ameliorated the basement membrane breakdown and had less invading cells in the stroma. Study demonstrates that ADAP1 is a critical mediator of TGF-beta-induced cancer invasion. | ADAP1 promotes invasive squamous cell carcinoma progression and predicts patient survival.
Van Duzer A, Taniguchi S, Elhance A, Tsujikawa T, Oshimori N., Free PMC Article | 07/25/2020 |
| Analyzed ArfGAP with dual PH domains 1 (ADAP1) using mass spectrometry and found that ADAP1 is phosphorylated at Y364. | A mass spectrometry based predictive strategy reveals ADAP1 is phosphorylated at tyrosine 364.
Reisdorph R, Littrell-Miller B, Powell R, Reisdorph N. | 11/24/2018 |
| This review highlights the functions of the neuron-specific protein ADAP1 in neuronal differentiation and neurodegenerative diseases, with an overview of structural and biochemical properties of ADAP1. [review] | Functions of the neuron-specific protein ADAP1 (centaurin-α1) in neuronal differentiation and neurodegenerative diseases, with an overview of structural and biochemical properties of ADAP1.
Stricker R, Reiser G. | 06/27/2015 |
| SH-SY5Y cells, stably transfected with GFP-tagged-p42(IP4), show an enhanced NRD protein expression already at an earlier time point after retinoic acid stimulation. | Retinoic acid-induced upregulation of the metalloendopeptidase nardilysin is accelerated by co-expression of the brain-specific protein p42(IP4) (centaurin α 1; ADAP1) in neuroblastoma cells.
Borrmann C, Stricker R, Reiser G. | 02/2/2013 |
| Tubulin potentiates the interaction of the metalloendopeptidase nardilysin with the neuronal scaffold protein p42IP4/centaurin-alpha1 (ADAP1). | Tubulin potentiates the interaction of the metalloendopeptidase nardilysin with the neuronal scaffold protein p42IP4/centaurin-α1 (ADAP1).
Borrmann C, Stricker R, Reiser G. | 02/25/2012 |
| Full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule. | Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin alpha1.
Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, MacKenzie F, Chishti AH, Park HW., Free PMC Article | 01/22/2011 |
| The ARFGAP domain of p42IP4 is involved in the interaction and co-localization with RanBPM protein, without being the only interaction site. | RanBPM, a novel interaction partner of the brain-specific protein p42IP4/centaurin alpha-1.
Haase A, Nordmann C, Sedehizade F, Borrmann C, Reiser G. | 08/16/2010 |
| Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator) | Polymorphisms in innate immunity genes and risk of childhood leukemia.
Han S, Lan Q, Park AK, Lee KM, Park SK, Ahn HS, Shin HY, Kang HJ, Koo HH, Seo JJ, Choi JE, Ahn YO, Chanock SJ, Kim H, Rothman N, Kang D., Free PMC Article | 06/30/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | See all PubMed (2) articlesRisk of meningioma and common variation in genes related to innate immunity.
Rajaraman P, Brenner AV, Neta G, Pfeiffer R, Wang SS, Yeager M, Thomas G, Fine HA, Linet MS, Rothman N, Chanock SJ, Inskip PD. Common variation in genes related to innate immunity and risk of adult glioma.
Rajaraman P, Brenner AV, Butler MA, Wang SS, Pfeiffer RM, Ruder AM, Linet MS, Yeager M, Wang Z, Orr N, Fine HA, Kwon D, Thomas G, Rothman N, Inskip PD, Chanock SJ. | 06/30/2010 |
| Centaurin-alpha1 contributes to ERK activation in growth factor signaling, linking the PI3K pathway to the ERK mitogen-activated protein kinase pathway. | Centaurin-alpha1 is a phosphatidylinositol 3-kinase-dependent activator of ERK1/2 mitogen-activated protein kinases.
Hayashi H, Matsuzaki O, Muramatsu S, Tsuchiya Y, Harada T, Suzuki Y, Sugano S, Matsuda A, Nishida E. | 01/21/2010 |
| The centaurin, alpha 1 protein is a high-affinity PtdIns(3,4,5)P3-binding protein enriched in brain. Sequence analysis indicates centaurin alpha-1 contains two pleckstrin homology domains, ankyrin repeats and an Arf GAP homology domain. | The arf6 GAP centaurin alpha-1 is a neuronal actin-binding protein which also functions via GAP-independent activity to regulate the actin cytoskeleton.
Thacker E, Kearns B, Chapman C, Hammond J, Howell A, Theibert A. | 01/21/2010 |
| Results show that nucleolin interacts with centaurin-alpha(1) protein, suggesting that centaurin-alpha(1) may be part of a ribonucleoprotein complex. | Centaurin-alpha 1 associates in vitro and in vivo with nucleolin.
Dubois T, Zemlickova E, Howell S, Aitken A. | 01/21/2010 |
| the up-regulated p42(IP4) in Alzheimer's disease neurons may serve as a docking protein to recruit signaling molecules such as different subtypes of casein kinase I to the plasma membrane. | Neurons and plaques of Alzheimer's disease patients highly express the neuronal membrane docking protein p42IP4/centaurin alpha.
Reiser G, Bernstein HG. | 01/21/2010 |
| Data show that membrane transport of p42(IP4) induced by epidermal growth factor is inhibited by stimulation of phospholipase C-coupled thrombin receptor. | p42(IP4)/centaurin alpha1, a brain-specific PtdIns(3,4,5)P3/Ins(1,3,4,5)P4-binding protein: membrane trafficking induced by epidermal growth factor is inhibited by stimulation of phospholipase C-coupled thrombin receptor.
Sedehizade F, von Klot C, Hanck T, Reiser G. | 01/21/2010 |
| centaurin-alpha1 negatively regulates ARF6 activity by functioning as an in vivo PIP3-dependent ARF6 GAP | Centaurin-alpha1 is an in vivo phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein for ARF6 that is involved in actin cytoskeleton organization.
Venkateswarlu K, Brandom KG, Lawrence JL. | 01/21/2010 |
| p42IP4 receptor is expressed and distributed throughout the cell in HEK cell lines and is located on chromosome 7, position 7p22.3. | Identification of gene structure and subcellular localization of human centaurin alpha 2, and p42IP4, a family of two highly homologous, Ins 1,3,4,5-P4-/PtdIns 3,4,5-P3-binding, adapter proteins.
Hanck T, Stricker R, Sedehizade F, Reiser G. | 01/21/2010 |
| By acting as a GTPase activating protein for ADP ribosylation factor 6 (ARF6), centaurin alpha 1 is able to switch off ARF6 and inhibit its ability to mediate beta 2-adrenoceptor internalization. | Centaurin-alpha 1, an ADP-ribosylation factor 6 GTPase activating protein, inhibits beta 2-adrenoceptor internalization.
Lawrence J, Mundell SJ, Yun H, Kelly E, Venkateswarlu K. | 01/21/2010 |
| p42IP4 binds to nardilysin via the acidic domain, and that this interaction is controlled by the cognate cellular ligands of p42IP4/centaurin-alpha1 | Interaction of the brain-specific protein p42IP4/centaurin-alpha1 with the peptidase nardilysin is regulated by the cognate ligands of p42IP4, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4, with stereospecificity.
Stricker R, Chow KM, Walther D, Hanck T, Hersh LB, Reiser G. | 01/21/2010 |
| Authors propose alternative concepts of how elevated levels of p42IP4 might relate to its interaction with nucleolin in the pathomechanisms of Alzheimer's disease. | Altered expression of protein p42IP4/centaurin-alpha 1 in Alzheimer's disease brains and possible interaction of p42IP4 with nucleolin.
Reiser G, Bernstein HG. | 01/21/2010 |