Relevant bibliographies by topics / PLEKHO1

Academic literature on the topic 'PLEKHO1'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'PLEKHO1.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "PLEKHO1"

1

He, Xiaojuan, Jin Liu, Chao Liang, Shaikh Atik Badshah, Kang Zheng, Lei Dang, Baosheng Guo, et al. "Osteoblastic PLEKHO1 contributes to joint inflammation in rheumatoid arthritis." EBioMedicine 41 (March 2019): 538–55. http://dx.doi.org/10.1016/j.ebiom.2019.02.009.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Liu, Jin, Chao Liang, Baosheng Guo, Xiaohao Wu, Defang Li, Zongkang Zhang, Kang Zheng, et al. "Increased PLEKHO1 within osteoblasts suppresses Smad-dependent BMP signaling to inhibit bone formation during aging." Aging Cell 16, no. 2 (January 13, 2017): 360–76. http://dx.doi.org/10.1111/acel.12566.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

He, Xiaojuan, Jin Liu, Chao Liang, Shaikh Atik Badshah, Kang Zheng, Lei Dang, Baosheng Guo, et al. "Corrigendum to ‘Osteoblastic PLEKHO1 contributes to joint inflammation in rheumatoid arthritis’ [EBioMedicine 41 (2019) 538–555]." EBioMedicine 52 (February 2020): 102669. http://dx.doi.org/10.1016/j.ebiom.2020.102669.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Ma, Hong-wei, Min Xie, Ming Sun, Tian-yu Chen, Rong-rong Jin, Tian-shi Ma, Qin-nan Chen, et al. "The pseudogene derived long noncoding RNA DUXAP8 promotes gastric cancer cell proliferation and migration via epigenetically silencing PLEKHO1 expression." Oncotarget 8, no. 32 (August 5, 2016): 52211–24. http://dx.doi.org/10.18632/oncotarget.11075.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

C. Han, Eric, Yu-Chuen Huang, Jane-Ming Lin, Hui-Ju Lin, Jer-Yuarn Wu, Cheng-Chun Lee, and Fuu-Jen Tsai. "Association of the PLEKHO2 and PLEKHH1 gene polymorphisms with type 2 diabetic retinopathy in a Taiwanese population." ScienceAsia 38, no. 4 (2012): 340. http://dx.doi.org/10.2306/scienceasia1513-1874.2012.38.340.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Xing, Xiangling, Ninni Mu, Xiaotian Yuan, Na Wang, C. Christofer Juhlin, Klas Strååt, Catharina Larsson, and Dawei Xu. "PLEKHS1 Over-Expression is Associated with Metastases and Poor Outcomes in Papillary Thyroid Carcinoma." Cancers 12, no. 8 (July 31, 2020): 2133. http://dx.doi.org/10.3390/cancers12082133.

Full text
Abstract:
Pleckstrin homology domain containing S1 (PLEKHS1) is a poorly characterized factor, although its promoter mutations were identified in human malignancies including thyroid carcinoma (TC). This study was designed to determine PLEKHS1 promoter hotspot mutations in papillary and anaplastic thyroid carcinomas (PTCs and ATCs) and to evaluate if PLEKHS1 expression influences clinical outcome. The PLEKHS1 promoter mutation was observed in 1/93 of PTCs and none of 18 ATCs in our cohort; however, PLEKHS1 expression was aberrantly up-regulated in TCs compared to adjacent non-tumorous thyroid tissues. ATC tumors, an undifferentiated TC, exhibited the highest PLEKHS1 expression. In both TCGA and present cohorts of PTCs, PLEKHS1 gene methylation density was inversely correlated with its mRNA expression and demethylation at the PLEKHS1 locus occurred at two CpGs. Higher PLEKHS1 expression was associated with lymph node and distant metastases, and shorter overall and disease-free survival in our cohort of PTC patients. Importantly, PLEKHS1 over-expression predicted shorter patient survival in PTCs lacking TERT promoter mutations. Cellular experiments showed that PLEKHS1 over-expression enhanced AKT phosphorylation and invasiveness. Collectively, the PLEKHS1 gene demethylation causes its over-expression in PTCs. PLEKHS1 promotes aggressive behavior of TCs possibly by increasing AKT activity, and its over-expression predicts poor patient outcomes.
APA, Harvard, Vancouver, ISO, and other styles
7

Marwaha, Rituraj, Subhash B. Arya, Divya Jagga, Harmeet Kaur, Amit Tuli, and Mahak Sharma. "The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to lysosomes." Journal of Cell Biology 216, no. 4 (March 21, 2017): 1051–70. http://dx.doi.org/10.1083/jcb.201607085.

Full text
Abstract:
Endocytic, autophagic, and phagocytic vesicles move on microtubule tracks to fuse with lysosomes. Small GTPases, such as Rab7 and Arl8b, recruit their downstream effectors to mediate this transport and fusion. However, the potential cross talk between these two GTPases is unclear. Here, we show that the Rab7 effector PLEKHM1 simultaneously binds Rab7 and Arl8b, bringing about clustering and fusion of late endosomes and lysosomes. We show that the N-terminal RUN domain of PLEKHM1 is necessary and sufficient for interaction with Arl8b and its subsequent localization to lysosomes. Notably, we also demonstrate that Arl8b mediates recruitment of HOPS complex to PLEKHM1-positive vesicle contact sites. Consequently, Arl8b binding to PLEKHM1 is required for its function in delivery and, therefore, degradation of endocytic and autophagic cargo in lysosomes. Finally, we also show that PLEKHM1 competes with SKIP for Arl8b binding, which dictates lysosome positioning. These findings suggest that Arl8b, along with its effectors, orchestrates lysosomal transport and fusion.
APA, Harvard, Vancouver, ISO, and other styles
8

Gill, Emily, Gurimaan Sandhu, Douglas G. Ward, Claire M. Perks, and Richard T. Bryan. "The Sirenic Links between Diabetes, Obesity, and Bladder Cancer." International Journal of Molecular Sciences 22, no. 20 (October 15, 2021): 11150. http://dx.doi.org/10.3390/ijms222011150.

Full text
Abstract:
There is considerable evidence of a positive association between the incidence of type 2 diabetes mellitus (T2DM) and obesity with bladder cancer (BCa), with the link between T2DM and obesity having already been established. There also appear to be potential associations between Pleckstrin homology domain containing S1 (PLEKHS1) and the Insulin-like Growth Factor (IGF) axis. Seven literature searches were carried out to investigate the backgrounds of these potential links. PLEKHS1 is a candidate biomarker in BCa, with mutations that are easily detectable in urine and increased expression seemingly associated with worse disease states. PLEKHS1 has also been implicated as a potential mediator for the onset of T2DM in people with obesity. The substantial evidence of the involvement of IGF in BCa, the role of the IGF axis in obesity and T2DM, and the global prevalence of T2DM and obesity suggest there is scope for investigating the links between these components. Preliminary findings on the relationship between PLEKHS1 and the IGF axis signal possible associations with BCa progression. This indicates that PLEKHS1 plays a role in the pathogenesis of BCa that may be mediated by members of the IGF axis. Further detailed research is needed to establish the relationship between PLEKHS1 and the IGF axis in BCa and determine how these phenomena overlap with T2DM and obesity.
APA, Harvard, Vancouver, ISO, and other styles
9

Tabata, Keisuke, Kohichi Matsunaga, Ayuko Sakane, Takuya Sasaki, Takeshi Noda, and Tamotsu Yoshimori. "Rubicon and PLEKHM1 Negatively Regulate the Endocytic/Autophagic Pathway via a Novel Rab7-binding Domain." Molecular Biology of the Cell 21, no. 23 (December 2010): 4162–72. http://dx.doi.org/10.1091/mbc.e10-06-0495.

Full text
Abstract:
The endocytic and autophagic pathways are involved in the membrane trafficking of exogenous and endogenous materials to lysosomes. However, the mechanisms that regulate these pathways are largely unknown. We previously reported that Rubicon, a Beclin 1–binding protein, negatively regulates both the autophagic and endocytic pathways by unidentified mechanisms. In this study, we performed database searches to identify potential Rubicon homologues that share the common C-terminal domain, termed the RH domain. One of them, PLEKHM1, the causative gene of osteopetrosis, also suppresses endocytic transport but not autophagosome maturation. Rubicon and PLEKHM1 specifically and directly interact with Rab7 via their RH domain, and this interaction is critical for their function. Furthermore, we show that Rubicon but not PLEKHM1 uniquely regulates membrane trafficking via simultaneously binding both Rab7 and PI3-kinase.
APA, Harvard, Vancouver, ISO, and other styles
10

Nishikawa, Masashi, Hidenori Ito, Hidenori Tabata, Hiroshi Ueda, and Koh-ichi Nagata. "Impaired Function of PLEKHG2, a Rho-Guanine Nucleotide-Exchange Factor, Disrupts Corticogenesis in Neurodevelopmental Phenotypes." Cells 11, no. 4 (February 16, 2022): 696. http://dx.doi.org/10.3390/cells11040696.

Full text
Abstract:
Homozygosity of the p.Arg204Trp variation in the Pleckstrin homology and RhoGEF domain containing G2 (PLEKHG2) gene, which encodes a Rho family-specific guanine nucleotide-exchange factor, is responsible for microcephaly with intellectual disability. However, the role of PLEKHG2 during neurodevelopment remains unknown. In this study, we analyzed mouse Plekhg2 function during cortical development, both in vitro and in vivo. The p.Arg200Trp variant in mouse (Plekhg2-RW), which corresponds to the p.Arg204Trp variant in humans, showed decreased guanine nucleotide-exchange activity for Rac1, Rac3, and Cdc42. Acute knockdown of Plekhg2 using in utero electroporation-mediated gene transfer did not affect the migration of excitatory neurons during corticogenesis. On the other hand, silencing Plekhg2 expression delayed dendritic arbor formation at postnatal day 7 (P7), perhaps because of impaired Rac/Cdc42 and p21-activated kinase 1 signaling pathways. This phenotype was rescued by expressing an RNAi-resistant version of wildtype Plekhg2, but not of Plekhg2-RW. Axon pathfinding was also impaired in vitro and in vivo in Plekhg2-deficient cortical neurons. At P14, knockdown of Plekhg2 was observed to cause defects in dendritic spine morphology formation. Collectively, these results strongly suggest that PLEKHG2 has essential roles in the maturation of axon, dendrites, and spines. Moreover, impairment of PLEKHG2 function is most likely to cause defects in neuronal functions that lead to neurodevelopmental disorders.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "PLEKHO1"

1

Dang, Lei. "Osteoblastic PLEKHO1 contributes to joint inflammation in rheumatoid arthritis." HKBU Institutional Repository, 2019. https://repository.hkbu.edu.hk/etd_oa/687.

Full text
Abstract:
Background: Osteoblasts participating in the inflammation regulation gradually obtain concerns. However, its role in joint inflammation of rheumatoid arthritis (RA) is largely unknown. Here, we investigated the role of osteoblastic pleckstrin homology domain-containing family O member 1 (PLEKHO1), a negative regulator of osteogenic lineage activity, in regulating joint inflammation in RA. Methods: The level of osteoblastic PLEKHO1 in RA patients and collagen-induced arthritis (CIA) mice was examined. The role of osteoblastic PLEKHO1 in joint inflammation was evaluated by a CIA mice model which was induced in osteoblast-specific Plekho1 conditional knockout mice and mice expressing high Plekho1 exclusively in osteoblasts, respectively. The effect of osteoblastic PLEKHO1 inhibition was explored in a CIA mice model. The mechanism of osteoblastic PLEKHO1 in regulating joint inflammation was performed by a series of in vitro studies. Results: PLEKHO1 was highly expressed in osteoblasts from RA patients and CIA mice. Osteoblastic Plekho1 deletion ameliorated joint inflammation, whereas overexpressing Plekho1 only within osteoblasts exacerbated local inflammation in CIA mice. PLEKHO1 was required for TNF receptor-associated factor 2 (TRAF2)-mediated the ubiquitination of receptor-interacting serine/threonine-protein kinase 1 (RIP1) to activate nuclear factor kappa-light-chain-enhancer of activated B (NF-kB) pathway for inducing inflammatory cytokines production in osteoblasts. Moreover, osteoblastic PLEKHO1 inhibition improved joint inflammation and attenuated bone formation reduction in CIA mice. Conclusions: These data strongly suggest that highly expressed PLEKHO1 in osteoblasts mediates joint inflammation in RA. Targeting osteoblastic PLEKHO1 may exert dual therapeutic action of alleviating joint inflammation and promoting bone repair in RA.
APA, Harvard, Vancouver, ISO, and other styles
2

Runne, Caitlin M. "Function and Activation Mechanism of PLEKHG2, A Novel G Beta Gamma-Activated RhoGEF in Leukemia Cells." Diss., University of Iowa, 2013. https://ir.uiowa.edu/etd/4907.

Full text
Abstract:
The Rho family of GTPases plays a crucial role in the regulation of diverse cellular processes, including proliferation and actin cytoskeletal rearrangement to promote cell migration. However, dysregulation of RhoGTPases has been associated with disease, particularly cancers such as leukemia. Despite this, RhoGTPases are rarely mutated in cancer. Rather, dysregulation of their regulatory proteins through mutation or overexpression contributes to disease pathogenesis. RhoGTPases are activated through Rho guanine nucleotide exchange factors (GEFs). Although over eighty RhoGEFs have been identified that activate the 25 RhoGTPases, the pathological role of the majority of these proteins remains unclear. Further, whereas the majority of RhoGEFs are activated through tyrosine phosphorylation, a small subset can be activated through heterotrimeric G proteins, including through GΒ;Γ; subunits. However, the mechanism by which GΒ;Γ; induces RhoGEF activation remains unclear. PLEKHG2 is a Dbl family RhoGEF that was originally identified as a gene upregulated in a leukemia mouse model, and later shown to be activated by heterotrimeric G protein Β;Γ; subunits. However, its function and activation mechanisms remain elusive. Here we show that, as compared to primary human T cells, the expression of PLEKHG2 is upregulated in leukemia cell lines. Downregulation of PLEKHG2 by siRNAs specifically inhibited GΒ;Γ;-stimulated Rac and Cdc42, but not RhoA activation. Consequently, inhibition of PLEKHG2 blocked actin polymerization, protrusion formation, and leukemia cell migration in response to SDF1alpha;. Additional studies indicate that GΒ;Γ; likely activates PLEKHG2 by binding the N-terminus of PLEKHG2. This interaction results in the release of autoinhibition imposed by the C-terminus within a region encompassing the catalytic DH domain. As a result, overexpressing either the N-terminus of PLEKHG2 that binds GΒ;Γ; or the C-terminus that autoinhibits PLEKHG2 blocked GΒ;Γ;-stimulated Rac and Cdc42 activation and the ability of leukemia cell to form membrane protrusions and to migrate. Together, our results have demonstrated that PLEKHG2 functions as a novel GΒ;Γ; -stimulated RhoGEF that could contribute to chemokine-induced leukemia cell dissemination and leukemia pathogenesis.
APA, Harvard, Vancouver, ISO, and other styles
3

Leveziel, Nicolas. "Génétique de la dégénérescence maculaire liée à l'âge variants majeurs de prédisposition à la forme exsudative." Paris 6, 2008. http://www.theses.fr/2008PA066183.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Sadras, Francisco. "A role for bivalent genes in epithelial to mesenchymal transition." Thesis, 2017. http://hdl.handle.net/2440/109800.

Full text
Abstract:
Epithelial to Mesenchymal Transition (EMT) is an important and complex cellular process in embryonic development, wound healing and tumour progression. EMT is often triggered or facilitated through the action of master EMT transcription factors including ZEB1 and TWIST. It has been proposed that prior to malignant progression a subset of tumour cells undergo an EMT which facilitates the development of key malignant properties. In recent years, a clear link between developmental and cancer associated EMT has triggered an increased interest in the role of developmental EMT genes in a cancer setting. Many key developmental genes have a bivalent or poised promoter signature which changes to active during differentiation; this is believed to elicit a faster response time in comparison to an exclusively repressed promoter. Owing to the relevance of EMT in development and pathologies my thesis aimed to answer the core question of whether bivalent genes are relevant in malignant EMT. To answer this question I undertook four aims: 1. To uncover novel bivalent genes that were activated in an EMT. 2. To characterise the expression and role of ADM2, PLEKHO1 and RASA3 in EMT. 3. To characterise ZEB1 isoform expression during EMT. 4. To identify novel ZEB1 target genes. Aim 1: We utilised a common model of human EMT, whereby human mammary epithelial cells (HMLE) undergo EMT in response to TGFβ to become mesenchymal (mesHMLE). We performed ChIP-seq against histone3 lysine4 tri-methylation (H3K4me3) and histone3 lysine27 tri-methylation (H3K27me3) alongside RNA-seq to identify genes that changed from a bivalent to an active epigenetic signature with concomitant changes to RNA levels. From this data set 429 genes that exhibited this epigenetic change including the well-known EMT factors ZEB1 and TWIST1. From this list four genes that were not previously associated with a bivalent signature were studied in detail. Three of these, ADM2, PLEKHO1 and RASA3, had not previously been associated with EMT but had EMT associated properties, while one, ZEB1 was a well-established master EMT transcription factor. Aim 2: Chromatin immunoprecipitation, ChIP-reChIP was used to confirm the change in epigenetic marks for ADM2, PLEKHO1 and RASA3 promoters alongside a combination of molecular and bioinformatics analyses to determine expression levels in epithelial and mesenchymal cell lines. Cellular migration assays where levels of these genes were manipulated showed that ADM2 and PLEKHO1 have both an individual and a synergistic effect on migration while RASA3 did not affect migration. Aim 3: ZEB1 isoform expression during EMT was analysed and it was determined that there was no significant change in relative expression over this process. Aim 4: ENCODE ZEB1 ChIP-seq was analysed to obtain insights into ZEB1 binding and to identify novel potential targets of importance to EMT. Established ZEB1 target genes such as CDH1 and CRB3 were identified and 26 novel genes with known or potential roles in EMT were chosen for further study. Of these, F11R and INADL were found to be ZEB1 responsive. Direct ZEB1 binding was confirmed through ChIP-qPCR. Interestingly, both of these genes are associated with tight-junctions as is the previously established ZEB1 target CRB3. This strongly implicates ZEB1 in mediating tight-junction regulation. While bivalent genes have not been ignored in the field of EMT they have, so far, been understudied. My work addressed this issue and identified ADM2 and PLEKHO1 as novel EMT associated genes that play an important role in migration. I also established ZEB1, a master regulator of EMT, as a bivalently regulated gene. These contributions help establish bivalently regulated genes as a valuable, underutilised resource for the identification of novel EMT genes.
Thesis (Ph.D.) -- University of Adelaide, School of Biological Sciences, 2017.
APA, Harvard, Vancouver, ISO, and other styles
5

Chen, Ke-Wei, and 陳克偉. "Roles of PLEKHF1 in endocytosis-related processes." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/93348812817055276224.

Full text
Abstract:
碩士
國立陽明大學
微生物及免疫學研究所
94
Based on a series of genomics analysis that targets differentially expressed genes in liver cancers, we have identified, from their distinctive endosomal localization patterns, two novel genes named PLEKHF1 (pleckstrin homology domain containing, family F (with FYVE domain) member 1, or PF1) and PLEKHF2 (PF2). Overexpression of either PF1 or PF2 resulted in the enlargement of the endosome. This study focuses on deciphering the signalling pathway underlying this intriguing phenotype of PF1. PF1 and PF2 represent two members of a new protein family called Phafins (protein containing both PH and FYVE domains), which consists of 14 genes from different species. GFP-tagged PF1 proteins were found in early endosomes and lysosomes, where they colocalized with EEA1 and LysoTracker Red, respectively, and this early endosomal localization is dependent on its FYVE domain. Increased expression of PF1 caused an enlargement of early endosome, as had been observed in cells expressing the constitutively active form of Rab5 gene. Endosomal enlargement caused by PF1 overespression was abolished by the simultaneous presence of the dominant negative Rab5, indicating that PF1 could regulate the endocytosis process in a Rab5-dependent manner. In addition, the presence of PF1 in the lysosome was reduced in cells containing the dominant negative Rab7. Transferrin uptake assay further showed that PF1 is involved in the early stages of endocytosis, but its overexpression had no effect on internalization rate. Furthermore, the C terminal sequence may comprise elements necessary for PF1 to enter lysosomal compartments. While confering PF2 the ability to enter lysosomes, the tail domain of PF1, when expressed alone, showed only minor colocalization with LysoTracker, suggesting tail domain may act in concert with upstream sequences to mediate lysosomal loclization. Taken together, our results suggested that PF1 represents a new player in Rab-mediated endocytosis precesses, as its effects on the formation of early endosomes was mediated by Rab5 signalling, whereas its continuous presence and metabolisms in the lysosome was modulated by the Rab7 signalling.We propose that PF1 may act as an adaptor functioning along the endocytic pathway through protein-lipid and possibly protein-protein interactions.
APA, Harvard, Vancouver, ISO, and other styles
6

Wang, Chi-Tang, and 王啓唐. "Investigating the role of pleckstrin homology domain containing, family A member 1 (PLEKHA1) in Age-related macular degeneration(AMD)." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/68389305876457615594.

Full text
Abstract:
碩士
國立陽明大學
生命科學系暨基因體科學研究所
103
Age-related macular degeneration (AMD) is a multifactorial disease for visual impairment in the senior population in developed countries. Clinical manifestations of AMD include the extracellular deposits of oxidized proteins and lipids within the retinal pigment epithelium (RPE). During the visual cycle, RPE supports the photoreceptor cells for the regeneration of visual pigments and breakdown of byproducts. Thus, dysfunction of RPE may result in metabolic burden to the photoreceptor cells. Although the exact cause of AMD is not clear, many studies have indicated that aging, oxidative stress, light damage and genetic factors may play significantly pathogenic roles. Both family and case-control studies revealed that genetic variants at 1q31 and 10q26 are the major genetic contributors. Further functional studies support that complement factor H (CFH) is the main player on chromosome 1q31, while the susceptibility gene on 10q26 remains to be elucidated. The aims of this study are (1) to reconstruct the risk haplotypes at 10q26 in exudative AMD, the prominent form of AMD in Asians strongly associated with the 10q26 variants, and (2) to investigate the role of candidate genes in this region during oxidative stress. Based on meta-analysis of GWAS data from studies of AMD, it was found that the risk locus extends more to the proximal region on 10q26 rather than to the distal region. In addition, due to no consensus on the functional roles for the other two candidates, ARMS2 and HTRA1, we therefore focused on PLEKHA1 as the candidate to investigate its possible role in AMD. So far, we have found that the two major isoforms of PLEKHA1 expressed differently in various tissues and the treatments of hydrogen peroxide, which mimics oxidative stress, induced translocations of PLEKHA1 isoform 1 to the plasma membrane but not isoform 2 in ARPE-19 cells. We further investigated the response of the two isoforms of PLEKHA1 under light exposure in the presence of N-retinyl-N-retinylidene ethanolamine (A2E), an autofluorescent pigment that accumulates in RPE cells in aging and some retinal disorders, which can induce generation of reactive oxygen species and cause serious toxicity to RPE cells. Similarly, A2E oxidative stress could induced translocations of PLEKHA1 isoform 1 to the plasma membrane in ARPE-19 cells. Induced phosphorylation of Akt (v-akt murine thymoma viral oncogen) in ARPE-19 cells under hydrogen peroxide or A2E oxidative stress was observed, but decreased level of phosphorylated Akt were observed in cells overexpressing PLEKHA1 isoform 1 rather than isoform 2. Both hydrogen peroxide and A2E oxidative stress induced cell death in ARPE-19 cells, but overexpressing PLEKHA1 isoform 1 slightly decrease resistance to oxidative stress whereas overexpression of PLEKHA1 isoform 2 slightly increase resistance to oxidative stress. To sum up, PLEKHA1 may play a role in cell survival under oxidative stress, thus it is a putative pathological cause for AMD.
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "PLEKHO1"

1

Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PLEKHO1 (Pleckstrin-Homology Domain Containing, Family O Member 1)." In Encyclopedia of Signaling Molecules, 1446. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101066.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Spallucci, Euro, Steven Duplij, Anatoly Nikitin, Alexander Galkin, Artur Sergyeyev, Steven Duplij, Omer Faruk Dayi, et al. "Plekton." In Concise Encyclopedia of Supersymmetry, 300. Dordrecht: Springer Netherlands, 2004. http://dx.doi.org/10.1007/1-4020-4522-0_398.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Plekhg5." In Encyclopedia of Signaling Molecules, 1446. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101065.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Horowitz, Arie. "SYX/PLEKHG5, A Rhoa Guanine Exchange Factor Involved in Cell Migration and Angiogenesis." In Encyclopedia of Signaling Molecules, 5295–98. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_567.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Dempsey, Brian R., Anne C. Rintala-Dempsey, Gary S. Shaw, Yuan Xiao Zhu, A. Keith Stewart, Jaime O. Claudio, Constance E. Runyan, et al. "SYX/PLEKHG5, A Rhoa Guanine Exchange Factor Involved in Cell Migration and Angiogenesis." In Encyclopedia of Signaling Molecules, 1827–30. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_567.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

"PLEKHO1." In Encyclopedia of Signaling Molecules, 4091. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_102971.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

"Plekhg5." In Encyclopedia of Signaling Molecules, 4091. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_102970.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "PLEKHO1"

1

Qian, J., and S. Nan. "307 The pathogenic mechanisms of systemic lupus erythematosus associated genes pnp, plekhf2 and ankrd44." In LUPUS 2017 & ACA 2017, (12th International Congress on SLE &, 7th Asian Congress on Autoimmunity). Lupus Foundation of America, 2017. http://dx.doi.org/10.1136/lupus-2017-000215.307.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Jeung, Hei-Cheul, Galina Kiriakova, Lynn Kirkpatrick, Martin Indarte, and Garth Powis. "Abstract A199: The plekstrin-homology-domain-containing protein PLEKHA7 is a novel target for selectively inhibiting mutant KRAS colon cancer cell proliferation." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-a199.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'PLEKHO1' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography