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Relevant bibliographies by topics / Arl15

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Journal articles

Academic literature on the topic 'Arl15'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "Arl15"

1

Brito, Cheila, Bruno Costa-Silva, Duarte C. Barral, and Marta Pojo. "Unraveling the Relevance of ARL GTPases in Cutaneous Melanoma Prognosis through Integrated Bioinformatics Analysis." International Journal of Molecular Sciences 22, no. 17 (2021): 9260. http://dx.doi.org/10.3390/ijms22179260.

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Cutaneous melanoma (CM) is the deadliest skin cancer, whose molecular pathways underlying its malignancy remain unclear. Therefore, new information to guide evidence-based clinical decisions is required. Adenosine diphosphate (ADP)-ribosylation factor-like (ARL) proteins are membrane trafficking regulators whose biological relevance in CM is undetermined. Here, we investigated ARL expression and its impact on CM prognosis and immune microenvironment through integrated bioinformatics analysis. Our study found that all 22 ARLs are differentially expressed in CM. Specifically, ARL1 and ARL11 are

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2

Corre, Tanguy, Francisco J. Arjona, Caroline Hayward, et al. "Genome-Wide Meta-Analysis Unravels Interactions between Magnesium Homeostasis and Metabolic Phenotypes." Journal of the American Society of Nephrology 29, no. 1 (2017): 335–48. http://dx.doi.org/10.1681/asn.2017030267.

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Magnesium (Mg2+) homeostasis is critical for metabolism. However, the genetic determinants of the renal handling of Mg2+, which is crucial for Mg2+ homeostasis, and the potential influence on metabolic traits in the general population are unknown. We obtained plasma and urine parameters from 9099 individuals from seven cohorts, and conducted a genome-wide meta-analysis of Mg2+ homeostasis. We identified two loci associated with urinary magnesium (uMg), rs3824347 (P=4.4×10−13) near TRPM6, which encodes an epithelial Mg2+ channel, and rs35929 (P=2.1×10−11), a variant of ARL15, which encodes a GT

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3

Zolotarov, Yevgen, Chao Ma, Irene González-Recio, et al. "ARL15 modulates magnesium homeostasis through N-glycosylation of CNNMs." Cellular and Molecular Life Sciences 78, no. 13 (2021): 5427–45. http://dx.doi.org/10.1007/s00018-021-03832-8.

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AbstractCyclin M (CNNM1-4) proteins maintain cellular and body magnesium (Mg2+) homeostasis. Using various biochemical approaches, we have identified members of the CNNM family as direct interacting partners of ADP-ribosylation factor-like GTPase 15 (ARL15), a small GTP-binding protein. ARL15 interacts with CNNMs at their carboxyl-terminal conserved cystathionine-β-synthase (CBS) domains. In silico modeling of the interaction between CNNM2 and ARL15 supports that the small GTPase specifically binds the CBS1 and CNBH domains. Immunocytochemical experiments demonstrate that CNNM2 and ARL15 co-lo

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4

Li, Yiping, Ying Yang, Yueting Yao, et al. "Association Study of ARL15 and CDH13 with T2DM in a Han Chinese Population." International Journal of Medical Sciences 11, no. 5 (2014): 522–27. http://dx.doi.org/10.7150/ijms.8206.

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5

de Baaij, Jeroen H. F., Yevgen Zolotarov, Chao Ma, Gijs Franken, Michel L. Tremblay, and Joost Hoenderop. "ARL15 Regulates CNNM2‐dependent Mg 2+ Transport by Modulating its N‐linked Glycosylation." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.06380.

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6

Richards, J. Brent, Dawn Waterworth, Stephen O'Rahilly, et al. "A Genome-Wide Association Study Reveals Variants in ARL15 that Influence Adiponectin Levels." PLoS Genetics 5, no. 12 (2009): e1000768. http://dx.doi.org/10.1371/journal.pgen.1000768.

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7

Yang, Yong-Kang, Hong Qu, Dong Gao, et al. "ARF-like Protein 16 (ARL16) Inhibits RIG-I by Binding with Its C-terminal Domain in a GTP-dependent Manner." Journal of Biological Chemistry 286, no. 12 (2011): 10568–80. http://dx.doi.org/10.1074/jbc.m110.206896.

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Retinoic acid-inducible gene I (RIG-I) recognizes RNA virus-derived nucleic acids, which leads to the production of type I interferon (IFN) in most cell types. Tight regulation of RIG-I activity is important to prevent ultra-immune responses. In this study, we identified an ARF-like (ARL) family member, ARL16, as a protein that interacts with RIG-I. Overexpression of ARL16, but not its homologous proteins ARL1 and ARF1, inhibited RIG-I-mediated downstream signaling and antiviral activity. Knockdown of endogenous ARL16 by RNAi potentiated Sendai virus-induced IFN-β expression and vesicular stom

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8

Benabdelkamel, Hicham, Afshan Masood, Meshail Okla, Mohammed Y. Al-Naami, and Assim A. Alfadda. "A Proteomics-Based Approach Reveals Differential Regulation of Urine Proteins between Metabolically Healthy and Unhealthy Obese Patients." International Journal of Molecular Sciences 20, no. 19 (2019): 4905. http://dx.doi.org/10.3390/ijms20194905.

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Metabolic dysfunction associated with obesity threatens to inundate health care resources by increasing the incidences of obesity-related diseases. The aim of the present study was to investigate the changes in the urinary proteome of 18 individuals classified into metabolically healthy obese (MHO) and metabolically unhealthy obese (MUHO) patients. Proteome analysis was performed using the two-dimensional difference in gel electrophoresis (2D-DIGE) coupled with mass spectrometry (MS). Upon analysis, a total of 54 proteins were found to be affected with ≥1.5-fold change (ANOVA, p ≤ 0.05), of wh

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9

Shen, Jiayi, Miao Liu, Jing Xu, Bao Sun, Heng Xu, and Wei Zhang. "ARL15 overexpression attenuates high glucose-induced impairment of insulin signaling and oxidative stress in human umbilical vein endothelial cells." Life Sciences 220 (March 2019): 127–35. http://dx.doi.org/10.1016/j.lfs.2019.01.030.

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10

Wicky, Sidonie, Heinz Schwarz, and Birgit Singer-Krüger. "Molecular Interactions of Yeast Neo1p, an Essential Member of the Drs2 Family of Aminophospholipid Translocases, and Its Role in Membrane Trafficking within the Endomembrane System." Molecular and Cellular Biology 24, no. 17 (2004): 7402–18. http://dx.doi.org/10.1128/mcb.24.17.7402-7418.2004.

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ABSTRACT Neo1p is an essential yeast member of the highly conserved Drs2 family of P-type ATPases with proposed aminophospholipid translocase activity. Here we present evidence that Neo1p localizes to endosomes and Golgi elements. In agreement with that finding, the temperature-sensitive neo1-37 and neo1-69 mutants exhibit defects in receptor-mediated endocytosis, vacuole biogenesis, and vacuolar protein sorting. Furthermore, neo1 mutants accumulate aberrantly shaped membranous structures most likely derived from vacuoles and the endosomal/Golgi system. At permissive temperatures, HA-Neo1-69p,

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