For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
6
views
119
references
 Top references
cited by
3
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
1 collections
    0
    shares
      179
      similar
       All similar

      Drug Design, Development and Therapy (submit here)

      This international, peer-reviewed Open Access journal by Dove Medical Press focuses on the design and development of drugs, as well as the clinical outcomes, patient safety, and programs targeted at the effective and safe use of medicines. Sign up for email alerts here.

      88,007 Monthly downloads/views I 4.319 Impact Factor I 6.6 CiteScore I 1.12 Source Normalized Impact per Paper (SNIP) I 0.784 Scimago Journal & Country Rank (SJR)

       

      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Forkhead Box Protein O1: Functional Diversity and Post-Translational Modification, a New Therapeutic Target?

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Forkhead box protein O1 (FoXO1) is a transcription factor involved in the regulation of a wide variety of physiological process including glucose metabolism, lipogenesis, bone mass, apoptosis, and autophagy. FoXO1 dysfunction is involved in the pathophysiology of various diseases including metabolic diseases, atherosclerosis, and tumors. FoXO1 activity is regulated in response to different physiological or pathogenic conditions by changes in protein expression and post-translational modifications. Various modifications cooperate to regulate FoXO1 activity and FoXO1 target gene transcription. In this review, we summarize how different post-translational modifications regulate FoXO1 physiological function, which may provide new insights for drug design and development.

          Most cited references119

          • Record: found
          • Abstract: found
          • Article: not found

          Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor.

          Anne Brunet, Azad Bonni, Michael Zigmond … (1999)
          Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/ threonine kinase Akt, which then phosphorylates and inactivates components of the apoptotic machinery, including BAD and Caspase 9. In this study, we demonstrate that Akt also regulates the activity of FKHRL1, a member of the Forkhead family of transcription factors. In the presence of survival factors, Akt phosphorylates FKHRL1, leading to FKHRL1's association with 14-3-3 proteins and FKHRL1's retention in the cytoplasm. Survival factor withdrawal leads to FKHRL1 dephosphorylation, nuclear translocation, and target gene activation. Within the nucleus, FKHRL1 triggers apoptosis most likely by inducing the expression of genes that are critical for cell death, such as the Fas ligand gene.
          Article 0 comments Cited 357 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Mammalian SIRT1 represses forkhead transcription factors.

            Maria Carla Motta, Nullin Divecha, Madeleine Lemieux … (2004)
            The NAD-dependent deacetylase SIR2 and the forkhead transcription factor DAF-16 regulate lifespan in model organisms, such as yeast and C. elegans. Here we show that the mammalian SIR2 ortholog SIRT1 deacetylates and represses the activity of the forkhead transcription factor Foxo3a and other mammalian forkhead factors. This regulation appears to be in the opposite direction from the genetic interaction of SIR2 with forkhead in C. elegans. By restraining mammalian forkhead proteins, SIRT1 also reduces forkhead-dependent apoptosis. The inhibition of forkhead activity by SIRT1 parallels the effect of this deacetylase on the tumor suppressor p53. We speculate how down-regulating these two classes of damage-responsive mammalian factors may favor long lifespan under certain environmental conditions, such as calorie restriction.
            Article 0 comments Cited 273 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Protein O-GlcNAcylation: emerging mechanisms and functions

              Xiaoyong Yang, Kevin Qian (2017)
              Many cellular proteins are reversibly modified by O-linked N-acetylglucosamine (O-GlcNAc) moieties on Ser and Thr residues. Studies on the mechanisms and functions of O-GlcNAcylation and its links to metabolism reveal the importance of this modification in the maintenance of cellular and organismal homeostasis.
              Article 0 comments Cited 249 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Drug Des Devel Ther
                Journal ID (iso-abbrev): Drug Des Devel Ther
                Journal ID (publisher-id): dddt
                Journal ID (pmc): dddt
                Title: Drug Design, Development and Therapy
                Publisher: Dove
                ISSN (Electronic): 1177-8881
                Publication date (Electronic): 03 May 2021
                Publication date Collection: 2021
                Volume: 15
                Pages: 1851-1860
                Affiliations
                [1 ]Department of Cardiology, Shandong Rongjun General Hospital , Jinan, 250013, People’s Republic of China
                [2 ]Department of Emergency, Shandong Rongjun General Hospital , Jinan, 250013, People’s Republic of China
                [3 ]Blood Purification Center, Affiliated Hospital of Shandong University of Traditional Chinese Medicine , Jinan, 250011, People’s Republic of China
                Author notes
                Correspondence: Huimin Liu Blood Purification Center, Affiliated Hospital of Shandong University of Traditional Chinese Medicine , No. 42, Wenhua West Road, Lixia District, Jinan, 250011, Shandong Province, People’s Republic of ChinaTel +86 531 6861 7808 Email hans4@126.com
                Article
                Publisher ID: 305016
                DOI: 10.2147/DDDT.S305016
                PMC ID: 8106445
                SO-VID: 3e78018f-dce5-4368-b157-7e09741a33f9
                Copyright statement: © 2021 Zhang et al.
                License:

                This work is published and licensed by Dove Medical Press Limited. The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License ( http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms ( https://www.dovepress.com/terms.php).

                History
                Date received : 02 February 2021
                Date accepted : 19 April 2021
                Page count
                Figures: 2, Tables: 2, References: 119, Pages: 10
                Categories
                Subject: Review

                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: forkhead box protein o1,post-translational modification,transcription
                Data availability:
                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: forkhead box protein o1, post-translational modification, transcription

                Comments

                Comment on this article

                scite_

                Similar content179

                See all similar

                Cited by3

                See all cited by

                Most referenced authors2,803

                See all reference authors