Efficient Demyristoylase Activity of SIRT2 Revealed by Kinetic and Structural Studies

Teng, Yan-Bin, Jing, Hui, Aramsangtienchai, Pornpun, He, Bin, Khan, Saba, Hu, Jing, Lin, Hening, Hao, Quan·2015·Scientific Reports
DOI 10.1038/srep08529

Cited by (194)

Items 101–194 of 194

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  2. Simple Nε-thioacetyl-lysine-containing cyclic peptides exhibiting highly potent sirtuin inhibition
    Yajun Huang, Jiajia Liu, Lingling Yan, Weiping Zheng · 2016 · Bioorganic & Medicinal Chemistry Letters
  3. Sirtuiny i ich rola w regulacji metabolizmu
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  4. Human Sirtuin 2 inhibitors, Their Mechanisms and Binding Modes
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  5. Recent Advances in the Discovery of SIRT1/2 Inhibitors via Computational Methods: A Perspective
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  6. An NAD + -Dependent Sirtuin Depropionylase and Deacetylase (Sir2La) from the Probiotic Bacterium Lactobacillus acidophilus NCFM
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  7. SIRT2 Affects Primary Cilia Formation by Regulating mTOR Signaling in Retinal Pigmented Epithelial Cells
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  8. Multifaceted regulation of sirtuin 2 (Sirt2) deacetylase activity
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  9. Expanding the Accessible Chemical Space of SIRT2 Inhibitors through Exploration of Binding Pocket Dynamics
    Nemanja Djoković, D. Ružić, M. Rahnasto-Rilla, T. Srdić-Rajić, M. Lahtela-Kakkonen, Katarina M. Nikolic · 2022 · Journal of Chemical Information and Modeling
  10. Novel sirtuin inhibitory warheads derived from the N ε -acetyl-lysine analog l -2-amino-7-carboxamidoheptanoic acid
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  11. Structural basis for sirtuin 2 activity and modulation: Current state and opportunities
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  12. Multifunctional activity-based chemical probes for sirtuins
    Chiranjeev Sharma, Dickson Donu, Alyson M. Curry, Elizabeth E. Barton, Yana Cen · 2023 · RSC Advances
  13. Role of sirtuins in hepatocellular carcinoma progression and multidrug resistance: Mechanistical and pharmacological perspectives
    María Paula Ceballos, Ariel D. Quiroga, Nicolás Francisco Palma · 2023 · Biochemical Pharmacology
  14. Structure–Activity Studies of 1,2,4-Oxadiazoles for the Inhibition of the NAD+-Dependent Lysine Deacylase Sirtuin 2
    Arianna Colcerasa, Florian Friedrich, Jelena Melesina, Patrick Moser, Anja Vogelmann, Pavlos Tzortzoglou, Emilia Neuwirt, Manuela Sum, Dina Robaa, Lin Zhang et al. · 2024 · Journal of Medicinal Chemistry
  15. Regulation of autophagy by protein lipidation
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  16. Effects of Dimerization on the Deacylase Activities of Human SIRT2
    Jie Yang, Nathan I. Nicely, Brian P. Weiser · 2023 · Biochemistry
  17. Continuous Sirtuin/HDAC (histone deacetylase) activity assay using thioamides as PET (Photoinduced Electron Transfer)–based fluorescence quencher
    Matthes Zessin, Marat Meleshin, Zeljko Simic, Diana Kalbas, Miriam Arbach, Philip Gebhardt, Jelena Melesina, Sandra Liebscher, Frank Bordusa, Wolfgang Sippl et al. · 2021 · Bioorganic Chemistry
  18. Isobavachalcone, a natural sirtuin 2 inhibitor, exhibits anti‐t riple‐negative breast cancer efficacy in vitro and in vivo
    Yali Ren, Jieting Lei, Tingrui Zhang, Peng Lu, Dan‐dan Cui, Bo Yang, Guiying Zhao, Fu Peng, Zhixing Cao, Cheng Yun Peng et al. · 2024 · Phytotherapy Research
  19. Rational Design and Development of HDAC Inhibitors for Breast Cancer Treatment
    Deepansh Mody, Julie Maria Jozefa Bouckaert, Savvas N. Savvides, Vibha Gupta · 2021 · Current Pharmaceutical Design
  20. Substrate-Dependent Modulation of SIRT2 by a Fluorescent Probe, 1-Aminoanthracene
    David Bi, Jie Yang, Jun Young Hong, Prashit Parikh, Nicole M. Hinds, Joseph Infanti, Hening Lin, Brian P. Weiser · 2020 · Biochemistry
  21. Peptide‐Based Fluorescent Probes for Deacetylase and Decrotonylase Activity: Toward a General Platform for Real‐Time Detection of Lysine Deacylation
    Debra R. Rooker, Yuliya Klyubka, Ritika Gautam, Elisa Tomat, D. Buccella · 2017 · ChemBioChem
  22. The role of metabolism in cardiac development
    Haruko Nakano, Atsushi Nakano · 2024 · Current topics in developmental biology/Current Topics in Developmental Biology
  23. The enigmatic role of SIRT2 in the cardiovascular system: Deciphering its protective and detrimental actions to unlock new avenues for therapeutic intervention
    Abdulaziz Hassan Alhasaniah, Mohammed Alissa, Fahmy G. Elsaid, Mahdi H. Alsugoor, Mohammed Saad Alqahtani, Anwer Alessa, Khalid Jambi, Ghadah Shukri Albakri, Faisal Miqad K. Albaqami, Elizabeth Bennett · 2024 · Current Problems in Cardiology
  24. Activation of Sirtuin 2 Inhibitors Employing Photoswitchable Geometry and Aqueous Solubility
    Christoph W. Grathwol, Nathalie Wössner, Steven Behnisch‐Cornwell, Lukas Schulig, Lin Zhang, Oliver Einsle, Manfred Jung, Andreas Link · 2020 · ChemMedChem
  25. Efficient Crystallization of Apo Sirt2 for Small-Molecule Soaking and Structural Analysis of Ligand Interactions
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  26. QSAR studies on the human sirtuin 2 inhibition by non-covalent 7,5,2-anilinobenzamide derivatives
    Gláucio Monteiro Ferreira, Juliana Gallottini Magalhães, Vinícius Gonçalves Maltarollo, Thales Kronenberger, Arasu Ganesan, Flávio da Silva Emery, Gustavo Henrique Goulart Trossini · 2019 · Journal of Biomolecular Structure and Dynamics
  27. Unexpected small molecules as novel SIRT2 suicide inhibitors
    Xiaoxue Chen, Yefang Zou, Jie Wang, Zhuoxian Cao, Jingzi Liu, Yan Li, Yong‐Long Zhao, Bin He · 2020 · Bioorganic & Medicinal Chemistry
  28. Validation of the Slow Off‐Kinetics of Sirtuin‐Rearranging Ligands (SirReals) by Means of Label‐Free Electrically Switchable Nanolever Technology
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  29. Identification of Bichalcones as Sirtuin Inhibitors by Virtual Screening and in Vitro Testing
    Berin Karaman, Zayan Alhalabi, Sören Swyter, Shetonde O. Mihigo, Kerstin Andrae‐Marobela, Manfred Jung, Wolfgang Sippl, Fidele Ntie‐Kang · 2018 · Preprints.org
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  31. Role of sirtuins in cardiovascular diseases
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  32. Distribution and diversity of classical deacylases in bacteria
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  33. HPLC-Based Enzyme Assays for Sirtuins
    Jun Young Hong, Xiaoyu Zhang, Hening Lin · 2018 · Methods in molecular biology
  34. Small Changes Make the Difference for SIRT2: Two Different Binding Modes for 3-Arylmercapto-Acylated Lysine Derivatives
    Diana Kalbas, Marat Meleshin, Sandra Liebscher, Matthes Zessin, Jelena Melesina, Cordelia Schiene‐Fischer, Emre Fatih Bülbül, Frank Bordusa, Wolfgang Sippl, Mike Schutkowski · 2022 · Biochemistry
  35. Structure-Based Design and Computational Studies of Sirtuin Inhibitors
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  36. Far from Inert: Membrane Lipids Possess Intrinsic Reactivity That Has Consequences for Cell Biology
    John M. Sanderson · 2020 · BioEssays
  37. Molecular dynamics simulations reveal the mechanism of the interactions between the inhibitors and SIRT2 at atom level
    Xiaoyu Wang, Menghua Song, Shuang Zhao, Huiyu Li, Qingjie Zhao, Jingshan Shen · 2020 · Molecular Simulation
  38. Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions
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  39. The Enzymatic Activities of Sirtuins
    Hening Lin · 2018 · Elsevier eBooks
  40. The mimics of Nε-acyl-lysine derived from cysteine as sirtuin inhibitors
    Chun Wang, Fang Wang, Xiaoxue Chen, Yefang Zou, Hong Zhu, Qingjie Zhao, Jingshan Shen, Yan Li, Yongjun Li, Bin He · 2018 · Bioorganic & Medicinal Chemistry Letters
  41. Catching Sirtuin-2 Intermediates One Structure at the Time
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  42. The curious case of mitochondrial sirtuin in rewiring breast cancer metabolism: Mr Hyde or Dr Jekyll?
    Jesline Shaji Tharayil, Amoolya Kandettu, Sanjiban Chakrabarty · 2025 · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
  43. Structural basis of SIRT2 pre-catalysis NAD + binding dynamics and mechanism
    Nan Zhang, Kah Chee Pow, Lanfang Chen, Quan Hao · 2025 · RSC Chemical Biology
  44. Fluorogenic Assays for the Defatty-Acylase Activity of Sirtuins
    Jun Young Hong, Ji Cao, Hening Lin · 2019 · Methods in molecular biology
  45. Investigation of Carboxylic Acid Isosteres and Prodrugs for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme**
    Nima Rajabi, Tobias N. Hansen, Alexander L. Nielsen, Huy T. Nguyen, Michael Bæk, Julie E. Bolding, Oskar Ø. Bahlke, Sylvester E. G. Petersen, Christian R. O. Bartling, Kristian Strømgaard et al. · 2022 · Angewandte Chemie
  46. Targeting cancers and metabolic disorders: The prospects of combining HDAC8 inhibitor and activator
    Mohammed Mukhtar Yusif · 2022 · European Journal of Medicinal Chemistry Reports
  47. Global Profiling of Sirtuin Deacylase Substrates Using a Chemical Proteomic Strategy and Validation by Fluorescent Labeling
    Shuai Zhang, Nicole A. Spiegelman, Hening Lin · 2019 · Methods in molecular biology
  48. Drugs Targeting Sirtuin 2 Exhibit Broad-Spectrum Anti-Infective Activity
    Thomas E. Shenk, John L. Kulp, Lillian W. Chiang · 2024 · Pharmaceuticals
  49. SIRT2 mediates integrated stress response by deacetylating and stabilizing 4E-BP1 to suppress translation
    Yanlin Zi, Jiaqi Zhao, Miao Wang, Dan Hou, Richard A. Cerione, Hening Lin · 2026 · EMBO Reports
  50. From Pharmacophore to Warhead: NAD + ‐Targeting Triazoles as Mechanism‐Based Sirtuin Inhibitors
    Florian Friedrich, Marat Meleshin, Niklas Papenkordt, Lena Gaitzsch, Isabel Prucker, Marco Borsò, Jan Ruprecht, Christopher Vorreiter, Sabrina Rast, Lin Zhang et al. · 2025 · Angewandte Chemie International Edition
  51. SIRT Family: Biological Functions and Therapeutic Targets
    Jia‐Yi Wang, Feng‐Li Jiang, FANG-YUAN ZHANG, Dong‐Hui Huang, X G Li, Song Gao, Hua You, Qijun Wu, Huanhuan Chen, T Q Gong · 2026 · MedComm
  52. The (patho)physiological roles of the individual deacylase activities of a sirtuin
    Weiping Zheng · 2024 · Chemical Biology & Drug Design
  53. Pyruvate kinase is post-translationally regulated by sirtuin 2 in Aedes aegypti mosquitoes
    Natthida Petchampai, Jun Isoe, Prashanth Balaraman, Max E. Oscherwitz, Brendan H. Carter, Cecilia G. Sánchez, Patricia Y. Scaraffia · 2023 · Insect Biochemistry and Molecular Biology
  54. A homogeneous time-resolved fluorescence screen to identify SIRT2 deacetylase and defatty-acylase inhibitors
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  55. Beyond deacetylation: crosstalk mechanisms and context-dependent regulation of sirtuin non-classical enzymatic functions in disease
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  56. N-myristoyltransferase-mediated protein myristoylation: molecular mechanisms, pathological roles, and targeted therapeutic strategies
    Wenqing Liu, Zhe Chen, Zhen Huang, Linxi Chen · 2026 · Journal of Advanced Research
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    Xiaoqiu Yuan, Howard C. Hang · 2016 · Springer protocols handbooks/Springer protocols
  58. Structural and Mechanistic Insights in Sirtuin Catalysis and Pharmacological Modulation
    S. Moniot, Weikang You, Clemens Steegborn · 2018 · Elsevier eBooks
  59. Relative Transcription Expression Level of SIRT1, SIRT2 and SIRT3 in Correlation to the Expression of a Set of Selected Cancer Related Genes in Human Breast Cancer
    Hamdy Hamed Swelim, O Mansour, Salah M. Abdel-Rahman, Mohamed H. Shwaireb, Amani Hussein Kazem · 2018 · OnLine Journal of Biological Sciences
  60. Identification of Sirt3 as an ‘Eraser’ for Histone Lysine Crotonylation Marks Using a Chemical Proteomics Approach
    Xiucong Bao · 2020 · Springer theses
  61. Development of a NanoBRET assay to validate dual inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration
    Anja Vogelmann, Matthias Schiedel, Nathalie Wössner, Annika Merz, Daniel Herp, Sören Hammelmann, Arianna Colcerasa, Garrison Komaniecki, Jun Young Hong, Manuela Sum et al. · 2021 · ChemRxiv
  62. Structure-activity studies of 1,2,4-oxadiazoles for the inhibition of the NAD+ dependent lysine deacylase Sirtuin2
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  63. Cyclic Peptide-Based Sirtuin Substrates
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  64. Structure-Based Design of Epigenetic Inhibitors
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  66. Introduction to Protein Posttranslational Modifications (PTMs)
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  67. Sirtuins in immunometabolism
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  68. Kinetic Characterization of Human Histone Deacetylase 8 With Medium-Chain Fatty Acyl Lysine
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  72. Structure-activity studies of 1,2,4-oxadiazoles for the inhibition of the NAD+ dependent lysine deacylase Sirtuin2
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  73. Estudo estrutural e comparativo entre Sirtuínas 2 de diferentes espécies de >i<Leishmania>/i> por meio de Modelagem Comparativa e Dinâmica Molecular
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  75. From Pharmacophore to Warhead: NAD + ‐Targeting Triazoles as Mechanism‐Based Sirtuin Inhibitors
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  77. Mapping the structural requirements for SIRT2 inhibition: Insights from a diverse in-house library and 3D-QSAR analysis
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  78. Alkyl-Branched Acyl-Lysine Peptides as Potent Cell-Permeable Slow-Substrate Inhibitors of SIRT2
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  84. BindingDB Entry 50020954: Structure-Activity Studies of 1,2,4-Oxadiazoles for the Inhibition of the NAD+-Dependent Lysine Deacylase Sirtuin 2.
    BindingDB · 2025 · UC San Diego
  85. BindingDB Entry 50001308: The mimics of N
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  86. BindingDB Entry 50011830: Sensitive fluorogenic substrates for sirtuin deacylase inhibitor discovery.
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  87. BindingDB Entry 50004507: Development of Peptide-Based Sirtuin Defatty-Acylase Inhibitors Identified by the Fluorescence Probe, SFP3, That Can Efficiently Measure Defatty-Acylase Activity of Sirtuin.
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  88. BindingDB Entry 50007852: Identification of Diketopiperazine-Containing 2-Anilinobenzamides as Potent Sirtuin 2 (SIRT2)-Selective Inhibitors Targeting the "Selectivity Pocket", Substrate-Binding Site, and NAD
    BindingDB · 2021 · UC San Diego
  89. BindingDB Entry 50010120: Novel Lysine-Based Thioureas as Mechanism-Based Inhibitors of Sirtuin 2 (SIRT2) with Anticancer Activity in a Colorectal Cancer Murine Model.
    BindingDB · 2021 · UC San Diego
  90. BindingDB Entry 50010551: An overview of Sirtuins as potential therapeutic target: Structure, function and modulators.
    BindingDB · 2021 · UC San Diego
  91. BindingDB Entry 50012973: Simultaneous Inhibition of SIRT2 Deacetylase and Defatty-Acylase Activities via a PROTAC Strategy.
    BindingDB · 2022 · UC San Diego
  92. BindingDB Entry 50010714: Unexpected small molecules as novel SIRT2 suicide inhibitors.
    BindingDB · 2021 · UC San Diego
  93. BindingDB Entry 50047170: Simple N(e)-thioacetyl-lysine-containing cyclic peptides exhibiting highly potent sirtuin inhibition.
    BindingDB · 2017 · UC San Diego
  94. BindingDB Entry 50006641: Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.
    BindingDB · 2020 · UC San Diego