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Иш: Design of competitive inhibitory peptides for 3-hydroxy-3-Methylglutaryl coenzyme A reductase

  1. Isolation and Identification of Peptides from Soy 11S-Globulin with Hypocholesterolemic Activity

    Valeriy V. Pak, Minseon Koo, T. D. Kasymova +1

    МақолаProtein Hydrolysis and Bioactive PeptidesChemistry of Natural Compounds200514 иқтибос
    ABI

  2. Statin inhibition of HMG-CoA reductase: a 3-dimensional view

    Eva S. Istvan

    Шарҳ мақола200313 иқтибос
    ABI

  3. Structure—Activity Relationships of the Peptide Ile-Ala-Val-Pro and Its Derivatives Revealed Using the Semi-Empirical AM1 Method

    Valeriy V. Pak, Minseon Koo, N. Lee +2

    Мақола200512 иқтибос
    ABI

  4. Peptide design of a competitive inhibitor for HMG‐CoA reductase based on statin structure

    Valeriy V. Pak, Sung Hee Kim, Minseon Koo +3

    МақолаComputational Drug Discovery MethodsBiopolymers200610 иқтибос
    ABI

  5. Modeling an active conformation for linear peptides and design of a competitive inhibitor for HMG‐CoA reductase

    Valeriy V. Pak, Minseon Koo, Min Jung Kim +3

    МақолаRNA and protein synthesis mechanismsJournal of Molecular Recognition20088 иқтибос
    ABI

  6. Binding effect and design of a competitive inhibitory peptide for HMG-CoA reductase through modeling of an active peptide backbone

    Valeriy V. Pak, Minseon Koo, Min Jung Kim +2

    МақолаComputational Drug Discovery MethodsBioorganic & Medicinal Chemistry20076 иқтибос
    ABI

  7. Structures of the Peptide Leu-Pro-Tyr-Pro and Its Derivatives and the Nicotinamide Part of NADPH by a Semi-Empirical PM3 Method

    Valeriy V. Pak, Meng-Yu Ku, Na Li +3

    МақолаEnzyme Structure and FunctionChemistry of Natural Compounds20055 иқтибос
    ABI

  8. Peptide fragmentation as an approach in modeling of an active peptide and designing a competitive inhibitory peptide for HMG-CoA reductase

    Valeriy V. Pak, Minseon Koo, Dae Young Kwon +2

    МақолаComputational Drug Discovery MethodsBioorganic & Medicinal Chemistry20105 иқтибос
    ABI

  9. Crystal structure of the catalytic portion of human HMG‐CoA reductase: insights into regulation of activity and catalysis

    Eva S. Istvan, Maya Palnitkar, Susan K. Buchanan +1

    Мақола20005 иқтибос
    ABI

  10. Syntheses of some α-cyclic tripeptides as potential inhibitors for HMG-CoA Reductase

    Subrata Chakraborty, Shih‐Hung Lin, David Shiuan +1

    Мақола20155 иқтибос
    ABI

  11. Design of a highly potent inhibitory peptide acting as a competitive inhibitor of HMG-CoA reductase

    Valeriy V. Pak, Minseon Koo, Dae Young Kwon +1

    МақолаComputational Drug Discovery MethodsAmino Acids20124 иқтибос
    ABI

  12. Design of Tripeptides as a Competitive Inhibitor for HMG-CoA Reductase

    Valeriy V. Pak, Dae Yong Kwon, Olim K. Khojimatov +2

    МақолаComputational Drug Discovery MethodsInternational Journal of Peptide Research and Therapeutics20214 иқтибос
    ABI

  13. In vitro and in silico studies of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase inhibitory activity of the cowpea Gln-Asp-Phe peptide

    Mariana Silva, Caio Souza, Biane Oliveira Philadelpho +7

    Мақола20184 иқтибос
    ABI

  14. IAF, QGF, and QDF Peptides Exhibit Cholesterol-Lowering Activity through a Statin-like HMG-CoA Reductase Regulation Mechanism: In Silico and In Vitro Approach

    Mariana Silva, Biane Oliveira Philadelpho, Johnnie Elton Machado dos Santos +9

    Мақола20214 иқтибос
    ABI

  15. Risk of incident diabetes among patients treated with statins: population based study

    A. A. Carter, Tara Gomes, Ximena Camacho +3

    Мақола20133 иқтибос
    ABI

  16. Peptides from cowpea present antioxidant activity, inhibit cholesterol synthesis and its solubilisation into micelles

    Marcelo Rodrigues Marques, Rosana Aparecida Manólio Soares Freitas, Amanda Caroline Corrêa Carlos +3

    Мақола20143 иқтибос
    ABI

  17. IAVPGEVA, IAVPTGVA, and LPYP, three peptides from soy glycinin, modulate cholesterol metabolism in HepG2 cells through the activation of the LDLR-SREBP2 pathway

    Carmen Lammi, Chiara Zanoni, Anna Arnoldi

    Мақола20153 иқтибос
    ABI

  18. Statin use and risk of diabetes mellitus in postmenopausal women

    Niki Katsiki, Maciej Banach

    Мақола20123 иқтибос
    ABI

  19. Lupin protein exerts cholesterol-lowering effects targeting PCSK9: From clinical evidences to elucidation of the in vitro molecular mechanism using HepG2 cells

    Carmen Lammi, Chiara Zanoni, Laura Calabresi +1

    Мақола20163 иқтибос
    ABI

  20. Hypocholesterolemic effect of sericin-derived oligopeptides in high-cholesterol fed rats

    Phakhamon Lapphanichayakool, Manote Sutheerawattananonda, Nanteetip Limpeanchob

    Мақола20163 иқтибос
    ABI

  21. Structure–activity studies of protease activating, lipase inhibiting, bile acid binding and cholesterol-lowering effects of pre-screened cumin seed bioactive peptides

    Hwee-Leng Siow, Sy Bing Choi, Chee‐Yuen Gan

    Мақола20163 иқтибос
    ABI

  22. The Global Burden of Cardiovascular Diseases and Risk Factors

    George A. Mensah, Gregory A. Roth, Valentı́n Fuster

    Таҳририят мақоласи20193 иқтибос
    ABI

  23. Design of competitive inhibitory peptides for HMG-CoA reductase and modeling structural preference for short linear peptides

    Valeriy V. Pak, Olim K. Khojimatov, Aleksandr V. Pak +1

    МақолаComputational Drug Discovery MethodsJournal of Molecular Structure20223 иқтибос
    ABI

  24. Structure-function properties of hypolipidemic peptides

    Satoshi Nagaoka

    Шарҳ мақола20182 иқтибос
    ABI

  25. Behavior of three hypocholesterolemic peptides from soy protein in an intestinal model based on differentiated Caco-2 cell

    Gilda Aiello, Simonetta Ferruzza, Giulia Ranaldi +4

    Мақола20182 иқтибос
    ABI