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Denis Albertovich Proshlyakov

TitleProf
InstitutionUniversity of Oklahoma Health Sciences Center
DepartmentBiochemistry & Physiology
AddressBMSB TBD
940 Stanton L Young Blvd
Oklahoma City OK 73104
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    Collapse Research 
    Collapse research activities and funding
    R01EY034133     (PROSHLYAKOV, DENIS A)Jul 1, 2023 - May 1, 2028
    NIH
    Correction of diabetic retinopathy by mitochondrial transfer
    Role: Principal Investigator
    R01EY028049     (PROSHLYAKOV, DENIS A)Apr 1, 2018 - Mar 31, 2022
    NIH
    Ceramide-mediated mitochondrial damage in diabetic retinopathy investigated by novel microfluidic O2 sensing and bio-mimetic electrochemistry
    Role: Principal Investigator
    R01GM096132     (PROSHLYAKOV, DENIS A)Dec 15, 2010 - Nov 30, 2015
    NIH
    Transient catalytic oxygen species in iron enzymes
    Role: Principal Investigator
    R01GM070544     (PROSHLYAKOV, DENIS A)Jun 1, 2004 - May 31, 2010
    NIH
    Protein radicals in O2 reduction by Cytochrome Oxidase
    Role: Principal Investigator

    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. Proshlyakov DA, Farrugia MA, Proshlyakov YD, Hausinger RP. Iron-Containing Ureases. Coord Chem Rev. 2021 Dec 01; 448. PMID: 35250039; PMCID: PMC8896516.
      Citations:    
    2. Hammer SS, Vieira CP, McFarland D, Sandler M, Levitsky Y, Dorweiler TF, Lydic TA, Asare-Bediako B, Adu-Agyeiwaah Y, Sielski MS, Dupont M, Longhini AL, Li Calzi S, Chakraborty D, Seigel GM, Proshlyakov DA, Grant MB, Busik JV. Fasting and fasting-mimicking treatment activate SIRT1/LXRa and alleviate diabetes-induced systemic and microvascular dysfunction. Diabetologia. 2021 07; 64(7):1674-1689. PMID: 33770194; PMCID: PMC8236268.
      Citations: 28     Fields:    Translation:AnimalsCells
    3. Frantz NL, Brakoniecki G, Chen D, Proshlyakov DA. Assessment of the Maximal Activity of Complex IV in the Inner Mitochondrial Membrane by Tandem Electrochemistry and Respirometry. Anal Chem. 2021 01 26; 93(3):1360-1368. PMID: 33319559; PMCID: PMC8772154.
      Citations: 1     Fields:    Translation:AnimalsCells
    4. Levitsky Y, Hammer SS, Fisher KP, Huang C, Gentles TL, Pegouske DJ, Xi C, Lydic TA, Busik JV, Proshlyakov DA. Mitochondrial Ceramide Effects on the Retinal Pigment Epithelium in Diabetes. Int J Mol Sci. 2020 May 28; 21(11). PMID: 32481596; PMCID: PMC7312467.
      Citations: 10     Fields:    Translation:AnimalsCells
    5. Levitsky Y, Pegouske DJ, Hammer SS, Frantz NL, Fisher KP, Muchnik AB, Saripalli AR, Kirschner P, Bazil JN, Busik JV, Proshlyakov DA. Micro-respirometry of whole cells and isolated mitochondria. RSC Adv. 2019; 9(57):33257-33267. PMID: 32123561; PMCID: PMC7051014.
      Citations: 5     
    6. John CW, Hausinger RP, Proshlyakov DA. Structural Origin of the Large Redox-Linked Reorganization in the 2-Oxoglutarate Dependent Oxygenase, TauD. J Am Chem Soc. 2019 09 25; 141(38):15318-15326. PMID: 31475523; PMCID: PMC7092798.
      Citations: 2     Fields:    Translation:Cells
    7. John CW, Swain GM, Hausinger RP, Proshlyakov DA. Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD. J Phys Chem B. 2019 09 19; 123(37):7785-7793. PMID: 31433947; PMCID: PMC7092797.
      Citations: 5     Fields:    Translation:Cells
    8. Stettler AM, John CW, Proshlyakov YD, Proshlyakov DA. G3F: Global, Multidimensional Spectral Regression Analysis. J Open Source Softw. 2019; 4(40). PMID: 32211578; PMCID: PMC7093062.
      Citations: 3     
    9. John CW, Proshlyakov DA. KinESim: Pre-equilibrium kinetic simulation of electrochemical reactions. J Open Source Softw. 2019; 4(40). PMID: 32123783; PMCID: PMC7051063.
      Citations: 1     
    10. John CW, Proshlyakov DA. Fourier Transform Infrared Spectrovoltammetry and Quantitative Modeling of Analytes in Kinetically Constrained Redox Mixtures. Anal Chem. 2019 08 06; 91(15):9563-9570. PMID: 31257856; PMCID: PMC7050292.
      Citations: 4     Fields:    Translation:Cells
    11. Proshlyakov DA, McCracken J, Hausinger RP. Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study. J Biol Inorg Chem. 2017 04; 22(2-3):367-379. PMID: 27812832; PMCID: PMC5352539.
      Citations: 15     Fields:    
    12. Dai Y, Proshlyakov DA, Swain GM. Effects of Film Morphology and Surface Chemistry on the Direct Electrochemistry of Cytochrome c at Boron-Doped Diamond Electrodes. Electrochim Acta. 2016 Apr 10; 197:129-138. PMID: 27103750; PMCID: PMC4834903.
      Citations:    
    13. Banerjee R, Proshlyakov Y, Lipscomb JD, Proshlyakov DA. Structure of the key species in the enzymatic oxidation of methane to methanol. Nature. 2015 Feb 19; 518(7539):431-4. PMID: 25607364; PMCID: PMC4429310.
      Citations: 74     Fields:    Translation:CellsPHPublic Health
    14. Carter EL, Proshlyakov DA, Hausinger RP. Apoprotein isolation and activation, and vibrational structure of the Helicobacter mustelae iron urease. J Inorg Biochem. 2012 Jun; 111:195-202. PMID: 22196017; PMCID: PMC3314087.
      Citations: 3     Fields:    Translation:Cells
    15. Dai Y, Zheng Y, Swain GM, Proshlyakov DA. Equilibrium and kinetic behavior of Fe(CN)6(3-/4-) and cytochrome c in direct electrochemistry using a film electrode thin-layer transmission cell. Anal Chem. 2011 Jan 15; 83(2):542-8. PMID: 21166441; PMCID: PMC3076141.
      Citations: 3     Fields:    Translation:Cells
    16. Grzyska PK, Appelman EH, Hausinger RP, Proshlyakov DA. Insight into the mechanism of an iron dioxygenase by resolution of steps following the FeIV=HO species. Proc Natl Acad Sci U S A. 2010 Mar 02; 107(9):3982-7. PMID: 20147623; PMCID: PMC2840172.
      Citations: 44     Fields:    Translation:Cells
    17. Grzyska PK, Hausinger RP, Proshlyakov DA. Metal and substrate binding to an Fe(II) dioxygenase resolved by UV spectroscopy with global regression analysis. Anal Biochem. 2010 Apr 01; 399(1):64-71. PMID: 19932076; PMCID: PMC2823959.
      Citations: 9     Fields:    Translation:Cells
    18. Qin L, Liu J, Mills DA, Proshlyakov DA, Hiser C, Ferguson-Miller S. Redox-dependent conformational changes in cytochrome C oxidase suggest a gating mechanism for proton uptake. Biochemistry. 2009 Jun 16; 48(23):5121-30. PMID: 19397279; PMCID: PMC2720787.
      Citations: 58     Fields:    Translation:Cells
    19. Dai Y, Proshlyakov DA, Zak JK, Swain GM. Optically transparent diamond electrode for use in ir transmission spectroelectrochemical measurements. Anal Chem. 2007 Oct 01; 79(19):7526-33. PMID: 17784734.
      Citations: 1     Fields:    Translation:Cells
    20. Proshlyakov DA. UV optical absorption by protein radicals in cytochrome c oxidase. Biochim Biophys Acta. 2004 Apr 12; 1655(1-3):282-9. PMID: 15100043.
      Citations: 8     Fields:    Translation:Animals
    21. Proshlyakov DA, Henshaw TF, Monterosso GR, Ryle MJ, Hausinger RP. Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase. J Am Chem Soc. 2004 Feb 04; 126(4):1022-3. PMID: 14746461.
      Citations: 73     Fields:    
    22. Egawa T, Proshlyakov DA, Miki H, Makino R, Ogura T, Kitagawa T, Ishimura Y. Effects of a thiolate axial ligand on the pi-->pi* electronic states of oxoferryl porphyrins: a study of the optical and resonance Raman spectra of compounds I and II of chloroperoxidase. J Biol Inorg Chem. 2001 Jan; 6(1):46-54. PMID: 11191222.
      Citations: 19     Fields:    
    23. Proshlyakov DA, Pressler MA, DeMaso C, Leykam JF, DeWitt DL, Babcock GT. Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244. Science. 2000 Nov 24; 290(5496):1588-91. PMID: 11090359.
      Citations: 71     Fields:    Translation:AnimalsCells
    24. Proshlyakov DA, Pressler MA, Babcock GT. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc Natl Acad Sci U S A. 1998 Jul 07; 95(14):8020-5. PMID: 9653133; PMCID: PMC20922.
      Citations: 72     Fields:    Translation:Animals
    25. Hoganson CW, Pressler MA, Proshlyakov DA, Babcock GT. From water to oxygen and back again: mechanistic similarities in the enzymatic redox conversions between water and dioxygen. Biochim Biophys Acta. 1998 Jun 10; 1365(1-2):170-4. PMID: 9693735.
      Citations: 7     Fields:    Translation:Cells
    26. Proshlyakov DA, Ogura T, Shinzawa-Itoh K, Yoshikawa S, Kitagawa T. Resonance Raman/absorption characterization of the oxo intermediates of cytochrome c oxidase generated in its reaction with hydrogen peroxide: pH and H2O2 concentration dependence. Biochemistry. 1996 Jul 02; 35(26):8580-6. PMID: 8679619.
      Citations: 17     Fields:    Translation:Animals
    27. Proshlyakov DA, Ogura T, Shinzawa-Itoh K, Yoshikawa S, Kitagawa T. Microcirculating system for simultaneous determination of Raman and absorption spectra of enzymatic reaction intermediates and its application to the reaction of cytochrome c oxidase with hydrogen peroxide. Biochemistry. 1996 Jan 09; 35(1):76-82. PMID: 8555201.
      Citations: 15     Fields:    Translation:AnimalsCells
    28. Proshlyakov DA, Ogura T, Shinzawa-Itoh K, Yoshikawa S, Appelman EH, Kitagawa T. Selective resonance Raman observation of the "607 nm" form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide. J Biol Chem. 1994 Nov 25; 269(47):29385-8. PMID: 7961916.
      Citations: 31     Fields:    Translation:AnimalsCells
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