• Tarasov A.S., et al. (Gd3+) Complexation with oligopeptide (SFVG) and amyloid peptide (Aβ13–23) in aqueous solution by NMR spectroscopy / A.S. Tarasov, I.Z. Rakhmatullin, D.S. Blokhin, A.V. Klochkov, K.A. Il'yasov, V.V. Klochkov // Results in Chemistry. - 2023. - Vol. 5. - № 100762. Pp. - 7. https://doi.org/10.1016/j.rechem.2023.100762.
  F_Revised_manuscript.pdf

• Sanchugova D.A. Spatial structure of the fibril-forming SEM1(86–107) peptide in a complex with dodecylphosphocholine micelles / Sanchugova D.A., Bikmullin A.G., Klochkov V.V., Aganov A.V., Blokhin D.S. // Russian Chemical Bulletin. – 2022. – V. 70 (12). – Р. 2422 – 2426.
• Kusova A, Abramova M, Skvortsova P, Structure of amyloidogenic PAP(85-120) peptide by high-resolution NMR spectroscopy//Journal of Molecular Structure. - 2022. - Vol.1253, Is.. - Art. №132294.

• Sanchugova D, Kusova A, Bikmullin A, The Structure of Fibril-Forming SEM1(86-107) Peptide Increasing the HIV Infectivity//BioNanoScience. - 2021. - Vol., Is.. - .
• Ishkaeva, R.A. Dithiophosphate-induced redox conversions of reduced and oxidized glutathione / R.A. Ishkaeva, I.S. Nizamov, D.S. Blokhin, E.A. Urakova, V.V. Klochkov, I.D. Nizamov, B.I. Gareev, D.V. Salakhieva, T.I. Abdullin // Molecules. 2021. V. 26. P. 2973. https://doi.org/10.3390/molecules26102973
• Sanchugova D.A, Bikmullin A.G, Klochkov V.V, Spatial structure of the fibril-forming SEM1(86?107) peptide in a complex with dodecylphosphocholine micelles//Russian Chemical Bulletin. - 2021. - Vol.70, Is.12. - P.2422-2426.
• Ishkaeva, R.A. Dithiophosphate-induced redox conversions of reduced and oxidized glutathione / R.A. Ishkaeva, I.S. Nizamov, D.S. Blokhin, E.A. Urakova, V.V. Klochkov, I.D. Nizamov, B.I. Gareev, D.V. Salakhieva, T.I. Abdullin // Molecules. 2021. V. 26. N 10. P. 2973. https://doi.org/10.3390/molecules26102973
• Sautina N.V, Rybakova A.I, Blokhin D.S, Effect of Intermolecular Interactions in a Water/AOT/Isopropyl Myristate System on the Release of Biologically Active Substances//Russian Journal of Physical Chemistry A. - 2021. - Vol.95, Is.11. - P.2325-2331.
• Ishkaeva, R.A. Dithiophosphate-induced redox conversions of reduced and oxidized glutathione / R.A. Ishkaeva, I.S. Nizamov, D.S. Blokhin, E.A. Urakova, V.V. Klochkov, I.D. Nizamov, B.I. Gareev, D.V. Salakhieva, T.I. Abdullin // Molecules. 2021. Vol.26, Is.10. P. 2973. https://doi.org/10.3390/molecules26102973

• Faizullina Adeliia R., Blokhin Dmitriy S., Kusova Aleksandra M., Investigation of the effect of transition metals (MN, CO, GD) on the spatial structure of fibrinopeptide B by NMR spectroscopy//JOURNAL OF MOLECULAR STRUCTURE. - 2020. - Vol.1204, Is.. - Art. №127484.
• Maksimov E.G, Laptev G.Y, Blokhin D.S, NMR resonance assignment and backbone dynamics of a C-terminal domain homolog of orange carotenoid protein//Biomolecular NMR Assignments. - 2020. - Vol., Is.. - .
• Bikmullin A.G, Nurullina L.I, Garaeva N.S, In vitro Reconstitution of the S. aureus 30S Ribosomal Subunit and RbfA Factor Complex for Structural Studies//Biochemistry (Moscow). - 2020. - Vol.85, Is.5. - P.545-552.

• Гумерова Д.Р. Электрохимические свойства солей глутатиона с дитиофосфорными кислотами/ Д.Р. Гумерова, Р.А. Ишкаева, Д.В. Салахиева, Е.А. Уракова, Д.С. Блохин, И.С. Низамов, Г.Р. Ахмедова, Т.И. Абдуллин // VI Международная конференция молодых ученых: биофизиков, биотехнологов, молекулярных биологов и вирусологов. Сборник тезисов. - Н., 2019. - С. 271-273.
  F_GS__DTP_materials_of_conference.pdf
• Blokhin, D.S. Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus / D.S. Blokhin, A.G. Bikmullin, L.I. Nurullina, N.S. Garaeva, S.Z. Validov, V.V. Klochkov, A.V. Aganov, I.S. Khusainov, M.M. Yusupov, K.S. Usachev // BIOMOLECULAR NMR ASSIGNMENTS. - 2019. - V. 13. - P. 27-30.

• Abdrakhmanov R, Blokhin D, Usachev K, Modeling the Co2+Binding to Amyloid Peptide A?13?23 in Water Environment by NMR Spectroscopy//BioNanoScience. - 2018. - Vol.8, Is.1. - P.423-427.
• Bikmullin A. NMR analysis of Staphylococcus aureus Ribosome Binding Factor A (RbfA) / A. Bikmullin, D. Blokhin, B. Fatkhullin, L. Nurullina, N. Garaeva, I. Khusainov, N. Trachtmann, Sh. Validov, M. Yusupov, K. Usachev // Proceedings of Ribosomes and Translation meeting St. Petersburg, Russia, 13-16 May, 2018. - P. 50
  ScanImage18.jpg
  F_NMR_analysis_of_Staphylococcus_aureus_Ribosome_Binding_Factor_A__RbfA_.pdf
• Golubev A., Blokhin D., Validov S. Z., Analysis of the polyproline protein content of Staphylococcus aureus.//MOLECULAR BIOLOGY OF THE CELL. - 2018. - Vol.29, Is.26. - .
• Blokhin D.S, Bikmullin A.G, Nurullina L.I, Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus//Biomolecular NMR Assignments. - 2018. - Vol., Is.. - .
• D. S. Blokhin Spatial Structure of YRFK Peptides with Triphenylphosphonium Moiety by NMR Spectroscopy [text] / D. S. Blokhin, R. Garifullin, T. I. Abdullin, V. V. Klochkov // Modern development of magnetic resonance: Abstracts of the international conference - Kazan, september 24–28, 2018
• Garifullin R, Blokhin D.S, Akhmadishina R.A, Effect of triphenylphosphonium moiety on spatial structure and biointeractions of stereochemical variants of YRFK motif//European Biophysics Journal. - 2018. - Vol.48, Is.1. - P.25 -34 .

• Abdrakhmanov R, Blokhin D, Usachev K, NMR Studies of the Mn2+ Interactions with Amyloid Peptide A?13-23 in Water Environment//BioNanoScience. - 2017. - Vol.7, Is.1. - P.204-206.
• Alzheimer's disease is a fatal neurodegenerative disorder involving the abnormal accumulation and deposition of peptides (amyloid-β, Aβ) derived from the amyloid precursor protein. Various factors that cause pathology data are revealed, but, at the moment, there is no clear understanding of the processes of plaque formation. This is interesting and actual problem because metals such as zinc, manganese, and others induce Aβ aggregation and fibril formation at high metal concentrations, while low concentration metal ions selectively destabilize the Aβ oligomeric species. In present paper, we report a structural studies of the Co2+ ion binding sites of Aβ fragments in water environment by 1D (1H) and 2D (1H-1H) NMR spectroscopy. According to the observed changes in the NMR spectra that were determined, the cobalt binding center of the Aβ13?23 peptide is associated with the aspartate and glutamine residues. Structural model of cobalt associated with Aβ peptide was obtained.
• Litvinov R.I. Comparison of the RGD- and AGDV-Containing Peptide Interactions with the Platelet Integrin Alphaiibbeta3/ Rustem Litvinov, Olga Kononova, Dmitry S. Blokhin, Vladimir V. Klochkov, Valeri Barsegov, Joel S. Bennett, John W. Weisel // Biophysical journal – 2017 – Volume 112, Issue 3, Supplement 1, p.350a

• Klochkov, V.V. Biomolecular high-resolution NMR spectroscopy in Institute of Physics KFU / V.V. Klochkov, K.S. Usachev, L.F. Galiullina, S.V. Efimov, D.S. Blokhin, O.V. Aganova, I.Z. Rakhmatullin, A.R. Yulmetov, A.V. Aganov // Международный симпозиум "Магнитный резонанс: от фундаментальных исследований к практическим приложениям": сборник тезисов. - Казань, 21-23 апреля, 2016. - С. 94-95
  Biomolecular_high_resolution_NMR_spectroscopy_in_Institute_of_Physics_KFU.pdf
• Abdrakhmanov R. NMR Studies of the Mn2+ Interactions with Amyloid Peptide Ab13-23 in Water Environment / R. Abdrakhmanov, D. Blokhin, K. Usachev, F. Karataeva, V. Klochkov // BioNanoScience. – 2016. – doi: 10.1007/s12668-016-0317-7
  art%3A10.1007%2Fs12668_016_0317_7.pdf
• Абдрахманов, Р. Ж. ОПРЕДЕЛЕНИЕ ВЗАИМОДЕЙСТВИЯ ИОНОВ Mn2+ С ФРАГМЕНТОМ БЕТА-АМИЛОИДА AΒ13-23 МЕТОДОМ ЯМР / Р.Ж. Абдрахманов, Д.С. Блохин, К.С. Усачев, Ф.Х. Каратаева, В.В. Клочков // Материалы и технологии XXI века: сборник тезисов. – Казань: Изд-во Казан. ун-та, 2016. – С.160.
  OPREDELENIE_VZAIMODEJSTVIYa_IONOV_MT.pdf
• Klochkov, V.V. Biomolecular high-resolution NMR spectroscopy in Institute of Physics KFU / V.V. Klochkov, K.S. Usachev, L.F. Galiullina, S.V. Efimov, D.S. Blokhin, O.V. Aganova, I.Z. Rakhmatullin, A.R. Yulmetov, A.V. Aganov // Международный симпозиум «Магнитный резонанс: от фундаментальных исследований к практическим приложениям«: сборник тезисов. - Казань, 21-23 апреля, 2016. - С. 94-95
• Sokurenko, Yulia The Role of Metals in the Reaction Catalyzed by Metal-Ion-Independent Bacillary RNase [text] / Yulia Sokurenko, Vera Ulyanova, Pavel Zelenikhin, Alexey Kolpakov, Dieter Müller, Dmitriy Blokhin, Vladimir Klochkov and Olga Ilinskaya //Bioinorganic Chemistry and Applications .- 2016.- Volume 2016, Article ID 4121960, 7 pages. http://dx.doi.org/10.1155/2016/4121960
• Sokurenko Y, Ulyanova V, Zelenikhin P, Kolpakov A., Müller D., Blokhin D, Klochkov V, Ilinskaya O. The Role of Metals in the Reaction Catalyzed by Metal-Ion-Independent Bacillary RNase//Bioinorganic Chemistry and Applications. - 2016. - Vol.2016, Is.. - Art. № 4121960. http://dx.doi.org/10.1155/2016/4121960
• Абдрахманов, Р. Ж. Определение взаимодействия ионов Mn2+ с фрагментом бета-амилоида Aβ13-23 методом ЯМР / Р.Ж. Абдрахманов, Д.С. Блохин, К.С. Усачев, Ф.Х. Каратаева, В.В. Клочков // Трансляционная медицина 2016: сборник тезисов междунар. конф. – Казань, 2016. – С. 3.
  BETA_AMILOIDA.pdf

• Blokhin, D.S. Spatial structures of PAP(262-270) and PAP(274-284), two selected fragments of PAP(248-286), the enhancer of HIV infectivity. [text]/D.S. Blokhin, A.V. Filippov, O.N. Antzutkin, S. Afonin, V.V. Klochkov // Applied Magnetic Resonance. 2015. V. 46. P. 757-769.
• Karataeva F.K. Spatial structure of fibrinopeptide B in water solution with DPC micelles by NMR spectroscopy [text] /D.S. Blokhin, A.R. Fayzullina, A.V. Filippov, F.K. Karataeva, V.V. Klochkov // Journal of Molecular Structure. 2015. V.1102. P.91-94.
• Spatial Structures of PAP(262?270) and PAP(274?284), Two Selected Fragments of PAP(248?286), an Enhancer of HIV Infectivity
• Spatial structure of fibrinopeptide B in water solution with DPC micelles by NMR spectroscopy
• Spatial Structures of PAP(262-270) and PAP(274-284), Two Selected Fragments of PAP(248-286), an Enhancer of HIV Infectivity
• Spatial Structures of PAP(262т??270) and PAP(274т??284), Two Selected Fragments of PAP(248т??286), an Enhancer of HIV Infectivity

• Blokhin, D.S. Spatial structure of oligopeptide PAP(248-261), the N-terminal fragment of the HIV enhancer prostatic acid phosphatase peptide PAP(248-286), in aqueous and SDS micelle solutions [Text] / D.S. Blokhin, A.V. Filippov, O.N. Antzutkin, F.K. Karataeva, V.V. Klochkov // J. Molecular Structure. 2014. V.1070.P.38-42.
• Blokhin, D.S. NOE effect of sodium dodecyl sulfate in monomeric and micellar systems by NMR spectroscopy [Text]/ D.S. Blokhin, E.A.Filippova, V.V. Klochkov // Applied Magnetic Resonance – 2014 – Vol. 45, I. 8, P. 715-721.
• Spatial structure of oligopeptide PAP(248-261), the N-terminal fragment of the HIV enhancer prostatic acid phosphatase peptide PAP(248-286), in aqueous and SDS micelle solutions
• Blokhin D.S. NOE effect of sodium dodecyl sulfate in monomeric and micellar systems by NMR spectroscopy [Text]/ D.S. Blokhin, E.A.Filippova, V.V. Klochkov // Applied Magnetic Resonance ? 2014 ? Vol. 45, I. 8, P. 715-721.
• Blokhin, D.S. Spatial structure of oligopeptide PAP(248-261), the N-terminal fragment of the HIV enhancer prostatic acid phosphatase peptide PAP(248-286), in aqueous and SDS micelle solutions [Text] / D.S. Blokhin, A.V. Filippov, O.N. Antzutkin, F.K. Karataeva, V.V. Klochkov // J. Molecular Structure. 2014. V.1070.P.38-42.

• Bloсhin,D.S. Spatial structure of heptapeptide Gly-Ile-Leu-Asn-His-Met-Lys, a fragment of HIV enhancer prostatic acid phosphatase, in aqueous and in SDS micelle solutions [text] /Bloсhin,D.S., Aganova,O.V., Yulmetov,A.R., Filippov,A.V., Antzutkin,O.N., Gizatullin,B.I., Afonin,S., Klochkov,V.V. //J. Molecular Structure. -2013. - Vol. 1033. - P.59-66.
• Blokhin, D.S. Spatial structure of tetrapeptide N-AC-Ser-Phe-Val-Gly-OMe in "protein-micelle of sodium dodecyl sulfate" complex and in solid state by NMR spectroscopy [Text] / D.S. Blokhin, S. Berger, V.V. Klochkov // Magnetic Resonance in Solids (Electronic Journal). - 2013. - Vol. 15, No.2. - 13202 (7 pp).
• Khodov, I.A. Spatial structure of felodipine dissolved in DMSO by 1D NOE and 2D NOESY spectroscopy / I.A. Khodov, M.Yu. Nikiforov, G.A. Alper, D.S. Blokhin, S.V. Efimov, V.V. Klochkov, N. Georgi // J. Molecular Structure - 2013. - Vol. 1035. - P. 358-362.
• Blokhin D.S, Berger S, Klochkov V.V., Spatial structure of tetrapeptide N-AC-Ser-Phe-Val-Gly-OMe in ««protein-micelle of sodium dodecyl sulfate«« complex and in solid state by NMR spectroscopy//Magnetic Resonance in Solids. - 2013. - Vol.15, Is.2. - .
• Khodov, I.A. Spatial structure of felodipine dissolved in DMSO by 1D NOE and 2D NOESY spectroscopy / I.A. Khodov, M.Yu. Nikiforov, G.A. Alper, D.S. Blokhin, S.V. Efimov, V.V. Klochkov, N. Georgi // J. Molecular Structure - 2013. - Vol. 1035. - P. 358-362 - DOI: 10.1016/j.molstruc.2012.11.040.
• Blochin D.S, Aganova O.V, Yulmetov A.R, Spatial structure of heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys, a fragment of the HIV enhancer prostatic acid phosphatase, in aqueous and SDS micelle solutions//Journal of Molecular Structure. - 2013. - Vol.1033, Is.. - P.59-66.
• Khodov I.A, Nikiforov M.Yu, Alper G.A, Spatial structure of felodipine dissolved in DMSO by 1D NOE and 2D NOESY NMR spectroscopy//Journal of Molecular Structure. - 2013. - Vol.1035, Is.. - P.358-362.
• Bloсhin, D.S. Spatial structure of heptapeptide Gly-Ile-Leu-Asn-His-Met-Lys, a fragment of HIV enhancer prostatic acid phosphatase, in aqueous and in SDS micelle solutions [text] / Bloсhin, D.S., Aganova, O.V., Yulmetov, A.R., Filippov, A.V., Antzutkin, O.N., Gizatullin, B.I., Afonin,S., Klochkov,V.V. //J. Molecular Structure. 2013. V.1033.P.59-66.

• Alakshin, E. M. Experimental Proof of the Existence of Water Clusters in Fullerene-Like PrF 3 Nanoparticles [text] / E.M. Alakshin, D.S. Blokhin, A.M. Sabitova, A.V. Klochkov, V.V. Klochkov, K. Kono, S.L. Korableva, M.S. Tagirov // JETP Letters. - 2012. - V.96.,No.3. - P.181-183.
• И.З.Рахматуллин, Д.С.Блохин, О.В.Аганова, А.Р.Юльметов, А.В.Филиппов, А.В.Аганов, В.В.Клочков. Пространственное строение усиливающего вич гептапептида Glu-Ile-Leu-Asn-His-Met-Lys в растворе и комплексе: гептапептид - модель биологической мембраны. Ученые Записки Казанского Университета. - 2012. - Т. 154, Серия Физико-математические науки, Книга 1. C. 63-73.
• Spatial structure of felodipine in DMSO-d6 solution by 1-D NOE and 2-D NOESY NMR spectroscopy / I. A. Khodov, M.Yu. Nikiforov, G.A. Alper [etc.] //XV International Youth Scientific School «Actual Problems of Magnetic Resonance and its Applications» - Kazan, 2012. - P. 122.
  F_22_26_Oktyabrya_2012_Kazan.pdf
• Galiullina, L.F. Investigation of cholesterol + model of biological membrane complex by NMR spectroscopy [Text] / L.F.Galiullina, D.S.Blokhin, A.V.Aganov, V.V.Klochkov // Magnetic Resonance in Solids (Electronic Journal). - 2012. - Vol. 14, No.2. - 12204 (7 pp). - ISSN 2072-5981.
• Galiullina L.F, Blokhin D.S, Aganov A.V, Investigation of Ћcholesterol + model of biological membraneЛ complex by NMR spectroscopy//Magnetic Resonance in Solids. - 2012. - Vol.14, Is.2. - P.12204-12210.
• Галиуллина, Л.Ф. Прямое наблюдение образования комплекса: холестерин - модель биологической мембраны методами ЯМР спектроскопии [Текст] / Галиуллина, Л.Ф., Блохин Д.С., Аганов А.В., Клочков В.В.// Клеточная трансплантология и тканевая инженерия.- 2012. - Т.VII, №3. С. 41-48.

• Д.С. Блохин, С.В. Ефимов, А.В. Клочков, И.З. Рахматуллин, К.С. Усачев, А.Ю. Юльметов, А.В. Филиппов, А.В. Аганов, В.В. Клочков. Пространственное строение некоторых олигопептидов в растворе и комплексе: олигопептид - модель биологической мембраны, III Региональная научно-практическая конференция с международным участием "Синтез и перспективы использования новых биологически активных соединений". -24 мая, Казань, 2011. С.32
• Blokhin, D.S. Spatial structure of the decapeptide Val-Ile-Lys-Lys-Ser-Thr-Ala-Leu-Leu-Gly in water and in a complex with sodium dodecyl sulfate micelles [Text] /D.S. Blokhin, S.V. Efimov, A.V. Klochkov, A.R. Yulmetov, A.V. Filippov, O.N.Antzutkin, A.V. Aganov, V.V. Klochkov// Applied Magnetic Resonance. 2011. Vol. 41, I. 2, P. 267-282.