S. Kozin

发表

Tetrapeptide Ac-HAEE-NH2 Protects α4β2 nAChR from Inhibition by Aβ

A. Makarov, A. Adzhubei, V. Tsetlin, 2020, International journal of molecular sciences.

Epitope mapping of cytochrome P450cam (CYP101).

A. Archakov, G. H. Hoa, S. Kozin, 1997, Archives of biochemistry and biophysics.

Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging*

A. Mazur, S. Zirah, S. Rebuffat, 2006, Journal of Biological Chemistry.

The N-domain of angiotensin-converting enzyme specifically hydrolyzes the Arg-5-His-6 bond of Alzheimer's Abeta-(1-16) peptide and its isoAsp-7 analogue with different efficiency as evidenced by quantitative matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

A. Makarov, E. Nikolaev, I. Popov, 2008, Rapid communications in mass spectrometry : RCM.

Supermetallization of peptides and proteins during electrospray ionization.

A. Makarov, E. Nikolaev, M. Indeykina, 2015, Journal of mass spectrometry : JMS.

Roles of zinc ions and structural polymorphism of β-amyloid in the development of Alzheimer’s disease

A. Makarov, S. Kozin, A. Kulikova, 2015, Molecular Biology.

Neurotoxic Effects of Aβ6-42 Peptides Mimicking Putative Products Formed by the Angiotensin Converting Enzyme.

A. Makarov, V. Mitkevich, A. Kopylov, 2018, Journal of Alzheimer's disease : JAD.

[Physico-chemical methods for studing β-amyloid aggregation].

A. Makarov, A. Archakov, E. Suprun, 2015, Biomeditsinskaia khimiia.

Extracellular GAPDH promotes Alzheimer disease progression by enhancing amyloid-β aggregation and cytotoxicity

A. Makarov, M. Tsolaki, E. Nudler, 2020 .

Electrochemical detection of protein post-translational modifications: Phosphorylation and nitration of amyloid-beta (1–16)

A. Makarov, A. Archakov, E. Suprun, 2017 .

Direct electrochemical oxidation of amyloid-β peptides via tyrosine, histidine, and methionine residues

A. Archakov, E. Suprun, S. Radko, 2016 .

Tyrosine Based Electrochemical Analysis of Amyloid-β Fragment (1-16) Binding to Metal(II) Ions

A. Makarov, A. Archakov, E. Suprun, 2015 .

Physico-chemical methods for studying amyloid-β aggregation

A. Makarov, A. Archakov, E. Suprun, 2015, Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry.

Chronic administration of Dimebon does not ameliorate amyloid-β pathology in 5xFAD transgenic mice.

V. Buchman, O. Peters, S. Brooks, 2013, Journal of Alzheimer's disease : JAD.

N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-β(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer’s disease

A. Makarov, A. Veselovsky, E. Nikolaev, 2018, Scientific Reports.

NMR Solution Structure of Rat A b (1–16): Toward Understanding the Mechanism of Rats’ Resistance to Alzheimer’s Disease

P. Tsvetkov, A. Makarov, S. Kozin, 2011 .

Direct Molecular Fishing of Zinc-Dependent Protein Partners of Amyloid-beta 1–16 with the Taiwan (D7H) Mutation and Phosphorylated Ser8 Residue

A. Makarov, V. Mitkevich, A. Ivanov, 2020, Molecular Biology.

STRUCTURAL-FUNCTIONAL ANALYSIS OF BIOPOLYMERS AND THEIR COMPLEXES

A. Makarov, V. Mitkevich, S. Radko, 2019 .

Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans

A. Makarov, V. Mitkevich, S. Radko, 2016, Molecular Biology.

Phosphorylation of Ser8 promotes zinc-induced dimerization of the amyloid-β metal-binding domain.

P. Tsvetkov, A. Makarov, E. Nudler, 2014, Molecular bioSystems.

Capabilities of MS for analytical quantitative determination of the ratio of α- and βAsp7 isoforms of the amyloid-β peptide in binary mixtures.

P. Tsvetkov, A. Makarov, M. Indeykina, 2011, Analytical chemistry.

Zn-dependent β-amyloid Aggregation and its Reversal by the Tetrapeptide HAEE

A. Makarov, E. Nudler, V. Mitkevich, 2023, Aging and disease.

Phosphorylation of the Amyloid-Beta Peptide Inhibits Zinc-Dependent Aggregation, Prevents Na,K-ATPase Inhibition, and Reduces Cerebral Plaque Deposition

Alexander A. Makarov, A. Makarov, V. Mitkevich, 2018, Front. Mol. Neurosci..

Isomerization of the Asp7 Residue Results in Zinc‐Induced Oligomerization of Alzheimer’s Disease Amyloid β(1–16) Peptide

P. Tsvetkov, A. Makarov, A. Archakov, 2008, Chembiochem : a European journal of chemical biology.

Interplay of histidine residues of the Alzheimer’s disease Aβ peptide governs its Zn-induced oligomerization

A. Makarov, A. Pastore, S. Kozin, 2016, Scientific Reports.

Application of Prussian Blue modified carbon electrodes for amperometric detection of amyloid-β peptides by flow injection analysis

A. Makarov, A. Karyakin, V. Mitkevich, 2022, Electrochimica Acta.

The Convergence of Alzheimer’s Disease Pathogenesis Concepts

A. Makarov, S. Kozin, A. A. Makarov, 2019, Molecular Biology.

The Effects of Endogenous Non-Peptide Molecule Isatin and Hydrogen Peroxide on Proteomic Profiling of Rat Brain Amyloid-β Binding Proteins: Relevance to Alzheimer’s Disease?

A. Makarov, A. Ivanov, A. Kopylov, 2014, International journal of molecular sciences.

Development of Peptide Biopharmaceuticals in Russia

S. Kozin, E. Poluektova, A. Beniashvili, 2022, Pharmaceutics.

Electrochemical Analysis in Studying β-Amyloid Aggregation

A. Makarov, V. Mitkevich, E. Suprun, 2023, Biochemistry (Moscow).

Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer’s Disease

S. Kozin, 2023, Biochemistry (Moscow).

Direct molecular fishing in molecular partners investigation in protein–protein and protein–peptide interactions

A. Makarov, V. Mitkevich, A. Ivanov, 2016, Russian Journal of Bioorganic Chemistry.

Anti-amyloid Therapy of Alzheimer’s Disease: Current State and Prospects

A. Makarov, V. Mitkevich, E. Barykin, 2018, Biochemistry (Moscow).

Intravenously Injected Amyloid-β Peptide With Isomerized Asp7 and Phosphorylated Ser8 Residues Inhibits Cerebral β-Amyloidosis in AβPP/PS1 Transgenic Mice Model of Alzheimer’s Disease

A. Makarov, V. Mitkevich, A. Adzhubei, 2018, Front. Neurosci..

Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms

A. Makarov, V. Mitkevich, A. Ivanov, 2018, Molecular Biology.

Chemical modifications of amyloid-β(1-42) have a significant impact on the repertoire of brain amyloid-β(1-42) binding proteins.

A. Makarov, V. Mitkevich, A. Kopylov, 2016, Biochimie.

Intracerebral Injection of Metal-Binding Domain of Aβ Comprising the Isomerized Asp7 Increases the Amyloid Burden in Transgenic Mice

A. Makarov, S. Kozin, M. Kukharsky, 2016, Neurotoxicity Research.

Intracerebral Injection of Metal-Binding Domain of Aβ Comprising the Isomerized Asp7 Increases the Amyloid Burden in Transgenic Mice

A. Makarov, S. Kozin, M. Kukharsky, 2016, Neurotoxicity Research.

Peripherally applied synthetic tetrapeptides HAEE and RADD slow down the development of cerebral β-amyloidosis in AβPP/PS1 transgenic mice.

P. Tsvetkov, O. Mediannikov, S. Kozin, 2016, Journal of Alzheimer's disease : JAD.

The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain.

P. Tsvetkov, A. Makarov, A. Ivanov, 2015, Metallomics : integrated biometal science.

Peripherally Applied Synthetic Peptide isoAsp7-Aβ(1-42) Triggers Cerebral β-Amyloidosis

P. Tsvetkov, A. Makarov, A. Lisitsa, 2013, Neurotoxicity Research.

Zinc-induced dimerization of the amyloid-β metal-binding domain 1-16 is mediated by residues 11-14.

P. Tsvetkov, A. Makarov, A. Ivanov, 2011, Molecular bioSystems.

Minimal Zn(2+) binding site of amyloid-β.

Alexander A. Makarov, Andrey V. Golovin, Philipp O. Tsvetkov, 2010, Biophysical journal.

Minimal Zn 2þ Binding Site of Amyloid-b

P. Tsvetkov, A. Makarov, A. Archakov, 2010 .

Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies

M. Przybylski, S. Zirah, S. Rebuffat, 2004 .

Zinc binding properties of the amyloid fragment Aβ(1–16) studied by electrospray-ionization mass spectrometry

J. Tabet, S. Zirah, S. Rebuffat, 2003 .

Zinc binding to Alzheimer's Abeta(1-16) peptide results in stable soluble complex.

G. H. Hoa, S. Zirah, S. Rebuffat, 2001, Biochemical and biophysical research communications.

Extracellular GAPDH Promotes Alzheimer Disease Progression by Enhancing Amyloid-β Aggregation and Cytotoxicity

A. Makarov, M. Tsolaki, E. Nudler, 2020, Aging and disease.

Amyloid-β with isomerized Asp7 cytotoxicity is coupled to protein phosphorylation

A. Makarov, V. Mitkevich, M. Serebryakova, 2018, Scientific Reports.

Isomerization of Asp7 in Beta-Amyloid Enhances Inhibition of the α7 Nicotinic Receptor and Promotes Neurotoxicity

A. Makarov, M. Hollmann, V. Mitkevich, 2019, Cells.

NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease.

P. Tsvetkov, A. Makarov, S. Kozin, 2012, Biophysical journal.

Zinc-Mediated Binding of Nucleic Acids to Amyloid-β Aggregates: Role of Histidine Residues.

A. Makarov, V. Mitkevich, A. Ivanov, 2016, Journal of Alzheimer's disease : JAD.

Direct Molecular Fishing of Zinc-Dependent Protein Partners of Amyloid-beta 1–16 with the Taiwan (D7H) Mutation and Phosphorylated Ser8 Residue

A. Makarov, V. Mitkevich, A. Ivanov, 2020, Molecular Biology.

The English (H6R) Mutation of the Alzheimer’s Disease Amyloid-β Peptide Modulates Its Zinc-Induced Aggregation

A. Makarov, V. Mitkevich, S. Radko, 2020, Biomolecules.

Heparin Modulates the Kinetics of Zinc-Induced Aggregation of Amyloid-β Peptides.

A. Makarov, V. Mitkevich, S. Radko, 2018, Journal of Alzheimer's disease : JAD.

Zinc-induced interaction of the metal-binding domain of amyloid-β peptide with DNA.

P. Tsvetkov, A. Makarov, A. Ivanov, 2013, Journal of Alzheimer's disease : JAD.

Effect of isomerization of aspartate-7 on the binding of copper (II) ion by the β-amyloid peptide

A. Makarov, A. Archakov, S. Kozin, 2009, Biofizika.

Possible role of region 152–156 in the structural duality of a peptide fragment from sheep prion protein

G. Bertho, S. Kozin, P. Debey, 2004, Protein science : a publication of the Protein Society.

Sheep Prion Protein Synthetic Peptide Spanning Helix 1 and β-Strand 2 (Residues 142–166) Shows β-Hairpin Structure in Solution*

A. Mazur, G. H. Hoa, G. Bertho, 2001, The Journal of Biological Chemistry.

Antigenic mapping of bacterial and animal cytochromes P-450.

A. Archakov, S. Kozin, G. Hui Bon Hoa, 1996, Biochimie.

Amyloid β Modification: A Key to the Sporadic Alzheimer's Disease?

A. Makarov, V. Mitkevich, E. Barykin, 2017, Front. Genet..

Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease

A. Makarov, V. Mitkevich, S. Kozin, 2016 .

Peripherally Applied Synthetic Peptide isoAsp7-Aβ(1-42) Triggers Cerebral β-Amyloidosis

P. Tsvetkov, S. Kozin, G. Telegin, 2013, Neurotoxicity Research.

HSP70 protects human neuroblastoma cells from apoptosis and oxidative stress induced by amyloid peptide isoAsp7-Aβ(1–42)

A. Makarov, V. Mitkevich, M. Yurinskaya, 2015, Cell Death and Disease.

Isomerization of Asp7 leads to increased toxic effect of amyloid-β42 on human neuronal cells

P. Tsvetkov, A. Makarov, V. Mitkevich, 2013, Cell Death and Disease.

Scanning ion-conductance microscopy for studying β-amyloid aggregate formation on living cell surface

A. Makarov, Y. Korchev, V. Mitkevich, 2022, bioRxiv.

Optimization of the methods for small peptide solution structure determination by NMR spectroscopy

S. Kozin, A. Mantsyzov, V. Polshakov, 2010, Molecular Biology.

Mass spectrometric studies of the variety of beta-amyloid proteoforms in Alzheimer's disease.

A. Makarov, N. Zakharova, V. Mitkevich, 2022, Mass spectrometry reviews.

Epitope mapping of the domains of human angiotensin converting enzyme.

A. Veselovsky, E. V. Kugaevskaya, Y. E. Elisseeva, 2006, Biochimica et biophysica acta.

Super-suppressor induced interallelic complementation

B. Simarov, S. Kozin, S. Inge-Vechtomov, 1966, Zeitschrift für Vererbungslehre.

Evaluation of MALDI-TOF/TOF Mass Spectrometry Approach for Quantitative Determination of Aspartate Residue Isomerization in the Amyloid-β Peptide

A. Makarov, N. Zakharova, M. Indeykina, 2019, Journal of The American Society for Mass Spectrometry.

N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-β(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer’s disease

A. Makarov, A. Veselovsky, E. Nikolaev, 2018, Scientific Reports.

Electrochemical detection of Zn(II)-induced amyloid-β aggregation: Insights into aggregation mechanisms

A. Makarov, V. Mitkevich, E. Suprun, 2018, Journal of Electroanalytical Chemistry.

Amyloid‐β Containing Isoaspartate 7 as Potential Biomarker and Drug Target in Alzheimer′s Disease

A. Makarov, V. Mitkevich, S. Kozin, 2016 .

Compressibility and uncoupling of cytochrome P450cam: high pressure FTIR and activity studies.

G. H. Hoa, S. Kozin, J. Chervin, 2003, Biochemical and biophysical research communications.

Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms

A. Makarov, V. Mitkevich, A. Ivanov, 2018, Molecular Biology.

Pharmacokinetics and Molecular Modeling Indicate nAChRα4-Derived Peptide HAEE Goes through the Blood–Brain Barrier

A. Makarov, V. Mitkevich, A. Adzhubei, 2021, Biomolecules.

Zinc-induced heterodimer formation between metal-binding domains of intact and naturally modified amyloid-beta species: implication to amyloid seeding in Alzheimer’s disease?

A. Makarov, A. Ivanov, Y. Mezentsev, 2016, Journal of biomolecular structure & dynamics.

Effect of mutations and modifications of amino acid residues on zinc-induced interaction of the metal-binding domain of β-amyloid with DNA

A. Makarov, V. Mitkevich, A. Ivanov, 2015, Molecular Biology.

Protein interactomics based on direct molecular fishing on paramagnetic particles: Practical realization and further SPR validation

A. Lisitsa, A. Ivanov, A. Archakov, 2014, Proteomics.

Aberrant interactions between amyloid-beta and alpha5 laminins as possible driver of neuronal disfunction in Alzheimer's disease.

A. Makarov, V. Mitkevich, S. Kozin, 2020, Biochimie.

Estimation of phosphorylation level of amyloid-beta isolated from human blood plasma: Ultrahigh-resolution mass spectrometry

A. Makarov, Y. Kostyukevich, A. Kononikhin, 2014, Molecular Biology.

[New biomarkers and drug targets for diagnosis and therapy of Alzheimer's disease (molecular determinants of zinc-dependent oligomerization of Β-amyloid)].

A. Makarov, S. Kozin, Makarov Aa, 2015, Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova.

ESI-MS identification of the minimal zinc-binding center in natural isoforms of β-amyloid domain 1–16

A. Makarov, A. Kononikhin, I. Popov, 2013, Molecular Biology.

Peripherally Applied Synthetic Tetrapeptides HAEE and RADD Slow Down the Development of Cerebral β-Amyloidosis in AβPP/PS1 Transgenic Mice.

P. Tsvetkov, O. Mediannikov, S. Kozin, 2015, Journal of Alzheimer's disease : JAD.

STRUCTURAL AND FUNCTIONAL ANALYSIS OF BIOPOLYMERS AND BIOPOLYMER COMPLEXES

A. Makarov, A. Kononikhin, I. Popov, 2014 .

Localization of zinc binding sites of Ab1-16 with English mutation during formation of monomers and dimers with zinc

A. Makarov, V. Mitkevich, E. Nikolaev, 2016 .

Solution structure of rat Aβ(1-16) and the mechanism of rats' resistance to Alzheimer's disease

P. Tsvetkov, A. Makarov, S. Kozin, 2012 .

Secondary structure of Aβ(1–16) complexes with zinc: A study in the gas phase using deuterium/hydrogen exchange and ultra-high-resolution mass spectrometry

A. Makarov, K. Bocharov, M. Indeykina, 2017, Molecular Biology.

Effect of mutations and modifications of amino acid residues on zinc-induced interaction of the metal-binding domain of β-amyloid with DNA

A. Makarov, V. Mitkevich, A. Ivanov, 2015, Molecular Biology.

Molecular Mechanism of Zinc-Dependent Oligomerization of Alzheimer’s Amyloid-β with Taiwan (D7H) Mutation

A. Makarov, V. Mitkevich, A. Adzhubei, 2023, International journal of molecular sciences.

Application of electrochemical method to a comparative study of spontaneous aggregation of amyloid-β isoforms

A. Makarov, V. Mitkevich, E. Suprun, 2020 .

A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-β Fragment with Taiwanese Mutation D7H.

A. Makarov, V. Mitkevich, A. Adzhubei, 2017, Angewandte Chemie.

[The role of zinc ions and structural polymorphism of β-amyloid in the Alzheimer's disease initiation].

A. Makarov, S. Kozin, A. Kulikova, 2015, Molekuliarnaia biologiia.

[Identification of the minimal zinc-binding center in natural isoforms of amyloid-beta domain 1-16 using ESI-MS].

A. Makarov, A. Kononikhin, I. Popov, 2013, Molekuliarnaia biologiia.

Super-suppressor induced interallelic complementation.

B. Simarov, S. Kozin, S. Inge-Vechtomov, 1966 .

Electrochemical detection of Zn(II)- and Cu(II)-induced amyloid-β aggregation: Quantitative aspects and application to amyloid-β isoforms

A. Makarov, A. Archakov, E. Suprun, 2017 .

Application of MALDI-TOF/TOF-MS for relative quantitation of α- and β-Asp7 isoforms of amyloid-β peptide

A. Makarov, K. Bocharov, E. Nikolaev, 2018, European journal of mass spectrometry.

Anti-amyloid Therapy of Alzheimer’s Disease: Current State and Prospects

V. Mitkevich, E. Barykin, S. Kozin, 2018, Biochemistry (Moscow).

The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain.

Y. Mezentsev, S. Kozin, A. Kulikova, 2015, Metallomics : integrated biometal science.

[The Convergence of Alzheimer's Disease Pathogenesis Concepts].

S. Kozin, A. A. Makarov, 2019, Molekuliarnaia biologiia.

Phosphorylation of Ser8 promotes zinc-induced dimerization of the amyloid-β metal-binding domain.

P. Tsvetkov, A. Makarov, E. Nudler, 2014, Molecular bioSystems.

Isomerization of the Asp7 Residue Results in Zinc‐Induced Oligomerization of Alzheimer’s Disease Amyloid β(1–16) Peptide

P. Tsvetkov, A. Makarov, A. Archakov, 2008, Chembiochem : a European journal of chemical biology.

[Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms].

V. Mitkevich, Y. Mezentsev, M. Yurinskaya, 2018, Molekuliarnaia biologiia.

Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms

A. Makarov, V. Mitkevich, A. Ivanov, 2018, Molecular Biology.

Switching On/Off Amyloid Plaque Formation in Transgenic Animal Models of Alzheimer’s Disease

V. Mitkevich, A. Adzhubei, S. Kozin, 2023, International journal of molecular sciences.

Zinc-induced interactions of the metal-binding domain of beta-amyloid with nucleic acids and glycosaminoglycans

A. Makarov, V. Mitkevich, S. Radko, 2016, Molecular Biology.

Mass spectrometric identification of posttranslational modifications in transthyretin from human blood

S. Kozin, N. Starodubtseva, E. Kukaev, 2013, Molecular Biology.