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Roles for α-Synuclein in Gene Expression.

Genes

Somayaji M, Lanseur Z, Choi SJ, Sulzer D, Mosharov EV.
PMID: 34440340
Genes (Basel). 2021 Jul 29;12(8). doi: 10.3390/genes12081166.

α-Synuclein (α-Syn) is a small cytosolic protein associated with a range of cellular compartments, including synaptic vesicles, the nucleus, mitochondria, endoplasmic reticulum, Golgi apparatus, and lysosomes. In addition to its physiological role in regulating presynaptic function, the protein plays...

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Somayaji M, Lanseur Z, Choi SJ, et al. Roles for α-Synuclein in Gene Expression. Genes (Basel). 2021;12(8)doi: 10.3390/genes12081166.
Somayaji, M., Lanseur, Z., Choi, S. J., Sulzer, D., & Mosharov, E. V. (2021). Roles for α-Synuclein in Gene Expression. Genes, 12(8), . https://doi.org/10.3390/genes12081166
Somayaji, Mahalakshmi, et al. "Roles for α-Synuclein in Gene Expression." Genes vol. 12,8 (2021). doi: https://doi.org/10.3390/genes12081166
Somayaji M, Lanseur Z, Choi SJ, Sulzer D, Mosharov EV. Roles for α-Synuclein in Gene Expression. Genes (Basel). 2021 Jul 29;12(8). doi: 10.3390/genes12081166. PMID: 34440340; PMCID: PMC8393936.
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Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation.

Frontiers in cell and developmental biology

Albrecht C, Kuznetsov AS, Appert-Collin A, Dhaideh Z, Callewaert M, Bershatsky YV, Urban AS, Bocharov EV, Bagnard D, Baud S, Blaise S, Romier-Crouzet B, Efremov RG, Dauchez M, Duca L, Gueroult M, Maurice P, Bennasroune A.
PMID: 33392200
Front Cell Dev Biol. 2020 Dec 16;8:611121. doi: 10.3389/fcell.2020.611121. eCollection 2020.

Sialidases, or neuraminidases, are involved in several human disorders such as neurodegenerative, infectious and cardiovascular diseases, and cancers. Accumulative data have shown that inhibition of neuraminidases, such as NEU1 sialidase, may be a promising pharmacological target, and selective inhibitors...

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Albrecht C, Kuznetsov AS, Appert-Collin A, et al. Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation. Front Cell Dev Biol. 2020;8:611121doi: 10.3389/fcell.2020.611121.
Albrecht, C., Kuznetsov, A. S., Appert-Collin, A., Dhaideh, Z., Callewaert, M., Bershatsky, Y. V., Urban, A. S., Bocharov, E. V., Bagnard, D., Baud, S., Blaise, S., Romier-Crouzet, B., Efremov, R. G., Dauchez, M., Duca, L., Gueroult, M., Maurice, P., & Bennasroune, A. (2020). Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation. Frontiers in cell and developmental biology, 8611121. https://doi.org/10.3389/fcell.2020.611121
Albrecht, Camille, et al. "Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation." Frontiers in cell and developmental biology vol. 8 (2020): 611121. doi: https://doi.org/10.3389/fcell.2020.611121
Albrecht C, Kuznetsov AS, Appert-Collin A, Dhaideh Z, Callewaert M, Bershatsky YV, Urban AS, Bocharov EV, Bagnard D, Baud S, Blaise S, Romier-Crouzet B, Efremov RG, Dauchez M, Duca L, Gueroult M, Maurice P, Bennasroune A. Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation. Front Cell Dev Biol. 2020 Dec 16;8:611121. doi: 10.3389/fcell.2020.611121. eCollection 2020. PMID: 33392200; PMCID: PMC7772355.
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Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function.

Topics in current chemistry

Bocharov EV, Pavlov KV, Blommers MJ, Arvinte T, Arseniev AS.
PMID: 23605462
Top Curr Chem. 2008;273:155-81. doi: 10.1007/128_2007_17.

In any organism, very precisely adjusted interaction and exchange of information between cellsis continuously required. These cooperative interactions involve numerous cytokines, acting throughcorresponding sets of cell-surface receptors. The transforming growth factor β (TGF-β)superfamily includes a variety of structurally related...

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Bocharov EV, Pavlov KV, Blommers MJ, et al. Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function. Top Curr Chem. 2008;273:155-81doi: 10.1007/128_2007_17.
Bocharov, E. V., Pavlov, K. V., Blommers, M. J., Arvinte, T., & Arseniev, A. S. (2008). Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function. Topics in current chemistry, 273155-81. https://doi.org/10.1007/128_2007_17
Bocharov, Eduard V, et al. "Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function." Topics in current chemistry vol. 273 (2008): 155-81. doi: https://doi.org/10.1007/128_2007_17
Bocharov EV, Pavlov KV, Blommers MJ, Arvinte T, Arseniev AS. Modulation of the Bioactive Conformation of Transforming Growth Factor β: Possible Implications of Cation Binding for Biological Function. Top Curr Chem. 2008;273:155-81. doi: 10.1007/128_2007_17. PMID: 23605462.
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Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome.

Cell

Bourdenx M, Martín-Segura A, Scrivo A, Rodriguez-Navarro JA, Kaushik S, Tasset I, Diaz A, Storm NJ, Xin Q, Juste YR, Stevenson E, Luengo E, Clement CC, Choi SJ, Krogan NJ, Mosharov EV, Santambrogio L, Grueninger F, Collin L, Swaney DL, Sulzer D, Gavathiotis E, Cuervo AM.
PMID: 33891876
Cell. 2021 May 13;184(10):2696-2714.e25. doi: 10.1016/j.cell.2021.03.048. Epub 2021 Apr 22.

Components of the proteostasis network malfunction in aging, and reduced protein quality control in neurons has been proposed to promote neurodegeneration. Here, we investigate the role of chaperone-mediated autophagy (CMA), a selective autophagy shown to degrade neurodegeneration-related proteins, in...

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Bourdenx M, Martín-Segura A, Scrivo A, et al. Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome. Cell. 2021;184(10):2696-2714.e25doi: 10.1016/j.cell.2021.03.048.
Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., Stevenson, E., Luengo, E., Clement, C. C., Choi, S. J., Krogan, N. J., Mosharov, E. V., Santambrogio, L., Grueninger, F., Collin, L., Swaney, D. L., Sulzer, D., Gavathiotis, E., & Cuervo, A. M. (2021). Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome. Cell, 184(10), 2696-2714.e25. https://doi.org/10.1016/j.cell.2021.03.048
Bourdenx, Mathieu, et al. "Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome." Cell vol. 184,10 (2021): 2696-2714.e25. doi: https://doi.org/10.1016/j.cell.2021.03.048
Bourdenx M, Martín-Segura A, Scrivo A, Rodriguez-Navarro JA, Kaushik S, Tasset I, Diaz A, Storm NJ, Xin Q, Juste YR, Stevenson E, Luengo E, Clement CC, Choi SJ, Krogan NJ, Mosharov EV, Santambrogio L, Grueninger F, Collin L, Swaney DL, Sulzer D, Gavathiotis E, Cuervo AM. Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome. Cell. 2021 May 13;184(10):2696-2714.e25. doi: 10.1016/j.cell.2021.03.048. Epub 2021 Apr 22. PMID: 33891876; PMCID: PMC8152331.
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Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.

Angewandte Chemie (International ed. in English)

Lesovoy DM, Georgoulia PS, Diercks T, Matečko-Burmann I, Burmann BM, Bocharov EV, Bermel W, Orekhov VY.
PMID: 34143912
Angew Chem Int Ed Engl. 2021 Oct 25;60(44):23540-23544. doi: 10.1002/anie.202102758. Epub 2021 Jul 13.

Dysregulation of post-translational modifications (PTMs) like phosphorylation is often involved in disease. NMR may elucidate exact loci and time courses of PTMs at atomic resolution and near-physiological conditions but requires signal assignment to individual atoms. Conventional NMR methods for...

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Lesovoy DM, Georgoulia PS, Diercks T, et al. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*. Angew Chem Int Ed Engl. 2021;60(44):23540-23544doi: 10.1002/anie.202102758.
Lesovoy, D. M., Georgoulia, P. S., Diercks, T., Matečko-Burmann, I., Burmann, B. M., Bocharov, E. V., Bermel, W., & Orekhov, V. Y. (2021). Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*. Angewandte Chemie (International ed. in English), 60(44), 23540-23544. https://doi.org/10.1002/anie.202102758
Lesovoy, Dmitry M, et al. "Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*." Angewandte Chemie (International ed. in English) vol. 60,44 (2021): 23540-23544. doi: https://doi.org/10.1002/anie.202102758
Lesovoy DM, Georgoulia PS, Diercks T, Matečko-Burmann I, Burmann BM, Bocharov EV, Bermel W, Orekhov VY. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*. Angew Chem Int Ed Engl. 2021 Oct 25;60(44):23540-23544. doi: 10.1002/anie.202102758. Epub 2021 Jul 13. PMID: 34143912; PMCID: PMC8596425.
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NMR assignments and secondary structure distribution of emfourin, a novel proteinaceous protease inhibitor.

Biomolecular NMR assignments

Bozin TN, Chukhontseva KN, Lesovoy DM, Filatov VV, Kozlovskiy VI, Demidyuk IV, Bocharov EV.
PMID: 34091855
Biomol NMR Assign. 2021 Jun 06; doi: 10.1007/s12104-021-10030-x. Epub 2021 Jun 06.

Emfourin (M4in) from Serratia proteamaculans is a new proteinaceous inhibitor of protealysin-like proteases (PLPs), a subgroup of the well-known and widely represented metallopeptidase M4 family. Although the biological role of PLPs is debatable, data published indicate their involvement in...

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Bozin TN, Chukhontseva KN, Lesovoy DM, et al. NMR assignments and secondary structure distribution of emfourin, a novel proteinaceous protease inhibitor. Biomol NMR Assign. 2021;doi: 10.1007/s12104-021-10030-x.
Bozin, T. N., Chukhontseva, K. N., Lesovoy, D. M., Filatov, V. V., Kozlovskiy, V. I., Demidyuk, I. V., & Bocharov, E. V. (2021). NMR assignments and secondary structure distribution of emfourin, a novel proteinaceous protease inhibitor. Biomolecular NMR assignments, . https://doi.org/10.1007/s12104-021-10030-x
Bozin, Timur N, et al. "NMR assignments and secondary structure distribution of emfourin, a novel proteinaceous protease inhibitor." Biomolecular NMR assignments vol. (2021). doi: https://doi.org/10.1007/s12104-021-10030-x
Bozin TN, Chukhontseva KN, Lesovoy DM, Filatov VV, Kozlovskiy VI, Demidyuk IV, Bocharov EV. NMR assignments and secondary structure distribution of emfourin, a novel proteinaceous protease inhibitor. Biomol NMR Assign. 2021 Jun 06; doi: 10.1007/s12104-021-10030-x. Epub 2021 Jun 06. PMID: 34091855.
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All.

Journal of medicinal chemistry

Bocharov EV, Gremer L, Urban AS, Okhrimenko IS, Volynsky PE, Nadezhdin KD, Bocharova OV, Kornilov DA, Zagryadskaya YA, Kamynina AV, Kuzmichev PK, Kutzsche J, Bolakhrif N, Müller-Schiffmann A, Dencher NA, Arseniev AS, Efremov RG, Gordeliy VI, Willbold D.
PMID: 34739758
J Med Chem. 2021 Nov 25;64(22):16464-16479. doi: 10.1021/acs.jmedchem.1c00632. Epub 2021 Nov 05.

Alzheimer's disease (AD) is a severe neurodegenerative pathology with no effective treatment known. Toxic amyloid-β peptide (Aβ) oligomers play a crucial role in AD pathogenesis. All

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Bocharov EV, Gremer L, Urban AS, et al. All. J Med Chem. 2021;64(22):16464-16479doi: 10.1021/acs.jmedchem.1c00632.
Bocharov, E. V., Gremer, L., Urban, A. S., Okhrimenko, I. S., Volynsky, P. E., Nadezhdin, K. D., Bocharova, O. V., Kornilov, D. A., Zagryadskaya, Y. A., Kamynina, A. V., Kuzmichev, P. K., Kutzsche, J., Bolakhrif, N., Müller-Schiffmann, A., Dencher, N. A., Arseniev, A. S., Efremov, R. G., Gordeliy, V. I., & Willbold, D. (2021). All. Journal of medicinal chemistry, 64(22), 16464-16479. https://doi.org/10.1021/acs.jmedchem.1c00632
Bocharov, Eduard V, et al. "All." Journal of medicinal chemistry vol. 64,22 (2021): 16464-16479. doi: https://doi.org/10.1021/acs.jmedchem.1c00632
Bocharov EV, Gremer L, Urban AS, Okhrimenko IS, Volynsky PE, Nadezhdin KD, Bocharova OV, Kornilov DA, Zagryadskaya YA, Kamynina AV, Kuzmichev PK, Kutzsche J, Bolakhrif N, Müller-Schiffmann A, Dencher NA, Arseniev AS, Efremov RG, Gordeliy VI, Willbold D. All. J Med Chem. 2021 Nov 25;64(22):16464-16479. doi: 10.1021/acs.jmedchem.1c00632. Epub 2021 Nov 05. PMID: 34739758.
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Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments.

Acta naturae

Mineev KS, Bocharov EV, Volynsky PE, Goncharuk MV, Tkach EN, Ermolyuk YS, Schulga AA, Chupin VV, Maslennikov IV, Efremov RG, Arseniev AS.
PMID: 22649687
Acta Naturae. 2011 Apr;3(2):90-8.

Specific interactions between transmembrane α-helices, to a large extent, determine the biological function of integral membrane proteins upon normal development and in pathological states of an organism. Various membrane-like media, partially those mimicking the conditions of multicomponent biological membranes,...

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Mineev KS, Bocharov EV, Volynsky PE, et al. Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments. Acta Naturae. 2011;3(2):90-8
Mineev, K. S., Bocharov, E. V., Volynsky, P. E., Goncharuk, M. V., Tkach, E. N., Ermolyuk, Y. S., Schulga, A. A., Chupin, V. V., Maslennikov, I. V., Efremov, R. G., & Arseniev, A. S. (2011). Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments. Acta naturae, 3(2), 90-8.
Mineev, K S, et al. "Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments." Acta naturae vol. 3,2 (2011): 90-8.
Mineev KS, Bocharov EV, Volynsky PE, Goncharuk MV, Tkach EN, Ermolyuk YS, Schulga AA, Chupin VV, Maslennikov IV, Efremov RG, Arseniev AS. Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments. Acta Naturae. 2011 Apr;3(2):90-8. PMID: 22649687; PMCID: PMC3347579.
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Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment.

Acta naturae

Goncharuk SA, Goncharuk MV, Mayzel ML, Lesovoy DM, Chupin VV, Bocharov EV, Arseniev AS, Kirpichnikov MP.
PMID: 22649697
Acta Naturae. 2011 Jul;3(3):77-84.

The fibroblast growth factor receptor 3 (FGFR3) is a protein belonging to the family of receptor tyrosine kinases. FGFR3 plays an important role in human skeletal development. Mutations in this protein, including Gly380Arg or Ala391Glu substitutions in the transmembrane...

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Goncharuk SA, Goncharuk MV, Mayzel ML, et al. Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment. Acta Naturae. 2011;3(3):77-84
Goncharuk, S. A., Goncharuk, M. V., Mayzel, M. L., Lesovoy, D. M., Chupin, V. V., Bocharov, E. V., Arseniev, A. S., & Kirpichnikov, M. P. (2011). Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment. Acta naturae, 3(3), 77-84.
Goncharuk, S A, et al. "Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment." Acta naturae vol. 3,3 (2011): 77-84.
Goncharuk SA, Goncharuk MV, Mayzel ML, Lesovoy DM, Chupin VV, Bocharov EV, Arseniev AS, Kirpichnikov MP. Bacterial Synthesis and Purification of Normal and Mutant Forms of Human FGFR3 Transmembrane Segment. Acta Naturae. 2011 Jul;3(3):77-84. PMID: 22649697; PMCID: PMC3347607.
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Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?.

Frontiers in neuroscience

Post MR, Lieberman OJ, Mosharov EV.
PMID: 29593491
Front Neurosci. 2018 Mar 14;12:161. doi: 10.3389/fnins.2018.00161. eCollection 2018.

Several lines of evidence place alpha-synuclein (aSyn) at the center of Parkinson's disease (PD) etiology, but it is still unclear why overexpression or mutated forms of this protein affect some neuronal populations more than others. Susceptible neuronal populations in...

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Post MR, Lieberman OJ, Mosharov EV. Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?. Front Neurosci. 2018;12:161doi: 10.3389/fnins.2018.00161.
Post, M. R., Lieberman, O. J., & Mosharov, E. V. (2018). Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?. Frontiers in neuroscience, 12161. https://doi.org/10.3389/fnins.2018.00161
Post, Michael R, et al. "Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?." Frontiers in neuroscience vol. 12 (2018): 161. doi: https://doi.org/10.3389/fnins.2018.00161
Post MR, Lieberman OJ, Mosharov EV. Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?. Front Neurosci. 2018 Mar 14;12:161. doi: 10.3389/fnins.2018.00161. eCollection 2018. PMID: 29593491; PMCID: PMC5861202.
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An Easy-to-Implement Protocol for Preparing Postnatal Ventral Mesencephalic Cultures.

Frontiers in cellular neuroscience

Lautenschläger J, Mosharov EV, Kanter E, Sulzer D, Kaminski Schierle GS.
PMID: 29556177
Front Cell Neurosci. 2018 Mar 02;12:44. doi: 10.3389/fncel.2018.00044. eCollection 2018.

Postnatally derived cultures of ventral mesencephalic neurons offer several crucial advantages over embryonic ventral mesencephalic cultures, including a higher content of TH-positive cells and the ability to derive cells from the substantia nigra, which contains the neurons most vulnerable...

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Lautenschläger J, Mosharov EV, Kanter E, et al. An Easy-to-Implement Protocol for Preparing Postnatal Ventral Mesencephalic Cultures. Front Cell Neurosci. 2018;12:44doi: 10.3389/fncel.2018.00044.
Lautenschläger, J., Mosharov, E. V., Kanter, E., Sulzer, D., & Kaminski Schierle, G. S. (2018). An Easy-to-Implement Protocol for Preparing Postnatal Ventral Mesencephalic Cultures. Frontiers in cellular neuroscience, 1244. https://doi.org/10.3389/fncel.2018.00044
Lautenschläger, Janin, et al. "An Easy-to-Implement Protocol for Preparing Postnatal Ventral Mesencephalic Cultures." Frontiers in cellular neuroscience vol. 12 (2018): 44. doi: https://doi.org/10.3389/fncel.2018.00044
Lautenschläger J, Mosharov EV, Kanter E, Sulzer D, Kaminski Schierle GS. An Easy-to-Implement Protocol for Preparing Postnatal Ventral Mesencephalic Cultures. Front Cell Neurosci. 2018 Mar 02;12:44. doi: 10.3389/fncel.2018.00044. eCollection 2018. PMID: 29556177; PMCID: PMC5840158.
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Dataset of phytoplankton productive parameters and environmental forces in autumn in the Kara Sea.

Data in brief

Mosharov SA, Sergeeva VM, Kremenetskiy VV, Sazhin AF, Stepanova SV.
PMID: 30705927
Data Brief. 2019 Jan 06;22:821-825. doi: 10.1016/j.dib.2019.01.001. eCollection 2019 Feb.

This data article contains data on the photosynthetic activity, shares of the main algae groups in the total phytoplankton biomass and the main environmental forces in the Kara Sea. The data were collected from 17 to 29 of September,...

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Mosharov SA, Sergeeva VM, Kremenetskiy VV, et al. Dataset of phytoplankton productive parameters and environmental forces in autumn in the Kara Sea. Data Brief. 2019;22:821-825doi: 10.1016/j.dib.2019.01.001.
Mosharov, S. A., Sergeeva, V. M., Kremenetskiy, V. V., Sazhin, A. F., & Stepanova, S. V. (2019). Dataset of phytoplankton productive parameters and environmental forces in autumn in the Kara Sea. Data in brief, 22821-825. https://doi.org/10.1016/j.dib.2019.01.001
Mosharov, Sergey A, et al. "Dataset of phytoplankton productive parameters and environmental forces in autumn in the Kara Sea." Data in brief vol. 22 (2019): 821-825. doi: https://doi.org/10.1016/j.dib.2019.01.001
Mosharov SA, Sergeeva VM, Kremenetskiy VV, Sazhin AF, Stepanova SV. Dataset of phytoplankton productive parameters and environmental forces in autumn in the Kara Sea. Data Brief. 2019 Jan 06;22:821-825. doi: 10.1016/j.dib.2019.01.001. eCollection 2019 Feb. PMID: 30705927; PMCID: PMC6348287.
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