Лаборатория генетического моделирования нейродегенеративных процессов

Бухман Владимир Львович канд. биол. наук

Ведущий научный сотрудник лаборатории.


Область научных интересов: Нейродегенеративные заболевания, семейство синуклеинов, синуклеинопатии, повреждения мозга, агрегация белков, ДНК/РНК-связывающие белки, нейропротекция.


Научные награды, общества:

- Член совета (Member of the Council) общества нейротоксикологов (Neurotoxisity Society) 2007-2010 и 2015-2019;
- Член редакционной коллегии журналов: Neurotoxicity Research (2010-2016); Journal of Alzheimer’s Disease (2013-2019); Scientific Reports (2016-2019);
- Член Комиссии по распределению грантов по исследованиям болезни Паркинсона Великобритании (Parkinson's UK Grant Assessment Panel GAP1) 2016-2019;
- Являлся членом Комиссии по распределению грантов по исследованиям болезни Альцгеймера Великобритании (Alzheimer’s Society Research Grant Panel);
- Являлся членом экспертного совета Фонда Сколково;


Контакты

buchmanvl@cardiff.ac.uk


Избранные публикации

M.H.R.Ludtmann, P.R.Angelova, N.N.Ninkina, S.Gandhi, V.L.Buchman* and A.Y.Abramov (2016) Monomeric alpha-synuclein exerts a physiological role on brain ATP synthase. Journal of Neuroscience, 36, 10510-10521

N.Connor-Robson, S.Millership, O.Peters, N.Ninkina and V.L.Buchman* (2016) Combinational losses of synucleins reveal their differential requirements for compensating age-dependent alterations in motor behavior and dopamine metabolism. Neurobiology of Aging, 46, 107-112

M.-B.Fares, B.Maco, A.Oueslati, E.Rockenstein, N.Ninkina, V.L.Buchman, E.Masliah and H.A.Lashuel (2016) Induction of de novo α-synuclein fibrillization in a novel neuronal model for Parkinson's disease. Proc. Natl. Acad. Sci. USA, 113, E912-921

N.Ninkina, N.Connor-Robson, A.A.Ustyugov, T.V.Tarasova, T.A.Shelkovnikova and V.L.Buchman* (2015) A novel resource for studying function and dysfunction of α-synuclein: mouse lines for modulation of endogenous Snca gene expression. Scientific Reports, 5, 16615

H.K.Robinson, A.V.Deykin, E.V. Bronovitsky, R.K.Ovchinnikov, A.A.Ustyugov, T.A.Shelkovnikova, M.S.Kukharsky, T.G.Ermolkevich, I.L.Goldman, E.R.Sadchikova, E.A.Kovrazhkina, S.O.Bachurin, V.L.Buchman* and N.N.Ninkina (2015) Early lethality and neuronal proteinopathy in mice expressing cytoplasm-targeted FUS that lacks the RNA recognition motif. Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, 16, 402-409

O.M.Peters, T.A.Shelkovnikova, J.R.Highley, J.Cooper-Knock, T.Hortobágyi, C.Troakes, N.N.Ninkina and V.L.Buchman* (2015) Gamma-synuclein pathology in amyotrophic lateral sclerosis. Annals of Clinical and Translational Neurology, 2, 29-37

T.A.Shelkovnikova, H.K.Robinson, J.A.Southcombe, N.Ninkina and V.L.Buchman* (2014) Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms. Human Molecular Genetics, 23, 5211-5226

T.A.Shelkovnikova, H.K.Robinson, C.Troakes, N.Ninkina and V.L.Buchman* (2014) Compromised paraspeckle formation as a pathogenic factor in FUSopathies. Human Molecular Genetics, 23, 2298-2312

T.A.Shelkovnikova, H.K.Robinson, N.Connor-Robson and V.L.Buchman* (2013) Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasm. Cell Cycle, 12, 3194-3202

P.Garcia-Reitböck, O.Anichtchik, J.W.Dalley, N.Ninkina, G.K.Tofaris, V.L.Buchman and M.G.Spillantini (2013) Endogenous alpha-synuclein influences the number of dopaminergic neurons in mouse substantia nigra. Experimental Neurology, 248, 541-545

T.A.Shelkovnikova, O.M.Peters, A.V.Deykin, N.Connor-Robson, H.Robinson, A.A.Ustyugov, S.O.Bachurin, T.G.Ermolkevich, I.L.Goldman, E.R.Sadchikova, E.A.Kovrazhkina, V.I.Skvortsova, S.Ling, S.Da Cruz, P.A.Parone, V.L.Buchman* and N.N.Ninkina (2013) Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice. Journal of Biological Chemistry, 288, 25266-25274

J.Cooper-Knock, A.Higginbottom, N.Connor-Robson, N.Bayatt, J.J.Bury, J.Kirby, N.Ninkina, V.L.Buchman and P.J.Shaw (2013) C9ORF72 transcription in a frontotemporal dementia case with two expanded alleles. Neurology, 81, 1719-1721

S.Millership, N.Ninkina, J.J.Rochford and V.L.Buchman* (2013) γ-synuclein is a novel player in the control of body lipid metabolism. Adipocyte, 2, 276-280

O.Peters, T.A.Shelkovnikova, T.Tarasova, S.Springe, M.S.Kukharsky, G.A.Smith, S.Brooks, S.A.Kozin, Y.Kotelevtsev, S.O.Bachurin, N.N.Ninkina and V.L.Buchman* (2013) Chronic administration of dimebon does not ameliorate amyloid-β pathology in 5xFAD transgenic mice. Journal of Alzheimer’s Disease, 36, 589-596

V.L.Buchman*, J.Cooper-Knock, N.Connor-Robson, A.Higginbottom, J.Kirby, O.D.Razinskaya, N.Ninkina and P.J.Shaw (2013) Simultaneous and independent detection of C9ORF72 alleles with low and high number of GGGGCC repeats using an optimised protocol of Southern blot hybridisation. Molecular Neurodegeneration, 8, 12

O.Peters, N.Connor-Robson, V.B.Sokolov, A.Yu.Aksinenko, M.S.Kukharsky, S.O.Bachurin, N.N.Ninkina and V.L.Buchman* (2013) Chronic administration of dimebon ameliorates pathology in tauP301S transgenic mice. Journal of Alzheimer’s Disease, 33, 1041-1049

S.Millership, N.Ninkina, I.Guschina, J.Norton, R.Brambilla, P.Oort, S.Adams, R.J.Dennis, P.Voshol, J.J.Rochford and V.L.Buchman* (2012) Increased lipolysis and altered lipid homeostasis protect γ-synuclein null mutant mice from diet-induced obesity. Proc. Natl. Acad. Sci. USA, 109, 20943-20948

N.Ninkina, O.Peters, N.Connor-Robson, O.Lytkina, E.Sharfeddin and V.L.Buchman* (2012) Contrasting effects of α-synuclein and γ-synuclein on the phenotype of Cysteine String Protein alpha (CSPα) null mutant mice suggest distinct function of these proteins in neuronal synapses. Journal of Biological Chemistry, 287, 44471-44477

O.Peters, S.J.Millership, T.A.Shelkovnikova, I.Soto, L.Keeling, A.Hann, N.Marsh-Armstrong, V.L.Buchman* and N.Ninkina (2012) Selective pattern of motor system damage in gamma-synuclein transgenic mice mirrors the respective pathology in amyotrophic lateral sclerosis. Neurobiology of Disease, 48, 124-131

* - corresponding author