Хайлтын үр дүнгүүд - Jean‐Marc Taymans

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  1. 1
    LRRK2 Kinase Inhibition as a Therapeutic Strategy for Parkinson's Disease, Where Do We Stand?

    LRRK2 Kinase Inhibition as a Therapeutic Strategy for Parkinson's Disease, Where Do We Stand? -н Jean‐Marc Taymans, Elisa Greggio

    Хэвлэсэн 2016
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  2. 2
    Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, α‐synuclein, and tau

    Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, α‐synuclein, and tau -н Jean‐Marc Taymans, Mark Cookson

    Хэвлэсэн 2010
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    Artigo
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  3. 3
    Distribution of PINK1 and LRRK2 in rat and mouse brain

    Distribution of PINK1 and LRRK2 in rat and mouse brain -н Jean‐Marc Taymans, Chris Van den Haute, Veerle Baekelandt

    Хэвлэсэн 2006
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  4. 4
    Alpha-Synuclein and Lipids: The Elephant in the Room?

    Alpha-Synuclein and Lipids: The Elephant in the Room? -н Alessia Sarchione, Antoine Marchand, Jean‐Marc Taymans, Marie‐Christine Chartier‐Harlin

    Хэвлэсэн 2021
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  5. 5
    LRRK2 Phosphorylation, More Than an Epiphenomenon

    LRRK2 Phosphorylation, More Than an Epiphenomenon -н Antoine Marchand, Matthieu Drouyer, Alessia Sarchione, Marie‐Christine Chartier‐Harlin, Jean‐Marc Taymans

    Хэвлэсэн 2020
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  6. 6
    Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation

    Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation -н Evy Lobbestael, Laura Civiero, Tina De Wit, Jean‐Marc Taymans, Elisa Greggio, Veerle Baekelandt

    Хэвлэсэн 2016
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    Artigo
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  7. 7
    Automated quantitative gait analysis in animal models of movement disorders

    Automated quantitative gait analysis in animal models of movement disorders -н Caroline Vandeputte, Jean‐Marc Taymans, Cindy Casteels, Frea Coun, Yicheng Ni, Koen Van Laere, Veerle Baekelandt

    Хэвлэсэн 2010
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  8. 8
    The Parkinson's Disease Associated LRRK2 Exhibits Weaker In Vitro Phosphorylation of 4E-BP Compared to Autophosphorylation

    The Parkinson's Disease Associated LRRK2 Exhibits Weaker In Vitro Phosphorylation of 4E-BP Compared to Autophosphorylation -н Azad Kumar, Elisa Greggio, Alexandra Beilina, Alice Kaganovich, Diane Chan, Jean‐Marc Taymans, Benjamin Wolozin, Mark Cookson

    Хэвлэсэн 2010
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  9. 9
    LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding

    LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding -н Jean‐Marc Taymans, Renée Vancraenenbroeck, Petri Ollikainen, Alexandra Beilina, Evy Lobbestael, Marc De Maeyer, Veerle Baekelandt, Mark Cookson

    Хэвлэсэн 2011
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  10. 10
    Resistance of HIV-1 reverse transcriptase against [2',5'-bis-O-(tert-butyldimethylsilyl)-3'-spiro-5“-(4”-amino-1“,2”- oxathiole-2“,2”-dioxide)] (TSAO) derivatives is determined by the mutation Glu138–>Lys on the p51 subunit.

    Resistance of HIV-1 reverse transcriptase against [2',5'-bis-O-(tert-butyldimethylsilyl)-3'-spiro-5“-(4”-amino-1“,2”- oxathiole-2“,2”-dioxide)] (TSAO) derivatives is determined by... -н Heidi Jonckheere, Jean‐Marc Taymans, Jan Balzarini, Sonsoles Velázquez, Marı́a-José Camarasa, Jan Desmyter, Erik De Clercq, Jozef Anné

    Хэвлэсэн 1994
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  11. 11
    In silico, in vitro and cellular analysis with a kinome-wide inhibitor panel correlates cellular LRRK2 dephosphorylation to inhibitor activity on LRRK2

    In silico, in vitro and cellular analysis with a kinome-wide inhibitor panel correlates cellular LRRK2 dephosphorylation to inhibitor activity on LRRK2 -н Renée Vancraenenbroeck, Joren De Raeymaecker, Evy Lobbestael, Fangye Gao, Marc De Maeyer, Arnout Voet, Veerle Baekelandt, Jean‐Marc Taymans

    Хэвлэсэн 2014
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  12. 12
    Perspective on the current state of the LRRK2 field

    Perspective on the current state of the LRRK2 field -н Jean‐Marc Taymans, Matt Fell, Tim Greenamyre, Warren D. Hirst, Adamantios Mamais, Shalini Padmanabhan, Inga Peter, Hardy J. Rideout, Avner Thaler

    Хэвлэсэн 2023
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  13. 13
    Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis

    Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis -н Loukia Parisiadou, Chengsong Xie, Hyun Jin Cho, Xian Lin, Xinglong Gu, Caixia Long, Evy Lobbestael, Veerle Baekelandt, Jean‐Marc Taymans, Lixin Sun, Huaibin Cai

    Хэвлэсэн 2009
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  14. 14
    The Current State-of-the Art of LRRK2-Based Biomarker Assay Development in Parkinson’s Disease

    The Current State-of-the Art of LRRK2-Based Biomarker Assay Development in Parkinson’s Disease -н Hardy J. Rideout, Marie‐Christine Chartier‐Harlin, Matthew Fell, Warren D. Hirst, Sarah Huntwork‐Rodriguez, Cheryl E. G. Leyns, Omar S. Mabrouk, Jean‐Marc Taymans

    Хэвлэсэн 2020
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  15. 15
    The Parkinson’s disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites

    The Parkinson’s disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites -н Elisa Greggio, Jean‐Marc Taymans, Yuejun Zhen, John Ryder, Renée Vancraenenbroeck, Alexandra Beilina, Peng Sun, Junpeng Deng, Howard Jaffe, Veerle Baekelandt, Kalpana Merchant, Mark Cookson

    Хэвлэсэн 2009
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  16. 16
    Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

    Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant -н Veronique Daniëls, Renée Vancraenenbroeck, Bernard M. H. Law, Elisa Greggio, Evy Lobbestael, Fangye Gao, Marc De Maeyer, Mark Cookson, Kirsten Harvey, Veerle Baekelandt, Jean‐Marc Taymans

    Хэвлэсэн 2010
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  17. 17
    Inhibition of FK506 Binding Proteins Reduces α-Synuclein Aggregation and Parkinson's Disease-Like Pathology

    Inhibition of FK506 Binding Proteins Reduces α-Synuclein Aggregation and Parkinson's Disease-Like Pathology -н Melanie Gérard, Angélique Deleersnijder, Veronique Daniëls, Sarah Schreurs, Sebastian Munck, Veerle Reumers, Hans Pottel, Yves Engelborghs, Chris Van den Haute, Jean‐Marc Taymans, Zeger Debyser, Veerle Baekelandt

    Хэвлэсэн 2010
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  18. 18
    Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle

    Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle -н Evy Lobbestael, Jing Zhao, Iakov N. Rudenko, Aleksandra Beylina, Fangye Gao, Justin Wetter, Monique Beullens, Mathieu Bollen, Mark Cookson, Veerle Baekelandt, R. Jeremy Nichols, Jean‐Marc Taymans

    Хэвлэсэн 2013
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  19. 19
    GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2

    GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2 -н Marian Blanca Ramírez, Antonio Jesús Lara Ordóñez, Elena Fdez, Jesús Madero‐Pérez, Adriano Gonnelli, Matthieu Drouyer, Marie‐Christine Chartier‐Harlin, Jean‐Marc Taymans, Luigi Bubacco, Elisa Greggio, Sabine Hilfiker

    Хэвлэсэн 2017
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  20. 20
    Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes

    Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes -н Kushal Sejwal, Mohamed Chami, Hervé Remigy, Renée Vancraenenbroeck, William Sibran, Rosmarie Sütterlin, Paul Baumgartner, Robert A. McLeod, Marie‐Christine Chartier‐Harlin, Veerle Baekelandt, Henning Stahlberg, Jean‐Marc Taymans

    Хэвлэсэн 2017
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