Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Laura M. Nederveen-Schippers"'
Autor:
Egon Deyaert, Lina Wauters, Giambattista Guaitoli, Albert Konijnenberg, Margaux Leemans, Susanne Terheyden, Arsen Petrovic, Rodrigo Gallardo, Laura M. Nederveen-Schippers, Panagiotis S. Athanasopoulos, Henderikus Pots, Peter J. M. Van Haastert, Frank Sobott, Christian Johannes Gloeckner, Rouslan Efremov, Arjan Kortholt, Wim Versées
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
The Parkinson’s disease‐associated LRRK2 protein is a multidomain Roco protein with GTPase activity. Here the authors use a multidisciplinary approach to characterize the GTPase mechanism of a homologous bacterial Roco protein and give mechanisti
Externí odkaz:
https://doaj.org/article/c26addf391a34197a5007b5002985a38
Autor:
Laura M Nederveen-Schippers, Jan Willem Borst, Adrie H. Westphal, Arjan Kortholt, Victor V. Skakun, Peter J.M. van Haastert, Pragya Pathak, Ineke Keizer-Gunnink
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 14
International Journal of Molecular Sciences, Vol 22, Iss 7300, p 7300 (2021)
International Journal of Molecular Sciences, 22(14)
International Journal of Molecular Sciences, 22(14):7300. MDPI AG
International Journal of Molecular Sciences 22 (2021) 14
Volume 22
Issue 14
International Journal of Molecular Sciences, Vol 22, Iss 7300, p 7300 (2021)
International Journal of Molecular Sciences, 22(14)
International Journal of Molecular Sciences, 22(14):7300. MDPI AG
International Journal of Molecular Sciences 22 (2021) 14
Protein dimerization plays a crucial role in the regulation of numerous biological processes. However, detecting protein dimers in a cellular environment is still a challenge. Here we present a methodology to measure the extent of dimerization of GFP
Autor:
Mikalai M. Yatskou, Laura M Nederveen-Schippers, Victor V. Skakun, Arjan Kortholt, Vladimir V. Apanasovich
Publikováno v:
Journal of applied spectroscopy, 87(4), 685-692. SPRINGER
A method is proposed for the complex analysis of fluctuations in the fluorescence intensity of molecular compounds, which allows determining the structural composition of protein oligomers. The idea of the method is to analyze the photon counting his
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb996651a448f97fe59080f39d341b56
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/98321
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/98321
Publikováno v:
Biochemical Society Transactions, 44(6), 1611-1616. PORTLAND PRESS LTD
Mutations in the human leucine-rich repeat kinase 2 (LRRK2) are the most frequent cause of hereditary Parkinson's disease (PD). LRRK2 belongs to the Roco family of proteins, which are characterized by the presence of a Ras of complex proteins domain
Autor:
Giambattista Guaitoli, Frank Sobott, Rodrigo Gallardo, Arjan Kortholt, Albert Konijnenberg, Egon Deyaert, Margaux Leemans, Lina Wauters, Henderikus Pots, Peter J.M. van Haastert, Rouslan G. Efremov, Arsen Petrovic, Christian Johannes Gloeckner, Susanne Terheyden, Laura M Nederveen-Schippers, Panagiotis S Athanasopoulos, Wim Versées
Publikováno v:
Nature Communications 8(1), 1008 (2017). doi:10.1038/s41467-017-01103-4
Nature Communications, 8(1):1008, 1-12. Nature Publishing Group
'Nature Communications ', vol: 8, pages: 1008-1-1008-12 (2017)
Nature Communications
Nature communications
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Nature Communications, 8(1):1008, 1-12. Nature Publishing Group
'Nature Communications ', vol: 8, pages: 1008-1-1008-12 (2017)
Nature Communications
Nature communications
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Mutations in LRRK2 are a common cause of genetic Parkinson’s disease (PD). LRRK2 is a multi-domain Roco protein, harbouring kinase and GTPase activity. In analogy with a bacterial homologue, LRRK2 was proposed to act as a GTPase activated by dimeri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66c1251c5ffe988d0260253b63eda115