Výsledky vyhledávání - "Bernd K Gilsbach"

Akademický článek

C2GAP2 is a common regulator of Ras signaling for chemotaxis, phagocytosis, and macropinocytosis

Autor: Xuehua Xu, Henderikus Pots, Bernd K. Gilsbach, Dustin Parsons, Douwe M. Veltman, Sharmila G. Ramachandra, Haoran Li, Arjan Kortholt, Tian Jin

Publikováno v: Frontiers in Immunology, Vol 13 (2022)

Phagocytosis, macropinocytosis, and G protein coupled receptor-mediated chemotaxis are Ras-regulated and actin-driven processes. The common regulator for Ras activity in these three processes remains unknown. Here, we show that C2GAP2, a Ras GTPase a

Externí odkaz: https://doaj.org/article/63ae01881cbf47c6a1fbbc45891e3fbe

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Allosteric Inhibition of Parkinson's-Linked LRRK2 by Constrained Peptides

Autor: Leah G. Helton, Panagiotis S Athanasopoulos, Bernd K Gilsbach, Scotty Hall, Ranjan Kumar Singh, Ahmed Soliman, Hardy J. Rideout, Felix von Zweydorf, Christian Johannes Gloeckner, Francesco Raimondi, Franz Y. Ho, Eileen J. Kennedy, Arjan Kortholt, Jascha Tobias Manschwetus, Timothy J LeClair, Friedrich W. Herberg, Wim Versées, Michalis Kentros

Publikováno v: ACS chemical biology 16(11), 2326-2338 (2021). doi:10.1021/acschembio.1c00487
ACS chemical biology, 16(11). AMER CHEMICAL SOC

Leucine-Rich Repeat Kinase 2 (LRRK2) is a large, multidomain protein with dual kinase and GTPase function that is commonly mutated in both familial and idiopathic Parkinson's Disease (PD). While dimerization of LRRK2 is commonly detected in PD models

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b37fc033b725a6992a27c05c3fcd9f95
https://doi.org/10.1021/acschembio.1c00487

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Structural model of the dimeric Parkinson’s protein LRRK2 reveals a compact architecture involving distant interdomain contacts

Publikováno v: 'Proceedings of the National Academy of Sciences of the USA ', vol: 113, pages: E4357-E4366 (2016)
Proceedings of the National Academy of Sciences of the United States of America, 113(30), E4357-E4366. NATL ACAD SCIENCES
Proceedings of the National Academy of Sciences of the United States of America 113(30), E4357-E4366 (2016). doi:10.1073/pnas.1523708113

Leucine-rich repeat kinase 2 (LRRK2) is a large, multidomain protein containing two catalytic domains: a Ras of complex proteins (Roc) G-domain and a kinase domain. Mutations associated with familial and sporadic Parkinson's disease (PD) have been id

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::874400366e144c61561b4b1271088eaa
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:44933

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Coordinated Ras and Rac Activity Shapes Macropinocytic Cups and Enables Phagocytosis of Geometrically Diverse Bacteria

Autor: Anton Nikolaev, Ben A. Phillips, Thierry Soldati, James H. Vines, Henderikus Pots, Jason S. King, David Traynor, Catherine M. Buckley, Aurélie Gueho, Christopher J. Munn, Arjan Kortholt, Bernd K Gilsbach, Andrew J. Parnell

Publikováno v: Current biology 30(15), 2912-2926.e5 (2020). doi:10.1016/j.cub.2020.05.049
Current Biology, Vol. 30, No 15 (2020) pp. 2912-2926
Current Biology, 30(15), 2912-2926.e5. CELL PRESS

Engulfment of extracellular material by phagocytosis or macropinocytosis depends on the ability of cells to generate specialized cup-shaped protrusions. To effectively capture and internalize their targets, these cups are organized into a ring or ruf

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e22b26e4171cbde7dce1d69d34b52af
https://doi.org/10.1016/j.cub.2020.05.049

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Biochemical and kinetic properties of the complex Roco G-protein cycle

Autor: Wim Versées, Bernd K Gilsbach, Panagiotis S Athanasopoulos, Giambattista Guaitoli, Arjan Kortholt, Alfred Wittinghofer, Margaux Leemans, Lina Wauters, Christian Johannes Gloeckner, Susanne Terheyden

Publikováno v: Biological Chemistry, 399(12), 1447-1456. Walter de Gruyter GmbH
Biological chemistry 399(12), 1447-1456 (2018). doi:10.1515/hsz-2018-0227

Roco proteins have come into focus after mutations in the gene coding for the human Roco protein Leucine-rich repeat kinase 2 (LRRK2) were discovered to be one of the most common genetic causes of late onset Parkinson’s disease. Roco proteins are c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e672c529f33ef47219f161c39b38691
https://research.rug.nl/en/publications/3e5d696b-48d5-402c-adb1-f50a20fa9880

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First model of dimeric LRRK2: the challenge of unrevealing the structure of a multidomain Parkinson's-associated protein

Autor: Bernd K Gilsbach, Giambattista Guaitoli, Christian Johannes Gloeckner, Francesco Raimondi

Publikováno v: Biochemical Society transactions 44(6), 1635-1641 (2016). doi:10.1042/BST20160226

Mutations within the leucine-rich repeat kinase 2 (LRRK2) gene represent the most common cause of Mendelian forms of Parkinson's disease, among autosomal dominant cases. Its gene product, LRRK2, is a large multidomain protein that belongs to the Roco

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::661258f235e98ab170f738faac051bc2
https://pubmed.ncbi.nlm.nih.gov/27913672

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Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations

Autor: Ingrid R. Vetter, Alfred Wittinghofer, Franz Y. Ho, Bernd K Gilsbach, Arjan Kortholt, Peter J.M. van Haastert

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 109(26), 10322-10327. NATL ACAD SCIENCES

Mutations in human leucine-rich-repeat kinase 2 (LRRK2) have been found to be the most frequent cause of late-onset Parkinson disease. Here we show that Dictyostelium discoideum Roco4 is a suitable model to study the structural and biochemical charac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d043be7a5a01a81b46496262eb981b77
https://doi.org/10.1073/pnas.1203223109

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Revisiting the Roco G-protein cycle

Autor: Bernd K Gilsbach, Susanne Terheyden, Arjan Kortholt, Alfred Wittinghofer, Franz Y. Ho

Publikováno v: Biochemical Journal, 465(1), 139-147. PORTLAND PRESS LTD

Mutations in leucine-rich-repeat kinase 2 (LRRK2) are the most frequent cause of late-onset Parkinson's disease (PD). LRRK2 belongs to the Roco family of proteins which share a conserved Ras-like G-domain (Roc) and a C-terminal of Roc (COR) domain ta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7195768c8d631260c8662535fde0e1a9
https://research.rug.nl/en/publications/de0ad625-c8e4-494b-94c4-10924f96eb88

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Structural biology of the LRRK2 GTPase and kinase domains: implications for regulation

Autor: Bernd K Gilsbach, Arjan Kortholt

Publikováno v: Frontiers in Molecular Neuroscience, 7:32. Frontiers Media SA
Frontiers in Molecular Neuroscience, Vol 7 (2014)
Frontiers in Molecular Neuroscience

Human leucine-rich-repeat kinase 2 (LRRK2) belongs to the Roco family of proteins, which are characterized by the presence of a Ras-like G-domain (Roc), a C-terminal of Roc domain (COR), and a kinase domain. Mutations in LRRK2 have been found to be t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fb7d7a1c32c102175727c40757c5eb1

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