Results 121 to 130 of about 28,054 (245)

PREDICT‐PD: A Two‐Stage Approach to Early Identification of Parkinson's Disease

Movement Disorders Clinical Practice, EarlyView.
Sasivimol Virameteekul, Sheena Waters, Brook Huxford, Ashvin Kuri, Manuela Tan, Laura Pérez‐Carbonell, Eduardo de Pablo‐Fernández, Anette Schrag, Alastair J. Noyce, Cristina Simonet   +9 more
wiley   +1 more source

Heterogenous Neuropathology in a Pedigree with RAB39B‐Related Parkinson's Disease

Movement Disorders, EarlyView.
Abstract Background In 2015, we reported a family with Parkinson's disease resulting from the RAB39B p.G192R (c.574G>A) variant. Since then, two affected brothers from the family have undergone autopsy. Objectives To characterize neuropathological findings, assess intracellular distribution of RAB39B protein, and examine the effect of p.G192R on α ...
Caitlin Latimer, Oswaldo Lorenzo‐Betancor, Dong‐Hui Chen, Kimmy Su, Marika Bogdani, Anna J. Park, Minsuh Kim, Joshua Weiss, Malia Callier, Ella H. Chiu, Sarah Fish, Jennifer L. Witt, Wendy H. Raskind, Marie Y. Davis, C. Dirk Keene, Cyrus P. Zabetian   +15 more
wiley   +1 more source

Electroencephalography‐Based Clustering Reveals Robust Neurophysiological Subtypes in Parkinson's Disease

Movement Disorders, EarlyView.
Abstract Background Parkinson's disease (PD) is clinically heterogeneous, with substantial variability in motor and cognitive features. Conventional clinical scales provide limited insight into underlying neural mechanisms and show poor longitudinal stability.
Daniel Vered, Zoya Katzir, Idan Daniel Grosbard, Avner Thaler, Inbal Maidan   +4 more
wiley   +1 more source

Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis [PDF]

, 2017
We previously reported that Parkinson's disease (PD) kinase LRRK2 phosphorylates a subset of Rab GTPases on a conserved residue in their switch-II domains (Steger et al., 2016) (PMID: 26824392). Here, we systematically analyzed the Rab protein family and
Alessi, Dario R., Dhekne, Herschel S., Diez, Federico, Karayel, Ozge, Lis, Pawel, Lorentzen, Esben, Mann, Matthias, Martinez, Terina N., Nirujogi, Raja S., Pfeffer, Suzanne R., Steger, Martin, Tonelli, Francesca   +11 more
core   +3 more sources

LRRK2 G2019S Promotes Colon Cancer Potentially via LRRK2–GSDMD Axis-Mediated Gut Inflammation

Cells
Leucine-rich repeat kinase 2 (LRRK2) is a serine–threonine protein kinase belonging to the ROCO protein family. Within the kinase domain of LRRK2, a point mutation known as LRRK2 G2019S has emerged as the most prevalent variant associated with Parkinson ...
Yuhang Wang, Joyce Z. Gao, Taylor Sakaguchi, Thorsten Maretzky, Prajwal Gurung, Nandakumar S. Narayanan, Sarah Short, Yiqin Xiong, Zizhen Kang   +8 more
doaj   +1 more source

Lack of Cerebrospinal Fluid α‐Synuclein Seeding in VPS35 D620N‐ and LRRK2 Y1699C‐Linked Parkinson's Disease

Movement Disorders, EarlyView.
Letizia Santinelli, Neringa Pratuseviciute, Lara M. Lange, Teresa Kleinz, Norbert Brüggemann, Linn Streubel‐Gallasch, Meret Möller, Alexander Zimprich, Christof Brücke, Jean‐Marc Good, Norman Griebner, Shalini Padmanabhan, Philip Seibler, Peter Bauer, Wim Vandenberghe, Esther Sammler, Cornelis Blauwendraat, Christine Klein, Max Borsche   +18 more
wiley   +1 more source

Rare‐Variant Burden across Lysosomal Genes Implicates Sialylation and Ganglioside Metabolism in Parkinson's Disease

Movement Disorders, EarlyView.
Abstract Background Lysosomal dysfunction is central to Parkinson's disease (PD) pathogenesis, with GBA1 representing the strongest established genetic risk factor. Numerous other genes involved in lysosomal sphingolipid, glycosphingolipid, and ceramide metabolism have been proposed as contributors to PD, highlighting the need for genetic analyses ...
Konstantin Senkevich, Sitki Cem Parlar, Cloe Chantereault, Lang Liu, Eric Yu, Uladzislau Rudakou, Jamil Ahmad, Jennifer A. Ruskey, Farnaz Asayesh, Dan Spiegelman, Cheryl Waters, Oury Monchi, Yves Dauvilliers, Nicolas Dupré, Lior Greenbaum, Sharon Hassin‐Baer, Irina Miliukhina, Alla Timofeeva, Anton Emelyanov, Sofya Pchelina, Roy N. Alcalay, Ziv Gan‐Or   +21 more
wiley   +1 more source

Neurodegenerative phenotypes in an A53T α-synuclein transgenic mouse model are independent of LRRK2 [PDF]

, 2017
Mutations in the genes encoding LRRK2 and α-synuclein cause autosomal dominant forms of familial Parkinson's disease (PD). Fibrillar forms of α-synuclein are a major component of Lewy bodies, the intracytoplasmic proteinaceous inclusions that are a ...
Biskup, Saskia, Daher, João Paulo L., Dawson, Ted M., Dawson, Valina L., Galter, Dagmar, Gellhaar, Sandra, Lee, Michael K., Moore, Darren J., Musso, Alessandra, Pletnikova, Olga, Troncoso, Juan C.   +10 more
core  

Crystal structure of the WD40 domain dimer of LRRK2 [PDF]

, 2019
Leucine-rich repeat kinase 2 (LRRK2) is a large multidomain protein with both a Ras of complex (ROC) domain and a kinase domain (KD) and, therefore, exhibits both GTPase and kinase activities.
Dario R. Alessi, de Rijk, Hao Wu, Heng Ru, Li Wang, Pengfei Zhang, Shojaee, Susan S. Taylor, Tan, Venkat Giri Magupalli, Ying Fan, Zhang   +11 more
core   +2 more sources

What Have We Learned from Cerebrospinal Fluid Studies about Biomarkers for Detecting LRRK2 Parkinson’s Disease Patients and Healthy Subjects with Parkinson’s-Associated LRRK2 Mutations?

Journal of Parkinson’s Disease, 2019
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are the most common known cause of autosomal dominant Parkinson’s disease (PD) and sporadic PD (sPD).
David A. Loeffler, Jan O. Aasly, Peter A. LeWitt, Mary P. Coffey   +3 more
doaj   +1 more source