Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Tyler P. Molitor"'
Autor:
Tyler P. Molitor, Enchi Liu, Alyssa M. A. Toda, Kristin M. Andruska, Molly Murphy, Paul Wren, Jessica M. Bright, Holly J. Carlisle, Carrolee Barlow
Publikováno v:
Movement Disorders
Background A common genetic mutation that causes Parkinson's disease (PD) is the G2019S LRRK2 mutation. A precision medicine approach that selectively blocks only excess kinase activity of the mutant allele could yield a safe and effective treatment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed6d2a9bbbc45b4e28d085fae888ae77
https://doi.org/10.1002/mds.28490
https://doi.org/10.1002/mds.28490
P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicity
Autor:
Marc Bolliger, Anna Memou, Hardy J. Rideout, Alexia F. Kalogeropulou, William H. Wilson, Jing Zhao, R. Jeremy Nichols, Tyler P. Molitor, Shreya Narasimha
Publikováno v:
Biochemical Journal. 475:1271-1293
Autosomal-dominant, missense mutations in the leucine-rich repeat protein kinase 2 (LRRK2) gene are the most common genetic predisposition to develop Parkinson's disease (PD). LRRK2 kinase activity is increased in several pathogenic mutations (N1437H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96946c4f8b27e2952762a39a49de42a9
https://doi.org/10.1042/bcj20170699
https://doi.org/10.1042/bcj20170699
Publikováno v:
Biochemical Journal
LRRK2 is normally phosphorylated at Ser910/935/955/973, but is dephosphorylated in certain PD associated mutations and after kinase inhibition. We ascribe a novel functional significance to the regulation of Ser910/935 as a switch for LRRK2 ubiquitin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feb3fd264ba2bf8151c9ed536b803729
http://europepmc.org/articles/PMC4613513
http://europepmc.org/articles/PMC4613513
Autor:
Paula Traktman, Tyler P. Molitor
Publikováno v:
Molecular Biology of the Cell
The VRK1 protein kinase regulates the phosphorylation of BAF, which binds to dsDNA and LEM domain–containing proteins. VRK1 depletion increases the immobile fraction of BAF at the nuclear periphery and disturbs nuclear envelope architecture. It als
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a3e3915e3b3218d5f9f0961780db25f
https://doi.org/10.1091/mbc.e13-10-0603
https://doi.org/10.1091/mbc.e13-10-0603
Publikováno v:
Biology of Reproduction. 82:182-193
The VRK1 protein kinase has been implicated as a pro-proliferative factor. Genetic analyses of mutant alleles of the Drosophila and Caenorhabditis elegans VRK1 homologs have revealed phenotypes ranging from embryonic lethality to mitotic and meiotic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2511893ffc8db343afe505bf5b50b2b8
https://doi.org/10.1095/biolreprod.109.079095
https://doi.org/10.1095/biolreprod.109.079095
Publikováno v:
Biology of reproduction. 82(1)
The VRK1 protein kinase has been implicated as a pro-proliferative factor. Genetic analyses of mutant alleles of the Drosophila and Caenorhabditis elegans VRK1 homologs have revealed phenotypes ranging from embryonic lethality to mitotic and meiotic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c41d15e78ec0daac8b0524041e778b06
https://pubmed.ncbi.nlm.nih.gov/19696012
https://pubmed.ncbi.nlm.nih.gov/19696012
Autor:
Paula Traktman, Tyler P. Molitor
Publikováno v:
Oncogenesis
The vaccinia-related kinases (VRKs) comprise a branch of the casein kinase family. VRK1, a ser/thr kinase with a nuclear localization, is the most well-studied paralog and has been described as a proproliferative protein. In lower eukaryotes, a loss
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e3fa28f3b1a4d92292bc0d66a3b5d25
http://europepmc.org/articles/PMC3740298
http://europepmc.org/articles/PMC3740298