Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Agne, Kazlauskaite"'
Autor:
Giancarlo Comi, Douglas Arnold, Ralf Benedict, Christine Lebrun, Agne Kazlauskaite, Licinio Craveiro, Catherine Lubetzki
Publikováno v:
Revue Neurologique. 179:S166-S167
Autor:
Agne Kazlauskaite, Van Kelly, Clare Johnson, Carla Baillie, C. James Hastie, Mark Peggie, Thomas Macartney, Helen I. Woodroof, Dario R. Alessi, Patrick G. A. Pedrioli, Miratul M. K. Muqit
Publikováno v:
Open Biology, Vol 4, Iss 3 (2014)
Mutations in PINK1 and Parkin are associated with early-onset Parkinson's disease. We recently discovered that PINK1 phosphorylates Parkin at serine65 (Ser65) within its Ubl domain, leading to its activation in a substrate-free activity assay. We now
Externí odkaz:
https://doaj.org/article/58e6e1eca9d44c9f95b5cbdf86b81aff
Autor:
Chandana Kondapalli, Agne Kazlauskaite, Ning Zhang, Helen I. Woodroof, David G. Campbell, Robert Gourlay, Lynn Burchell, Helen Walden, Thomas J. Macartney, Maria Deak, Axel Knebel, Dario R. Alessi, Miratul M. K. Muqit
Publikováno v:
Open Biology, Vol 2, Iss 5 (2012)
Summary Missense mutations in PTEN-induced kinase 1 (PINK1) cause autosomal-recessive inherited Parkinson's disease (PD). We have exploited our recent discovery that recombinant insect PINK1 is catalytically active to test whether PINK1 directly phos
Externí odkaz:
https://doaj.org/article/a7ccab88220e49e2ad360b217db36be0
Autor:
Agne Kazlauskaite, Miratul M. K. Muqit
Publikováno v:
The Febs Journal
The discovery of mutations in genes encoding protein kinase PTEN-induced kinase 1 (PINK1) and E3 ubiquitin ligase Parkin in familial Parkinson's disease and their association with mitochondria provides compelling evidence that mitochondrial dysfuncti
Autor:
Agne, Kazlauskaite, Chandana, Kondapalli, Robert, Gourlay, David G, Campbell, Maria Stella, Ritorto, Kay, Hofmann, Dario R, Alessi, Axel, Knebel, Matthias, Trost, Miratul M K, Muqit
Publikováno v:
Biochemical Journal
We have previously reported that the Parkinson's disease-associated kinase PINK1 (PTEN-induced putative kinase 1) is activated by mitochondrial depolarization and stimulates the Parkin E3 ligase by phosphorylating Ser65 within its Ubl (ubiquitin-like
Publikováno v:
Chembiochem
Ubiquitin phosphorylation is emerging as an important regulatory layer in the ubiquitin system. This is exemplified by the phosphorylation of ubiquitin on Ser65 by the Parkinson's disease-associated kinase PINK1, which mediates the activation of the
Autor:
Susan M. Hancock, Kaihang Wang, Tamanna Haq, Nicolas Huguenin-Dezot, Agne Kazlauskaite, Jason W. Chin, Andrew M. Fry, Daniel T. Rogerson, Richard Bayliss, Miratul M. K. Muqit, Amit Sachdeva
Publikováno v:
Nature chemical biology. 11(7)
A newly engineered phosphoserine synthetase/tRNA pair allows quantitative insertion of phosphoserine or, when coupled with metabolic rewiring, a non-hydrolyzable analog into protein sequences, leading to high yields of modified constructs for functio
Autor:
David G. Campbell, Maria Deak, Helen I. Woodroof, Dario R. Alessi, Robert Gourlay, Ning Zhang, Miratul M. K. Muqit, Agne Kazlauskaite, Helen Walden, Axel Knebel, Thomas Macartney, Chandana Kondapalli, Lynn Burchell
Publikováno v:
Open Biology
Open Biology, Vol 2, Iss 5 (2012)
Open Biology, Vol 2, Iss 5 (2012)
Summary Missense mutations in PTEN-induced kinase 1 (PINK1) cause autosomal-recessive inherited Parkinson's disease (PD). We have exploited our recent discovery that recombinant insect PINK1 is catalytically active to test whether PINK1 directly phos
Autor:
Matthias Trost, Axel Knebel, Chandana Kondapalli, Miratul M. K. Muqit, Kay Hofmann, Ritorto, Alessi, David G. Campbell, Agne Kazlauskaite, Robert Gourlay
Publikováno v:
Journal of Neurology, Neurosurgery & Psychiatry. 85:e4.148-e4
Mutations in the PINK1 and Parkin genes are associated with autosomal-recessive Parkinson9s disease. PINK1 encodes a mitochondrial localized protein kinase and Parkin encodes an ubiquitin E3 ligase. Several lines of evidence indicate that the enzymes