Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Tara L. Mastro"'
Publikováno v:
Biology Open, Vol 2, Iss 7, Pp 728-738 (2013)
Summary The DDK complex is a conserved kinase complex, consisting of a catalytic subunit, Hsk1 (Cdc7), and its regulatory subunit Dfp1 (Dbf4). This kinase is essential for DNA replication. In this work, we show that dfp1-r35, which truncates the Dfp1
Externí odkaz:
https://doaj.org/article/8b3684d1a97f449b945ca3c26b8165b2
Autor:
Tara L Mastro, Anthony Preza, Shinjini Basu, Sumantra Chattarji, Sally M Till, Peter C Kind, Mary B Kennedy
Publikováno v:
eLife, Vol 9 (2020)
SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of Syngap1 in mice is correlated with increased steady-state levels of other key PSD proteins t
Externí odkaz:
https://doaj.org/article/a09aac89c04d418884f82e7fb1029d4d
Autor:
Ward G Walkup IV, Tara L Mastro, Leslie T Schenker, Jost Vielmetter, Rebecca Hu, Ariella Iancu, Meera Reghunathan, Barry Dylan Bannon, Mary B Kennedy
Publikováno v:
eLife, Vol 5 (2016)
Externí odkaz:
https://doaj.org/article/7c1fdca11be34a00b03a3bae8ef2ffec
Autor:
Ward G Walkup IV, Tara L Mastro, Leslie T Schenker, Jost Vielmetter, Rebecca Hu, Ariella Iancu, Meera Reghunathan, Barry Dylan Bannon, Mary B Kennedy
Publikováno v:
eLife, Vol 5 (2016)
SynGAP is a Ras/Rap GTPase-activating protein (GAP) that is a major constituent of postsynaptic densities (PSDs) from mammalian forebrain. Its α1 isoform binds to all three PDZ (PSD-95, Discs-large, ZO-1) domains of PSD-95, the principal PSD scaffol
Externí odkaz:
https://doaj.org/article/d93758de746f4669a474bb8687ebcddf
Autor:
Anoop Rawat, J. Mario Isas, Ali Khoshnan, Jung Hyun Yoo, Tara L Mastro, Nitin K. Pandey, Mary B. Kennedy, Anjalika Chongtham, Ralf Langen
Publikováno v:
Neurobiology of Disease, Vol 159, Iss, Pp 105517-(2021)
Neurobiol Dis
Neurobiol Dis
Huntington's disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeat in the exon-1 of huntingtin protein (HTT). The expanded polyQ enhances the amyloidogenic propensity of HTT exon 1 (H
Autor:
Anjalika Chongtham, Ali Khoshnan, Anoop Rawat, Ralf Langen, Nitin K. Pandey, Jung Hyun Yoo, Mary B. Kennedy, Jose Mario Isas, Tara L Mastro
Huntington’s disease (HD) is a genetically inherited neurodegenerative disorder caused by expansion of a polyglutamine (polyQ) repeats in the exon-1 of huntingtin protein (HTT). The expanded polyQ enhances the amyloidogenic propensity of HTT exon 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bf8fa0f42ec70dc489baafb538f0610b
https://doi.org/10.1101/2021.04.16.440200
https://doi.org/10.1101/2021.04.16.440200
Autor:
Anthony Preza, Mary B. Kennedy, Sally M. Till, Peter C. Kind, Tara L Mastro, Sumantra Chattarji, Shinjini Basu
Publikováno v:
Mastro, T L, Preza, A, Basu, S, Chattarji, S, Till, S M, Kind, P C & Kennedy, M B 2020, ' A sex difference in the response of the rodent postsynaptic density to synGAP haploinsufficiency ', eLIFE, vol. 9, e52656 . https://doi.org/10.7554/eLife.52656
eLife, Vol 9 (2020)
eLife
eLife, Vol 9 (2020)
eLife
SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of Syngap1 in mice is correlated with increased steady-state levels of other key PSD proteins t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca32e7c5249e0c085c282e60ae4a951e
https://www.pure.ed.ac.uk/ws/files/136586067/10_10_2019_ADV_eLife_52656_submit_revised_clean.pdf
https://www.pure.ed.ac.uk/ws/files/136586067/10_10_2019_ADV_eLife_52656_submit_revised_clean.pdf
Publikováno v:
J Cell Sci
Translesion synthesis polymerases (TLSPs) are non-essential error-prone enzymes that ensure cell survival by facilitating DNA replication in the presence of DNA damage. In addition to their role in bypassing lesions, TLSPs have been implicated in mei
Autor:
Sumantra Chattarji, Mary B. Kennedy, Peter C. Kind, Shinjini Basu, Anthony Preza, Sally M. Till, Tara L Mastro
SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of synGAP in mice is correlated with increased steady-state levels of other key PSD proteins th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83c019b0d3c269e5f8e6f305c9da42b7
https://doi.org/10.1101/802538
https://doi.org/10.1101/802538