Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Da Nae R. Woodard"'
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
Scientific Reports
Scientific Reports
Distinct mutations in the secreted extracellular matrix protein, fibulin-3 (F3), have been associated with a number of ocular diseases ranging from primary open angle glaucoma to cuticular age-related macular degeneration to a rare macular dystrophy,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::701ef35636951b6a4e7b56dec3753be8
https://doaj.org/article/f4d1cbf2ae3f44988272f1e62004c969
https://doaj.org/article/f4d1cbf2ae3f44988272f1e62004c969
Autor:
Nicole Poulides, Erdal Toprak, Madhu Sudan Manna, Uttam K. Tambar, Xiaoyu Wang, Da Nae R. Woodard, Ali Rana Atilgan, Yusuf Talha Tamer, John D. Hulleman, Noelle S. Williams, Andrew Y. Koh, Dominika Borek, Ayesha Ahmed, Canan Atilgan, Furkan C.R. Toprak, Ilona K. Gaszek
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
The antibiotic trimethoprim (TMP) is used to treat a variety of Escherichia coli infections, but its efficacy is limited by the rapid emergence of TMP-resistant bacteria. Previous laboratory evolution experiments have identified resistance-conferring
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad8f209dc60d5b2781ad16a89a1b65fc
https://doi.org/10.1038/s41467-021-23191-z
https://doi.org/10.1038/s41467-021-23191-z
Autor:
Marian Renwick, Da Nae R. Woodard, B. Chen, John D. Hulleman, Rafael Ufret-Vincenty, Prerana Ramadurgum, Steffi Daniel, Shyamtanu Datta, B. Aredo, Hui Peng
SummaryTheEscherichia colidihydrofolate reductase (DHFR) destabilizing domain (DD) serves as a promising approach to conditionally regulate protein abundance in a variety of tissues. In the absence of TMP, a DHFR stabilizer, the DD is degraded by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::150a5efd0f89cd53fa8383bdc959f168
https://doi.org/10.1101/2021.04.13.438468
https://doi.org/10.1101/2021.04.13.438468
Autor:
Prema L. Mallipeddi, Prerana Ramadurgum, Viet Q. Chau, Hui Peng, Bruce A. Posner, John D. Hulleman, Da Nae R. Woodard, Hanspeter Niederstrasser, Melina Mihelakis, Steffi Daniel, Peter M. Douglas
Publikováno v:
Cell Chem Biol
Destabilizing domains (DDs), such as a mutated form of Escherichia coli dihydrofolate reductase (ecDHFR), confer instability and promote protein degradation. However, when combined with small-molecule stabilizers (e.g., the antibiotic trimethoprim),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f566a533cc17fcb27868b494f0b7993
https://pubmed.ncbi.nlm.nih.gov/32330442
https://pubmed.ncbi.nlm.nih.gov/32330442
Autor:
Dailu Chen, Da Nae R. Woodard, Levent Sari, Omar M. Kashmer, Lukasz A. Joachimiak, Valerie A. Perez, Kenneth W. Drombosky, Marc I. Diamond, Milo M. Lin, Bryan D. Ryder, Zhiqiang Hou
Publikováno v:
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Tauopathies are neurodegenerative diseases characterized by intracellular amyloid deposits of tau protein. Missense mutations in the tau gene (MAPT) correlate with aggregation propensity and cause dominantly inherited tauopathies, but their biophysic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5520b89cfb50c07b0f9b472bf03ebe2
https://doi.org/10.1038/s41467-019-10355-1
https://doi.org/10.1038/s41467-019-10355-1
Publikováno v:
eLife, Vol 7 (2018)
eLife
eLife
Tauopathies have diverse presentation, progression, and neuropathology. They are linked to tau prion strains, self-replicating assemblies of unique quaternary conformation, whose origin is unknown. Strains can be propagated indefinitely in cultured c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53d65ea1e54ab66e84df7b20357e4b8a
https://elifesciences.org/articles/37813
https://elifesciences.org/articles/37813
Autor:
Levent Sari, Dailu Chen, Bryan D. Ryder, Marc I. Diamond, Omar M. Kashmer, Milo M. Lin, Valerie A. Perez, Kenneth W. Drombosky, Zhiqiang Hou, Lukasz A. Joachimiak, Da Nae R. Woodard
Tauopathies are neurodegenerative diseases characterized by intracellular amyloid deposits of tau protein. Missense mutations in the tau gene (MAPT) correlate with aggregation propensity and cause dominantly inherited tauopathies, but their biophysic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a28d063d5b3305fc464d1f74b79fe8a2
https://doi.org/10.1101/330266
https://doi.org/10.1101/330266