Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Martin J. Egan"'
Autor:
Martin J. Egan, Mark A. McClintock, Ian H.L. Hollyer, Hunter L. Elliott, Samara L. Reck-Peterson
Publikováno v:
Cell Reports, Vol 11, Iss 2, Pp 201-209 (2015)
Eukaryotes have evolved multiple strategies for maintaining cellular protein homeostasis. One such mechanism involves neutralization of deleterious protein aggregates via their defined spatial segregation. Here, using the molecular disaggregase Hsp10
Externí odkaz:
https://doaj.org/article/45e68f48247f467183caaf3c6c0f161b
Autor:
Jun Zhang, Rongde Qiu, Baronger D. Bieger, C. Elizabeth Oakley, Berl R. Oakley, Martin J. Egan, Xin Xiang
Publikováno v:
bioRxiv
Functions of protein SUMOylation remain incompletely understood in different cell types. The budding yeast SUMOylation machinery interacts with LIS1, a protein critical for dynein activation, but dynein-pathway components were not identified as SUMO-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::377a57977aae168911b09638e53a153b
https://europepmc.org/articles/PMC10153134/
https://europepmc.org/articles/PMC10153134/
Autor:
Audra Mae Rogers, Martin J. Egan
Publikováno v:
Molecular Biology of the Cell
The chaperone-mediated sequestration of misfolded proteins into specialized quality control compartments represents an important strategy for maintaining protein homeostasis in response to stress. However, precisely how this process is controlled in
Autor:
Yong Wang, Venkata Rao Krishnamurthi, Martin J. Egan, Baronger Dowell Bieger, Nawaraj Dulal, Rohana Liyanage, Rinalda Proko, Audra Mae Rogers
Publikováno v:
Journal of Cell Science. 134
The fungus Magnaporthe oryzae uses a specialized pressure-generating infection cell called an appressorium to break into rice leaves and initiate disease. Appressorium functionality is dependent on the formation of a cortical septin ring during its m
Autor:
Shiv D. Kale, Jesús F. Peña, Ilkka Kronholm, Brian Lovett, Jason E. Stajich, Alex Hopke, Derreck Carter-House, Sophie Altamirano, Daniel Irimia, Kevin McCluskey, Michelle Momany, Hiral Shah, Martin J. Egan, Paul Guerette, Bryan R. Coad, Edyta Szewczyk, Alex Mela, Felix Ellett, David N. Breslauer
Publikováno v:
PloS one, vol 16, iss 9
PLoS ONE
PLoS ONE, Vol 16, Iss 9, p e0257823 (2021)
PLoS ONE
PLoS ONE, Vol 16, Iss 9, p e0257823 (2021)
Fungal hyphal growth and branching are essential traits that allow fungi to spread and proliferate in many environments. This sustained growth is essential for a myriad of applications in health, agriculture, and industry. However, comparisons betwee
Publikováno v:
Traffic (Copenhagen, Denmark)REFERENCES. 21(7)
In filamentous fungi, early endosomes are continuously trafficked to, and from, the growing hyphal tip by microtubule-based motor proteins, serving as platforms for the long-distance transport of diverse cargos including mRNA, signaling molecules, an
Publikováno v:
Fungal Genet Biol
Cytoplasmic dynein is a minus end-directed microtubule motor that can be activated by cargo adapters. In Aspergillus nidulans, overexpression of ΔC-HookA, the early endosomal adapter HookA missing its cargo-binding site, causes activated dynein to a
Publikováno v:
Fungal Genetics and Biology. 140:103385
The rice blast fungus Magnaporthe oryzae differentiates a specialized infection structure called an appressorium, which is used to break into plant cells by directed application of enormous turgor force. Appressorium-mediated plant infection requires
Publikováno v:
The FASEB Journal. 34:1-1
Publikováno v:
The Journal of cell biology, vol 212, iss 3
The Journal of Cell Biology
The Journal of Cell Biology
Microtubule-based motility of peroxisomes is achieved by hitchhiking on early endosomes using the novel endosome-associated linker protein PxdA.
Eukaryotic cells use microtubule-based intracellular transport for the delivery of many subcellular
Eukaryotic cells use microtubule-based intracellular transport for the delivery of many subcellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54341d7e4bbf428810a8b1b438f9dce3