Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Douglas M. Freymann"'
Autor:
Hiromi Watari, Hiromu Kageyama, Nami Masubuchi, Hiroya Nakajima, Kako Onodera, Pamela J. Focia, Takumi Oshiro, Takashi Matsui, Yoshio Kodera, Tomohisa Ogawa, Takeshi Yokoyama, Makoto Hirayama, Kanji Hori, Douglas M. Freymann, Misa Imai, Norio Komatsu, Marito Araki, Yoshikazu Tanaka, Ryuichi Sakai
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
The mode of cytokine receptor activation is diverse. Here, the authors find that the marine-sponge derived lectin ThC, a bivalent sugar binding protein, activates human cytokine receptor MPL. This mode of action resembles the pathogenic activation of
Externí odkaz:
https://doaj.org/article/738b2a8a80c14fc9844ae3c420641088
Autor:
Marito Araki, Kako Onodera, Kanji Hori, Hiromu Kageyama, Pamela J. Focia, Hiromi Watari, Yoshio Kodera, Makoto Hirayama, Yoshikazu Tanaka, Ryuichi Sakai, Takeshi Yokoyama, Hiroya Nakajima, Douglas M. Freymann, Takashi Matsui, Norio Komatsu, Tomohisa Ogawa, Nami Masubuchi, Takumi Oshiro
N-glycan-mediated activation of the thrombopoietin receptor (MPL) under pathological conditions has been implicated in myeloproliferative neoplasms induced by mutant calreticulin, which forms an endogenous receptor-agonist complex that constitutively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4600ca3460eb1687989236b0b6b08774
https://doi.org/10.1101/2021.10.29.466502
https://doi.org/10.1101/2021.10.29.466502
Autor:
Kyle P. Smith, Eric C. Landahl, Douglas M. Freymann, Pamela J. Focia, Sarah E. Rice, Julian L. Klosowiak, Srinivas Chakravarthy
Publikováno v:
J Struct Biol
Dysfunction in mitochondrial dynamics is believed to contribute to a host of neurological disorders and has recently been implicated in cancer metastasis. The outer mitochondrial membrane adapter protein Miro functions in the regulation of mitochondr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dab9a53a55f4ea860f8efa77ffbd26c6
https://doi.org/10.1016/j.jsb.2020.107656
https://doi.org/10.1016/j.jsb.2020.107656
Autor:
Christopher Ing, Megumi Yamashita, Régis Pomès, Douglas M. Freymann, Murali Prakriya, Priscilla S.-W. Yeung
Publikováno v:
Proceedings of the National Academy of Sciences. 115
Store-operated Orai1 channels are activated through a unique inside-out mechanism involving binding of the endoplasmic reticulum Ca2+ sensor STIM1 to cytoplasmic sites on Orai1. Although atomic-level details of Orai structure, including the pore and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6db2b5a1baa55a3d58c704d34a5aaf2
https://doi.org/10.1073/pnas.1718373115
https://doi.org/10.1073/pnas.1718373115
Autor:
Srinivas Chakravarthy, Pamela J. Focia, Sarah E. Rice, Eric C. Landahl, Douglas M. Freymann, Julian L. Klosowiak
Publikováno v:
EMBO reports. 14:968-974
Miro is a highly conserved calcium-binding GTPase at the regulatory nexus of mitochondrial transport and autophagy. Here we present crystal structures comprising the tandem EF hand and carboxy terminal GTPase (cGTPase) domains of Drosophila Miro. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21ee6d5875fb6d13a7b19fadc282ad9b
https://doi.org/10.1038/embor.2013.151
https://doi.org/10.1038/embor.2013.151
Autor:
Michael E. French, Sungjin Park, Sarah E. Rice, Julian L. Klosowiak, Kyle P. Smith, Douglas M. Freymann, Pamela J. Focia
Publikováno v:
Scientific Reports
Hereditary Parkinson’s disease is commonly caused by mutations in the protein kinase PINK1 or the E3 ubiquitin ligase Parkin, which function together to eliminate damaged mitochondria. PINK1 phosphorylates both Parkin and ubiquitin to stimulate ubi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ed2f7236d9568d60b29078b9c8977a6
Autor:
Julian L. Klosowiak, Douglas M. Freymann, Pamela J. Focia, Yongbo Zhang, Kyle P. Smith, Sarah E. Rice
Publikováno v:
Biophysical Journal. 112:177a-178a
Mitochondria motility and dynamics are tightly linked. Dysfunction in mitochondrial dynamics cause a host of neurological disorders. The outer mitochondrial membrane protein Miro contains two GTPase domains that control mitochondrial dynamics. While
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a00b1027f41806c33c627b6873f8cf7
https://doi.org/10.1016/j.bpj.2016.11.982
https://doi.org/10.1016/j.bpj.2016.11.982
Autor:
Christopher Ing, Priscilla S.-W. Yeung, Régis Pomès, Murali Prakriya, Megumi Yamashita, Douglas M. Freymann
Publikováno v:
Biophysical Journal. 114:285a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e68a071d1305be8037f84f81fe4a1977
https://doi.org/10.1016/j.bpj.2017.11.1636
https://doi.org/10.1016/j.bpj.2017.11.1636
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
Crystal structures of the Ffh NG GTPase domain at < 1.24 Å resolution reveal multiple overlapping nucleotide binding modes.
Two structures of the nucleotide-bound NG domain of Ffh, the GTPase subunit of the bacterial signal recognition particle
Two structures of the nucleotide-bound NG domain of Ffh, the GTPase subunit of the bacterial signal recognition particle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3768dec3379073f802ba420c574e36f3
https://doi.org/10.1107/s090744490802444x
https://doi.org/10.1107/s090744490802444x
Autor:
Julian L. Klosowiak, Srinivas Chakravarthy, Sarah E. Rice, Pamela J. Focia, Douglas M. Freymann
Publikováno v:
Biophysical Journal. 108(2)
The outer mitochondrial membrane protein Miro is a highly conserved calcium-binding GTPase that is at the regulatory nexus of several processes, including mitochondrial transport and autophagy. Miro attaches mitochondria to the microtubule-based moto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::830d1e4c6e181337fb8741c46619b9ca