Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Suzanne J. Norwood"'
Autor:
Mintu Chandra, Yanni K.-Y. Chin, Caroline Mas, J. Ryan Feathers, Blessy Paul, Sanchari Datta, Kai-En Chen, Xinying Jia, Zhe Yang, Suzanne J. Norwood, Biswaranjan Mohanty, Andrea Bugarcic, Rohan D. Teasdale, W. Mike Henne, Mehdi Mobli, Brett M. Collins
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Phox homology (PX) domains are membrane interacting domains that bind to various lipids. Here authors screen all human PX domains systematically for their phospholipid preferences and define four classes and provide the basis for defining and predict
Externí odkaz:
https://doaj.org/article/837519800813434db7bd127742edba4b
Autor:
Asma Rehman, Julia K. Archbold, Shu-Hong Hu, Suzanne J. Norwood, Brett M. Collins, Jennifer L. Martin
Publikováno v:
IUCrJ, Vol 1, Iss 6, Pp 505-513 (2014)
Membrane fusion is essential for human health, playing a vital role in processes as diverse as neurotransmission and blood glucose control. Two protein families are key: (1) the Sec1p/Munc18 (SM) and (2) the soluble N-ethylmaleimide-sensitive attachm
Externí odkaz:
https://doaj.org/article/5a897808d3b24427a18bf7d1ed3630bb
Autor:
Amy Kendall, Zhe Yang, Yi Cui, David A. Stroud, Robert G. Parton, Ryan J. Hall, Toby Passioura, Rajesh Ghai, Robert Reid, Timothy A. Hill, Boyang Xie, Joanna Sacharz, Suzanne J. Norwood, Michael D. Healy, Natalya Leneva, David P. Fairlie, Rohan D. Teasdale, Qian Guo, Sachini Fonseka, Kai-En Chen, Hiroaki Suga, Lauren P. Jackson, Brett M. Collins
Publikováno v:
Science Advances
Description
Novel macrocyclic peptides are found that bind and modulate the function of the retromer membrane trafficking complex.
The retromer complex (Vps35-Vps26-Vps29) is essential for endosomal membrane trafficking and signaling. Mutat
Novel macrocyclic peptides are found that bind and modulate the function of the retromer membrane trafficking complex.
The retromer complex (Vps35-Vps26-Vps29) is essential for endosomal membrane trafficking and signaling. Mutat
Autor:
Mehdi Mobli, Suzanne J. Norwood, Brett M. Collins, Xinying Jia, Rohan D. Teasdale, Kai-En Chen, Sanchari Datta, W. Mike Henne, Mintu Chandra, Caroline Mas, Biswaranjan Mohanty, Yanni K.-Y. Chin, Zhe Yang, J. Ryan Feathers, Andrea Bugarcic, Blessy Paul
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Nature Communications
Nature Communications
Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lip
Autor:
Toby Passioura, Ryan J. Hall, Rohan D. Teasdale, Brett M. Collins, Amy Kendall, Yi Cui, Suzanne J. Norwood, Lauren P. Jackson, Hiroaki Suga, Zhe Yang, Boyang Xie, David P. Fairlie, Rajesh Ghai, Timothy A. Hill, Joanna Sacharz, Natalya Leneva, David A. Stroud, Kai-En Chen, Qian Guo
The Retromer complex (Vps35-Vps26-Vps29) is essential for endosomal membrane trafficking and signalling. Mutations in Retromer cause late-onset Parkinson’s disease, while viral and bacterial pathogens can hijack the complex during cellular infectio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f02ce50fc604aed9f469987f315d037
https://doi.org/10.1101/2020.12.03.410779
https://doi.org/10.1101/2020.12.03.410779
Autor:
Rohan D. Teasdale, Zhe Yang, Brett M. Collins, Nicholas Ariotti, Jordan Follett, Robert G. Parton, Suzanne J. Norwood, Andrea Bugarcic
Publikováno v:
Journal of Biological Chemistry. 291:18283-18298
Endosomal sorting is a highly orchestrated cellular process. Retromer is a heterotrimeric complex that associates with endosomal membranes and facilitates the retrograde sorting of multiple receptors, including the cation-independent mannose 6-phosph
Autor:
Wayne A. Johnston, Marta H. Kubala, Sergey Mureev, Guillermo A. Gomez, Kirill Alexandrov, Alpha S. Yap, Alun Jones, Suzanne J. Norwood
Publikováno v:
Biochemical and Biophysical Research Communications. 468:580-586
The protein farnesyltransferase (FTase) mediates posttranslational modification of proteins with isoprenoid lipids. FTase is a heterodimer and although the beta subunit harbors the active site, it requires the a subunit for its activity. Here we expl
Autor:
Michelle P. Christie, Gordon J. King, Asma Rehman, Brett M. Collins, Zakir Tnimov, Jennifer L. Martin, Shu-Hong Hu, Suzanne J. Norwood, Andrew E. Whitten, Kirill Alexandrov, Russell Jarrott
Publikováno v:
PLoS ONE, Vol 12, Iss 8, p e0183366 (2017)
PLoS ONE
PLoS ONE
Vesicular transport of cellular cargo requires targeted membrane fusion and formation of a SNARE protein complex that draws the two apposing fusing membranes together. Insulin-regulated delivery and fusion of glucose transporter-4 storage vesicles at
Autor:
Julia K. Archbold, Brett M. Collins, Suzanne J. Norwood, Jennifer L. Martin, Asma Rehman, Shu-Hong Hu
Publikováno v:
IUCrJ
IUCrJ, Vol 1, Iss 6, Pp 505-513 (2014)
IUCrJ, Vol 1, Iss 6, Pp 505-513 (2014)
Mammalian Munc18 proteins are essential for membrane fusion and human health. Here, we review the literature describing structural and in vitro data, and identify a possible explanation for the conflicting functional roles that have been reported.
Autor:
Peter A. Silburn, Stephanie Tay, Jordan Follett, Brett M. Collins, George D. Mellick, Andrea Bugarcic, Rohan D. Teasdale, Oleksiy Kovtun, Nicholas A. Hamilton, Stephen A. Wood, Suzanne J. Norwood, Megha Mohan, Yang Zhe
Publikováno v:
Traffic. 15:230-244
The retromer is a trimeric cargo-recognition protein complex composed of Vps26, Vps29 and Vps35 associated with protein trafficking within endosomes. Recently, a pathogenic point mutation within the Vps35 subunit (D620N) was linked to the manifestati