Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Rajesh Ghai"'
Autor:
Rajesh Ghai, Ximing Du, Huan Wang, Jiangqing Dong, Charles Ferguson, Andrew J. Brown, Robert G. Parton, Jia-Wei Wu, Hongyuan Yang
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
ORP5/8 are endoplasmic reticulum (ER) membrane proteins implicated in lipid trafficking that localize to ER-plasma membrane (PM) contacts and maintain membrane homeostasis. Here the authors show that PtdIns(4,5)P 2 plays a critical role in the target
Externí odkaz:
https://doaj.org/article/df6fc894509848fab3fe25b78c872533
Autor:
Michael D Healy, Manuela K Hospenthal, Ryan J Hall, Mintu Chandra, Molly Chilton, Vikas Tillu, Kai-En Chen, Dion J Celligoi, Fiona J McDonald, Peter J Cullen, J Shaun Lott, Brett M Collins, Rajesh Ghai
Publikováno v:
eLife, Vol 7 (2018)
The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which
Externí odkaz:
https://doaj.org/article/52ef44e3fdd642e78e446da5ae0c2ac6
Autor:
James D Swarbrick, Daniel J Shaw, Sandeep Chhabra, Rajesh Ghai, Eugene Valkov, Suzanne J Norwood, Matthew N J Seaman, Brett M Collins
Publikováno v:
PLoS ONE, Vol 6, Iss 5, p e20420 (2011)
VPS29 is a key component of the cargo-binding core complex of retromer, a protein assembly with diverse roles in transport of receptors within the endosomal system. VPS29 has a fold related to metal-binding phosphatases and mediates interactions betw
Externí odkaz:
https://doaj.org/article/4201cafbff204af4adff59089ce4261c
Autor:
Michael D. Healy, Kerrie E. McNally, Rebeka Butkovic, Molly Chilton, Kohji Kato, Joanna Sacharz, Calum McConville, Edmund R.R. Moody, Shrestha Shaw, Vicente J. Planelles-Herrero, Sathish K.N. Yadav, Jennifer Ross, Ufuk Borucu, Catherine S. Palmer, Kai-En Chen, Tristan I. Croll, Ryan J. Hall, Nikeisha J. Caruana, Rajesh Ghai, Thi H.D. Nguyen, Kate J. Heesom, Shinji Saitoh, Imre Berger, Christiane Schaffitzel, Tom A. Williams, David A. Stroud, Emmanuel Derivery, Brett M. Collins, Peter J. Cullen
SUMMARYThe Commander complex is required for endosomal recycling of diverse transmembrane cargos and is mutated in Ritscher-Schinzel syndrome. It comprises two subassemblies; Retriever composed of VPS35L, VPS26C and VPS29, and the CCC complex which c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23d210a5342199c943249b9d1af8c0d6
https://doi.org/10.2139/ssrn.4330804
https://doi.org/10.2139/ssrn.4330804
Autor:
Michael D. Healy, Kerrie E. McNally, Rebeka Butkovič, Molly Chilton, Kohji Kato, Joanna Sacharz, Calum McConville, Edmund R.R. Moody, Shrestha Shaw, Vicente J. Planelles-Herrero, Sathish K.N. Yadav, Jennifer Ross, Ufuk Borucu, Catherine S. Palmer, Kai-En Chen, Tristan I. Croll, Ryan J. Hall, Nikeisha J. Caruana, Rajesh Ghai, Thi H.D. Nguyen, Kate J. Heesom, Shinji Saitoh, Imre Berger, Christiane Schaffitzel, Tom A. Williams, David A. Stroud, Emmanuel Derivery, Brett M. Collins, Peter J. Cullen
Publikováno v:
Cell. 186:2219-2237.e29
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:
Michael D. Healy, Joanna Sacharz, Kerrie E. McNally, Calum McConville, Vikas A. Tillu, Ryan J. Hall, Molly Chilton, Peter J. Cullen, Mehdi Mobli, Rajesh Ghai, David A. Stroud, Brett M. Collins
Publikováno v:
Structure. 30:1590-1602.e6
The sorting nexin SNX17 controls endosomal recycling of transmembrane cargo proteins including integrins, the amyloid precursor protein, and lipoprotein receptors. This requires association with the Commander trafficking complex and depends on the C
Autor:
David A. Stroud, Rajesh Ghai, Michael D. Healy, Calum McConville, Molly Chilton, Ryan J. Hall, Joanna Sacharz, Brett M. Collins, Mehdi Mobli, Peter J. Cullen, Kerrie E. McNally
The sorting nexin SNX17 controls endosome-to-cell surface recycling of diverse transmembrane cargo proteins including integrins, the amyloid precursor protein and lipoprotein receptors. This requires association with the multi-subunit Commander traff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e13ee45c517c3e54b7f048b8a1f4847
https://doi.org/10.1101/2021.07.29.454387
https://doi.org/10.1101/2021.07.29.454387
Autor:
Joanna Sacharz, Ryan J. Hall, Mehdi Mobli, Brett M. Collins, Rajesh Ghai, Peter J. Cullen, Michael D. Healy, Calum McConville, David A. Stroud, Molly Chilton, Kerrie E. McNally
Publikováno v:
SSRN Electronic Journal.
The sorting nexin SNX17 controls endosome-to-cell surface recycling of diverse transmembrane cargo proteins including integrins, the amyloid precursor protein and lipoprotein receptors. This requires association with the multi-subunit Commander traff
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