Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Kai-En Chen"'
Autor:
Yue Wu, Zhenling Cui, Yen-Hua Huang, Simon J. de Veer, Andrey V. Aralov, Zhong Guo, Shayli V. Moradi, Alexandra O. Hinton, Jennifer R. Deuis, Shaodong Guo, Kai-En Chen, Brett M. Collins, Irina Vetter, Volker Herzig, Alun Jones, Matthew A. Cooper, Glenn F. King, David J. Craik, Kirill Alexandrov, Sergey Mureev
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
Generic approach for rapid prototyping is essential for the progress of synthetic biology. Here the authors modify the cell-free translation system to control protein aggregation and folding and validate the approach by using single conditions for pr
Externí odkaz:
https://doaj.org/article/4f078ffc82bf47b0b496a47fa5dcdbdc
Autor:
Qian Guo, Kai-en Chen, Gimenez-Andres, Manuel, Jellett, Adam P., Ya Gao, Simonetti, Boris, Meihan Liu, Danson, Chris M., Heesom, Kate J., Cullen, Peter J., Collins, Brett M.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 8/13/2024, Vol. 121 Issue 33, p1-12, 34p
Autor:
Gagan Sharma, Carolyne B. Braga, Kai-En Chen, Xinying Jia, Venkatraman Ramanujam, Brett M. Collins, Roberto Rittner, Mehdi Mobli
Publikováno v:
Current Research in Structural Biology, Vol 3, Iss , Pp 179-186 (2021)
Chlorotoxin (ClTx) is a 36-residue disulfide-rich peptide isolated from the venom of the scorpion Leiurus quinquestriatus. This peptide has been shown to selectively bind to brain tumours (gliomas), however, with conflicting reports regarding its dir
Externí odkaz:
https://doaj.org/article/af52d3404ddf4994b4ff881afbc923be
Autor:
Boris Simonetti, Qian Guo, Manuel Giménez-Andrés, Kai-En Chen, Edmund R R Moody, Ashley J Evans, Mintu Chandra, Chris M Danson, Tom A Williams, Brett M Collins, Peter J Cullen
Publikováno v:
PLoS Biology, Vol 20, Iss 4, p e3001601 (2022)
Coat complexes coordinate cargo recognition through cargo adaptors with biogenesis of transport carriers during integral membrane protein trafficking. Here, we combine biochemical, structural, and cellular analyses to establish the mechanistic basis
Externí odkaz:
https://doaj.org/article/844881cd71af4ba98857830ac0cd310b
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:
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, 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:
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::001a432f260a60ee9ee88d785a8ef286
https://doi.org/10.1016/j.cell.2023.04.003
https://doi.org/10.1016/j.cell.2023.04.003
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bad1a951f22f51ed878b0d84d5eba63
https://doi.org/10.1126/sciadv.abg4007
https://doi.org/10.1126/sciadv.abg4007
Autor:
Boris Simonetti, Qian Guo, Manuel Giménez-Andrés, Kai-En Chen, Edmund R. R. Moody, Ashley J. Evans, Mintu Chandra, Chris M. Danson, Tom A. Williams, Brett M. Collins, Peter J. Cullen
Publikováno v:
Simonetti, B, Guo, Q, Gimenez Andres, M, Chen, K E, Moody, E R R, Evans, A J, Chandra, M, Danson, C M, Williams, T, Collins, B M & Cullen, P J 2022, ' SNX27–Retromer directly binds ESCPE-1 to transfer cargo proteins during endosomal recycling ', PLoS Biology, vol. 20, no. 4, e3001601 . https://doi.org/10.1371/journal.pbio.3001601
Coat complexes coordinate cargo recognition through cargo adaptors with biogenesis of transport carriers during integral membrane protein trafficking. Here, we combine biochemical, structural, and cellular analyses to establish the mechanistic basis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4737fd4aa6267f0f63f2c7711c5738f6
https://pubmed.ncbi.nlm.nih.gov/35417450
https://pubmed.ncbi.nlm.nih.gov/35417450