Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Johan C. Hill"'
Autor:
Kevin P. Guay, Roberta Ibba, J.L. Kiappes, Snežana Vasiljević, Francesco Bonì, Maria De Benedictis, Ilaria Zeni, James D. Le Cornu, Mario Hensen, Anu V. Chandran, Anastassia L. Kantsadi, Alessandro T. Caputo, Juan I. Blanco Capurro, Yusupha Bayo, Johan C. Hill, Kieran Hudson, Andrea Lia, Juliane Brun, Stephen G. Withers, Marcelo Martí, Emiliano Biasini, Angelo Santino, Matteo De Rosa, Mario Milani, Carlos P. Modenutti, Daniel N. Hebert, Nicole Zitzmann, Pietro Roversi
Publikováno v:
iScience, Vol 26, Iss 10, Pp 107919- (2023)
Summary: Misfolded glycoprotein recognition and endoplasmic reticulum (ER) retention are mediated by the ER glycoprotein folding quality control (ERQC) checkpoint enzyme, UDP-glucose glycoprotein glucosyltransferase (UGGT). UGGT modulation is a promi
Externí odkaz:
https://doaj.org/article/65e937022caf475ebc2513beca012f73
Autor:
Gabor Tax, Kevin P Guay, Tatiana Solde, Charlie J Hitchman, Johan C Hill, Snezana Vasilievic, Andrea Lia, Carlos P Modenutti, Kornelis R Straatman, Maurizio Molinari, Angelo Santino, Daniel N Hebert, Nicole Zitzmann, Pietro Roversi, Marco Trerotola
Publikováno v:
bioRxiv
Endoplasmic reticulum (ER) retention of mis-folded glycoproteins is mediated by the ER- localised eukaryotic glycoprotein secretion checkpoint, UDP-glucose glycoprotein glucosyl-transferase (UGGT). The enzyme recognises a mis-folded glycoprotein and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b90fd45800bd78bfd0c9fe66596f07ed
https://doi.org/10.1101/2023.05.30.542711
https://doi.org/10.1101/2023.05.30.542711
Autor:
Kevin P. Guay, Roberta Ibba, JL Kiappes, Maria De Benedictis, Ilaria Zeni, James D. Le Cornu, Mario Hensen, Anu V. Chandran, Anastassia L. Kantsadi, Alessandro T. Caputo, Juan I. Blanco Capurro, Yusupha Bayo, Johan C. Hill, Kieran Hudson, Andrea Lia, Snežana Vasiljević, Carlos P. Modenutti, Stephen G. Withers, Marcelo Martí, Emiliano Biasini, Angelo Santino, Daniel N. Hebert, Nicole Zitzmann, Pietro Roversi
Publikováno v:
SSRN Electronic Journal.
The Endoplasmic Reticulum (ER) glycoprotein folding Quality Control (ERQC) machinery aids folding of glycoproteins in the ER. Misfolded glycoprotein recognition and ER-retention is mediated by the ERQC checkpoint enzyme, the 170 kDa UDP-Glucose glyco
Autor:
Carlos P. Modenutti, Dominic S. Alonzi, Roberta Ibba, Anu V. Chandran, Gabor Tax, Thomas Waksman, Andrea Lia, Angelo Santino, Jonathan Rushton, Abhinav Kumar, Snežana Vasiljević, Marcelo A. Martí, Mauro N. Song, Mario Hensen, Lucia Marti, Juan I. Blanco Capurro, Pietro Roversi, Simone Rubichi, Nicole Zitzmann, Johan C. Hill
Publikováno v:
Structure(London, England:1993)
Structure (Lond.) 29 (2021): 357–370.e9. doi:10.1016/j.str.2020.11.017
info:cnr-pdr/source/autori:Modenutti C.P.; Blanco Capurro J.I.; Ibba R.; Alonzi D.S.; Song M.N.; Vasiljevic S.; Kumar A.; Chandran A.V.; Tax G.; Marti L.; Hill J.C.; Lia A.; Hensen M.; Waksman T.; Rushton J.; Rubichi S.; Santino A.; Marti M.A.; Zitzmann N.; Roversi P./titolo:Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase/doi:10.1016%2Fj.str.2020.11.017/rivista:Structure (Lond.)/anno:2021/pagina_da:357/pagina_a:370.e9/intervallo_pagine:357–370.e9/volume:29
Structure (Lond.) 29 (2021): 357–370.e9. doi:10.1016/j.str.2020.11.017
info:cnr-pdr/source/autori:Modenutti C.P.; Blanco Capurro J.I.; Ibba R.; Alonzi D.S.; Song M.N.; Vasiljevic S.; Kumar A.; Chandran A.V.; Tax G.; Marti L.; Hill J.C.; Lia A.; Hensen M.; Waksman T.; Rushton J.; Rubichi S.; Santino A.; Marti M.A.; Zitzmann N.; Roversi P./titolo:Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase/doi:10.1016%2Fj.str.2020.11.017/rivista:Structure (Lond.)/anno:2021/pagina_da:357/pagina_a:370.e9/intervallo_pagine:357–370.e9/volume:29
Summary UDP-glucose:glycoprotein glucosyltransferase (UGGT) flags misfolded glycoproteins for ER retention. We report crystal structures of full-length Chaetomium thermophilum UGGT (CtUGGT), two CtUGGT double-cysteine mutants, and its TRXL2 domain tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ba809d96b8e8640d443e2d32e298256
https://ora.ox.ac.uk/objects/uuid:7ebfcefe-a06c-4124-aabf-01bc5589b350
https://ora.ox.ac.uk/objects/uuid:7ebfcefe-a06c-4124-aabf-01bc5589b350
Autor:
Mark Freeman, Victoria Head, Binesh Shrestha, Michael Faller, Elizabeth Hardaker, Mark R Dowling, Rene Hemmig, Lucy Elphick, Johan C. Hill, Darren Le Grand, David D. Pascoe, Florence Zink, Christopher Thomson, Andrew Lister, S. Rieffel, David Beattie, Oliver Ross Steward
Publikováno v:
Bioorganicmedicinal chemistry letters. 31
A series of inhibitors of Autotaxin (ATX) have been developed from a high throughput screening hit, 1a, which shows an alternative binding mode to known catalytic site inhibitors. Selectivity over the hERG channel and microsomal clearance were depend
Autor:
J. L. Kiappes, Alessandro T. Caputo, Raymond A. Dwek, Pietro Roversi, Nicholas Sheets, Kelly L. Warfield, Anthony M. Treston, Matthew Duchars, Nicole Zitzmann, Johan C. Hill, Dale L. Barnard, Dominic S. Alonzi, Sujan Shresta, Julia E. Biggins
Publikováno v:
Journal of medicinal chemistry. 63(8)
Influenza and dengue viruses present a growing global threat to public health. Both viruses depend on the host endoplasmic reticulum (ER) glycoprotein folding pathway. In 2014, Sadat et al. reported two siblings with a rare genetic defect in ER α-gl
Autor:
Gabor Tax, Angelo Santino, Anu V. Chandran, Snežana Vasiljević, Thomas Waksman, Roberta Ibba, Abhinav Kumar, Lucia Marti, Dominic S. Alonzi, Nicole Zitzmann, Juan I. Blanco Capurro, Johan C. Hill, Marcelo A. Martí, Mario Hensen, Jonathan Rushton, Carlos P. Modenutti, Andrea Lia, Pietro Roversi, Simone Rubichi
Publikováno v:
SSRN Electronic Journal.
UDP-glucose: glycoprotein glucosyltransferase (UGGT) is the glycoprotein folding checkpoint in the eukaryotic glycoprotein secretory pathway. The enzyme detects misfolded glycoproteins in the Endoplasmic Reticulum, and flags them for retention by re-
Autor:
Shabir Najmudin, Johan C. Hill, Guido Pintacuda, Kinlin L. Chao, John Moult, Arnaud Baslé, T.H. Nguyen, Kaspars Tars, Harry J. Gilbert, Krzysztof Fidelis, Christopher S. Hayes, Marco Nardini, Reinhard Albrecht, Mark J. van Raaij, Valentina Nardone, Roman I. Koning, Celia W. Goulding, Pedro Bule, A.K. Singh, Nicole Zitzmann, Andrzej Joachimiak, Osnat Herzberg, Leila Lo Leggio, Carlos M. G. A. Fontes, Eric J. Sundberg, Pietro Roversi, Didier Ndeh, Andriy Kryshtafovych, Amir Shimon, Gert Wieland Kohring, Folmer Fredslund, Alessandro T. Caputo, Ana Luísa Carvalho, Marco Mangiagalli, Karolina Michalska, Sandra Postel, Marcus D. Hartmann, Torsten Schwede, Ron Diskin
Publikováno v:
Proteins, vol 86 Suppl 1, iss Suppl 1
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2018, 86, pp.27-50. ⟨10.1002/prot.25392⟩
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2018, 86, pp.27-50. ⟨10.1002/prot.25392⟩
International audience; The functional and biological significance of the selected CASP12 targets are described by the authors of the structures. The crystallographers discuss the most interesting structural features of the target proteins and assess
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2375c05a4f68a2d15edec25c29dd5e2f
https://escholarship.org/uc/item/21s8k249
https://escholarship.org/uc/item/21s8k249
Autor:
Petra Lukacik, Shabaz Mohammed, Lucia Marti, James Patrick McIvor, Andrea Lia, Abhinav Kumar, Alessandro T. Caputo, Snežana Vasiljević, Kristin Qian, Angelo Santino, Martin A. Walsh, Souradeep Basu, Johan C. Hill, Kyle Dent, Colette B. Lipp, Pietro Roversi, Dritan Siliqi, Mikail D. Levasseur, Dominic S. Alonzi, Thomas Waksman, Yentli Soto Albrecht, Nicole Zitzmann
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America 114 (2017): 8544–8549. doi:10.1073/pnas.1703682114
info:cnr-pdr/source/autori:Roversi P.; Marti L.; Caputo A.T.; Alonzi D.S.; Hill J.C.; Dent K.C.; Kumar A.; Levasseur M.D.; Lia A.; Waksman T.; Basu S.; Soto Albrecht Y.; Qian K.; McIvor J.P.; Lipp C.B.; Siliqi D.; Vasiljevic S.; Mohammed S.; Lukacik P.; Walsh M.A.; Santino A.; Zitzmann N./titolo:Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint/doi:10.1073%2Fpnas.1703682114/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2017/pagina_da:8544/pagina_a:8549/intervallo_pagine:8544–8549/volume:114
info:cnr-pdr/source/autori:Roversi P.; Marti L.; Caputo A.T.; Alonzi D.S.; Hill J.C.; Dent K.C.; Kumar A.; Levasseur M.D.; Lia A.; Waksman T.; Basu S.; Soto Albrecht Y.; Qian K.; McIvor J.P.; Lipp C.B.; Siliqi D.; Vasiljevic S.; Mohammed S.; Lukacik P.; Walsh M.A.; Santino A.; Zitzmann N./titolo:Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint/doi:10.1073%2Fpnas.1703682114/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2017/pagina_da:8544/pagina_a:8549/intervallo_pagine:8544–8549/volume:114
Glycoproteins traversing the eukaryotic secretory pathway begin life in the endoplasmic reticulum (ER), where their folding is surveyed by the 170 kDa UDP-glucose:glycoprotein glucosyltransferase (UGGT). The enzyme acts as the single glycoprotein fol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92a7783e7d55e7e326dc2c215686d665