Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Russell Jarrott"'
Autor:
Andrew E. Whitten, Asma Rehman, Shu-Hong Hu, Jennifer L. Martin, Gordon J. King, Michelle P. Christie, Brett M. Collins, Russell Jarrott
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 10, p e0187302 (2017)
PLoS ONE, Vol 12, Iss 10, p e0187302 (2017)
The efficient delivery of cellular cargo relies on the fusion of cargo-carrying vesicles with the correct membrane at the correct time. These spatiotemporal fusion events occur when SNARE proteins on the vesicle interact with cognate SNARE proteins o
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:
Matthew A. Perugini, Christine L. Gee, Mark A. Schembri, Begoña Heras, Kate M. Peters, Jason J. Paxman, Makrina Totsika, Andrew E. Whitten, Russell Jarrott
Publikováno v:
Proceedings of the National Academy of Sciences. 111:457-462
Aggregation and biofilm formation are critical mechanisms for bacterial resistance to host immune factors and antibiotics. Autotransporter (AT) proteins, which represent the largest group of outer-membrane and secreted proteins in Gram-negative bacte
Autor:
Gordon J. King, Shu-Hong Hu, Andrew E. Whitten, Jagath Reddy Junutula, Jacqueline Stöckli, Christopher C. Meoli, David E. James, Russell Jarrott, Brit Winnen, Jennifer L. Martin, Wilko Duprez
Publikováno v:
Journal of Biological Chemistry. 287:40996-41006
The APPL1 and APPL2 proteins (APPL (adaptor protein, phosphotyrosine interaction, pleckstrin homology (PH) domain, and leucine zipper-containing protein)) are localized to their own endosomal subcompartment and interact with a wide range of proteins
Autor:
Russell Jarrott, Michelle P. Christie, Brett M. Collins, Kai-En Chen, Andrew E. Whitten, Philip Callow, David E. James, Shu-Hong Hu, Jennifer L. Martin, Anthony P. Duff, Gordon J. King
Publikováno v:
Proceedings of the National Academy of Sciences. 109:9816-9821
When nerve cells communicate, vesicles from one neuron fuse with the presynaptic membrane releasing chemicals that signal to the next. Similarly, when insulin binds its receptor on adipocytes or muscle, glucose transporter-4 vesicles fuse with the ce
Autor:
Makrina Totsika, Mark A. Schembri, Stephen R. Shouldice, Gregor Gunčar, Russell Jarrott, Begoña Heras
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:601-604
Pathogens require protein-folding enzymes to produce functional virulence determinants. These foldases include the Dsb family of proteins, which catalyze oxidative folding in bacteria. Bacterial disulfide catalytic processes have been well characteri
Autor:
Stephen R. Shouldice, Russell Jarrott, Pooja Sharma, Begoña Heras, Jennifer L. Martin, Martin J. Scanlon
Publikováno v:
Antioxidants & Redox Signaling. 12:921-931
Bacterial antibiotic resistance is an emerging global crisis, and treatment of multidrug-resistant gram-negative infections, particularly those caused by the opportunistic human pathogen Pseudomonas aeruginosa, remains a major challenge. This problem
Autor:
Daniel Stephan, Mareike Kurz, Stephen R. Shouldice, Begonña Heras, Russell Jarrott, Annie Hiniker, Danming Tang, Guoping Ren, Zhaohui Xu, Jennifer L. Martin, Rosemary S. Harrison, Ying Zheng, James C.A. Bardwell
Publikováno v:
The Journal of Biological Chemistry
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single
Autor:
Russell Jarrott, Patrick Frei, Gordon J. King, Alun Jones, Jennifer L. Martin, Gautier Robin, Scott Leslie O'Neill, Mareike Kurz, Rudi Glockshuber, Begoña Heras, Inaki Iturbe-Ormaetxe, Nathan Cowieson
Publikováno v:
Protein Expression and Purification. 59:266-273
Wolbachia pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by manipulating the host reproduction machinery to enhance their own transmission. This unusual phenotyp
Autor:
Jennifer L. Martin, Begoña Heras, Scott Leslie O'Neill, Karl A. Byriel, Inaki Iturbe-Ormaetxe, Mareike Kurz, Russell Jarrott
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64:94-97
alpha-DsbA1 is one of two DsbA homologues encoded by the Gram-negative alpha-proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The