Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Molecular Chaperones/chemistry"'
Autor:
Rasmussen, Helena Ø, Kumar, Amit, Shin, Ben, Stylianou, Fisentzos, Sewell, Lee, Xu, Yingqi, Otzen, Daniel E, Pedersen, Jan Skov, Matthews, Steve J
Publikováno v:
Rasmussen, H Ø, Kumar, A, Shin, B, Stylianou, F, Sewell, L, Xu, Y, Otzen, D E, Pedersen, J S & Matthews, S J 2023, ' FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC ', Journal of Molecular Biology, vol. 435, no. 2, 167878 . https://doi.org/10.1016/j.jmb.2022.167878
Bacterial functional amyloids contribute to biofilm development by bacteria and provide protection from the immune system and prevent antibiotic treatment. Strategies to target amyloid formation and interrupt biofilm formation have attracted recent i
Autor:
zur Lage, Petra, Stefanopoulou, Panagiota, Styczynska-Soczka, Katarzyna, Quinn, Niall, Mali, Girish, von Kriegsheim, Alex, Mill, Pleasantine, Jarman, Andrew P.
Publikováno v:
The Journal of Cell Biology
zur Lage, P, Stefanopoulou, P, Styczynska, K, Quinn, N, Mali, G, Von Kriegsheim, A, Mill, P & Jarman, A 2018, ' Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP ', Journal of Cell Biology . https://doi.org/10.1083/jcb.201709026
Zur Lage, P, Stefanopoulou, P, Styczynska-Soczka, K, Quinn, N, Mali, G, von Kriegsheim, A, Mill, P & Jarman, A P 2018, ' Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP ', The Journal of cell biology, vol. 217, no. 7, pp. 2583-2598 . https://doi.org/10.1083/jcb.201709026
zur Lage, P, Stefanopoulou, P, Styczynska, K, Quinn, N, Mali, G, Von Kriegsheim, A, Mill, P & Jarman, A 2018, ' Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP ', Journal of Cell Biology . https://doi.org/10.1083/jcb.201709026
Zur Lage, P, Stefanopoulou, P, Styczynska-Soczka, K, Quinn, N, Mali, G, von Kriegsheim, A, Mill, P & Jarman, A P 2018, ' Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP ', The Journal of cell biology, vol. 217, no. 7, pp. 2583-2598 . https://doi.org/10.1083/jcb.201709026
Wdr92 is associated with the multifunctional cochaperone, R2TP, but its function is unknown. In this study, the authors show that Drosophila Wdr92 is exclusively required for preassembly of ciliary dynein motor complexes, which are confined to sensor
Autor:
Gabriel Waksman, Alison E. Ashcroft, Gregory T. Costakes, R.J. Rose, Scott J. Hultgren, Han Remaut, Tina Daviter, Emanuele Paci, Denis Verger, Sheena E. Radford
Publikováno v:
Structure. 16:1724-1731
P pili are important adhesive fibers involved in kidney infection by uropathogenic Escherichia coli. Pilus subunits are characterized by a large groove resulting from lack of a β strand. Polymerization of pilus subunits occurs via the donor-strand e
Publikováno v:
Journal of Molecular Biology. 379:174-187
Bacterial pili are important virulence factors involved in host cell attachment and/or biofilm formation, key steps in establishing and maintaining successful infection. Here we studied Salmonella atypical fimbriae (or Saf pili), formed by the conser
Autor:
Gordana Cogelja Cajo, Pierre Genevaux, Françoise Schwager, Costa Georgopoulos, William L. Kelley, B. Erin Horne
Publikováno v:
Journal of Biological Chemistry, Vol. 281, No 18 (2006) pp. 12436-12444
To perform effectively as a molecular chaperone, DnaK (Hsp70) necessitates the assistance of its DnaJ (Hsp40) co-chaperone partner, which efficiently stimulates its intrinsically weak ATPase activity and facilitates its interaction with polypeptide s
Publikováno v:
Protein Science. 14:1993-2002
Pathogenic Yersinia species use a type III secretion (TTS) system to deliver a number of cytotoxic effector proteins directly into the mammalian host cell. To ensure effective translocation, several such effector proteins transiently bind to specific
Autor:
Abel Garcia-Pino, Sarah Haesaerts, Frank Sobott, Annika Butterer, Henri De Greve, Albert Konijnenberg, Remy Loris, Steven De Gieter, Ariel Talavera
Publikováno v:
Journal of biological chemistry
The Journal of biological chemistry, 289 (49
The Journal of biological chemistry, 289 (49
The toxin Doc from the phd/doc toxin-antitoxin module targets the cellular translation machinery and is inhibited by its antitoxin partner Phd. Here we show that Phd also functions as a chaperone, keeping Doc in an active, correctly folded conformati
Autor:
Gabriel Waksman, Han Remaut, Andreas Larsson, Nils Pemberton, Veronica Åberg, Jerome S. Pinkner, Eric L. Miller, Mattias Hedenström, Fredrik Almqvist, Floris Buelens, Scott J. Hultgren, Patrick C. Seed
A chemical synthesis platform with broad applications and flexibility was rationally designed to inhibit biogenesis of adhesive pili assembled by the chaperone–usher pathway in Gram-negative pathogens. The activity of a family of bicyclic 2-pyridon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee0fde14dfcc00b5a46fa21b46dd1455
https://hdl.handle.net/20.500.14017/c4b46c73-a575-4ec5-87c8-615b92d1cb3b
https://hdl.handle.net/20.500.14017/c4b46c73-a575-4ec5-87c8-615b92d1cb3b
Autor:
Gabriel Waksman, Sheena E. Radford, Scott J. Hultgren, Thomas J. Hannan, Alison E. Ashcroft, R.J. Rose, Han Remaut
Gram-negative pathogens commonly use the chaperone-usher pathway to assemble adhesive multisubunit fibers on their surface. In the periplasm, subunits are stabilized by a chaperone that donates a beta strand to complement the subunits' truncated immu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb8745e44033d3c3b506813da25f004c
https://biblio.vub.ac.be/vubir/donorstrand-exchange-in-chaperoneassisted-pilus-assembly-proceeds-through-a-concerted-beta-strand-displacement-mechanism(2902e9fb-2e56-423a-872f-312c8e7173a3).html
https://biblio.vub.ac.be/vubir/donorstrand-exchange-in-chaperoneassisted-pilus-assembly-proceeds-through-a-concerted-beta-strand-displacement-mechanism(2902e9fb-2e56-423a-872f-312c8e7173a3).html
Publikováno v:
Journal of Molecular Neuroscience, vol. 30, no. 3, pp. 249-265
The formation of toxic protein aggregates is a common denominator to many neurodegenerative diseases and aging. Accumulation of toxic, possibly infectious protein aggregates induces a cascade of events, such as excessive inflammation, the production
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1900::edad01130ffe764882fa3960034648d9
https://serval.unil.ch/resource/serval:BIB_EC859331588D.P001/REF.pdf
https://serval.unil.ch/resource/serval:BIB_EC859331588D.P001/REF.pdf