Search

Your search keyword '"Rasmussen, Tim"' showing total 32 results
Start Over Author "Rasmussen, Tim" Search Limiters Full Text
32 results on '"Rasmussen, Tim"'

2. Mechanosensitive channel gating by delipidation

Author

Flegler, Vanessa Judith, Rasmussen, Akiko, Borbil, Karina, Boten, Lea, Chen, Hsuan-Ai, Deinlein, Hanna, Halang, Julia, Hellmanzik, Kristin, Löffler, Jessica, Schmidt, Vanessa, Makbul, Cihan, Kraft, Christian, Hedrich, Rainer, Rasmussen, Tim, and Böttcher, Bettina

Published
2021

9. The role of lipids in mechanosensation

Author

Pliotas, Christos, Dahl, A Caroline E, Rasmussen, Tim, Mahendran, Kozhinjampara R, Smith, Terry K, Marius, Phedra, Gault, Joseph, Banda, Thandiwe, Rasmussen, Akiko, Miller, Samantha, Robinson, Carol V, Bayley, Hagan, Sansom, Mark S P, Booth, Ian R, and Naismith, James H

Published
2015
Full Text
View/download PDF

15. The photochemical thiol–ene reaction as a versatile method for the synthesis of glutathione S-conjugates targeting the bacterial potassium efflux system Kef† †Electronic supplementary information (ESI) available: Further experimental details and NMR spectra. See DOI: 10.1039/c5qo00436e Click here for additional data file

Author

Healy, Jess, Rasmussen, Tim, Miller, Samantha, Booth, Ian R., and Conway, Stuart J.

Subjects
Chemistry, Condensed Matter::Mesoscopic Systems and Quantum Hall Effect, Nuclear Experiment
Abstract

The thiol–ene coupling reaction is emerging as an important conjugation reaction that is suitable for use in a biological setting., The thiol–ene coupling reaction is emerging as an important conjugation reaction that is suitable for use in a biological setting. Here, we explore the utility of this reaction for the synthesis of glutathione-S-conjugates (GSX) and present a general, operationally simple, protocol with a wide substrate scope. The GSX afforded are an important class of compounds and provide invaluable molecular tools to study glutathione-binding proteins. In this study we apply the diverse library of GSX synthesised to further our understanding of the structural requirements for binding to the glutathione-binding protein, Kef, a bacterial K+ efflux system, found in many bacterial pathogens. This system is vital to the survival of bacteria upon exposure to electrophiles, and plays an essential role in the maintenance of intracellular pH and K+ homeostasis. Consequently, Kef is an appealing target for the development of novel antibacterial drugs.

Published
2016

16. Cell entry of a host-targeting protein of oomycetes requires gp96

Author

Loebach, Lars, Wawra, Stephan, Durward, Elaine, Wuensch, Andreas, Iberahim, Nurul Aqilah, De Bruijn, Irene, MacKenzie, Kevin, Willems, Ariane, Toloczko, Aleksandra, Diéguez-Uribeondo, Javier, Rasmussen, Tim, Schrader, Thomas, Bayer, Peter, Secombes, Chris J., and Van West, Pieter

Subjects
fungi
Abstract

The animal-pathogenic oomycete Saprolegnia parasitica causes serious losses in aquaculture by infecting and killing freshwater fish. Like plant-pathogenic oomycetes, S. parasitica employs similar infection structures and secretes effector proteins that translocate into host cells to manipulate the host. Here, we show that the host-targeting protein SpHtp3 enters fish cells in a pathogen-independent manner. This uptake process is guided by a gp96-like receptor and can be inhibited by supramolecular tweezers. The C-terminus of SpHtp3 (containing the amino acid sequence YKARK), and not the N-terminal RxLR motif, is responsible for the uptake into host cells. Following translocation, SpHtp3 is released from vesicles into the cytoplasm by another host-targeting protein where it degrades nucleic acids. The effector translocation mechanism described here, is potentially also relevant for other pathogen-host interactions as gp96 is found in both animals and plants., This work is supported by the [European Community’s] Seventh Framework Programme [FP7/2007–2013] under grant agreement no. [238550] (L.L., J.D.-U., C.J.S., P.v.W.); BBSRC [BBE007120/1, BB/J018333/1 and BB/G012075/1] (F.T., I.d.B., C.J.S., S.W., P.v.W.); Newton Global Partnership Award [BB/N005058/1] (F.T., P.v.W.), the University of Aberdeen (A.D.T., T.R., C.J.S., P.v.W.) and Deutsche Forschungsgemeinschaft [CRC1093] (P.B., T.S.). We would like to acknowledge the Ministry of Higher Education Malaysia for funding INA. We would like to thank Brian Haas for his bioinformatics support. We would like to acknowledge Neil Gow and Johannes van den Boom for critical reading of the manuscript. We would like to acknowledge Svetlana Rezinciuc for technical help with pH-studies.

Published
2018

17. Cell entry of a host-targeting protein of oomycetes requires gp96

Author

Trusch, Franziska, primary, Loebach, Lars, additional, Wawra, Stephan, additional, Durward, Elaine, additional, Wuensch, Andreas, additional, Iberahim, Nurul Aqilah, additional, de Bruijn, Irene, additional, MacKenzie, Kevin, additional, Willems, Ariane, additional, Toloczko, Aleksandra, additional, Diéguez-Uribeondo, Javier, additional, Rasmussen, Tim, additional, Schrader, Thomas, additional, Bayer, Peter, additional, Secombes, Chris J., additional, and van West, Pieter, additional

Published
2018
Full Text
View/download PDF

18. The Cryptococcus neoformans Titan cell is an inducible and regulated morphotype underlying pathogenesis

Author

Dambuza, Ivy M., primary, Drake, Thomas, additional, Chapuis, Ambre, additional, Zhou, Xin, additional, Correia, Joao, additional, Taylor-Smith, Leanne, additional, LeGrave, Nathalie, additional, Rasmussen, Tim, additional, Fisher, Matthew C., additional, Bicanic, Tihana, additional, Harrison, Thomas S., additional, Jaspars, Marcel, additional, May, Robin C., additional, Brown, Gordon D., additional, Yuecel, Raif, additional, MacCallum, Donna M., additional, and Ballou, Elizabeth R., additional

Published
2018
Full Text
View/download PDF

21. Consolidation simplifies storage infrastructures: networked storage--NAS or SAN--can facilitate resource consolidation and centralized management

Author

Rasmussen, Tim

Subjects
Network attached storage -- Comparative analysis -- Usage, Corporations -- Information management -- Comparative analysis -- Usage, Network architecture -- Comparative analysis -- Usage, Computer storage devices -- Usage, Peer to peer computing -- Comparative analysis -- Usage, Storage area networks -- Usage -- Comparative analysis, RAID systems -- Usage, RAID array system, Data storage device, Company systems management, Network architecture, Network-attached storage, Storage Area Network, Business, Computers and office automation industries, Computers, Library and information science
Abstract

Data warehousing, data mining, CRM, ERP, e-business, databases, e-mail. All of these applications contribute to the massive amounts of information that businesses need to store. Rather than maintaining a direct-attached [...]

Published
2003

30. Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.

Author

Bamford, Vicki A., Bruno, Stefano, Rasmussen, Tim, Appia-Ayme, Corinne, Cheesman, Myles R., Berks, Ben C., and Hemmings, Andrew M.

Subjects
BACTERIA, OXIDATION, CYTOCHROMES, ENZYMES, PROTEINS, THIOSULFATES
Abstract

Reduced inorganic sulfur compounds are utilized by many bacteria as electron donors to photosynthetic or respiratory electron transport chains. This metabolism is a key component of the biogeochemical sulfur cycle. The SoxAX protein is a heterodimeric c-type cytochrome involved in thiosulfate oxidation. The crystal structures of SoxAX from the photosynthetic bacterium Rhodovulum sulfidophilum have been solved at 1.75 A resolution in the oxidized state and at 1,5 A resolution in the dithionite-reduced state, providing the first structural insights into the enzymatic oxidation of thiosulfate. The SoxAX active site contains a haem with unprecedented cysteine persulfide (cysteine sulfane) coordination. This unusual post- translational modification is also seen in sulfurtransferases such as rhodanese. Intriguingly, this enzyme shares further active site characteristics with SoxAX such as an adjacent conserved arginine residue and a strongly positive electrostatic potential. These similarities have allowed us to suggest a catalytic mechanism for enzymatic thiosulfate oxidation. The atomic coordinates and experimental structure factors have been deposited in the PDB with the accession codes 1H31, 1H32 and 1H33. [ABSTRACT FROM AUTHOR]

Published
2002
Full Text
View/download PDF

31. The Structure of YnaI Implies Structural and Mechanistic Conservation in the MscS Family of Mechanosensitive Channels

Author

Böttcher, Bettina, Prazak, Vojtech, Rasmussen, Akiko, Black, Susan S., and Rasmussen, Tim

Subjects
Structural Biology, protein-lipid interaction, cryo-electron microscopy, fluorescence, osmotic stress, bacteria, Molecular Biology
Abstract

Mechanosensitive channels protect bacteria against lysis caused by a sudden drop in osmolarity in their surroundings. Besides the channel of large conductance (MscL) and small conductance (MscS), Escherichia coli has five additional paralogs of MscS that are functional and widespread in the bacterial kingdom. Here, we present the structure of YnaI by cryo-electron microscopy to a resolution of 13 Å. While the cytosolic vestibule is structurally similar to that in MscS, additional density is seen in the transmembrane (TM) region consistent with the presence of two additional TM helices predicted for YnaI. The location of this density suggests that the extra TM helices are tilted, which could induce local membrane curvature extending the tension-sensing paddles seen in MscS. Off-center lipid-accessible cavities are seen that resemble gaps between the sensor paddles in MscS. The conservation of the tapered shape and the cavities in YnaI suggest a mechanism similar to that of MscS.

Full Text
View/download PDF

32. KTN (RCK) Domains Regulate K+ Channels and Transporters by Controlling the Dimer-Hinge Conformation

Author

Roosild, Tarmo P., Castronovo, Samantha, Miller, Samantha, Li, Chan, Rasmussen, Tim, Bartlett, Wendy, Gunasekera, Banuri, Choe, Senyon, and Booth, Ian R.

Subjects
*PROTEIN binding, *NUCLEOTIDES, *POTASSIUM channels, *CELL membranes, *CELLULAR control mechanisms, *CYTOPLASM, *DIMERS, *ELECTROPHYSIOLOGY
Abstract

Summary: KTN (RCK) domains are nucleotide-binding folds that form the cytoplasmic regulatory complexes of various K+ channels and transporters. The mechanisms these proteins use to control their transmembrane pore-forming counterparts remains unclear despite numerous electrophysiological and structural studies. KTN (RCK) domains consistently crystallize as dimers within the asymmetric unit, forming a pronounced hinge between two Rossmann folds. We have previously proposed that modification of the hinge angle plays an important role in activating the associated membrane-integrated components of the channel or transporter. Here we report the structure of the C-terminal, KTN-bearing domain of the E. coli KefC K+ efflux system in association with the ancillary subunit, KefF, which is known to stabilize the conductive state. The structure of the complex and functional analysis of KefC variants reveal that control of the conformational flexibility inherent in the KTN dimer hinge is modulated by KefF and essential for regulation of KefC ion flux. [Copyright &y& Elsevier]

Published
2009
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results