Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Martin Raunest"'
Publikováno v:
Interdisciplinary Sciences: Computational Life Sciences. 6:1-12
The continuous rise of bacterial resistance against formerly effective pharmaceuticals is a major challenge for biomedical research. Since the first computational studies published seven years ago the simulation-based investigation of antibiotics res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f989b342fe12314d80753105d843a4ae
https://doi.org/10.1007/s12539-014-0191-3
https://doi.org/10.1007/s12539-014-0191-3
Publikováno v:
Biochemistry. 52:178-187
Acting as an efflux duct in the MexA-MexB-OprM multidrug efflux pump, OprM plays a major role in the antibiotic resistance capability of Pseudomonas aeruginosa, trafficking substrates through the outer cell membrane. Whereas the available crystal str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca98cff0e4f2143d615ad1daa296bb75
https://doi.org/10.1021/bi3014714
https://doi.org/10.1021/bi3014714
Publikováno v:
Biochimica et biophysica acta. 1858(7 Pt)
One way by which bacteria achieve antibiotics resistance is preventing drug access to its target molecule for example through an overproduction of multi-drug efflux pumps of the resistance nodulation division (RND) protein super family of which AcrAB
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34a3a2cb0d4f5caeac2988009660e9ee
https://pubmed.ncbi.nlm.nih.gov/27045078
https://pubmed.ncbi.nlm.nih.gov/27045078
Autor:
Christian Kandt, Martin Raunest
Publikováno v:
Journal of Molecular Graphics and Modelling. 29:895-905
Empty space in a protein structure can provide valuable insight into protein properties such as internal hydration, structure stabilization, substrate translocation, storage compartments or binding sites. This information can be visualized by means o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea37f4076241b39dbd406c5df0f56855
https://doi.org/10.1016/j.jmgm.2011.02.003
https://doi.org/10.1016/j.jmgm.2011.02.003
Autor:
Christian Kandt, Martin Raunest
Publikováno v:
Biochemistry. 51(8)
Playing a major role in the expulsion of antibiotics and the secretion of cell toxins in conjunction with inner membrane transporters of three protein superfamilies, the outer membrane channel TolC occurs in at least two states blocking or permitting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35251be0b01b0a0f03bb03cfe73a3942
https://pubmed.ncbi.nlm.nih.gov/22313049
https://pubmed.ncbi.nlm.nih.gov/22313049
Publikováno v:
Biophysical Journal. 100(3)
With known antibiotics losing their efficiency faster than new ones can be developed, a better understanding of the underlying molecular mechanisms is paramount. Multidrug resistance is often caused by an over-production of efflux transporters that e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66a1225afa5d3edde457c8a2fa8b0473
Autor:
Christian Kandt, Martin Raunest
Publikováno v:
Biophysical Journal. 100(3)
Empty space in a protein structure can provide valuable insight into protein properties such as internal hydration, structure stabilization, substrate translocation, storage compartments or binding sites. This information can be visualized by means o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e243ba155f898cc8c614c1fd9e85993
Publikováno v:
Biophysical Journal. 98(3)
Over-production of multi-drug efflux pumps is a prominent example of how bacteria gain resistance against antibiotics. In Escherichia coli the AcrA/B-TolC efflux pump is capable to expel a broad range of drugs, using the energy of proton-motive force
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ea2073cd213789c239de0fad33db0c9
Autor:
Christian Kandt, Martin Raunest
Publikováno v:
Biophysical Journal. 102:622a-623a
In Escherichia coli TolC functions as an efflux duct interacting with various inner membrane translocases including the multi-drug efflux pump AcrB. To investigate TolC wild-type dynamics, we performed five 150ns molecular dynamics simulations of Tol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f6448b32be5122cf91cf4caee100e5b
https://doi.org/10.1016/j.bpj.2011.11.3392
https://doi.org/10.1016/j.bpj.2011.11.3392
Computer Simulation of TolC Ground State Dynamics and Spontaneous Binding of the AcrB Docking Domain
Publikováno v:
Biophysical Journal. 100:132a
In Escherichia coli the AcrAB-TolC efflux pump expels a broad range of drugs and other molecules. While AcrB is the engine in this system, the outer membrane protein TolC functions as an efflux duct interacting with numerous inner membrane translocas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da26282214b65a016e5357bcaddce14e
https://doi.org/10.1016/j.bpj.2010.12.926
https://doi.org/10.1016/j.bpj.2010.12.926