Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Outer-membrane phospholipase A"'
Publikováno v:
Current Research in Microbial Sciences, Vol 3, Iss , Pp 100172- (2022)
Bordetella pertussis is the causative agent of a respiratory infection known as whooping cough. With the goal of improving the production of outer-membrane vesicles (OMVs), we studied here the mechanisms that are involved in maintaining lipid asymmet
Externí odkaz:
https://doaj.org/article/f1417f9939ea4efc8f2982d4cf3a5d23
Autor:
De jonge, Eline F., Vogrinec, Lana, Van boxtel, Ria, Tommassen, Jan, Molecular Microbiology, Sub Molecular Microbiology
Publikováno v:
Current Research in Microbial Sciences, 3. Elsevier BV
Bordetella pertussis is the causative agent of a respiratory infection known as whooping cough. With the goal of improving the production of outer-membrane vesicles (OMVs), we studied here the mechanisms that are involved in maintaining lipid asymmet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd06cdf0bd3c57c26bd0058d9f408f96
https://dspace.library.uu.nl/handle/1874/425089
https://dspace.library.uu.nl/handle/1874/425089
Autor:
Koki Kamiya, Seren Ohnishi
Publikováno v:
Biophysical Journal. 120:226a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::521cb1357df35f4d0067719992491161
https://doi.org/10.1016/j.bpj.2020.11.1509
https://doi.org/10.1016/j.bpj.2020.11.1509
Autor:
Erik Frotscher, Michael Schlierf, Philip Gröger, Sandro Keller, Andreas Hartmann, Neharika Chamachi, Pablo Gracia, Georg Krainer
Publikováno v:
Biophysical Journal. 114:243a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22ca8cef6d0460f636e208194fdc8708
https://doi.org/10.1016/j.bpj.2017.11.1355
https://doi.org/10.1016/j.bpj.2017.11.1355
Autor:
Peter Tieleman, Shelby Lipes, Linda Columbus, Svetlana Baoukina, Ashton T. Brock, Ryan C. Oliver
Publikováno v:
Biophysical Journal. 110:571a-572a
Micelles and bicelles are used to isolate membrane proteins for biophysical characterization, functional assays, and high-resolution structure determination. Utilizing these membrane mimics requires an extensive screening process to identify the appr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bc8dfc9f8cc6e070405c6d2d6ae7aa3
https://doi.org/10.1016/j.bpj.2015.11.3058
https://doi.org/10.1016/j.bpj.2015.11.3058
Publikováno v:
Journal of Structural Biology, 141(2), 122-131. ACADEMIC PRESS INC ELSEVIER SCIENCE
The structure of the detergent in crystals of outer membrane phospholipase A (OMPLA) has been determined using neutron diffraction contrast variation. Large crystals were soaked in stabilising solutions, each containing a different H2O/D2O contrast.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed4abcbc2c6c3a7e63730e29a5bfa6e6
https://doi.org/10.1016/S1047-8477(02)00579-8
https://doi.org/10.1016/S1047-8477(02)00579-8
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Publikováno v:
FEBS Letters, 373(1), 10-12. Wiley
The outer membrane phospholipase A (OMPLA) of Escherichia coli is one of the few integral outer membrane proteins displaying enzymatic activity, It is encoded as a mature protein of 269 amino acids preceded by a signal sequence of 20 amino acids. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6175548ba746f5c2836004879552d37f
https://doi.org/10.1016/0014-5793(95)01002-v
https://doi.org/10.1016/0014-5793(95)01002-v
Publikováno v:
Biophysical Journal. 108:254a
Membrane protein research is hampered by the difficulty in selecting a membrane mimic that solubilizes and stabilizes protein fold and function. While detergents are often utilized, identifying the appropriate detergent composition to maintain protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d25993bf08690d2e01442100901c50e7
https://doi.org/10.1016/j.bpj.2014.11.1407
https://doi.org/10.1016/j.bpj.2014.11.1407
Autor:
R.L. Kingma, Maarten R. Egmond
Publikováno v:
FEBS letters. 516(1-3)
Outer membrane phospholipase A (OMPLA) activity is regulated by reversible dimerisation with the dimer being the active species. Observed lag phases in activity indicated that dimerisation may be slow relative to turnover. A covalent OMPLA dimer inde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c098757f7adc90487a8319ee94005c5b
https://pubmed.ncbi.nlm.nih.gov/11959097
https://pubmed.ncbi.nlm.nih.gov/11959097