Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Candan Ariöz"'
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e88153 (2014)
Synthesis of monogalactosyldiacylglycerol (GalDAG) and digalactosyldiacylglycerol (GalGalDAG), the major membrane lipids in cyanobacteria, begins with production of the intermediate precursor monoglucosyldiacylglycerol (GlcDAG), by monoglucosyldiacyl
Externí odkaz:
https://doaj.org/article/aa5fb41e0d16499fb9edad9d94181f89
Publikováno v:
Quarterly reviews of biophysics. 51
Copper is a redox–active transition metal ion required for the function of many essential human proteins. For biosynthesis of proteins coordinating copper, the metal may bind before, during or after folding of the polypeptide. If the metal binds to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4e2cd3b505736250430e5078efdfaad
https://pubmed.ncbi.nlm.nih.gov/30912494
https://pubmed.ncbi.nlm.nih.gov/30912494
Autor:
Yaozong Li, Ranjeet Kumar, Candan Ariöz, Pernilla Wittung-Stafshede, Niklas Bosaeus, Sandra Rocha
Publikováno v:
Biometals
After cellular uptake, Copper (Cu) ions are transferred from the chaperone Atox1 to the Wilson disease protein (ATP7B) for incorporation into Cu-dependent enzymes in the secretory pathway. Human ATP7B is a large multi-domain membrane-spanning protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea6787b3ba16d91b0fbf8336066c9247
https://doi.org/10.1007/s10534-016-9976-7
https://doi.org/10.1007/s10534-016-9976-7
Publikováno v:
Biomolecular Concepts, Vol 7, Iss 1, Pp 29-39 (2016)
Copper (Cu) ions are cofactors in many essential enzymes. As free Cu ions are toxic, most organisms have highly specialized Cu transport systems involving dedicated proteins. The human cytoplasmic Cu chaperone Atox1 delivers Cu to P1B-type ATPases in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5852a79da5a31484595827696af596cf
https://doaj.org/article/2693ac5f413e405d97097c02d5cd458b
https://doaj.org/article/2693ac5f413e405d97097c02d5cd458b
Autor:
Nicole Hansmeier, Åke Wieslander, Candan Ariöz, Daniel O. Daley, Sabine Hunke, Amélie A. Kelly, Filippa Stenberg-Bruzell, Rebecca Keller, Malin Burstedt, David Vikström
Publikováno v:
Biochemistry. 54:3670-3676
The Cpx stress response system is induced by various environmental and cellular stimuli. It is also activated in Escherichia coli strains lacking the major phospholipid, phosphatidylethanolamine (PE). However, it is not known whether CpxA directly se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0ee26a64e9b4cf7122dfd48fba24d3d
https://doi.org/10.1021/acs.biochem.5b00242
https://doi.org/10.1021/acs.biochem.5b00242
Autor:
Jobst Liebau, Weihua Ye, Changrong Ge, Lena Mäler, Åke Wieslander, Amin al Bakali, Hansjörg Götzke, Andreas Barth, Candan Ariöz
Publikováno v:
Biochemistry. 52:5533-5544
Certain membrane proteins involved in lipid synthesis can induce formation of new intracellular membranes in Escherichia coli, i.e., intracellular vesicles. Among those, the foreign monotopic glycosyltransferase MGS from Acholeplasma laidlawii trigge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02bcdf99dcf0a726c75c42655fb3dc88
https://doi.org/10.1021/bi400616n
https://doi.org/10.1021/bi400616n
Publikováno v:
Biochimica et biophysica acta. 1858(9)
Solution-state NMR requires small membrane mimetic systems to allow for acquiring high-resolution data. At the same time these mimetics should faithfully mimic biological membranes. Here we characterized two novel fast-tumbling bicelle systems with l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c1f53b01e20541fa9587b9e79eece74
https://pubmed.ncbi.nlm.nih.gov/27317394
https://pubmed.ncbi.nlm.nih.gov/27317394
Publikováno v:
Applied Biochemistry and Biotechnology. 160:2187-2197
Multipoint covalent bonding of glucose oxidase (EC 1.1.3.4) to hydrophilic natural polymer dextran and optimization of procedures to obtain, with enhanced temperature and pH stabilities, were studied. Purified enzyme was conjugated with various molec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::650722410e7d5cb8f5facd2d47950d49
https://doi.org/10.1007/s12010-009-8812-8
https://doi.org/10.1007/s12010-009-8812-8
Publikováno v:
Open Chemistry, Vol 7, Iss 3, Pp 423-428 (2009)
Stabilization of Horseradish Peroxidase (HRP; EC 1.11.1.7) against temperature and pH via the formation of the conjugates obtained by multipoint covalent bonding of dextran aldehyde (DA) to the enzyme were studied. Hence, three different molar weight
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ca69593c7242d62bf4b770f3f97e733
https://doaj.org/article/1d84e076295447a8ba87d2f27157e73c
https://doaj.org/article/1d84e076295447a8ba87d2f27157e73c
Autor:
Ljubica Lindholm, Candan Ariöz, Jobst Liebau, Andreas Barth, Åke Wieslander, Lena Mäler, Christopher von Ballmoos, Michael Jawurek
The significance of specific lipids for proton pumping by the bacterial rhodopsin proteorhodopsin (pR) was studied. To this end, it was examined whether pR preferentially binds certain lipids and whether molecular properties of the lipid environment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18990e03e13e621e32e8cf7c39dcaedc
