Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Guifu Xie"'
Autor:
Patricia C. Edwards, Maikel Fransen, Guifu Xie, Gebhard F. X. Schertler, Aaron M. D’Antona, Jörg Standfuss, Daniel D. Oprian
Publikováno v:
Nature. 471:656-660
Structural studies of active states of the visual pigment rhodopsin, a G protein-coupled receptor, have previously been limited to apoprotein or opsin forms that do not contain the agonist all-trans-retinal. Two groups now report structures that reve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab5894b1c75cb234ed0f152be9beec15
https://doi.org/10.1038/nature09795
https://doi.org/10.1038/nature09795
Autor:
Guifu Xie, Maikel Fransen, Gebhard F. X. Schertler, Aaron M. D’Antona, Jörg Standfuss, Patricia C. Edwards, Daniel D. Oprian
Publikováno v:
Biochemistry
The interaction of rhodopsin and transducin has been the focus of study for more than 30 years, but only recently have efforts to purify an activated complex in detergent solution materialized. These efforts have used native rhodopsin isolated from b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecb2084da0bc3929cad42ce133009455
Publikováno v:
Journal of Biological Chemistry. 282:14875-14881
Nanodiscs are nanometer scale planar membranes of controlled size that are rendered soluble in aqueous solution via an encircling amphipathic membrane scaffold protein "belt" (Bayburt, T. H., Grinkova, Y. V., and Sligar, S. G. (2002) Nano. Lett. 2, 8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e3d6d1a6e11af627d310e600d59e976
https://doi.org/10.1074/jbc.m701433200
https://doi.org/10.1074/jbc.m701433200
Autor:
Serge N. Timasheff, Guifu Xie
Publikováno v:
Biophysical Chemistry. 105:421-448
The interactions involved in the denaturation of lysozyme in the presence of urea were examined by thermal transition studies and measurements of preferential interactions of urea with the protein at pH 7.0, where it remains native up to 9.3 M urea,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eea95fcf4954bcd7dc3590cdf672aecc
https://doi.org/10.1016/s0301-4622(03)00106-6
https://doi.org/10.1016/s0301-4622(03)00106-6
Publikováno v:
Biochemistry. 42:2002-2008
In an examination of the effect of three rhodopsin night blindness mutations on the rate of association of 11-cis-retinal with opsin, one of the mutations (G90D) was found to slow the rate of reaction by more than 80-fold. This effect does not appear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79a3fbb98b5fa7f452d991616daf3a3f
https://doi.org/10.1021/bi020612r
https://doi.org/10.1021/bi020612r
Publikováno v:
Biochemistry. 42:1995-2001
This report describes the biochemical characterization of a double mutant of rhodopsin (N2C,D282C) in which Cys residues engineered into the protein at positions 2 (in the amino-terminal extracellular domain) and 282 (in the extracellular loop betwee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfafbc84b94fbd3c43385245060e5ca2
https://doi.org/10.1021/bi020611z
https://doi.org/10.1021/bi020611z
Autor:
Serge N. Timasheff, Guifu Xie
Publikováno v:
Protein Science. 6:222-232
The temperature dependence of preferential solvent interactions with ribonuclease A in aqueous solutions of 30% sorbitol, 0.6 M MgCl2, and 0.6 M MgSO4 at low pH (1.5 and 2.0) and high pH (5.5) has been investigated. This protein was stabilized by all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1304449ead2143f9607817124b625cf
https://doi.org/10.1002/pro.5560060124
https://doi.org/10.1002/pro.5560060124
Autor:
Serge N. Timasheff, Guifu Xie
Publikováno v:
Protein Science. 6:211-221
The effect of interactions of sorbitol with ribonuclease A (RNase A) and the resulting stabilization of structure was examined in parallel thermal unfolding and preferential binding studies with the application of multicomponent thermodynamic theory.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c68dd4b277ea494cdf756cef3130d2ce
https://doi.org/10.1002/pro.5560060123
https://doi.org/10.1002/pro.5560060123
Publikováno v:
Biochemistry. 53(1)
The formation and characterization of an activated complex of the visual pigment rhodopsin and its downstream signaling partner transducin has been the subject of intense focus by several research groups. While the subunit composition of the activate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ea2ae697f07d3d85464844c3acdd6fd
https://pubmed.ncbi.nlm.nih.gov/24328127
https://pubmed.ncbi.nlm.nih.gov/24328127
Autor:
Patricia C. Edwards, Jörg Standfuss, Manfred Burghammer, Gebhard F. X. Schertler, Daniel D. Oprian, Guifu Xie
We determined the structure of the rhodopsin mutant N2C/D282C expressed in mammalian cells; the first structure of a recombinantly produced G protein-coupled receptor (GPCR). The mutant was designed to form a disulfide bond between the N terminus and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::306d2e3cf1217103388d214b5be9839d
https://europepmc.org/articles/PMC2258155/
https://europepmc.org/articles/PMC2258155/
