Zobrazeno 1 - 10
of 87
pro vyhledávání: '"T. Hastings Wilson"'
Autor:
Ohsuk Kwon, Laura Baldomà, Edmund C. C. Lin, T. Hastings Wilson, Marı́a Felisa Núñez, Juan Aguilar
Publikováno v:
Biochemical and Biophysical Research Communications. 290:824-829
To examine the substrate specificity of the membrane transport carriers LldP ( l -lactate permease) and GlcA (glycolate permease) of Escherichia coli, a mutant strain lacking their structural genes and blocked in the metabolism of the tested substrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9cf73d9e050a4f0556837c2c455f544
https://doi.org/10.1006/bbrc.2001.6255
https://doi.org/10.1006/bbrc.2001.6255
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1510:231-242
The melibiose carrier from Escherichia coli is a cation-substrate cotransporter that catalyzes the accumulation of galactosides at the expense of H(+), Na(+), or Li(+) electrochemical gradients. Charged residues on transmembrane domains in the amino-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c30b1460c4ee0a89d59774f4c196687b
https://doi.org/10.1016/s0005-2736(00)00353-9
https://doi.org/10.1016/s0005-2736(00)00353-9
Autor:
T. Hastings Wilson
Publikováno v:
Nutrition Reviews. 23:33-35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2618801c705b5f8e86058c85287e365f
https://doi.org/10.1111/j.1753-4887.1965.tb02064.x
https://doi.org/10.1111/j.1753-4887.1965.tb02064.x
Autor:
Dorothy M. Wilson, T. Hastings Wilson
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1374:77-82
The melibiose carrier of Escherichia coli is a cation-sugar cotransport protein. Asp124 in membrane-spanning helix IV of the carrier protein was replaced with Ser, Ile or Phe by site-directed mutagenesis of a plasmid containing the melB gene. Each of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::869f021744b71df3cda7102bc7ea621b
https://doi.org/10.1016/s0005-2736(98)00132-1
https://doi.org/10.1016/s0005-2736(98)00132-1
Autor:
Tomofusa Tsuchiya, T. Hastings Wilson, Audrey C. Weissborn, Masayuki Kuroda, Martyn C. Botfield
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1329(2):237-244
The melibiose carrier of E. coli is a cation-sugar cotransport system. This membrane protein contains four cysteine residues and the transport function is inhibited by sulfhydryl reagents. In order to investigate the importance of the cysteines, we h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7aa1d0b34f4a0e41e3fed0d5d1399169
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1278:111-118
Site-directed mutagenesis and second-site suppressor analysis have proven to be useful approaches to examine the role of charged amino acids in the structure and function of the lactose carrier of Escherichia coli . A lactose carrier mutant Glu-325
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70efb83dc2317a5eef200bf14d0e87d9
https://doi.org/10.1016/0005-2736(95)00209-x
https://doi.org/10.1016/0005-2736(95)00209-x
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1062:177-186
The lacY from Escherichia coli strains 020 and AE43 have been cloned on plasmids which were designated p020-K358T and pAE43-D237N. These lacY mutants contain amino acid substitutions changing Lys-358 to Thr or Asp-237 to Asn, respectively. The charge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80753ed09771f633741a6ac04292ce75
https://doi.org/10.1016/0005-2736(91)90390-t
https://doi.org/10.1016/0005-2736(91)90390-t
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1029:113-116
The lactose carrier activity of Escherichia coli in inhibited by the binding of dephosphorylated glucose enzyme III. Saier et al. (1978) J. Bacteriol. 133, 1358–1367) isolated lac Y mutants that escaped this inhibition. This communication reports t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e220033225acd055a25e6e3089d3253f
https://doi.org/10.1016/0005-2736(90)90443-r
https://doi.org/10.1016/0005-2736(90)90443-r
Autor:
Ping Z. Ding, T. Hastings Wilson
Publikováno v:
Biochemistry. 40(18)
The melibiose carrier of Escherichia coli is a sugar-cation cotransport system that utilizes Na(+), Li(+), or H(+). This membrane transport protein consists of 12 transmembrane helices. Starting with the cysteine-less melibiose carrier, cysteine has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12b31ce4bb117ecd36dd3c55dbe066d4
https://pubmed.ncbi.nlm.nih.gov/11331015
https://pubmed.ncbi.nlm.nih.gov/11331015
Autor:
Ping Z. Ding, T. Hastings Wilson
Publikováno v:
Biochemical and biophysical research communications. 268(2)
In a previous study 23 residues in helix XI of the cysteine-less melibiose carrier were changed individually to cysteine. Several of these cysteine mutants (K377C, A383C, F385C, L391C, G395C) had low transport activity and they were white on melibios
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::491a25aa3833b48dd2a62f9ee473856e
https://pubmed.ncbi.nlm.nih.gov/10679218
https://pubmed.ncbi.nlm.nih.gov/10679218