Zobrazeno 1 - 10 of 147 pro vyhledávání: '"T H, Wilson"'
2
The Melibiose Carrier of Escherichia coli: Cysteine Substitutions for Individual Residues in Helix XI
Autor: T. H. Wilson, Ping Z. Ding
Publikováno v: Journal of Membrane Biology. 174:135-140
The melibiose carrier from Escherichia coli is a sugar-cation cotransport system. Previously evidence was obtained that this integral membrane protein consists of 12 transmembrane helices. Starting with the cysteine-less melibiose carrier, cysteine h
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3a64ea86ea4e6b3362c96d4127d5925
https://doi.org/10.1007/s002320001038
Zobrazit plný text záznamu
3
DERMATITIS FROM DYED UNIFORM
Autor: Etain Cronin, H. T. H. Wilson
Publikováno v: British Journal of Dermatology. 85:67-69
SUMMARY.— Five nursing sisters developed dermatitis from their blue uniform. In each case patch tests showed them to be sensitive not to the blue dye but to a green anthraquinone dye used as a shading component.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b925e3b360ee717e3bd6c92382a71025
https://doi.org/10.1111/j.1365-2133.1971.tb07181.x
Zobrazit plný text záznamu
4
Replacement of alanine 58 by asparagine enables the melibiose carrier of Klebsiella pneumoniae to couple sugar transport to Na+
Autor: H Hama, T H Wilson
Publikováno v: Journal of Biological Chemistry. 269:1063-1067
The melibiose carrier of Klebsiella pneumoniae couples sugar transport to H+ and Li+, while that of Escherichia coli uses Na+ besides the other two cation species (Hama and Wilson, 1992). We have shown that the K. pneumoniae melibiose carrier is capa
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::893446d62b6577cb00b1712323830aa3
https://doi.org/10.1016/s0021-9258(17)42221-6
Zobrazit plný text záznamu
6
Lysine 319 interacts with both glutamic acid 269 and aspartic acid 240 in the lactose carrier of Escherichia coli
Autor: Pung Pung Hwang, Jong-In Lee, T H Wilson
Publikováno v: Journal of Biological Chemistry. 268:20007-20015
It is believed that there are several charged amino acid residues in membrane-spanning alpha-helices of the lactose carrier of Escherichia coli. Evidence has previously been presented for two different salt bridges in membrane-spanning regions of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f7167e613e711587906715e3fe2d589a
https://doi.org/10.1016/s0021-9258(20)80687-5
Zobrazit plný text záznamu
7
Cation-coupling in chimeric melibiose carriers derived from Escherichia coli and Klebsiella pneumoniae. The amino-terminal portion is crucial for Na+ recognition in melibiose transport
Autor: H Hama, T H Wilson
Publikováno v: Journal of Biological Chemistry. 268:10060-10065
The melibiose carrier of Escherichia coli couples sugar transport to H+, Na+, and Li+, while that of Klebsiella pneumoniae utilizes only H+ and Li+. We made five chimeric carriers derived from the two carriers to identify the region(s) involved in Na
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c70a9441be1d1e3b8b7fe66dfd3ba6ed
https://doi.org/10.1016/s0021-9258(18)82172-x
Zobrazit plný text záznamu
10
Possible salt bridges between transmembrane alpha-helices of the lactose carrier of Escherichia coli
Autor: C. Hansen, Pung Pung Hwang, Jong-In Lee, T H Wilson
Publikováno v: Journal of Biological Chemistry. 267:20758-20764
Although it is energetically extremely unfavorable to have charged amino acid residues of a polypeptide in the hydrophobic environment of the membrane phospholipid bilayer, a few such charged residues are found in membrane-spanning regions of membran
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d6dea516c75d90f2e578d16791ae344b
https://doi.org/10.1016/s0021-9258(19)36751-1
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje