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S J Rosselet

Explore the profile of S J Rosselet including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 7
Citations 164
Followers 0
Related Specialties
Biochemistry
Science
Top 10 Co-Authors
T Marti
H G Khorana
M P Heyn
H Otto
K Titani
J Schaller
K A Walsh
E E RICKLI
S Subramaniam
P W Moser
Published In
J Biol Chem
Proc Natl Acad Sci U S A
Eur J Biochem
Biochemistry
Affiliations
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Recent Articles
1.
Anion binding to the Schiff base of the bacteriorhodopsin mutants Asp-85----Asn/Asp-212----Asn and Arg-82----Gln/Asp-85----Asn/Asp-212----Asn
Marti T, Otto H, Rosselet S, Heyn M, Khorana H
J Biol Chem . 1992 Aug; 267(24):16922-7. PMID: 1512233
Studies of bacteriorhodopsin have indicated that the charge environment of the protonated Schiff base consists of residues Asp-85, Asp-212, and Arg-82. As shown recently (Marti, T., Rösselet, S. J., Otto,...
2.
Consequences of amino acid insertions and/or deletions in transmembrane helix C of bacteriorhodopsin
Marti T, Otto H, Rosselet S, Heyn M, Khorana H
Proc Natl Acad Sci U S A . 1992 Feb; 89(4):1219-23. PMID: 1531536
Six bacterioopsin mutants containing either single amino acid deletions (delta A84, delta L87), insertions (delta 85A, delta 88A), or both deletions and insertions (delta A84/delta 88A, delta 85A/delta L87) within...
3.
The retinylidene Schiff base counterion in bacteriorhodopsin
Marti T, Rosselet S, Otto H, Heyn M, Khorana H
J Biol Chem . 1991 Oct; 266(28):18674-83. PMID: 1917991
Previous studies of bacteriorhodopsin have indicated interactions between Asp-85, Asp-212, Arg-82, and the retinylidene Schiff base. The counterion environment of the Schiff base has now been further investigated by using...
4.
Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation
Marti T, Otto H, Mogi T, Rosselet S, Heyn M, Khorana H
J Biol Chem . 1991 Apr; 266(11):6919-27. PMID: 1849896
To study their role in proton translocation by bacteriorhodopsin, 22 serine and threonine residues presumed to be located within and near the border of the transmembrane segments have been individually...
5.
The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates
Subramaniam S, Marti T, Rosselet S, Rothschild K, Khorana H
Proc Natl Acad Sci U S A . 1991 Mar; 88(6):2583-7. PMID: 2006195
The reaction of the retinylidene Schiff base in bacteriorhodopsin (bR) to the water-soluble reagent hydroxylamine is enhanced by greater than 2 orders of magnitude under illumination. We have used this...
6.
Identification of disulfide-bridged substructures within human von Willebrand factor
Marti T, Rosselet S, Titani K, Walsh K
Biochemistry . 1987 Dec; 26(25):8099-109. PMID: 3502076
In the course of identifying substructural domains within the homooligomeric protein von Willebrand factor [270 kilodaltons (kDa) per polypeptide chain], seven large fragments of 8-90 kDa have been generated by...
7.
Complete amino acid sequence of bovine plasminogen. Comparison with human plasminogen
Schaller J, Moser P, Rosselet S, Kampfer U, RICKLI E
Eur J Biochem . 1985 Jun; 149(2):267-78. PMID: 3846532
The amino acid sequence of the single polypeptide chain of bovine plasminogen (786 residues, Mr 88092) was determined. Cleavage with CNBr yielded 13 fragments of which six originated from cleavage...