Results 261 to 270 of about 40,867 (306)
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Disulfide Bridges in Defensins
Current Topics in Medicinal Chemistry, 2015Defensins are small cationic cysteine rich peptides, which usually contain 18-45 amino acids and possess amphiphilic properties. The term "defensin" was coined as the sequences of rabbit and human leukin/phagocytin molecules were first reported in 1985.
Bing-Chuan, Zhao +4 more
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A centric thiuram disulfide. Structure of tetraisopropylthiuram disulfide
Acta Crystallographica Section C Crystal Structure Communications, 1990C 14 H 28 N 2 S 4 cristallise dans P2 1 /n avec a=6,137, b=11,392, c=13,446 A, β=91,98 o , Z=2; affinement jusqu'a R=0,041. La molecule est centrosymetrique. Dans le centre de la molecule, la moitie C-S-S-C adopte une conformation trans plane.
V. Kumar, G. Aravamudan, M. Seshasayee
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American Journal of Kidney Diseases, 2000
A 45-year-old nondiabetic man presented with features resembling diabetic triopathy. He worked in a rayon manufacturing plant and was exposed to toxic levels of carbon disulfide (CS(2)). Clinical abnormalities included peripheral and central nervous system abnormalities as well as retinopathy, dyslipidemia, cardiovascular disease, and nephrotic ...
P J, Klemmer, A A, Harris
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A 45-year-old nondiabetic man presented with features resembling diabetic triopathy. He worked in a rayon manufacturing plant and was exposed to toxic levels of carbon disulfide (CS(2)). Clinical abnormalities included peripheral and central nervous system abnormalities as well as retinopathy, dyslipidemia, cardiovascular disease, and nephrotic ...
P J, Klemmer, A A, Harris
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Catalysis of Disulfide Isomerization in Thrombospondin 1 by Protein Disulfide Isomerase
Biochemistry, 1996Thrombospondin 1 is a multidomain glycoprotein from platelets and most cells that participates in diverse biological processes. The structure and some functional properties of thrombospondin 1 are regulated by disulfide interchange in the Ca(2+)-binding repeats and C-globular domain. The recent identification of the enzyme, protein disulfide isomerase,
K A, Hotchkiss +2 more
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Mechanistic insights into a copper–disulfide interaction in oxidation of imines by disulfides
Chemical Communications, 2009The concept of using disulfides as an oxidant for Cu(i) is introduced as part of a Cu-catalyzed process leading to the formation of benzothiazole from an iminodisulfide under an inert atmosphere.
Jiri, Srogl +3 more
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Anodic Oxidation of Disulfides: Detection and Reactions of Disulfide Radical Cations
The Journal of Organic Chemistry, 2013The anodic oxidation of five diaryldisulfides have been studied in a dichloromethane/[NBu4][B(C6F5)4] electrolyte. Cyclic voltammetry scans of (p-RC6H4)2S2 (R = Me, 1a; R = F, 1b; R = OMe, 1c) show modest chemical reversibility for the 1(0/+) couple (E1/2 values vs ferrocene: 1.04 V for 1a, 1.21 V for 1b, 0.92 V for 1c), providing the first ...
Kevin, Lam, William E, Geiger
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Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
1984Publisher Summary Protein disulfide-isomerase (PDI) catalyzes the formation of native proteins from the reduced denatured state. When incubated in the presence of a thiol compound, PDI catalyzes the regain of native ribonuclease structure from the scrambled ribonuclease, with concomitant return of activity toward RNA.
D A, Hillson, N, Lambert, R B, Freedman
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Chemical reduction of disulfides
1987Publisher Summary This chapter discusses the chemical reduction of disulfides. Disulfides are easily and specifically reduced by thiols, which are the most used reagents for this purpose. However, the excess of the thiol used as a reductant has to be removed before it is possible to assay the newly generated SH groups.
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