Results 171 to 180 of about 20,641 (189)

Display of disulfide-rich proteins by complementary DNA display and disulfide shuffling assisted by protein disulfide isomerase

Analytical Biochemistry, 2011
We report an efficient system to produce and display properly folded disulfide-rich proteins facilitated by coupled complementary DNA (cDNA) display and protein disulfide isomerase-assisted folding. The results show that a neurotoxin protein containing four disulfide linkages can be displayed in the folded state.
Mohammed Naimuddin, Tai Kubo, Tai Kubo
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The role of the disulfide group in disulfide-based polymeric gene carriers

Expert Opinion on Drug Delivery, 2009
An essential prerequisite for successful gene therapy is the development of safe and efficient gene delivery carriers. For this purpose, cationic polymers have been widely studied as non-viral carriers, but they generally suffer from low transfection efficiency and/or high cytotoxicity.
C. Lin, Johannes F.J. Engbersen
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Disulfides by reduction of thiosulfunic S-esters

Tetrahedron Letters, 1982
Abstract Disulfides are smoothly prepared from thiosulfonic S-esters by chlorotrimethylsilane and sodium iodide. In addition, thiosulfonic S-esters have been shown to be probable intermediates in other already known reactions leading to disulfides.
PALUMBO, GIOVANNI, PARRILLI, MICHELANGELO, O. Neri, FERRERI, CARLA, CAPUTO, ROMUALDO   +4 more
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Catalysis of Disulfide Isomerization in Thrombospondin 1 by Protein Disulfide Isomerase

Biochemistry, 1996
Thrombospondin 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,
Colin N. Chesterman, Kylie A. Hotchkiss, Philip J. Hogg   +2 more
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Electrochemical reduction of disulfides

1987
Publisher Summary Electrochemical reduction of disulfides has been reported to give higher yields of thiols than alternative zinc-acid or borohydride reductions. The use of electrochemical reduction is exemplified by the low toxicity, high yield, selective analysis of urinary captopril [(S,S)-l-(3-mercapto-2-D-methyl-l-oxopropyl)-L-proline], an ...
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Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase

1984
Publisher 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.
David A. Hillson, Nigel Lambert, Robert B. Freedman   +2 more
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Electrical properties of the Group IV disulfides, titanium disulfide, zirconium disulfide, hafnium disulfide and tin disulfide

Inorganic Chemistry, 1968
Lawrence E. Conroy, Kyu Chang Park
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Chemical reduction of disulfides

1987
Publisher 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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The Preparation of Acetylsalicylyl Disulfide and Salicylyl Disulfide

Journal of the American Chemical Society, 1942
Harold Wittcoff, Byron Riegel
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Disulfides and Polysulfides

1977
Disulfides and polysulfides have the structure R1SSnR2, in which chains of sulfur atoms are terminated by two groups that may be the same, different, or connected in a ring. Chapter 7 considers only substances where the S-R bond involves a carbon linkage; a review is available of structures such as ROSnOR and R2NSnNR2) Disulfides (n = 1) and their ...
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