ライフサイエンスコーパス: selenol

1 eleno groups without handling free thiols or selenols.

2 e C3 position in the presence of thiophenols/selenols.

3 various thiol-based auxiliaries and thiol or selenol amino acid surrogates that have been developed s

4 The dechalcogenation of thiol or selenol amino acids is nowadays a particularly flourishi

5 ssion and permits physical separation of the selenol and the general acid.

6 nes involving diselenide, selenenyl sulfide, selenol, and selenenic acid as intermediates using (77)S

7 ns aliphatic and aromatic thiols (as well as selenols) are able to convert NO to HNO, albeit at diffe

8 nt methyltransferases that utilize thiols or selenols as methyl acceptors.

9 nd that has the capacity to form a catalytic selenol(ate).

10 esis, when used in combination with thiol or selenol-based chemoselective peptide ligation chemistrie

11 (2) stabilize the newly formed intermediate selenol by N-ethylmaleimide; (3) deproteinization.

12 ethod for labeling antibodies which involves selenol-catalyzed reduction of native disulfide bonds in

13 These and similar results with carborane-selenol derivatives suggest that, in contrast to carbon-

14 anical calculations on 5-MTA ethyl thiol and selenol ethyl esters allowed us to identify the conforma

15 no acids and emphasize the importance of the selenol function in the mechanism of organic selenium to

16 hat, in vitro, the complete oxidation of the selenol function of selenocysteine or selenohomocysteine

17 results were obtained from a 3R-substituted selenol function, incorporated in the context of an oxid

18 inuclear Ni(II)-bis(ONO) complex with thiols/selenols give access to unusual dinickel(II)-nitrito-thi

19 ucturally similar to cysteine (Cys), the Sec selenol group has unique properties that are attractive

20 An ionized selenol group in place of a cysteine sulfhydryl group co

21 The nucleophilic selenol group of selenocysteine endows this rare amino a

22 s enabling the dechalcogenation of thiols or selenols have been investigated and developed for a long

23 heir ability to bind vicinal thiols or thiol selenols in prefolded proteins thereby compromising cell

24 The naphthyl-based compounds having two selenols in the peri-positions exhibit much higher deiod

25 tage conferred on the eukaryotic enzyme by a selenol is the ability to function at acidic pH.

26 s from solution, replacement of thiolates by selenols is rapid and complete, and is well described by

27 (1H)-ones with alcohols, amines, thiols, and selenols leading to the formation of C-O, C-N, C-S, and

28 With the use of selenols, meso-seleno-substituted porphyrins can also be

29 an be ascribed to the deprotonation of thiol/selenol moiety by the amino group, which not only increa

30 It would be expected that an ionized selenol of a selenocysteine in place of a catalytically

31 t, revealing two different binding modes for selenols on gold: molecules at bridge sites have lower c

32 vity than those having two thiols or a thiol-selenol pair.

33 s unimportant because the lower pK(a) of the selenol relative to a thiol obviates its need to be prot

34 nism for diselenide 6 was proposed involving selenol, selenosulfide and seleninic acid intermediates.

35 and hydrogen peroxide was proposed involving selenol, selenosulfide, and selenenic acid as intermedia

36 ar modeling for 5-MTA in the active sites of selenol-subtilisin and N155G selenol-subtilisin confirms

37 y mutagenesis, by creating the N155G form of selenol-subtilisin and the P225A form of thiol-subtilisi

38 active sites of selenol-subtilisin and N155G selenol-subtilisin confirms the findings from Raman spec

39 -site Raman probe, acyl enzymes of thiol- or selenol-subtilisin exhibit no polarization even though t

40 The Raman spectra of 5-MTA thiol and selenol subtilisins both showed that the acyl group bind

41 he compound exists as the selone rather than selenol tautomer, a result that is in accord with DFT ca

42 ystem, thiols induce the release of aromatic selenols that catalyze the oxidation of thiols by organi

43 of this pair that might be analogous to the selenol-thiol pair near the C terminus of animal thiored

44 d reaction conditions, and avoids the use of selenol which is difficult to manipulate, easily oxidize