ライフサイエンスコーパス: selenol

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1 eleno groups without handling free thiols or selenols.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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