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1 site-directed mutagenesis using pCMBS as the thiol reagent.
2 cking uncyanylated sulfhydryls with a second thiol reagent.
3 ed by anaerobic growth conditions or reduced thiol reagents.
4 les, they have different reactivities toward thiol reagents.
5 amined using monofunctional and bifunctional thiol reagents.
6 17 and Cys270), both of which are targets of thiol reagents.
7 y change in pH or temperature or addition of thiol reagents.
8 ntly to allow reactivity with these cationic thiol reagents.
9                          A novel radioactive thiol reagent, 1-S-[3H]carboxymethyl-dithiothreitol (DTT
10  and sites were identified by use of a novel thiol reagent, 1-S-mono[(14)C]carboxymethyldithiothreito
11 escribe the use of a specific and reversible thiol reagent, 2,2'-dithiodipyridine, to generate purifi
12                  The synthesized radioactive thiol reagent [3H]CM-DTT proved to be very efficient and
13 centrations, NEM does not act as a selective thiol reagent and activates RyRs without alkylating crit
14 The octanoylated LipB linkage was cleaved by thiol reagents and by neutral hydroxylamine, strongly su
15 ces IV and V are more reactive/accessible to thiol reagents and more exposed to solvent than the peri
16 lf of helix X is more reactive/accessible to thiol reagents and more exposed to solvent than the peri
17                                              Thiol reagents and oxidative stress may modify two thiol
18  DNA hybridization solutions, application of thiol reagents, and incorporation of a polyadenine block
19 smic pathway were reacted to completion with thiol reagents, and the effects on transport and sugar b
20 dium alone increases the reactivity with the thiol reagents as compared to sodium-free medium.
21 s (Cys284 and Cys373) became inaccessible to thiol reagents because of this modification.
22 ) using a protocol that minimizes the use of thiol reagents believed to be the source of the third li
23 rtially purified enzyme is very sensitive to thiol reagents but insensitive to other kinds of proteas
24                                        Thus, thiol reagents commonly added to NOS enzyme preparations
25  induction, but simultaneous addition of the thiol reagents dithiothreitol or glutathione, which ofte
26 s as substrate specificity and inhibition by thiol reagents for each protein.
27                                              Thiol reagents have no significant effect on the activit
28 region that react rapidly with water-soluble thiol reagents in the open state but not the closed stat
29 zyme inhibition by OA-NO2 is not reversed by thiol reagents, including glutathione, beta-mercaptoetha
30 rynic acid (EA), a mitochondrion-penetrating thiol reagent, induced rapid and extensive depletion of
31 Tritrichomonas foetus was inactivated by the thiol reagents iodoacetate and 5,5'-dithiobis(2-nitroben
32 athway, that the accessibility to impermeant thiol reagents is influenced (blocked or stimulated) by
33 ion and secretion was studied using covalent thiol reagents, maleimides, or mercuribenzoates, or usin
34 ited a membrane conductance sensitive to the thiol reagent maleimidobutyryl biocytin (MBB).
35 ty of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate-ethyltrimethlammonium
36 teine residues with the membrane-impermeable thiol reagent methoxypolyethylene glycol maleimide.
37                        Experiments using the thiol reagent MTSEA+ to modify the channel protein showe
38 annels was increased by a positively charged thiol reagent (MTSEA), and was reduced by the negatively
39           The membrane-permeant, radioactive thiol reagent N-[ethyl-1-14C]ethylmaleimide ([14C]NEM) i
40 ate, by dicyclohexylcarbodiimide, and by the thiol reagent N-ethylmaleimide.
41  covalent perturbation by treatment with the thiol reagent, N-ethylmaleimide (NEM).
42                   We evaluated the effect of thiol reagents on the proliferation of the Jurkat human
43 inomethylenediphosphonate (AMDP), and by the thiol reagent p-hydroxymercuribenzoate at concentrations
44  of 5.15 and was reversibly inhibited by the thiol reagent p-hydroxymercuribenzoic acid.
45  order of fluorogenic o-phthalaldehyde (OPA)/thiol reagent (pH 10.0) in the carrier stream (0.63 mL/m
46 lsulfonate (MTSES), a hydrophilic impermeant thiol reagent, show that most of the positions that reac
47 ethiosulfonate ethylsulfonate, an impermeant thiol reagent shown clearly in this paper to be impermea
48  can be removed from the GR active site with thiol reagents such as 2-mercaptoethanol.
49 f [14C]NEM labeling with membrane-impermeant thiol reagents such as methanethiosulfonate ethylsulfona
50                The results of treatment with thiol reagents suggested that the conserved cysteine is
51 r was observed in the presence or absence of thiol reagents, suggesting that membrane potential may i
52 ysteine to IscU in the absence of additional thiol reagents, suggesting that transfer can occur direc
53  demonstrated with detergents and impermeant thiol reagents suggests that the protein may have a diff
54                         After washout of the thiol reagent the channels were tested at potentials at
55 y but not that of the parent is inhibited by thiol reagents; these results confirm that this residue
56  pretreatment of HL60 cells with a maleimide thiol reagent, ThioGlo1, prevents redox-cycling of etopo
57 m(3)(2,2,7)GTP was reversibly increased when thiol reagents were removed.
58  above this site are not modified by charged thiol reagents when the channel is closed.

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