ライフサイエンスコーパス: Schiff base

1 favor of the oxoenamine tautomer (protonated Schiff base).

2 changes dramatically with protonation of the Schiff base.

3 derivative, bound to a protein (opsin) via a Schiff base.

4 nal and form a covalent bond as a protonated Schiff base.

5 as an internal aldimine with a deprotonated Schiff base.

6 r proton transfer in the external PLP-L-dopa Schiff base.

7 proton-conduction pathway from Asp96 to the Schiff base.

8 side chain of Tyr57 and with the C15H of the Schiff base.

9 tate as an alternate proton acceptor for the Schiff base.

10 group (PRG) on the extracellular side of the Schiff base.

11 strongly in favor of that with CP-accessible Schiff base.

12 m the pyridine nitrogen (N1) of the internal Schiff base.

13 nanomolar binding of retinal as a protonated Schiff base.

14 ted at the edge of PLP opposite the reactive Schiff base.

15 channel occurs prior to deprotonation of the Schiff base.

16 oplasmic half-channel, located 15 A from the Schiff base.

17 as the internal proton donor to the retinal Schiff base.

18 ium(II) and tin(II) by using the substituted Schiff base 2,6-diacetylpyridinebis(2,6-diisopropylanil)

19 scent molecular rotors of boron derived from Schiff bases: (2,4,8,10-tetra-tert-butyl-6-phenyldibenzo

20 The N-alkylated indanylidenepyrroline (NAIP) Schiff base 3 is an unnatural alpha-amino acid precursor

21 rization of substrate Schiff base to product Schiff base, a facile aromatization of the latter result

22 n mutants incapable of forming the requisite Schiff base, a highly ordered water molecule was identif

23 neC backbone of all-trans retinal protonated Schiff base accelerates the electronic decay in solution

24 protease through the formation of a covalent Schiff base adduct of the pBzF residue with the epsilon-

25 aracteristics and they were more stable than Schiff base adducts at 60 degrees C.

26 tion of an isocyanide to a hydrazine derived Schiff base affords unique six-membered pyridotriazine s

27 n nanotubes/BaFe12O19-chitosan (MCNTs/BF-CS) Schiff base Ag (I) complex composites were synthesized s

28 The results show that the BF-CS Schiff base Ag (I) complexes are embedded into MCNT netw

29 ges in the K-state propagating away from the Schiff base along the polyene chain.

30 panied by the perturbations of Asp96 and the Schiff base, although in different ways from what is obs

31 est results were obtained using a tridentate Schiff base aluminum(III) Lewis acidic complex, 1H-1,2,3

32 UV-absorbing photoreceptor with deprotonated Schiff base and allowed reconstitution into native-like

33 by formation of a direct H-bond between the Schiff base and Asn87.

34 n surrounded by protein residues between the Schiff base and Asp96.

35 crements of 54 and 134 amu, corresponding to Schiff base and dihydropyridine (DHP)-type adducts, resp

36 Specifically, interconversion of Schiff base and enamine intermediates, formed covalently

37 e phenolic oxygen to maintain the protonated Schiff base and enhance the electron sink function of th

38 ses strain in the Lys pyridoxal 5'-phosphate Schiff base and increases the pK(a), resulting in proton

39 the connectivity of the active site once the Schiff base and its counterion are neutralized by proton

40 ine residue (Lys265) as an internal aldimine/Schiff base and the active site is composed of residues

41 observe a deuterium equidistant between the Schiff base and the C-terminal carboxylate of the substr

42 the late M- (M2) with a deprotonated retinal Schiff base and the consecutive green-absorbing N-state

43 n involves both hydrolysis of the protonated Schiff base and thermal isomerization of 11-cis to all-t

44 f the carbinolamine intermediate to give the Schiff base and to function as a general acid/base.

45 ct asymmetric aldol reaction between glycine Schiff bases and aldehydes is reported.

46 hat DOPAL interacts with aS via formation of Schiff-base and Michael-addition adducts with Lys residu

47 ied interaction network between chromophore, Schiff base, and counterion complex explaining the alter

48 ex counterion to the protonated retinylidene Schiff base, and neutralization of the negatively charge

49 arbonyl groups in helix G with Tyr57 and the Schiff base, and separation of Tyr57 from Arg82, may be

50 study, including a reaction intermediate, 2 Schiff bases, and 28 bis- or tris(pyrazol-3(4)-yl)methan

51 n and the deprotonation/reprotonation of the Schiff base, are coupled to the channel-opening mechanis

52 adily available halogen sources and a simple Schiff base as the chiral catalyst.

53 ation of the opsin upon deprotonation of the Schiff base at pH 12.5 eliminates the induced CD bands i

54 erived from a new water-soluble pentadentate Schiff base backbone ligand has been prepared and charac

55 The Schiff base becomes protonated in the transition to Meta

56 Asparagine reacted with fructose to form a Schiff base before decarboxylation to produce acrylamide

57 ing sugars react with asparagine to form the Schiff base before decarboxylation, to generate acrylami

58 the bound product reveals the presence of a Schiff base between C-4' of the PLP cofactor and the ami

59 which is consistent with the formation of a Schiff base between Top1 and the ring open aldehyde form

60 cally isomerizes the retinylidene protonated Schiff base both thermally and photochemically.

61 omerization and dark state hydrolysis of the Schiff base by 1-2 orders of magnitude.

62 rt cycle includes protonation of the retinal Schiff base by Asp96 (M-->N reaction) and reprotonation

63 accepts a proton from H2O as it attacks the Schiff base carbon of saccharopine to form the carbinola

64 DA) reaction catalyzed by Jacobsen's Cr(III) Schiff base catalyst, followed by a novel, highly diaste

65 Here we show that by localizing manganese-Schiff base catalysts at the oil droplet-water interface

66 t the ability of substrates to form covalent Schiff base catalytic intermediates and to initiate chem

67 lar surface coverage confirm the efficacy of Schiff base chemistry, at least with the terephthalaldeh

68 The reductive half-reaction proceeds via Schiff base chemistry, in which the primary amine substr

69 ss I aldolase family on the basis of similar Schiff-base chemistry and fold.

70 Recently, the Schiff-base chemistry or dynamic imine-chemistry has bee

71 nd synthetic strategies toward COFs based on Schiff-base chemistry, collects and rationalizes their p

72 hysical properties of the retinal-protonated Schiff base chromophore in solution.

73 itory action of a biologically inert Co(III) Schiff base (Co(III)-sb) complex.

74 e activation of a biologically inert Co(III) Schiff base [Co(III)-SB] complex to its protein inhibito

75 trate that neither the oligo, or the Co(III) Schiff base complex alone, are sufficient for inactivati

76 A Co(III) Schiff base complex modified with a 17-bp DNA sequence i

77 ed pyrolysis of a series of heterobimetallic Schiff base complexes ensures a rigorous control of the

78 ation of bithiophene-substituted cadmium(II) Schiff base complexes forms thin conducting metallopolym

79 hemoglobin amino groups to produce unstable Schiff base complexes that can dissociate or rearrange t

80 became trapped by MR1 as reversible covalent Schiff base complexes.

81 ohydride reduction confirmed the presence of Schiff base complexes.

82 etization), and Hc (coercivity) of the BF-CS Schiff base composites reach 1.908 S cm(-1), 28.20 emu g

83 edominance of intermediate MRPs, such as the Schiff base compounds.

84 For pi-conjugated COFs, the Schiff base condensation of aldehydes and amines is the

85 by employing the solvothermal aldehyde-amine Schiff base condensation reaction.

86 Schiff-base condensation between an amine and an aldehyd

87 transfer between the zwitterionic protonated Schiff base configuration and the neutral hydroxyimine t

88 tinal leads to the formation of a protonated Schiff base conjugate, all-trans-retinal dimer-phosphati

89 ccumulation of excess 11-cis-retinal and its Schiff-base conjugate and the formation of toxic bisreti

90 inylidene-phosphatidylethanolamine (PE), the Schiff-base conjugate of 11-cis-retinal and PE, from the

91 we detected the presence of emixustat-atRAL Schiff base conjugates, indicating that emixustat also a

92 , we show that 5fC bases in DNA readily form Schiff-base conjugates with Lys side chains of nuclear p

93 tochemical reactions, the conformer with the Schiff base connected to the cytoplasmic (CP) half-chann

94 ctant signal, whereas the conformer with the Schiff base connected to the extracellular (EC) half-cha

95 ns in the HtrI subunit of the complex on SRI Schiff base connectivity indicate that the two proteins

96 f the SRI-HtrI attractant conformer causes a Schiff base connectivity switch from inwardly connected

97 Mutation of the primary Schiff base counterion (VCOP(D108A)) produced a pigment

98 ncluding the D121-H87 cluster of the retinal Schiff base counterion and a glutamate at position 132 t

99 However, no changes are observed in the Schiff base counterion Asp-75, which remains unprotonate

100 ide pH range and interacts directly with the Schiff base counterion Asp-97; and (ii) photoisomerizati

101 lier observations that neutralization of the Schiff base counterion, Asp97, does not block the format

102 The unusual charge neutrality of both Schiff base counterions in the P2 (380) conducting state

103 of an abasic site by a mechanism involving a Schiff-base covalent intermediate with the abasic site.

104 Four inhibitors that prevented Schiff base cross-linking to the conserved 3'-terminal a

105 adipic and gamma-glutamic semialdehydes) and Schiff base cross-links.

106 the amyloid fibril through the formation of Schiff bases, cross-linking the fibrils, which may preve

107 or other residues slows reprotonation of the Schiff base (decay of the M intermediate) by more than 2

108 re model compound 11-cis-retinyl-propylamine Schiff base demonstrate the direct isomerization of visu

109 the protein sequence controls the extent of Schiff base deprotonation and accumulation of intermedia

110 and is described by a multisquare model with Schiff base deprotonation at the lumirhodopsin I interme

111 I-Lumi II process that immediately precedes Schiff base deprotonation in the activation of rhodopsin

112 uncated and full-length versions accelerates Schiff base deprotonation more than 10-fold.

113 c scheme, the human rhodopsin exhibited more Schiff base deprotonation than bovine rhodopsin, which c

114 absorbance spectrum at earlier times or the Schiff base deprotonation-reprotonation which occurs dur

115 rs faster charge movements that occur before Schiff base deprotonation.

116 e nanodisc environment leading to an earlier Schiff base deprotonation.

117 13)=C(14) and C(15)=NZ double-bonds, and the Schiff base does not lose its connection to Wat402 and,

118 and its ability to accept a proton from the Schiff base during the photocycle.

119 The formation of cross-links (assessed as Schiff bases) during freezing and the subsequent process

120 of retinal model compounds reveals that the Schiff base environment is polar.

121 yme showed L-methionine bound in an external Schiff base (ESB) linkage to PLP as the enzyme was isola

122 talytic cycle is facilitated by a protonated Schiff base form of the holoenzyme in which the linking

123 he equilibrium in favor of the EC-accessible Schiff base form, and suppressor mutations shift the equ

124 he equilibrium back toward the CP-accessible Schiff base form, restoring the wild-type phenotype.

125 mpounds that transiently sequester atRAL via Schiff base formation ameliorate retinal degeneration.

126 for all steps of the mechanism, most notably Schiff base formation and hydrolysis.

127 rimary alkoxides and diaminopyrimidines with Schiff base formation and subsequent annulation in the p

128 stable 1,3-thiazines, whereas the reversible Schiff base formation between aldehydes and amino groups

129 addition reaction with propynal coupled with Schiff base formation between Lys99 and the carbonyl gro

130 Schiff base formation between Lys99 and the imine of the

131 slides having aldehyde groups via transient Schiff base formation followed by reduction to produce a

132 ation of the ion/ion intermediate results in Schiff base formation generated via reaction between a p

133 te lysine residue that is initially used for Schiff base formation in the internal aldimine and later

134 tent of protein oxidation (carbonylation and Schiff base formation) and their sensory profile (quanti

135 s binding to 8-oxoG-containing DNA, promotes Schiff base formation, and stimulates its glycosylase an

136 When combined with amino acids they undergo Schiff base formation, decarboxylation and alpha-aminoke

137 idues is poised to activate the substrate by Schiff base formation, promote mechanistically important

138 ns result from 1,4 conjugate addition and/or Schiff base formation, they occur at multiple locations

139 active site does not appreciably change upon Schiff base formation.

140 trategically located -COOH which accelerates Schiff base formation.

141 Schiff-base formation between Abeta and the aldehyde-bea

142 Schiff-base formation between DOB and histone proteins i

143 midoxime acts as an internal general acid in Schiff-base formation.

144 rities beyond the common use of a lysine for Schiff-base formation.

145 ise to water loss in conjunction with imine (Schiff base) formation.

146 ctions of TCNQF (-) radicals (H2valpn is the Schiff base from the condensation of o-vanillin with 1,3

147 ox-mediated coupling of benzylic ethers with Schiff bases has been accomplished.

148 certain cases, however, compounds other than Schiff bases have been reported to result from such reac

149 nd cone visual pigments undergoes reversible Schiff base hydrolysis and dissociation following photob

150 Accelerating Schiff base hydrolysis and subsequent ATR dissociation,

151 not from inherent differences in the rate of Schiff base hydrolysis but rather from differences in th

152 e visual pigments is necessary for efficient Schiff base hydrolysis.

153 polarized in a manner that would facilitate Schiff base hydrolysis.

154 ecedes the deprotonation of the retinylidene Schiff base (i.e., formation of an M intermediate).

155 ow that several ionizable groups besides the Schiff base imine are affected by the structural changes

156 n screening using either disulfide bridge or Schiff base imine immobilization chemistries on plasmach

157 nes), forming either hemiaminal (+148 Da) or Schiff base (imine, +130 Da) products.

158 embrane voltage modulates protonation of the Schiff base in a 13-cis photocycle intermediate (M right

159 d from hydroxyl-bearing amino acids near the Schiff base in different visual pigments: at site 292 (A

160 refore suggest that the reprotonation of the Schiff base in ESR is preceded by transient protonation

161 The (15)N chemical shift of the Schiff base in K indicates that contact has been lost wi

162 water molecules interact with Asp96 and the Schiff base in L, although with a less rigid structure t

163 rs to be capable of stabilizing a protonated Schiff base in Meta III, but not of constraining the rec

164 energetics and the protonation state of the Schiff base in retinal, the covalently bound ligand resp

165 nts of proton transfer from the retinylidene Schiff base in several channelrhodopsin variants express

166 The protonation of Asp85 by the Schiff base in the L-->M reaction is likely to occur, th

167 of the internal proton donor to the retinal Schiff base in the light-driven proton pump of Exiguobac

168 fference spectroscopy reveals a deprotonated Schiff base in the photoproducts of the mutant up to the

169 ffer by their connection of the retinylidene Schiff base in the SRI photoactive site to inner or oute

170 g the intermediate Opsin-derived, protonated Schiff base in the visual cycle with simple polarized al

171 photoisomerization of the retinal protonated Schiff-base in bacteriorhodopsin, isorhodopsin and rhodo

172 eins was confirmed by NaBH4 reduction of the Schiff base intermediate and kinetics studies.

173 rupture of the C1'-O4' bond, resulting in a Schiff base intermediate at the N-glycosidic bond.

174 the pyrimidine ring is maintained, while the Schiff base intermediate is preferred if the C5 horizont

175 occurs before a conformational change of the Schiff base intermediate toward a cyclic structure.

176 proline as the nucleophile, MmuNeil3 forms a Schiff base intermediate via its N-terminal valine.

177 Such a Schiff base intermediate was trapped and characterized b

178 4, which is responsible for formation of the Schiff base intermediate, and Asp33 and Tyr153, which ar

179 Strand scission proceeds via a Schiff base intermediate, but the DNA-protein cross-link

180 dently of divalent cation and proceeds via a Schiff base intermediate, indicating that it occurs via

181 avage of beta-hydroxy-ketones via a covalent Schiff base intermediate.

182 Enzymes that utilize a Schiff-base intermediate formed with their substrates an

183 for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformatio

184 arbonyl of TPQ, forming a series of covalent Schiff base intermediates.

185 When the mass ratio of MCNTs and BF-CS Schiff base is 0.95:1, the conductivity, Ms (saturation

186 e capable of binding retinal as a protonated Schiff base is described.

187 the proton dissociation from the protonated Schiff base is not affected, the rate of its reprotonati

188 the hydroxyimine form of the PLP(H+)-L-dopa Schiff base is predicted to be the major isomer with a r

189 romophore covalently linked to Lys(296) by a Schiff base is subsequently hydrolyzed, but little is kn

190 kes place shortly after deprotonation of the Schiff base (L-to-M transition) and results in an increa

191 rption spectrum consistent with a protonated Schiff base (lambda(max) = 420 nm).

192 Schiff base ligands have long been successfully employed

193 One of the most widely used Schiff base ligands, the "salen" ligand, has been extens

194 plex has an outwardly connected retinylidene Schiff base like the repellent signaling forms of the SR

195 cis-retinal and hydrolysis of the protonated Schiff base linkage between the 11-cis-retinal chromopho

196 )N NMR chemical shift measurements of such a Schiff base linkage in the resting holoenzyme form, the

197 in the product the enzyme no longer makes a Schiff base linkage to the pyridoxal 5'-phosphate (PLP)

198 ter-mediated H-bonding interactions with the Schiff base linkage.

199 ly bound to the protein through a protonated Schiff base linkage.

200 is-retinal (11CR), by a covalent, protonated Schiff base linkage.

201 forms a covalent bond with retinal through a Schiff base linkage.

202 t Arch variants, the pK(a) of the protonated Schiff-base linkage to retinal is near neutral pH, a use

203 l salt bridge between the retinal protonated Schiff base linked to H7 and Glu113 on H3 is one of the

204 on of Phe-86 that converted the unprotonated Schiff base-linked 11-cis-retinal to a protonated form.

205 n the retinal binding pocket of rhodopsin, a Schiff base links the retinal ligand covalently to the L

206 methyl-4-carboxy-2,2'-bipyridine, and L is a Schiff base macrocycle derived from 2,6-diformyl-4-methy

207 inuclear magnesium complex of a polypyrrolic Schiff base macrocycle results in the formation of a new

208 arth trication in a binucleating polypyrrole Schiff-base macrocycle (Pacman) and bridged through a ur

209 , however our results suggest an alternative Schiff base mechanism which may be responsible for the r

210 The mammalian class I FBPA employs a Schiff base mechanism, whereas the human parasitic proto

211 We suggest a mechanism where Schiff base-mediated deimination forms DMQ(6) quinone, t

212 t had been immobilized to silica through the Schiff base method (i.e., an amine-based coupling techni

213 HDL was immobilized by the Schiff base method onto silica and gave HPAC columns wit

214 mutant that can bind retinal as a protonated Schiff base, mimicking the binding observed in rhodopsin

215 Furthermore, Schiff-base-modified peptides exhibit on average a 20% i

216 lished by replacing the rapidly hydrolyzable Schiff-base moiety of first-generation members with a cy

217 h the internal aldimine is protonated on the Schiff base N.

218 The influence of a Schiff base namely N,N'-(pyridine-2,6-diyl)bis(1-(4-meth

219 omophore and the (15)N chemical shift of the Schiff base nitrogen in the active metarhodopsin II inte

220 between positions C10 and C15 as well as the Schiff base nitrogen in the ground state in comparison t

221 lamine, and protonation/deprotonation of the Schiff base nitrogen of all-trans-retinal dimer-ethanola

222 ce experiments confirm the assignment of the Schiff base nitrogen, and additional (13)C, (15)N, and (

223 Replacing the n-butylamine Schiff base normally chosen to mimic the saturated linka

224 fluctuations in the protonation state of the Schiff base occur prior to forming the activated MII sta

225 ed bond-length alternation of the protonated Schiff base of 11-cis-retinal chromophore, induced by N8

226 e in opsin visual pigments is the protonated Schiff base of 11-cis-retinaldehyde (11cRAL).

227 0) energy surfaces (Phi(CI)) of a protonated Schiff base of all-trans retinal in protic and aprotic s

228 ly converted to an agonist, the unprotonated Schiff base of all-trans retinal, upon light activation.

229 nfirmed the formations of Michael adduct and Schiff base of HMF with amino acids.

230 e where the protein (opsin)-bound protonated Schiff base of retinal displays a remarkable range of re

231 lidene-pyrroline chromophore that mimics the Schiff base of rhodopsin and can be used to introduce li

232 on of the salt bridge between the protonated Schiff base of the receptor's retinylidene chromophore a

233 ble to maintain a counterion function to the Schiff base on the activation pathway of rhodopsin in th

234 been exploited for over 150 years to produce Schiff bases, one of the most popular classes of compoun

235 Alkylation of glycine-derived Schiff bases or nitroacetates with cyclic ether electrop

236 e conclude that Lumi II (the last protonated Schiff base photointermediate under physiological condit

237 the complex [(UO2 )(THF)(H2 L)] (L="Pacman" Schiff-base polypyrrolic macrocycle), is found and expla

238 ly conjugated oligomers of secondary imines (Schiff bases) present at relatively low concentrations.

239 Heterobis imine Schiff base probe L is able to discriminate geometrical

240 lision-induced dissociation (CID) produces a Schiff base product anion.

241 )methane derivatives instead of the expected Schiff base products.

242 wever, the rapid and reversible formation of Schiff base prohibits formation of alternative products,

243 that occupy the positions of the chromophore Schiff base proton acceptor and donor, a hallmark of rho

244 3) (Asp(253) in CrChR2) receives the retinal Schiff base proton during M-state formation.

245 ) photoisomerization-induced transfer of the Schiff base proton to the Asp-97 counterion disrupts its

246 the mutation of which to Glu produced early Schiff base proton transfer and strongly inhibited chann

247 hodopsin acts as the primary acceptor of the Schiff-base proton in low-efficiency channelrhodopsins.

248 to approximately 40 kcal/mol for protonated Schiff base (PSB) chromophore in rhodopsin.

249 11-cis retinyl chromophore with a protonated Schiff-base (PSB11), UV pigments uniquely contain an unp

250 ond via hyperconjugation with the conjugated Schiff base/pyridine ring pi system.

251 r the synthesis of a library of 442 Ru-arene Schiff-base (RAS) complexes.

252 p-Azo and Tp-Stb) were synthesized using the Schiff base reaction between triformylphloroglucinol (Tp

253 etic strategy that regulates the sequence of Schiff base reaction via weak secondary interactions.

254 ly immobilized to the host IL through simple Schiff base reaction.

255 Syntheses of these COFs were done by the Schiff base reactions of 1,3,5-triformylphloroglucinol (

256 t M-states have been observed reflecting the Schiff base reorientation after the deprotonation step.

257 gen of the PLP and the imino nitrogen of the Schiff base, respectively.

258 m chemical models of three distinct types of Schiff base rotary motors.

259 photoisomerization of the retinal protonated Schiff base (RPSB) chromophore.

260 es (MWCNT), chitosan and a novel synthesized Schiff base (SB) (TiO2/MWCNT/CHIT/SB) on the surface of

261 of 11-cis-retinal followed by hydrolysis of Schiff base (SB) and 2) hydrolysis of SB in dark state r

262 e dark state, VCOP-D108A has an unprotonated Schiff base (SB) chromophore (lambdamax = 357 nm).

263 donor, respectively, of the photoactive site Schiff base (SB) proton.

264 he retinyl chromophore and hydrolysis of the Schiff base (SB) through which the retinyl chromophore i

265 es E90, E123, D253, N258, and the protonated Schiff base (SBH), as well as nearby residues K93, T127,

266 embly of paramagnetic Cu(2) complexes with a Schiff base scaffold possessing extended electron deloca

267 Partial proteolysis of the Schiff base shows that the DNA lyase activity resides in

268 carboxylate anion on the alpha-carbon of the Schiff base stabilizes the zwitterions and shifts the eq

269 oxidised to alpha-aminoadipic acid and form Schiff bases structures.

270 imple model where backbone modifications and Schiff base substituents control barrier heights on the

271 Acid catalysis, which is often employed in Schiff base synthesis, radically changes the course of r

272 rtate 253 accepts the proton released by the Schiff base (t(1/2) = 10 mus), with the latter being rep

273 ilibrium between the phenolic and protonated Schiff base tautomeric forms of this intermediate.

274 r molecule, would trigger the formation of a Schiff base that can undergo further dehydration reactio

275 achieved by preventing reprotonation of the Schiff base through a mutation of the primary proton don

276 It involves the formation of a Schiff base through a reaction between the ketone and th

277 tion, and is driven by the attraction of the Schiff base to a new counterion.

278 sfer-catalyzed Michael addition of a glycine Schiff base to a variety of acceptors.

279 ing the primary phototransition and from the Schiff base to Glu-169 during P2 (380) formation.

280 s the pK(a), resulting in protonation of the Schiff base to initiate transaldimination.

281 s the light-induced proton transfer from the Schiff base to its counterion Asp-97 during the photocyc

282 owing the initial isomerization of substrate Schiff base to product Schiff base, a facile aromatizati

283 e in ADC nor norspermidine in CANSDC, form a Schiff base to pyridoxal 5'-phosphate, suggesting that t

284 ate a first-order conversion of the internal Schiff base to the alpha-aminoacrylate intermediate at a

285 connection of their retinylidene protonated Schiff bases to the outwardly located periplasmic side a

286 rtate residue, the counterion to the retinal Schiff base, to a histidine.

287 ostatic effects surrounding the unprotonated Schiff base (USB) retinyl chromophore in the UV pigment.

288 UV pigments uniquely contain an unprotonated Schiff-base (USB11).

289 and amino acid side chains in the immediate Schiff base vicinity are very well conserved.

290 The pKa of the retinylidene protonated Schiff base was modulated from 2.4 to 8.1, giving rise t

291 mining step of the process is formation of a Schiff base, which is followed by rapid intramolecular r

292 been proposed to give an alpha-aminoacrylate Schiff base, which releases iminopyruvate that ultimatel

293 The Kd values for formation of the external Schiff base with cysteine and serine, obtained by spectr

294 actions with His910 and Phe889, an essential Schiff base with Lys907 and a hydrogen bond with Tyr892.

295 s selectivity by forming an unusually stable Schiff base with lysine 907 in the IRE1 endonuclease dom

296 VitB antigens reach this location and form a Schiff base with MR1, triggering a 'molecular switch' th

297 PLP forms a Schiff base with the -amino group of a lysine residue of

298 n studies suggest that compound 1 may form a Schiff base with the epsilon-amino group of Lys214, whic

299 ed active site lysine residue, which forms a Schiff base with the PLP cofactor.

300 factors and does not form a protein-mediated Schiff base with the substrate, unlike most aldolases.