ライフサイエンスコーパス: AMP-PNP

1 AMP-PNP binding induces an inward rotation and shift of

2 AMP-PNP by itself supported hydrolysis of casein and oth

3 AMP-PNP or ATPgammaS activation required both nucleotide

4 AMP-PNP, a nonhydrolyzable ATP analog, at a concentratio

5 at 3.8 angstrom, both in complex with Mg(2+)-AMP-PNP.

6 e of fast turnover, the non-hydrolyzable N(3)AMP-PNP bound preferentially to NBD1.

7 5'-Adenylylimidodiphosphate (AMP-PNP) and pyrophosphate, two compounds that disrupt c

8 ysable analogue 5'-adenylylimidodiphosphate (AMP-PNP) and the inhibitory effect of ATPgammaS was reve

9 le ATP analogue 5'-adenylylimidodiphosphate (AMP-PNP) to prevent the run-down of IK(IR))and the Mg2+

10 the presence of 5'-adenylylimidodiphosphate (AMP-PNP), ADP, and ATP, yielding maximal values between

11 e ATP analogue, 5'-adenylylimidodiphosphate (AMP-PNP), bound preferentially to NBD1, but upon additio

12 lls loaded with 5'-adenylylimidodiphosphate (AMP-PNP), KN93, or the CaMKII inhibitory peptide, ICl(Ca

13 nalogue of ATP, 5'-adenylylimidodiphosphate (AMP-PNP), reduced the amplitude and rate of activation o

14 le ATP analogue 5'-adenylylimidodiphosphate (AMP-PNP; 3-5 mM), the leptin-induced hyperpolarization a

15 e ATP analogues 5'-adenylylimidodiphosphate, AMP-PNP (2 mM) or beta, gamma-methylene-adenosine 5'-tri

16 ions were varied by adding ATP, Mg(2+), ADP, AMP-PNP, and KCl.

17 + uptake in the presence of ATP but not ADP, AMP-PNP, or BA.

18 n became cooperative in the presence of ADP, AMP-PNP, or ADP.Vi yielding Hill coefficients of 1.8 and

19 P; no binding occurs in the presence of ADP, AMP-PNP, or ATPgammaS.

20 Strong dissociating agents, AMP-PNP and PPi, made significant differences at all rat

21 cked murine CFTR Cl- channels open, although AMP-PNP increased the Po of murine CFTR.

22 ional reconstruction of endogenous p97 in an AMP-PNP bound state at 24 A resolution.

23 ted whether interactions with the ATP analog AMP-PNP and ADP can shift the conformational ensemble of

24 The nonmetabolizable ATP analog AMP-PNP cannot be substituted for ATP in this action.

25 rfusion with the non-hydrolyzable ATP analog AMP-PNP dramatically reduce the amplitude of dBest1 curr

26 as those with the nonhydrolyzable ATP analog AMP-PNP had a mean lifetime of 4.8 +/- 0.7 min.

27 nactive state bound to either the ATP analog AMP-PNP or to one of the two small-molecule inhibitors J

28 P, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates t

29 lish that, in the presence of the ATP analog AMP-PNP, or ADP, a maximum of six DnaC monomers bind coo

30 tor with the hydrolysis-resistant ATP analog AMP-PNP.

31 red ligand selectivity toward the ATP analog AMP-PNP.

32 es in complex with GlcNAc and the ATP analog AMP-PNP.

33 th either ATP or the non-hydrolyzable analog AMP-PNP, and these cycles of elongation and compression

34 presence of the ATP non-hydrolyzable analog AMP-PNP, have been performed, using the fluorescence sto

35 The nonhydrolyzable analog AMP-PNP and ATP-gamma S also stimulate ADP release from

36 e presence of the ATP nonhydrolyzable analog AMP-PNP, the DnaB helicase binds polymer DNA with a site

37 nd is not supported by the nucleotide analog AMP-PNP.

38 tate, ATP, or a non-hydrolyzable ATP analog (AMP-PNP), with differential effects on matrix Ca(2+) buf

39 inability of the nonhydrolyzable ATP analog, AMP-PNP, to cause a similar effect is explained by the i

40 presence of the ATP nonhydrolyzable analog, AMP-PNP, the DnaB helicase fully preserves its hexameric

41 presence of the ATP nonhydrolyzable analog, AMP-PNP, the E. coli DnaB helicase preferentially binds

42 with an RNA oligonucleotide and ATP analogs AMP-PNP, ADP-BeF(3)(-), or ADP-AlF(4)(-).

43 presence of the nonhydrolyzable ATP analogue AMP-PNP (adenyl-5'-yl imidophosphate), the ectonucleotid

44 GspE structures in complex with ATP analogue AMP-PNP and Mg(2+) reveal for the first time, alternatin

45 resence of the non-hydrolysable ATP analogue AMP-PNP at an overall resolution of 3.1 angstrom.

46 The nonhydrolyzable ATP analogue AMP-PNP binds in a unique mode that fails to induce lobe

47 d to ADP or the nonhydrolyzable ATP analogue AMP-PNP cannot nucleate actin filaments, but addition of

48 RNA complex, and binding of the ATP analogue AMP-PNP induces a conformational change in the enzyme.RN

49 presence of the nonhydrolyzable ATP analogue AMP-PNP, the drug binding site was in a low-affinity con

50 of ADP or the non-hydrolysable ATP analogue AMP-PNP, the interaction with short ssDNA oligonucleotid

51 r by using the non-hydrolysable ATP analogue AMP-PNP.

52 by ATP or the non-hydrolyzable ATP analogue AMP-PNP.

53 affinity in the presence of the ATP analogue AMP-PNP.

54 PGK in complex with the nucleotide analogue AMP-PNP.

55 he presence and absence of the ATP analogue, AMP-PNP.

56 drolysis products, or with the ATP analogues AMP-PNP or ADP.BeF(x)() the myosin filaments are substan

57 g interactions for Vertex-11e, GDC-0994, and AMP-PNP with active vs. inactive ERK2, where the extent

58 ATP affinity but reduced ATPase activity and AMP-PNP-dependent N-terminal association, whereas the ts

59 T22I displayed enhanced ATPase activity and AMP-PNP-dependent N-terminal dimerization, indicating a

60 he magnitude at which the binding of ADP and AMP-PNP affects the affinity of DNA binding by RSCt sugg

61 uirement for ATP in the cis ring, as ADP and AMP-PNP are unable to promote folding.

62 of the structures presented herein, ADP and AMP-PNP bound, are new structures, and the ADP x AlF3 st

63 litate a robust coprotease activity, ADP and AMP-PNP do not activate RecA at all.

64 ween the structures of RecA bound to ADP and AMP-PNP, which differ from uncomplexed RecA only in a sl

65 head 1 is able to distinguish ATP, ADP, and AMP-PNP to signal head 2 to bind the microtubule and rel

66 sm studies with nucleotide analogues AMP and AMP-PNP, product ADP, and an analogue of the peptide sub

67 dition to their roles in protection, ATP and AMP-PNP also slowly stimulate cyclase activity.

68 When ATP and AMP-PNP were combined in the pipette, however, the maint

69 P; ADP is ineffective, whereas ATPgammaS and AMP-PNP are considerably less able to promote binding an

70 nonhydrolyzable ATP analogues ATPgammaS and AMP-PNP, however, only a single thermal transition is ob

71 When vitamin B12 and AMP-PNP are simultaneously present, the extent of comple

72 dence that in the presence of forked DNA and AMP-PNP, higher-order complexes can form.

73 However, magnesium and AMP-PNP do not affect the mechanism of enzyme-ssDNA inte

74 TP binding was reversed by ATP, AMP-PCP, and AMP-PNP with KIs of approximately 3.2, 4.2, and 4.6 mM,

75 ted in the presence of hydrogen peroxide and AMP-PNP, an ATP analog and competitive inhibitor of ATPa

76 of 5'-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted association of N-termini in intact Hsp

77 ADP and GTP were less potent, and AMP-PNP was inactive.

78 rmation that promotes strand separation, and AMP-PNP does not mimic ATP in this regard.

79 SAXS analyses of ADP, ATPgammaS, ADP-Vi, and AMP-PNP-bound states in solution showed that asymmetric

80 r representative ATP hydrolysis states: APO, AMP-PNP, hydrolysis transition state ADP x AlF3, and ADP

81 ven in the presence of non-hydrolysable ATP (AMP-PNP).

82 hate = tripolyphosphate > ATP-Mg(2+) = ATP = AMP-PNP > ADP = tetrapolyphosphate > cAMP = Mg(2+).

83 y at 10 mM: for myosin II ATP-Mg(2+) = ATP = AMP-PNP (5'-adenylyl imidodiphosphate) > pyrophosphate =

84 The non-hydrolysable analogue of ATP, AMP-PNP, did not substitute for ATP in its effects on th

85 esence of the nonhydrolyzable analog of ATP, AMP-PNP.

86 er preincubation at 30 degrees C unless ATP, AMP-PNP, or GCAP is present.

87 Structures of ArsA with ATP, AMP-PNP, or ADP.AlF(3) bound at the A2 nucleotide bindin

88 d MEK1 (npMEK1) has a high affinity for both AMP-PNP and ADP (Kd approximately 2microM).

89 Most notably, bound AMP-PNP was only observed when trapped in the closed sta

90 -containing loops interacting with the bound AMP-PNP and elucidate allosteric communications between

91 hosphorylation of NBD1-R was reduced >75% by AMP-PNP or AMP-PCP (0.25 mM) and >50% by TNP-ATP (0.25 m

92 9D mutation strongly disrupted activation by AMP-PNP but not by ATPgammaS, indicating that these anal

93 The enhanced affinity afforded by AMP-PNP/Mn(2+) may be a useful strategy for increasing a

94 se inhibitor KT5823 or replacement of ATP by AMP-PNP reduced NP(o), while activation of cGMP-dependen

95 Since the delay of closing by AMP-PNP is thought to occur via NBD2, K464A's effect on

96 f ERK2, protection from hydrogen exchange by AMP-PNP binding was observed within conserved ATP bindin

97 contrast, higher protection from exchange by AMP-PNP was observed in active ERK2 compared to inactive

98 membrane domains (TMDs) is not influenced by AMP-PNP binding, a notion confirmed by double electron-e

99 ion is facilitated by Mg(2+) ions but not by AMP-PNP or ATP gamma S.

100 structure, the beta(TP) site was occupied by AMP-PNP and the beta(DP) site by ADP, where its binding

101 - and beta(TP)-subunits are both occupied by AMP-PNP, whereas in the earlier structure, the beta(TP)

102 n the channel was locked in an open state by AMP-PNP.

103 contrast to high concentrations of calcium, AMP-PNP, and the E157D mutation in Dmc1, each of which p

104 was not mimicked by stable ATP derivatives (AMP-PNP or AMP-PCP) and was abolished by incubation of c

105 of this C-terminal structure also diminished AMP-PNP binding, as well as the catalytic activity of th

106 the presence of 5'-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted association of N-termini

107 dition of 1 mM 5'-adenylylimido-diphosphate (AMP-PNP, an inhibitor of kinesins) or incubation with ki

108 ion coefficient of the ternary complex DnaB-(AMP-PNP)-depsilonA(pepsilonA)19, s20,w = 12.4, suggests

109 the ATP binding site of the 6-PF-2-K domain (AMP-PNP, PO(4), and water).

110 anosarcina mazei PylRS complexed with either AMP-PNP, Pyl-AMP plus pyrophosphate, or the Pyl analogue

111 ower steady-state open probability following AMP-PNP addition (0.68 +/- 0.08 vs. 0.92 +/- 0.03 for wi

112 increased the apparent affinity of Hsp90 for AMP-PNP and completely inhibited the ATPase activity.

113 nucleotides: ATP approximately ATPgammaS >> AMP-PNP approximate GTP > ADP.

114 However, AMP-PNP binding together with K+ can induce a form of Hs

115 ble of unloading PCNA using non-hydrolyzable AMP-PNP.

116 the presence of 5'-adenylim-idodiphosphate (AMP-PNP), the motor domain of ncd binds to the microtubu

117 ith verapamil and adenylyl imidodiphosphate (AMP-PNP) (3.2 angstrom).

118 The inhibitor adenylyl imidodiphosphate (AMP-PNP) induces stochastic pauses in the movement of be

119 olysable analogue adenylyl imidodiphosphate (AMP-PNP) partially substituted for ATP, although none wa

120 olyzable analogue adenylyl imidodiphosphate (AMP-PNP) protects equally well.

121 re effective than adenylyl imidodiphosphate (AMP-PNP), a hydrolysis-resistant ATP analog; however, th

122 pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable analogue.

123 g in wild type by adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable ATP analogue, is markedly d

124 or its analogue, adenylyl imidodiphosphate (AMP-PNP), is required for the strong activation.

125 or followed by 5'-adenylyl imidodiphosphate (AMP-PNP)-induced microtubule affinity purification of th

126 t nonhydrolyzable adenylyl-imidodiphosphate (AMP-PNP) can be used to preload CMG onto a forked DNA su

127 In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-1 d

128 ell as GTP and 5'-adenylyl-imidodiphosphate (AMP-PNP), were accompanied by a corresponding decrease i

129 ) (ATPgammaS) and adenylyl-imidodiphosphate (AMP-PNP).

130 P, 5'-adenylyl beta, gamma-imidodiphosphate (AMP-PNP) and adenosine 5'-(alpha, beta-methylene)triphos

131 log 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP) similarly stabilize the packaged viral genome d

132 , and 5'-adenyl-beta,gamma-imidodiphosphate (AMP-PNP) with the two domains of functional membrane-bou

133 og 5'-adenylyl-beta, gamma-imidodiphosphate (AMP-PNP), ADP, or ADP + Pi using both dimeric (MC1) and

134 with adenylyl beta, gamma-imidodiphosphate (AMP-PNP), some protection from cold dissociation was obs

135 ine 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), was determined at 2.6 A resolution.

136 ue, 5'-adenylyl beta,gamma-imidodiphosphate (AMP-PNP), was investigated by using the fluorescence ani

137 ue, 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), which in the gating models was proposed to bin

138 st, 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP).

139 sence of ATPgammaS, adenylyl imidophosphate (AMP-PNP), ADP, diadenosine tetraphosphate and GTPgammaS.

140 (adenosine 5'-beta,gamma-imidotriphosphate [AMP-PNP]) served as the negative control.

141 inished in K464A mutants due to reduction in AMP-PNP's apparent on-rate and acceleration of its appar

142 inhibited with 1 mM of the kinesin inhibitor AMP-PNP (adenylyl-imidodiphosphate) and by anti-kinesin

143 bitor blebbistatin and the kinesin inhibitor AMP-PNP had no significant effect.

144 were inhibited by the ATP synthase inhibitor AMP-PNP (gamma-imino ATP, a nonhydrolyzable ATP analog)

145 n an unbound form, in complex with inhibitor AMP-PNP, and in complex with ATP and heme.

146 es of the protein with 55% displaying intact AMP-PNP and an unphosphorylated substrate and 45% displa

147 ystal structures of apo Pim-1 kinase and its AMP-PNP (5'-adenylyl-beta,gamma-imidodiphosphate) comple

148 bearing the modification on the ribose, MANT-AMP-PNP and MANT-ADP, and on the base, epsilonAMP-PNP an

149 th magnesium 5'-adenylylimidodiphosphate (Mg-AMP-PNP) and 3-phospho-D-glycerate (3-PG) has been deter

150 sidues from the N-terminal domain and the Mg-AMP-PNP interacting with residues from the C-terminal do

151 thout ADP or the nonhydrolysable ATP mimetic AMP-PNP.

152 otubule complexes formed in 1 mM ADP, 0.5 mM AMP-PNP, suggesting that release of a single AMP-PNP mol

153 hereas ADP-DnaA was predominantly monomeric, AMP-PNP-DnaA (a non-hydrolysable ATP-analog bound-DnaA)

154 spite this apparently tight binding, neither AMP-PNP nor ATPgammaS activated even the strongest GOF m

155 TP, but in the presence of K+, Cs+, or NH4+, AMP-PNP activated casein degradation even better than AT

156 Nonhydrolyzable AMP-PNP and adenosine 5'-(beta,gamma-methylenetriphospha

157 In contrast, neither nonhydrolyzable (AMP-PNP, AMP-PCP) nor hydrolyzable ATP analogs (GTP, CTP

158 The presence of either ATP or ADP but not AMP-PNP leads to GroEL dissociation at lower pressures.

159 GroEL-alphabeta complex with Mg-ATP, but not AMP-PNP, resulted in the release of alpha monomers.

160 the presence of a nonhydrolyzable nucleotide AMP-PNP, have been imaged with the atomic force microsco

161 The ITC-determined affinity of nucleotide (AMP-PNP, ADP) binding to the npMEK1.PD0325901 complex wa

162 ration-dependent manner with the addition of AMP-PNP having more pronounced effect.

163 Strikingly, addition of AMP-PNP to the solution containing preformed GroEL14(Gro

164 me as the affinity of ATP, the affinities of AMP-PNP and AMP-PCP are approximately 2 and approximatel

165 ylate cyclase inhibitors; and application of AMP-PNP, a competitive substrate for adenylate cyclase.

166 Although binding of AMP-PNP is not disrupted by the mutation, the apparent a

167 We find that binding of AMP-PNP shifts the ensemble towards more extended rather

168 he dissociation rate on the concentration of AMP-PNP and ADP indicated that polypeptide dissociation

169 presence of the saturating concentration of AMP-PNP, the sedimentation coefficient of the hexamer is

170 t from pauses occurs at 2 s-1 independent of AMP-PNP concentration.

171 Interaction of AMP-PNP-Mg(2+) and a MBP that is locked in a closed conf

172 3) The binding mode of AMP-PNP to Pim-1 kinase is unique and does not involve a

173 isplaying transfer of the gamma-phosphate of AMP-PNP onto the substrate peptide yielding AMP-PN and a

174 ing the metal ion and the gamma phosphate of AMP-PNP.

175 ation of wild-type kinase in the presence of AMP-PNP (an unhydrolyzable ATP analog) or the autophosph

176 f RSCt for DNA is reduced in the presence of AMP-PNP and ADP in a concentration-dependent manner with

177 F(1)-ATPase, crystallized in the presence of AMP-PNP and ADP, but in the absence of azide, has been d

178 sin bound to microtubules in the presence of AMP-PNP and found close agreement with previous models d

179 , DnaC-DnaB-ssDNA, formed in the presence of AMP-PNP as compared to ADP.

180 (binding to microtubules in the presence of AMP-PNP but not ATP).

181 Moreover, the presence of AMP-PNP diminishes the intrinsic affinity of the PriA pr

182 main to the protofilament in the presence of AMP-PNP is very similar for both motors.

183 d-type Rad51 bound to DNA in the presence of AMP-PNP was trapped in the elongated state.

184 hout the kinase extension in the presence of AMP-PNP.

185 cts bound to microtubules in the presence of AMP-PNP.

186 4 (GroES7) complex formed in the presence of AMP-PNP.

187 Substitution of AMP-PNP or ADP for ATP markedly prolonged the decay of I

188 SAXS performed on AMP-PNP-DnaA (H136Q) indicates that the protein has lost

189 tants reveal that nucleotide binding (ADP or AMP-PNP (adenosine 5'-(beta,gamma-imino)triphosphate)) i

190 In contrast, in the presence of ADP or AMP-PNP only one molecule of oligomeric GroES can be tig

191 n the presence of a 10-fold excess of ADP or AMP-PNP over ATP.

192 apo state and bound to phospholipid, ADP or AMP-PNP to a resolution of 3.3-4.1 angstrom and establis

193 0 mM KCl the addition of ATP, but not ADP or AMP-PNP, resulted in a time-dependent, linear increase i

194 as well as in the presence of either ADP or AMP-PNP.

195 or both npMEK1 and pMEK1 using either ADP or AMP-PNP.

196 g currents were repeatedly evoked in ADP- or AMP-PNP-loaded cells, but dialysis of adenosine 5'-O-(3-

197 Binding of ATP or AMP-PNP (adenosine 5'-(beta, gamma-imino)triphosphate),

198 While ATP or AMP-PNP (adenylyl-imidodiphosphate) binding to wild-type

199 Interestingly, ATP or AMP-PNP prevented the effects of Pi on Ca(2+) uptake.

200 h more slowly, and is facilitated by ATP (or AMP-PNP) and Ca(2+).

201 n had no effect, whereas perfusion of ATP or AMP-PNP, a nonhydrolyzable analog of ATP, significantly

202 s and prevented further activation by ATP or AMP-PNP.

203 (LptB(2)FGC), trapped in either the LPS- or AMP-PNP-bound state.

204 ssary to accommodate the cryo-EM map of "p97-AMP-PNP", suggesting a change in the orientation of N do

205 d [gamma-32P]ATP in the presence of AMP-PCP, AMP-PNP, or TNP-ATP.

206 orm of scallop Ca-ATPase was occupied by Pi, AMP-PNP, AMP-PCP, or ADP despite the presence of saturat

207 n velocity measurements of the DnaB protein-(AMP-PNP)-5'-fluorescein-(dT)20 ternary complex show that

208 rom the structure of the binary complex RepA-AMP-PNP, indicating that, in equilibrium, the RepA hexam

209 C-terminal truncation mutants also required AMP-PNP-dependent dimerization.

210 t conditions, using either ATP, ATP gamma S, AMP-PNP or ADP as nucleotide cofactors, we always find t

211 Since AMP-PNP does not naturally activate P2X receptors, the F

212 AMP-PNP, suggesting that release of a single AMP-PNP molecule from the enzyme is the common rate-limi

213 that, in equilibrium, the RepA hexamer-ssDNA-AMP-PNP complex exists as a mixture of partially open st

214 structure of the tertiary complex RepA-ssDNA-AMP-PNP is very different from the structure of the bina

215 metric bacterial ABC protein that shows that AMP-PNP binds selectively to the noncanonical NBD to pre

216 This argues strongly that AMP-PNP does not inhibit ATP hydrolysis at NBD2 and ther

217 ormational change in a region associated the AMP-PNP adenine binding site.

218 s not adopted by the apo protein, nor by the AMP-PNP bound protein.

219 ate I in TM5 helices, later confirmed by the AMP-PNP-bound BtuCD-F crystal structure.

220 In the AMP-PNP preincubation, low Ca2+ concentrations are not r

221 likely catalysis-competent placement of the AMP-PNP and Mg(2+) components and indicates a tendency f

222 hodopsin is essential for development of the AMP-PNP incubation effect.

223 We also found that the AMP-PNP incubation effect was not altered by addition of

224 1-cis-retinal and hydroxylamine prior to the AMP-PNP incubation and by measurement of the GCAP2 conce

225 translocation channel in agreement with the AMP-PNP.BtuCD-F x-ray structure.

226 Thus, AMP-PNP binding simultaneously protects residues within

227 N-tail mutant had both a slower response to AMP-PNP (activation half-time of 140 +/- 20 s vs. 21 +/-

228 t exhibited a markedly inhibited response to AMP-PNP, a poorly hydrolysable ATP analogue that can nea

229 , beta,gamma-imidoadenosine 5'-triphosphate (AMP-PNP), and copper and undergoes nucleotide-dependent

230 , beta,gamma-imidoadenosine-5'-triphosphate (AMP-PNP), have been examined, using the fluorescence int

231 o beta,gamma-imidoadenosine 5'-triphosphate (AMP-PNP).

232 adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP) bound at the degenerate site.

233 adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP), and maleate.

234 adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP), even though it cannot support steady-state cat

235 adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP), onto a substrate peptide within protein crysta

236 adenosine 5'-[beta,gamma-imido]triphosphate (AMP-PNP), a non-hydrolyzable ATP analog, has no effect o

237 adenosine 5'-(beta,gamma-imino)triphosphate (AMP-PNP) and adenosine 5'-O-(thiotriphosphate) (ATPgamma

238 denosine 5'-(beta,gamma -imino)triphosphate (AMP-PNP) or ADP, less than 10% of the LOOP1 epitopes wer

239 adenosine 5'-(beta,gamma-imino)triphosphate (AMP-PNP), and guanosine 5'-3-O-(thio)triphosphate (GTPga

240 adenosine 5'-(beta,gamma-imino)triphosphate (AMP-PNP), or other NTPs do not support the activity.

241 nformational state of the helicase, with two AMP-PNP molecules bound, has dramatically higher ssDNA-a

242 mutant channels deactivated very slowly upon AMP-PNP or ATPgammaS removal (taudeac approximately 100

243 ATP analog; however, this study mainly used AMP-PNP to focus on the role of adenine nucleotide bindi

244 ographic characterization of inactive versus AMP-PNP-liganded structures of FAK1 showed that a large

245 e from inactivation by NEM is also lost when AMP-PNP is present during the IAAmide treatment.

246 With AMP-PNP, binding of a small amount (<20%) of a second Gr

247 (108-268) holoenzyme structure (1.62 A) with AMP-PNP/Mn(2+) showed that we trapped the RIIbeta subuni

248 mulated 4-6-fold the peptidase activity with AMP-PNP present and eliminated the time lag, but KCl had

249 reased intracellular calcium amplitudes with AMP-PNP compared to the WT receptor and has a much lower

250 GTP in the pipette, or by replacing ATP with AMP-PNP or UTP.

251 Movement did not occur without ATP, with AMP-PNP, or with ATP plus antibody.

252 that although the structure in complex with AMP-PNP is in an "alphaC-out" inactive conformation, tho

253 utophosphorylated HipT(Lp), its complex with AMP-PNP, and the structure of HipT(Lp)-HipS(Lp) complex,

254 e structure of G. lamblia CK in complex with AMP-PNP.

255 y structure of active 2P-ERK2 complexed with AMP-PNP reveals a shift in the Gly-rich loop along with

256 that mediate non-canonical interactions with AMP-PNP.

257 A complex of RON(M1254T) with AMP-PNP and Mg(2+) reveals a substratelike positioning o

258 er segment homogenates are preincubated with AMP-PNP (EC50 = 0.65 +/- 0.20 mM), GCAP2 enhanced the re

259 ent on twitchin phosphorylation is seen with AMP-PNP and ATPgammaS.

260 domain, bound C subunit poorly, whereas with AMP-PNP, a non-hydrolyzable ATP analog, the affinity was

261 Without AMP-PNP, GCAP2 stimulated the control activity only 3-4-

262 ciation of the Mt.MC1 complex at 14 s-1, yet AMP-PNP has no effect on the Mt.MC1 complex.