ライフサイエンスコーパス: Kd

1 Kd values for the dissociation of WY 14,643 from the oxi

2 optimal antibody dose of (111)In-PD-L1.3.1 (Kd = 1 nmol/L) for SPECT/CT imaging was </=1 mug.

3 tial loss of affinity for [Fe(bisDHBS)](2-) (Kd approximately 0.5 +/- 0.2 microM).

4 zed, supported lipid bilayers, yielding a 2D Kd of approximately 5,000 molecules/mum(2) This value is

5 magnitude higher than previously measured 2D Kd values for interacting leukocyte surface proteins.

6 ar Kd for stachydrine and trigonelline and a Kd in the millimolar range for betonicine.

7 ve as a novel ligand for DRAK2, displaying a Kd value of 1.6 muM.

8 differences in DNA binding affinity, from a Kd of 27 +/- 3 nM for (Delta,Lambda)-Piz to a Kd of 622

9 Scatchard analysis gave a Kd of approximately 10 nM consistent with RvD2 bioactive

10 The interaction between RWD and Ubc9 has a Kd of 32 +/- 4 muM.

11 Compound 19 was found to have a Kd of 410 nM and a favorable thermodynamic profile, and

12 o free nucleobases (U, T, hmU), indicating a Kd >> 10 mM.

13 f heme binding to Rev-erbbeta and provided a Kd for Fe(3+)-heme of approximately 0.1 nm Loss of the H

14 factors enhanced ELC1 binding 49-fold (to a Kd of 12 nm).

15 d of 27 +/- 3 nM for (Delta,Lambda)-Piz to a Kd of 622 +/- 55 nM for (Lambda,Delta)-Piz.

16 le independent binding sites for EGCG with a Kd approximately 10-fold lower than that for the Abeta(1

17 that suggested a new consensus design with a Kd approximately 140 pM.

18 p130Cas CCHD (in a 1:1 stoichiometry with a Kd approximately 4.2 mum) and elucidated the structure o

19 pol nu binds to DNA with a Kd for DNA of 9.2 nm, with an off-rate constant of 0.013

20 ing substrates but binds abasic sites with a Kd of <1.4 mum.

21 termined by surface plasmon resonance with a Kd of 0.57 mum In an in vitro decatenation assay, Mus101

22 IRF1 peptide interacted with USP7-NTD with a Kd of 2.0 mum.

23 tic measurements were also consistent with a Kd of 200 nm We determined that PLC-beta3 hysteresis, wh

24 e shown binding to collagen receptors with a Kd of 3.45 +/- 1.06 muM.

25 entially to the inactive Ras GDP form with a Kd of 4 nM and structural studies support its selectivit

26 ed that binding to PDI was reversible with a Kd of 62 nM, suggesting LOC14 to be the most potent PDI

27 in trans SBT3 was inhibited by SBT3PP with a Kd of 74 nm for the enzyme-inhibitor complex.

28 dies show that IIA(Glc) binds to LacY with a Kd of about 5 muM and a stoichiometry of unity and that

29 y with the TrkB extracellular domain, with a Kd of approximately 10 nm.

30 an intermediate-affinity interaction, with a Kd of approximately 200 nM.

31 rf2-interacting kelch domain of Keap1 with a Kd of approximately 6 muM, as demonstrated by x-ray co-c

32 that the two proteins bind each other with a Kd of ~5 mum.

33 KU675 also displayed binding to Hsc70 with a Kd value at 76.3 muM, which was supported in cellular by

34 Pyrophosphorylation occurs with a Kd value for PPi of 3.7 mm and a maximal rate constant o

35 that AE1 and beta1 interact directly, with a Kd value of 0.81 muM.

36 CMG demonstrate Pol epsilon binds CMG with a Kd value of 12 nM, but Pol delta binding CMG is undetect

37 ity for BoHV-1, which bound to BoHV-1 with a Kd value of 3.519 nM and demonstrated the greatest virus

38 a high affinity for Abeta aggregates with a Kd value of 3.5nM.

39 ed to the development of compound 32, with a Kd value of 32 nM and an EC50 value of 0.67 muM in a sur

40 nalysis of the self-blocking scans yielded a Kd estimate of 3.4 nM and Bmax of 125-350 nM, in good ag

41 The U(VI) adsorption Kd values steadily increased as the mass fraction of chl

42 had unprecedentedly high binding affinities (Kd approximately 10(-12) m) and high specificity.

43 for two adnectins with distinct affinities (Kd, Adnectin1 approximately 6.2 pM vs Kd, Adnectin2 appr

44 n agreement with a reduced binding affinity (Kd = 1.2 x 10(-9) vs 2.7 x 10(-11) M, saturation experim

45 ectively) conferred potent binding affinity (Kd = 1.47 +/- 0.03 nm) in vitro and membrane translocati

46 In WT, the apparent binding affinity (Kd = 10.2 +/- 0.8 microM) is comparable to that of cAMP

47 ts C1 domain has very weak binding affinity (Kd = 2890 +/- 240 nm for [(3)H]phorbol 12,13-dibutyrate.

48 The binding affinity (Kd) for Hsp90alpha was determined to be 191 muM, whereas

49 SH3) domain with an unusually high affinity (Kd 24 nm).

50 d flexible, and it binds with high affinity (Kd = 98 nM) to calmodulin without major conformational c

51 C-xdhR intergenic region with high affinity (Kd approximately 0.5 nM).

52 pproximately 300 s), and very high affinity (Kd approximately 10 nM).

53 bind single-stranded DNA with high affinity (Kd approximately 50 nM).

54 53-derived peptide binds with high affinity (Kd value of 150nM) and causes the formation of an extens

55 technology based on the ultra-high-affinity (Kd approximately 10(-14)-10(-17) M) complex between the

56 We obtained eight high-affinity (Kd approximately 12-30 nM) selective competitive inhibit

57 ates amphiphiles that exhibit high-affinity (Kd in low nanomolar range) binding to HSA.

58 inds to human P-sel with nanomolar affinity (Kd~22 nM).

59 th the FRET efficiency (E) and the affinity (Kd) of the molecular interaction from intermolecular FRE

60 constant for Zn(2+) and human serum albumin (Kd = (5.62 +/- 0.93) x 10(-7) M) under physiological con

61 MR signal of the Tby tert-butyl group allows Kd measurements using less concentrated protein solution

62 tly weaker than that of the C1 domain alone (Kd = 8.2 +/- 1.1 nm for the full-length protein containi

63 ivity (11)C-GSK1482160, receptor density and Kd were 1.15 +/- 0.12 nM and 3.03 +/- 0.10 pmol/mg, resp

64 in the observed discrepancy between EC50 and Kd These results indicate that the mechanism by which Ga

65 d to obtain the kinetic parameters, kpol and Kd, for correct nucleotide incorporation, incorrect nucl

66 en probability (Kd Eu(3+) = 167 +/- 5 nM and Kd Sm(3+) = 63 +/- 3 nM), but in nominally 0 [Ca(2+)], l

67 ha7 activation with EC50 values of 70 nM and Kd values for AChBP in a similar range.

68 s found to have Kd = 24 +/- 3 nM by PXCE and Kd = 17 +/- 2 nM using isothermal calorimetry (ITC).

69 ) binds with low affinity to the apoprotein (Kd 120 mm), with a particularly low kon value (5.1 m(-1)

70 f PI(4,5)P2 with moderate affinity (apparent Kd=17muM).

71 The sensor achieved an apparent Kd of 45 +/- 12 microM, and a limit of detection of 0.9

72 wed a kred value of 24 s(-1) and an apparent Kd value estimated in the low micromolar range.

73 nd to the orthosteric binding site (apparent Kd: 0.87 and 0.31 nM, respectively).

74 Factor Va reduced by 100-fold the apparent Kd of myosin for factor Xa (Kd approximately 0.48 nM), p

75 ts showed similar affinity toward aprotinin (Kd's of 3-9 muM), which were not significantly different

76 e by using specific anti-E.coli DNA aptamer (Kd 14nM), screened by new in-situ developed SELEX metho

77 ual aspects of indicator performance such as Kd, wavelength, and ratiometric measurements, the use of

78 reening approaches are discussed, as well as Kd determination, ligand-efficiency calculations and dru

79 he sensitivity 4-6 orders of magnitude below Kd, they compromise temporal resolution.

80 Enzymologists distinguish binding (Kd) and catalytic (kcat) steps.

81 1)) and especially tight nucleotide binding (Kd (dNTP) approximately 1.7 mum), compared with DNA poly

82 modynamic parameters for nucleotide binding (Kd , DeltaG, DeltaH, and DeltaS at 37 degrees C) and kin

83 Escherichia coli, exhibited strong binding (Kd </= 2 nm) with lysozyme and abrogated its lytic activ

84 F4A-eIF4B-ATP increases 40S subunit binding (Kd = 120 +/- 10 nm) to the conserved stem-loop I of the

85 is(2,3-dihydroxybenzoyl-l-Ser) (H5-bisDHBS) (Kd = 10.1 +/- 3.8 nM).

86 Bm12.Kd.IE CD4 T cells survived long term when transferred to

87 Bm12.Kd.IE heart grafts provoked strong germinal centre alloa

88 cardiac transplantation was developed (bm12.Kd.IE to C57BL/6).

89 el of cardiac transplantation was used (bm12.Kd.IE to C57BL/6).

90 we found that (i) 40S subunits bind to BTE (Kd = 350 +/- 30 nm), (ii) the helicase complex eIF4F-eIF

91 relatively low affinity of Cal-590 for Ca2+ (Kd=561 nM), single-action potential-evoked Ca2+ transien

92 h-affinity ligand for NRP1 with a calculated Kd of 38.7 nm Furthermore, we showed that NRP1 binds to

93 erfect correspondence between the calculated Kd and the experimental EC50 on HIV-infected cells confi

94 molecules of the catabolite p-coumaroyl-CoA (Kd = 11 +/- 1 muM).

95 elatively high affinity for p-coumaroyl-CoA (Kd = 89 +/- 6 muM).

96 sorbed-to-solution distribution coefficient (Kd) and desorption rate constants (k-1) decreased wherea

97 order of magnitude distribution coefficient (Kd) for absorbing of the radioactive cesium ion.

98 Distribution coefficients (Kd) for trace Tl adsorption indicated a moderate pH-depe

99 homoionic clays with sorption coefficients (Kd) decreasing as follows: Kd(Na(+)) > Kd(NH4(+)) >/= Kd

100 herms and solid-water sorption coefficients (Kd) for four organic cations (benzylamine, 2,4-dichlorob

101 els of organic cation sorption coefficients (Kd).

102 t CID/NCBD formed a relatively weak complex (Kd approximately 5 microM).

103 inity measurements with purified components, Kd values for unpurified proteins in crude cell lysates

104 t of the submicromolar dissociation constant Kd (0.2 muM) of the complex between glutamate and the Es

105 AD with high affinity (dissociation constant Kd = 11-41 nM), kill TnCAD-expressing insect cells that

106 ator, which displays a dissociation constant Kd = 3.1 mM suitable for the detection of low millimolar

107 kinase activity with a dissociation constant Kd = ~1 muM.

108 The measured binding constant (Kd = 5.645 x 10(3) M(-1)) indicated strong interactions

109 The binding constant (Kd) discerned for the dye and HRP-II to Ni(2+) were 1.4

110 in an estimate of the dissociation constant (Kd ) for this interaction of 8 mum These results prompt

111 d protein YscI with a dissociation constant (Kd ) of 3.8 mum and with 1:1 stoichiometry.

112 ucan laminarin with a dissociation constant (Kd ) of approximately 26 mum and displayed higher affini

113 lose to heme 2 with a dissociation constant (Kd) = 490 muM, in good agreement with recent experimenta

114 ligomer has a similar dissociation constant (Kd) and free energy of association to the Vpu homooligom

115 sensors is set by the dissociation constant (Kd) between analytes and probes.

116 mbrane target and the dissociation constant (Kd) between Src and isorhamnetin was 3.81 muM.

117 is - with an apparent dissociation constant (Kd) equal to about 1 nM, indicating a high affinity bind

118 measured equilibrium dissociation constant (Kd) for the binding of free SDF1 or the fusion protein t

119 ssay, the equilibrium dissociation constant (Kd) for the interaction was established in the range of

120 ic DNA aptamer with a dissociation constant (Kd) of 232 nM.

121 The apparent dissociation constant (Kd) of Man-SNPs with fluorescein isothiocyanate (FITC)-c

122 re, we determined the dissociation constant (Kd) of ORF3 interactions with the viral helicase, papain

123 determine equilibrium dissociation constant (Kd) values.

124 The determined dissociation constant (Kd) was affected more than 50% when increasing the AmAc

125 e occupancy plot; the dissociation constant (Kd) was determined by fitting self-blocking occupancies

126 50-fold change in the dissociation constant (Kd).

127 ing to McpX(PR) with dissociation constants (Kd ) in the nanomolar range for choline and glycine beta

128 fetimes (1/koff) and dissociation constants (Kd = koff/kon), determined by mechanically dissociating

129 ed DNA aptamer, with dissociation constants (Kd values) of 0.6 muM.

130 termination of their dissociation constants (Kd's).

131 ; giving equilibrium dissociation constants (Kd) = 8-50 nM.

132 t surprisingly their dissociation constants (Kd) are low, between 10 and 200 pM.

133 s from which precise dissociation constants (Kd) for protein-peptide interactions can be inferred.

134 inding isotherm with dissociation constants (Kd) of 0.9 and 7.4 mum.

135 /ml (at S/N=3), with dissociation constants (Kd) of 5.65+/-2.5mIU/ml and 7.28+/-2.6mIU/ml, respective

136 d to examine (i) the dissociation constants (Kd) of individual PFOS and PFOA isomers with human serum

137 Aptamers with dissociation constants (Kd) of nanomolar range were isolated.

138 ity, interaction and dissociation constants (Kd) of the peptide-ligand Delta-somatostatin (AGSKNFFWKT

139 similar equilibrium dissociation constants (Kd), approximately 2 nM.

140 Thus, the dissociation constants (Kd, muM) of 4 (11.2) and 5 (0.16) are similar to those o

141 s of the equilibrium dissociation constants, Kd, of oxidized (hAR*NADP(+)) and reduced (hAR*NADPH) ho

142 nding studies shows high affinity for CXCR3 (Kd = 0.65 nM) and reasonably fast association (kon= 0.03

143 ole and ketaminazole bound tightly to CYP51 (Kd </= 2 to 11 nM).

144 and itraconazole bound strongest to CYP5218 (Kd ~1.6, 0.5 and 0.4 muM) indicating CYP5218 to be only

145 Derived Kd values (20-104 muM) for the binding variants were sim

146 S-CoV 3CL(pro) is a weakly associated dimer (Kd approximately 52 mum) with a slow off-rate.

147 ory MCR.CoB7SH complex is highly disfavored (Kd = 56 mM).

148 with a cysteine that bind tightly to EcDsbA (Kd = 2.0 +/- 0.3 muM) and inhibit its activity (IC50 = 5

149 of the hexadentate siderophore enterobactin (Kd approximately 0.4 +/- 0.1 microM), preferentially bin

150 ACP (CurB) had high affinity for the enzyme (Kd = 0.5 muM) and could not be substituted by the accept

151 ived from baseline VT and from the estimated Kd and the nondisplaceable distribution volume (VND).

152 greement with recent experimental estimates, Kd = 255 muM.

153 oB7SH.MCR(Ni(I)).CH3SCoM) is highly favored (Kd = 79 muM).

154 for laminin (Kd = 9.26 nM) and fibronectin (Kd = 10.19 nM), but slightly less to vitronectin (Kd = 1

155 ion coefficients (Kd) decreasing as follows: Kd(Na(+)) > Kd(NH4(+)) >/= Kd(K(+)) > Kd(Ca(2+)) >/= Kd(

156 ods that employ direct protein detection for Kd measurements.

157 domain of pyoS2 (pyoS2(NTD)) bound to FpvAI (Kd = 240 pM) reveals that the pyocin mimics Fe-Pvd, indu

158 ) >/= Kd(K(+)) > Kd(Ca(2+)) >/= Kd(Mg(2+)) > Kd(Al(3+)).

159 llows: Kd(Na(+)) > Kd(NH4(+)) >/= Kd(K(+)) > Kd(Ca(2+)) >/= Kd(Mg(2+)) > Kd(Al(3+)).

160 ents (Kd) decreasing as follows: Kd(Na(+)) > Kd(NH4(+)) >/= Kd(K(+)) > Kd(Ca(2+)) >/= Kd(Mg(2+)) > Kd

161 ) > Kd(NH4(+)) >/= Kd(K(+)) > Kd(Ca(2+)) >/= Kd(Mg(2+)) > Kd(Al(3+)).

162 asing as follows: Kd(Na(+)) > Kd(NH4(+)) >/= Kd(K(+)) > Kd(Ca(2+)) >/= Kd(Mg(2+)) > Kd(Al(3+)).

163 ts are full CXCR4 antagonists, and four have Kd values <5 nm.

164 ozyme-antibody interaction was found to have Kd = 24 +/- 3 nM by PXCE and Kd = 17 +/- 2 nM using isot

165 ciated athanogene 3 (Bag3) was found to have Kd = 25 +/- 5 nM by PXCE which agrees with Kd values rep

166 ransfer yet formed a stable complex with Hb (Kd = 6 +/- 2 mum) in solution with spectroscopic feature

167 ng the actin-binding affinity measured here (Kd = 0.6 muM) is in the physiologically relevant range.

168 his complex was found to be relatively high (Kd approximately 1.6 mM) compared with other monovalent

169 ranged from low nanomolar to 50 times higher Kd values.

170 dissociation constants of c-Fos homodimers (Kd = 6.7 +/- 1.7 muM) and c-Fos-c-Jun heterodimers (on t

171 Measurement of HSA Kd's demonstrated that linear PFOS (Kd=8(+/-4)x10(-8) M)

172 ds) RNAs bind to RIG-I with nearly identical Kd values and activate RIG-I's ATPase and cellular signa

173 ted the advantage that (19)F offers improved Kd precision due to higher spectrum resolution and great

174 of binding resulting in a factor of 41000 in Kd for the H-to-iBu transformation.

175 ration gradient does not involve a change in Kd for sugar on either side of the membrane, but the pKa

176 The largest step-changes in Kd involved the F11A peptide modification which implies

177 utations result in a 13-800-fold increase in Kd values.

178 A further reduction in Kd obtains in binding studies with human Importin alpha5

179 ute to the observed NADPH-dependent shift in Kd.

180 ome duplication, the affinity had increased (Kd approximately 200 nM) and was maintained in further s

181 nd to HSA compared to branched PFOA isomers (Kd range from 4(+/-2)x10(-4) M to 3(+/-2)x10(-4) M).

182 re tightly bound than branched PFOS isomers (Kd range from 8(+/-1)x10(-5) M to 4(+/-2)x10(-4) M).

183 for TRIM24 and BRPF1 (ITC Kd = 31 nM and ITC Kd = 14 nM, respectively).

184 nomolar affinities for TRIM24 and BRPF1 (ITC Kd = 31 nM and ITC Kd = 14 nM, respectively).

185 plex for peptides with K786I or H782Q/K786I (Kd(app) = 0.2-0.5 mum, as determined by SPR) compared wi

186 ATPase turnover rate and thus a high katpase/Kd.

187 ncentration data compared well to laboratory Kd values reported in the literature.

188 splayed a high binding affinity for laminin (Kd = 9.26 nM) and fibronectin (Kd = 10.19 nM), but sligh

189 o generate the extensive data sets of linear Kd values required for the development of predictive sor

190 Mean distribution coefficients, log Kd(*), ranged from 0.2 to 2.1 for the PFPAs and PFPiAs a

191 The log Kd(*) of PFPiAs calculated here (1.6-2.1) were similar t

192 model fits our experimental results with log Kd = -9.7 +/- 0.3 and a 2:1 prevalent stoichiometry of t

193 Five promising aptamers presenting low Kd values and good specificity were generated.

194 ound fibronectin with higher affinity, lower Kd, than several bacterial pathogens and competitively e

195 all proteins exhibit tighter binding (lower Kd ) as the proportion of anionic lipid increases.

196 ities in the low micromolar range (1.6 muM < Kd < 14.6 muM) and had rapid blood clearance.

197 ing assays on HCT 116 cells indicated a mean Kd of 3.04+/-0.52nM.

198 i (1,4)-regioisomers as revealed by measured Kd values.

199 se CPR-CYP2C9 interactions, and the measured Kd values are highly dependent on the redox state of CPR

200 The measured Kd was not altered either by the presence of phospholipi

201 e domain contributing to a 156 +/- 18 microM Kd interaction: a hydrophobic pocket lined by 4 critical

202 for choline and glycine betaine, micromolar Kd for stachydrine and trigonelline and a Kd in the mill

203 cid derivatives and bind with low micromolar Kd values to Siglec-7.

204 y binding, characterized by a low micromolar Kd, that is selective for the murine Importin alpha1 (mI

205 was least sensitive, with a near millimolar Kd value.

206 e instead of an ethylene spacer (t1/2 3 min, Kd 2.0 nM).

207 ltaH = -80.3 kJ/mol; -TDeltaS = 37.9 kJ/mol, Kd = 39 nm) whereby the thioimide adduct is formed with

208 with a stoichiometry of 1:1 and a nanomolar Kd determined in vitro.

209 native G4DNA topologies with a low nanomolar Kd value of approximately 2 nm, similar to that observed

210 with TFB2M or TFAM on LSP with low-nanomolar Kd values, but these two-component complexes lack the me

211 th the substrate analogue, 5-nitrovanillate (Kd = 5.0 nM), was determined to a resolution of 1.07 A.

212 oA peptide, consistent with the stable 10 nm Kd measured by isothermal titration calorimetry.

213 of human RIPK1 enzymatic activity with a nM Kd; has a non-ATP competitive mode of action and a novel

214 d and unbound protein allowed calculation of Kd values from the resulting data.

215 ein-protein complex for the determination of Kd's was also explored.

216 mmonium Kd values, allowed for estimation of Kd values for more structurally complex organic cations

217 que properties of Q7R enabled measurement of Kd values across 3 orders of magnitude and at concentrat

218 ic Hg(II) binding affinities in the range of Kd = 0.2-2.0 muM, depending on the buffer conditions.

219 quantitative binding data (e.g. Ki, IC50 or Kd).

220 the lowest-affinity double-alanine peptide (Kd(app) = 3.8 mum).

221 Similarly, linear PFOA (Kd=1(+/-0.9)x10(-4) M) was more strongly bound to HSA co

222 t of HSA Kd's demonstrated that linear PFOS (Kd=8(+/-4)x10(-8) M) was much more tightly bound than br

223 sorption, along with phenyltrimethylammonium Kd values, allowed for estimation of Kd values for more

224 M) while affinity for the ATP site was poor (Kd = ~8 muM).

225 facilitating measurements of highly potent (Kd < nM) compounds.

226 kly identify new inhibitors with a predicted Kd as low as 18 nM.

227 ) potently inhibited RyR's open probability (Kd Eu(3+) = 167 +/- 5 nM and Kd Sm(3+) = 63 +/- 3 nM), b

228 cific and high-affinity RNA-binding protein (Kd < 1 nM).

229 binding motif enables fluorescent proteins (Kd = 14.7 muM) to confluently stain DNA molecules and su

230 nomers is lower than for Abeta protofibrils (Kd values are submillimolar rather than micromolar) yet

231 issociation constant in the picomolar range (Kd 0.044 nM, SK-N-MC cells) and very high Y1R selectivit

232 sulting mass-sensitive measurements revealed Kd of dopamineHCl, haloperidol, and (+)-SCH23390 at 0.87

233 Ch), although all three ligands have similar Kd values for M3R.

234 n (rHSA) towards cholesteryl-modified siRNA (Kd>1x10(-7)M) dependent on number of modifications.

235 ong affinity for the substrate-binding site (Kd = 20 nM) while affinity for the ATP site was poor (Kd

236 of thrombin at high-affinity binding sites (Kd = 0.15 muM).

237 bin molecules at low-affinity binding sites (Kd = 2.8 muM) and approximately 0.3 molecules of thrombi

238 In situ Kd values (Pu concentration ratio of sediment/groundwate

239 d SP-B(N) were able to interact in solution (Kd = 0.4 muM), which enabled their binding to bacteria w

240 Equivalent Pu(IV) and Pu(V) sorption Kd values obtained at 1 and 2-week sampling time points

241 raction between Cu(2+) and SRE was stronger (Kd = 7.181 x 10(4) M(-1)) but varies for the individual

242 acids with linoleic acid binding strongest (Kd 36 muM), although no metabolism could be detected in

243 ucleic acids (XNAs), also bind PLN strongly (Kd <10 nm) and relieve inhibition of SERCA.

244 3)H]-(2R,7R)-10, [(3)H]18) with subnanomolar Kd values.

245 ffinity to the Kunitz-1 (K1) domain of TFPI (Kd approximately 1 nM).

246 The Kd construct captured most of the data trends above and

247 The Kd of anti-ATX aptamer was calculated by electrochemical

248 The Kd value of the binding between vancomycin and Zn(II) wa

249 The Kd was approximately 2 microM.

250 ence of high Na(+) concentrations (above the Kd for Na(+)) the dissociation constants for aspartate w

251 FR-TS binding kinetic parameters such as the Kd value being below 10 microM (both methods), k(on) = 0

252 were no significant differences between the Kd values of chitopentaose and chitohexaose, supporting

253 rated mechanochemical sensing that broke the Kd limit by 9 orders of magnitude for Hg detection witho

254 wed trends similar to those observed for the Kd values, the variation among the proteins was much low

255 Interestingly, the Kd that was calculated from the aptasensor signal showed

256 le sizes (5, 13, 23 nm) and by modifying the Kd of the bioreceptor using wild-type and mutant hDHFR.

257 in the presence of OS with its impact on the Kd for linoleic acid substrate binding, we conclude that

258 high proportions of phosphatidylserine, the Kd values of all four proteins began to converge.

259 gressively introduced and shown to raise the Kd from 103 + 47 muM until the point where binding was a

260 th UV-visible difference titrations that the Kd value is in the low nanomolar range, and the Fe(3+)-h

261 o be reduced to 25 pM, which is close to the Kd value of the protease dimer.

262 Unexpectedly, the Kd values for guests binding to Q7R and to unmodified Q7

263 ha was determined to be 191 muM, whereas the Kd for Hsp90beta was 726 muM, demonstrating a preference

264 tin alpha1 (mImpalpha1) minor site, with the Kd strengthening to approximately 140 nM for the full ly

265 This Kd is 50-100 times greater than the EC50 for Galphaq-med

266 in solutions than usual, providing access to Kd values 1 order of magnitude lower than established NM

267 itors of three deltaPKC substrates (in vitro Kd approximately 3 nm); two greatly reduced ischemia-ind

268 h affinity for the microRNA let-7b in vitro (Kd = approximately 6 nM) in cells.

269 10.19 nM), but slightly less to vitronectin (Kd = 16.51 nM).

270 ities (Kd, Adnectin1 approximately 6.2 pM vs Kd, Adnectin2 approximately 46 nM).

271 in partitioning coefficients of solid-water (Kd), total organic carbon-water (KTOC), and dissolved or

272 e designed a peptidomimetic that binds WDR5 (Kd approximately 3 nm) and selectively inhibits activity

273 thought to be a heme sensor based on a weak Kd value for the Rev-erbbeta.heme complex of 2 mum deter

274 voriconazole and ketaminazole bound weakly (Kd ~107 and ~12 muM), whereas ketoconazole, clotrimazole

275 In contrast, the compounds bind more weakly (Kd values from 600nM to 12muM) and induce an incomplete

276 ibitor of Arabidopsis subtilase SBT4.13 with Kd and Ki values in the picomolar range.

277 4 glycans, which are recognized by 2G12 with Kd's as low as 1.7 nM.

278 to M1 mAChR in the presence of 1 mM ACh with Kd, 4.23 nM, and saturable binding capacity (Bmax), 6.38

279 e Kd = 25 +/- 5 nM by PXCE which agrees with Kd values reported without cross-linking.

280 hat the most potent MIF inhibitors bind with Kd values of ca. 50 nM; two are from our laboratory, and

281 t YKL-39 binds to chitooligosaccharides with Kd values in the micromolar concentration range and that

282 buricol and obtusifoliol bound to CYP51 with Kd values of 32, 23 and 28 muM, respectively, catalyzing

283 protein could bind directly with G4 DNA with Kd values in the low nanomolar range and revealed that t

284 binds the soluble fibrin fragment DD(E) with Kd = 110 nM.

285 E aptamers are highly sensitive for EE, with Kd of 0.5-1.0 muM.

286 exists as a dimer-tetramer equilibrium with Kd = 1.0 +/- 0.9 muM.

287 affinity for insoluble beta-1,3-glucans with Kd values of approximately 2-10 mum but lacked affinity

288 olution, and that the proteins interact with Kd = 13.5 +/- 0.8 muM.

289 higher affinity for the same membranes with Kd values of 12 to 16.4 nM.

290 cytoplasmic domain of band 3 (cdb3-PO4) with Kd = 14 nM; (iii) binding of cdb3-PO4 to erythrocyte mem

291 dNTP binding is rapid with Kd values of 20 and 476 mum for the correct and incorrec

292 eveloped through 12 rounds of selection with Kd of 0.971microM and 0.309microM, respectively.

293 re determined to be the most sensitive, with Kd values in the tens of micromolar, whereas the C2D dom

294 hat human FUS binds all these sequences with Kd (app) values spanning a 10-fold range.

295 lded a potent ligand, sulfonamide-WIVP, with Kd = 6.7 +/- 2.1 nM, a 20-fold improvement compared with

296 old the apparent Kd of myosin for factor Xa (Kd approximately 0.48 nM), primarily by reducing koff, i

297 anthraniloyl) analogs of ATP and ADP yielded Kd values for ATP, ADP, AMP, and adenosine of 20 +/- 3,

298 velocity and fluorescence anisotropy yielded Kd = 84 (54-123) nm Dimer dissociation kinetics were mea

299 wo physically distinct methods, both yielded Kd values of about 200 nm for PLC-beta3-Galphaq binding.

300 We measured the zinc Kd zinc ionophore activity, ability to restore zinc to p