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 n was similar in both groups (KdD, 69 [22%]; Kd, 38 [25%]).

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

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

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

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

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

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

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

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

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

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

15 its recognition site (LacO) in vitro with a Kd about 10 picomolar (pM), it is often assumed that Lac

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 showed that it binds gentiobiose-6'-P with a Kd of 0.04 mM and with lower affinity also other phospho

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

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

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

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

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

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

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

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

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

35 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

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

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

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

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

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

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

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

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

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

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

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

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

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

49 53-derived peptide binds with high affinity (Kd value of 150nM) and causes the formation of an extens

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

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

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

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

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

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

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

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

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

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

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

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

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

63 ressor operator system and found an apparent Kd of ~0.6 muM, four orders of magnitude higher than tha

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

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

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

67 ing of the features that affect the apparent Kd of TF in cells.

68 (iv) LacO sequence, we reduced the apparent Kd to <10 nM.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

94 els of organic cation sorption coefficients (Kd).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

112 measurements of TFs' dissociation constant (Kd) in vitro, their apparent Kdin vivo are usually unkno

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

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

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

116 lecule assay in which dissociation constant (Kd) of the conjugate can be separately evaluated from th

117 determine equilibrium dissociation constant (Kd) values.

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

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

120 50-fold change in the dissociation constant (Kd).

121 igh-binding affinity (dissociation constant, Kd, 4.6 +/- 0.8 nM).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

138 D-Kd was well tolerated with low neutropenia rates, and it

139 umumab plus carfilzomib and dexamethasone (D-Kd) in patients with RRMM after 1 to 3 prior lines of th

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

141 umab (KdD) or carfilzomib and dexamethasone (Kd).

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

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

144 a general affinity for double stranded DNA (Kd ~ 350 nM) and binds specifically to a 50 bp A+T rich

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

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

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

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

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

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

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

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

153 We found Kd of 0.8 nM for PA-PDS, which is much lower than PDS (K

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

170 ch sequence flanking each side of the D IES (Kd ~ 43 nM).

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

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

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

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

175 y beads allowed recovery of hits improved in Kd over wild-type ZIgE by up to 3.5-fold, while a consen

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

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

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

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

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

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

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

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

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

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

186 (LCFAs) into skeletal muscle and knockdown (Kd) of a subset of RabGAP substrates, Rab8, Rab10, or Ra

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

212 cellular domain, we showed that the obtained Kd values were within the limits accepted for modified t

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

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

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

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

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

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

219 is much lower than PDS (Kd ~ 450 nM) or PA (Kd ~ 35 nM).

220 nM for PA-PDS, which is much lower than PDS (Kd ~ 450 nM) or PA (Kd ~ 35 nM).

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

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

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

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

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

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

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

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

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

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

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

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

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

234 te both chemokines having virtually the same Kd, suggesting a mechanism of signal amplification in DC

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

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

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

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

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

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

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

242 s against AQP4 ranged from modest to strong (Kd 15.2-559 nM), none of the germline revertants display

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

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

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

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

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 d in the KdD group versus 15.8 months in the Kd group (hazard ratio 0.63; 95% CI 0.46-0.85; p=0.0027)

256 the KdD group and 113 (74%) patients in the Kd group.

257 r nonspecific protein-protein binding in the Kd ~ 10-mM regime.

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

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

260 concentration is close to the binding of the Kd to the receptor, and least potent when the mean conce

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

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

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

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

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

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

267 nt duration was longer in the KdD versus the Kd group (70.1 vs 40.3 weeks).

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

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

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

271 y prolonged progression-free survival versus Kd in patients with relapsed or refractory multiple myel

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

273 10.19 nM), but slightly less to vitronectin (Kd = 16.51 nM).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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