ライフサイエンスコーパス: FKBP

1 FKBP family members are targets for drugs such as rapamy

2 FKBP gene expression coordinately induces the expression

3 FKBP-domain proteins (FKBPs) are pivotal modulators of c

4 t of rapamycin and FK506-binding protein 12 (FKBP), respectively, the optimized FRB-N-terminal lucife

5 ELP nanoparticles, FK506 binding protein 12 (FKBP), which is the cognate protein target of Rapa, was

6 athrin by using an FK506-binding protein 12 (FKBP)-clathrin fusion protein that is specifically oligo

7 membrane-bound, adipocyte-specific caspase 8-FKBP fusion protein.

8 The slyD gene encodes a FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase).

9 e show here that induced dimerization of Abl-FKBP, but not the kinase-defective AblKD-FKBP, inhibits

10 Abl-FKBP, but not the kinase-defective AblKD-FKBP, inhibits cell spreading on fibronectin.

11 Activation of this nuclear AblNuk-FKBP by dimerization with AP20187 in anaplastic thyroid

12 as in its closed state or when applied after FKBP binding had occurred, whereas diamide was always ef

13 A second major conformation of apo AIPL1-FKBP was identified by NMR studies.

14 e solved the crystal structures of the AIPL1-FKBP domain and its pathogenic mutant V71F, both in the

15 We find that although FKBP-ERGIC-53 of the ER-Golgi intermediate compartment (

16 This procedure involves coexpressing an FKBP-tagged Golgi enzyme with an ER-retained protein fus

17 FRAP (FKBP-rapamycin-associated protein), an FKBP-tagged Golgi enzyme can be trapped when it visits t

18 FKBP12-tagged Golgi enzyme for binding to an FKBP-rapamycin binding domain (FRB)-tagged ER trap.

19 rin-coated vesicles (CCVs), together with an FKBP and rapamycin-binding domain-containing construct w

20 hat is recognized by the cyclophilin-CsA and FKBP-FK506 complexes.

21 , cyclophilin A-cyclosporin A (CyPA-CsA) and FKBP-FK506.

22 mily immunophilins that contain both CyP and FKBP domains for which we propose the name FCBP (FK506-

23 e) were also identified in which the CyP and FKBP domains were in the reverse order.

24 D, Tmp-SLF, which dimerizes E. coli DHFR and FKBP and has no endogenous mammalian targets that would

25 rotein-protein interactions between DHFR and FKBP preclude formation of a trimeric complex.

26 A combined model of the RyR fragment and FKBP docked into the cryo-EM map suggests that the fragm

27 mycin in samples overexpressing both FRB and FKBP (FRB.rapamycin+FKBP, Kd approximately 100 fM; FKBP.

28 ion of these domains to the proteins FRB and FKBP enabled their induced assembly by the natural produ

29 eveloped CIT by rationally splitting FRB and FKBP.

30 e different proteins, calmodulin, NmerA, and FKBP, shows that selective labeling with [(13)C]methyl g

31 Evidence for an interaction between RyR and FKBP is well documented, both in skeletal muscle (RyR1-F

32 Rapadocin is a potent, isoform-specific and FKBP-dependent inhibitor of the equilibrative nucleoside

33 owed that controlled homodimerization of APP-FKBP leads to a 50% reduction in total Abeta levels in t

34 P20187 induces rapid dimerization of the APP-FKBP chimera.

35 FKBP(*), but Q53D unfolded twice as fast as FKBP(*).

36 apamycin-binding proteins are abbreviated as FKBPs.

37 development of novel drugs against bacterial FKBPs will be discussed.

38 hat the chromatin binding ability of 'basic' FKBPs is shared amongst related orthologues present in f

39 n, which induces a tight association between FKBP (FK506-binding protein) and FRAP (FKBP-rapamycin-as

40 apamycin induces a tight association between FKBP and FRAP, one would expect rapamycin to trap the FK

41 The rapamycin-controlled interaction between FKBP and FRB proteins could be detected in vitro and in

42 No interaction between FKBP and FRB was detected in the absence of rapamycin.

43 horough analysis of the interactions between FKBP, rapamycin, and the rapamycin-binding domain of mTO

44 506-binding protein-FKBP-rapamycin-binding- (FKBP-FRB)-rapamycin system have been widely used to prob

45 Both FKBPs and CYPs can be classified into single domain and

46 prevented the formation of BiFC complexes by FKBP and FRB fusions, but did not disrupt existing BiFC

47 asive and antimetastatic effects produced by FKBP gene expression.

48 This canonical FKBP domain actively increases the rate of isomerization

49 both a 50-residue insertion in the catalytic FKBP domain, also called 'Insert-in-Flap' or IF domain,

50 lathrin function with a clathrin light chain-FKBP chimera oligomerizable by the drug AP20187.

51 (NLuc)/C-terminal luciferase fragment (CLuc)-FKBP luciferase complementation imaging (LCI) pair recon

52 plants of cells expressing the FRB-NLuc/CLuc-FKBP LCI pair, dose- and time-dependent luciferase activ

53 s validated on two protein-ligand complexes: FKBP complexed to 2-(3'-pyridyl)-benzimidazole and MurA

54 ost, such as Escherichia coli In conclusion, FKBP domains from thermostable SlyD proteins are highly

55 s composed of three domains: two consecutive FKBP domains and a three-unit repeat of the TPR (tetratr

56 ur helices within FRB, we have created cpFRB-FKBP pairs that respond to ligand with varying activatio

57 This is because ER-Golgi-cycling FKBP proteins contain a C-terminal KDEL-like sequence, b

58 nants using FRET, we created five single-Cys FKBP variants labeled with Alexa Fluor 488 (denoted D-FK

59 ants labeled with Alexa Fluor 488 (denoted D-FKBP) and then targeted these D-FKBPs to full-length RyR

60 stance analysis of FRET measured from each D-FKBP variant to Cy3NTA bound to each His tag.

61 Results indicate that D-FKBP binds proximal to both N-terminal and central domai

62 8 (denoted D-FKBP) and then targeted these D-FKBPs to full-length RyR1 constructs containing decahist

63 gulatable protein destabilization domain (dd-FKBP).

64 supporting a novel hypothesis that declining FKBP function plays a major role in unhealthy brain agin

65 monstrated that oxidizing reagents decreased FKBP binding.

66 BPs covering ten of the twenty-two different FKBP domains.

67 ) fusion protein was stimulated by a dimeric FKBP ligand.

68 localized AtCYP57, and one nucleus directed FKBP known as AtFKBP65.

69 osase with ERT2 and two degradation domains (FKBP-DD, DHFR-DD), in multiple orientations, and determi

70 a critical role for Hsp90 binding by either FKBP.

71 Of the many eukaryotic FKBPs that have been identified, FKBP65 is an endoplasmi

72 The complexes of CsA-CyP and of FK506-FKBP both bind to and inhibit the activity of the calciu

73 Assessment of fluorescent FKBP binding in myocyte revealed a high FKBP12.6-RyR2 af

74 Each of the five fluorescent FKBPs retained the ability to inhibit [(3)H]ryanodine bi

75 FRB.rapamycin+FKBP, Kd approximately 100 fM; FKBP.rapamycin+FRB, Kd = 12 nM).

76 we show that the best potential binders for FKBP proteins optimally expose the two contiguous carbon

77 onyl oxygen in the proline-mimetic chain for FKBP docking and are characterized by the abundance of r

78 bic cluster within SPRY1 that is crucial for FKBP binding.

79 As one of four FKBPs within the yeast Saccharomyces cerevisiae, Fpr4 ha

80 istone prolyl isomerase activities, the Fpr4 FKBP domain binds to nucleosomes and nucleosome arrays i

81 The interaction of the Fpr4 FKBP with recombinant chromatin complexes condenses nucl

82 tween FKBP (FK506-binding protein) and FRAP (FKBP-rapamycin-associated protein), an FKBP-tagged Golgi

83 on of FKBP (FK-506 binding protein) and FRB (FKBP-rapamycin binding protein) upon UV irradiation.

84 eta produces GSK-3beta fused to a tag, FRB* (FKBP/rapamycin binding), resulting in a rapidly destabil

85 tein-protein interactions can be imaged (FRB-FKBP, Fos-Jun, and neuroligin-PSD-95), with as little as

86 Using a model receptor-ligand pair (FRB-FKBP), we first test physical and computational predicti

87 phosphatase module through the rapamycin/FRB/FKBP system or by treatment with ionomycin.

88 a inhibitor GRK2ct (GRK2ct-KERE) and the FRB/FKBP heterodimerization system.

89 e FKBP12-rapamycin-binding (FRB) domain from FKBP-12-rapamycin associated protein 1 (FRAP1, also know

90 activity, indicating that it is a functional FKBP.

91 We made a calpain-GFP-FKBP fusion through single cross-over integration at the

92 lial cells stably expressing a chimeric HER2-FKBP molecule that could be conditionally induced to hom

93 duced growth of MCF10A cells expressing HER2-FKBP.

94 21 (43%) genes overexpressed by HGA were HIF/FKBP-associated genes.

95 sequence and structural comparison of human FKBP domains.

96 ficacy is decreased in the presence of human FKBP due to the high concentration of FKBP and its tight

97 ta are available for eight of fourteen human FKBPs covering ten of the twenty-two different FKBP doma

98 mycin that also express invariant chain (Ii)-FKBP in the ER.

99 ST-FRB is trapped in the ER even without Ii-FKBP upon rapamycin addition.

100 when added to cells expressing an alpha(IIb)(FKBP)(2) chimera complexed with beta(3).

101 mutation, N760D, appears to directly impact FKBP binding through interfering with SPRY1 folding.

102 in the urea-unfolded state that were not in FKBP(*), indicating that the mutations had a more substa

103 hibits mTOR function by interacting with its FKBP-rapamycin-binding (FRB) domain.

104 Clustering of GP Ib-IX(FKBP)(2) also stimulated rapid tyrosine phosphorylation

105 tail to tandem repeats of FKBP, and GP Ib-IX(FKBP)(2) and alpha(IIb)beta(3) were expressed in Chinese

106 Moreover, clustering of GP Ib-IX(FKBP)(2) by AP20187 led to an increase in alpha(IIb)beta

107 Conditional oligomerization of GP Ib-IX(FKBP)(2) by AP20187, a cell-permeable FKBP dimerizer, ca

108 ll shear rates of up to 2000 s(-1), GP Ib-IX(FKBP)(2) mediated cell tethering to immobilized VWF, jus

109 FKBP51 (the 51-kDa FKBP) associates with heat shock protein 90 (Hsp90) and

110 eptor-labeled CaM binding near donor-labeled FKBP (FK506-binding protein 12.6) on the cytoplasmic dom

111 split pairs of FRB or FKBP with full-length FKBP or FRB, respectively, by rapamycin.

112 ponses via isomerase-independent mechanisms, FKBPs are most highly expressed in the nervous system, w

113 GIC) rapidly cycles through the ER (30 min), FKBP-Golgi enzyme chimeras remain stably associated with

114 horylation within 1 min, whereas a monomeric FKBP ligand had no effect.

115 natural products, which tightly bind to most FKBP family members, including FKBP51 and FKBP52.

116 This structure of a multi-FKBP domain protein clarifies the arrangement of these d

117 ne the pharmacological relevance of multiple FKBP members in the immunosuppressant-induced T-cell ina

118 cking the macrolide structure of the natural FKBP binders FK506 and Rapamycin.

119 RyR2 channel complex, did not restore normal FKBP binding under oxidizing conditions.

120 and by extension to mTOR, in the absence of FKBP is of little consequence under physiological condit

121 these findings, we propose that addition of FKBP-binding groups might partially overcome the poor ph

122 To investigate the structural basis of FKBP interactions with the RyR1 and RyR2 isoforms, we us

123 human FKBP due to the high concentration of FKBP and its tight affinity for MTXSLF.

124 cin derivative induced rapid dimerization of FKBP (FK-506 binding protein) and FRB (FKBP-rapamycin bi

125 d in other systems where the dimerization of FKBP has been used to initiate signaling pathways, offer

126 cation of chemically induced dimerization of FKBP to create nearly instantaneous high-affinity bivale

127 d by the synthetic oligomerization domain of FKBP, which confers conditional transformation propertie

128 their delivery was impaired by expression of FKBP-clathrin chimeras and AP20187 incubation.

129 ng as a gatekeeper residue in the folding of FKBP(*).

130 The AP20187-induced dimeric form of FKBP-Cdc34 was substantially more active than the monome

131 The fusion of FKBP to these nanoparticles slowed the terminal half-lif

132 e showed that Shld1, the chemical inducer of FKBP-DD, does not interfere with stem cell differentiati

133 Treatment with the FK506 inhibitor of FKBP-FRB interaction prevented the formation of BiFC com

134 These findings show the involvement of FKBP proteins at different stages of PrP(C) biogenesis a

135 of mechanistic interest within FRET range of FKBP.

136 at its cytoplasmic tail to tandem repeats of FKBP, and GP Ib-IX(FKBP)(2) and alpha(IIb)beta(3) were e

137 Thus, a subclass of FKBP prolyl isomerase enzymes is recruited to linker reg

138 tes of Q53N and Q53T were similar to that of FKBP(*), but Q53D unfolded twice as fast as FKBP(*).

139 etic folding intermediate similar to that of FKBP(*).

140 s in Arabidopsis is that a large fraction of FKBPs and CYPs are localized in the chloroplast, a possi

141 FKBP12 is the only FKBP family member that plays a key role in immunosuppre

142 crocycles (named rapafucins) using optimized FKBP-binding domains.

143 6- and rapamycin-binding protein (FKBP12, or FKBP) and the FKBP-rapamycin binding (FRB) domain of the

144 ntly in samples overexpressing either FRB or FKBP alone (rapamycin+FKBP, Kd approximately 0.2 nM; rap

145 cient trimerization of split pairs of FRB or FKBP with full-length FKBP or FRB, respectively, by rapa

146 n of DNA sequences encoding FRB+rapamycin or FKBP+rapamycin in samples overexpressing both FRB and FK

147 Unlike any other FKBP characterized so far, FKBP65 is developmentally reg

148 PIase domains differs from that of the other FKBP family members.

149 Other FKBPs, especially the larger ones, participate in import

150 ugh FKBP51 shares characteristics with other FKBPs, it also has unique features, especially the role

151 ase in both adherence and spreading of PECAM/FKBP-2-transfected cells on immobilized fibronectin, a r

152 Ib-IX(FKBP)(2) by AP20187, a cell-permeable FKBP dimerizer, caused a decrease in cell translocation

153 ncentration of the weaker binding Plasmodium FKBP has no effect on the inhibitory potency of MTXSLF i

154 the complex of FK506 and its binding protein FKBP also binds.

155 ovalently linked to a ligand for the protein FKBP to create a bifunctional molecule called MTXSLF.

156 h-level expression of FK506-binding protein (FKBP) 12 by HGA.

157 ytes deficient in the FK506-binding protein (FKBP) 12, a target of rapamycin activity, had reduced pr

158 Cas9) in complex with FK506-binding protein (FKBP) and a CEM consisting of FK506 linked to a molecule

159 fusion protein of the FK506 binding protein (FKBP) and caspase 8 under control of the albumin promote

160 osed of the canonical FK506-binding protein (FKBP) and circular permutants of FKBP12-rapamycin bindin

161 teraction between the FK506 binding protein (FKBP) and the FKBP-rapamycin binding domain (FRB).

162 y relies on a mutated FK506-binding protein (FKBP) destabilizing domain (dd) fused to the protein of

163 containing one or two FK506-binding protein (FKBP) domains at their COOH terminus.

164 s gammatolerans SlyD FK-506-binding protein (FKBP) domains suitable for presentation of the predefine

165 The FK506-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is

166 The FK506 binding protein (FKBP) family of proteins provide an interesting series o

167 BP38, a member of the FK506-binding protein (FKBP) family that is structurally related to FKBP12.

168 Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylpr

169 constructed an AblNuk-FK506-binding protein (FKBP) fusion protein to enforce the nuclear accumulation

170 ion of a TRH receptor-FK506-binding protein (FKBP) fusion protein was stimulated by a dimeric FKBP li

171 cule used to dimerize FK506-binding protein (FKBP) fusion proteins and initiate biological signaling

172 incorporated into an FK506 binding protein (FKBP) fusion to allow for its specific activation using

173 erized member of the FK-506-binding protein (FKBP) gene family down-regulated in aggressive tumors.

174 The FK506-binding protein (FKBP) is an important regulator of channel activity, and

175 teine variants of the FK506-binding protein (FKBP) labeled with a donor probe, and DPc10 labeled with

176 l-permeable, bivalent FK506-binding protein (FKBP) ligand stimulated clustering when added to cells e

177 e dimerization domain FK506-binding protein (FKBP) or to the hexameric protein CcmK4 from cyanobacter

178 20-2, belongs to the FK-506 binding protein (FKBP) subfamily that functions as peptidyl-prolyl isomer

179 binary complexes with FK506-binding protein (FKBP) through a shared FKBP-binding domain before formin

180 se 9 fused to a human FK506 binding protein (FKBP) to allow conditional dimerization using a small mo

181 using a domain of the FK506-binding protein (FKBP) to the C terminus of APP.

182 thermore, fusion of a FK506-binding protein (FKBP) to the N terminus of human Cdc34 yielded FKBP-Cdc3

183 d by interaction with FK506-binding protein (FKBP), and disruption of the RyR-FKBP association has be

184 es with a fluorescent FK506-binding protein (FKBP), and FRET was determined following incubations in

185 Expression of FK506 binding protein (FKBP)-clathrin light chain chimeras, to inhibit clathrin

186 tures two independent FK506-binding protein (FKBP)-like and tetratricopeptide repeat domains.

187 evealed that both the FK506 binding protein (FKBP)-like domain and the tetratricopeptide repeat (TPR)

188 ytoplasmic chaperone, FK506-binding protein (FKBP).

189 n, and 2 copies of an FK506-binding protein (FKBP).

190 in is located next to FK506-binding protein (FKBP).

191 nts involving RyR and FK506-binding protein (FKBP).

192 CID tools such as the FK506-binding protein-FKBP-rapamycin-binding- (FKBP-FRB)-rapamycin system have

193 Using green fluorescent protein-FKBP-MCAK CRISPR cells we found that one deleterious hot

194 associated with the FK506 binding proteins (FKBP) -52 and -51 response to cortisol exposure in neuro

195 The FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signa

196 FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signa

197 FK506-binding proteins (FKBP) are immunophilins that interact with the immunosup

198 FK506-binding proteins (FKBPs) are cellular receptors for immunosuppressants tha

199 FK506-binding proteins (FKBPs) are peptidyl-prolyl cis/trans isomerases PPIases)

200 similarity to human FK506-binding proteins (FKBPs) in residues 166 to 252 located in the globular do

201 FK506-binding proteins (FKBPs) represent one of the three families of enzymes sh

202 amily, cyclophilins, FK506 binding proteins (FKBPs), and parvulins in bacteria.

203 nophilins, including FK506-binding proteins (FKBPs), are protein chaperones with peptidyl-prolyl isom

204 amily comprising the FK506-binding proteins (FKBPs), cyclophilins, and parvulins.

205 ly of immunophilins, FK506 binding proteins (FKBPs).

206 ressive ligands for FK-506 binding proteins (FKBPs).

207 ilins (CyPs) and the FK506-binding proteins (FKBPs).

208 include calstabins [FK506-binding proteins (FKBPs)], calmodulin (CaM), phosphodiesterase, kinases, p

209 FKBP-domain proteins (FKBPs) are pivotal modulators of cellular signaling, pro

210 nd simultaneously to two different proteins, FKBP and mTOR.

211 ns in the first LP dipeptide in the putative FKBP binding domain eliminated FKBP12 and FKBP52 interac

212 bond from Tyr(113) that mimics the putative FKBP transition state.

213 e immunophilins, among which 23 are putative FKBPs and 29 are putative CYPs.

214 pressing either FRB or FKBP alone (rapamycin+FKBP, Kd approximately 0.2 nM; rapamcyin+FRB, Kd = 26 mu

215 rexpressing both FRB and FKBP (FRB.rapamycin+FKBP, Kd approximately 100 fM; FKBP.rapamycin+FRB, Kd =

216 orylation, and is inhibited by the Rapamycin/FKBP-12 complex.

217 colocalizes with endogenous and recombinant FKBP chimeric clathrin polypeptides in PC12-cell endosom

218 ite biology, we adapted a ligand-regulatable FKBP protein destabilization domain (ddFKBP) for use in

219 ere stably transfected with siRNA-resistant, FKBP-tagged subunits of the adaptor protein (AP) complex

220 ng protein (FKBP), and disruption of the RyR-FKBP association has been implicated in cardiomyopathy,

221 esent study, we investigated whether the RyR-FKBP association is redox-regulated.

222 Several FKBP family members such as FKBP12, FKBP12.6, and FKBP51

223 K506-binding protein (FKBP) through a shared FKBP-binding domain before forming ternary complexes wit

224 cted parasites could be modulated by a small FKBP ligand, Shield1 (Shld1).

225 Some FKBPs, notably FKBP12 (the 12-kDa FK506-binding protein)

226 ursor of beta-secretase cleavage, C99/SPA4CT-FKBP.

227 that the protein heterodimerization switches FKBP-rapalog-FRB can be harnessed in engineered COS-7 ce

228 for its specific activation using synthetic FKBP ligands.

229 eoplasmin-like (NPL) domain and a C-terminal FKBP peptidyl-proline isomerase domain.

230 , a protozoan parasite, contained N-terminal FKBP and C-terminal CyP domains joined by tetratricopept

231 Although the N-terminal FKBP-like domain of AIPL1 binds the farnesylated PDE6alp

232 e additional residues at the amino terminus (FKBP(*)).

233 D and Q53T mutants also refolded faster than FKBP(*) but lacked the folding intermediate, indicating

234 folding trajectory and transition state than FKBP(*) and Q53N.

235 The FKBP and FRB domains, which are dimerized by rapamycin a

236 onally induced to homodimerize by adding the FKBP ligand AP1510, or instead induced to heterodimerize

237 eening a small dipeptide library against the FKBP-FRB protein complex involved in cell cycle arrest.

238 strained by both the RyR cryo-EM map and the FKBP atomic structure docked to the RyR.

239 in-binding protein (FKBP12, or FKBP) and the FKBP-rapamycin binding (FRB) domain of the mammalian tar

240 een the FK506 binding protein (FKBP) and the FKBP-rapamycin binding domain (FRB).

241 at the HD2-type histone deacetylases and the FKBP-type PPIases may have evolved from a common ancesto

242 We believe the FKBP-based PB transposon induction will be useful for tr

243 inities of two protein-ligand complexes: the FKBP protein bound with small molecules 4-hydroxy-2-buta

244 We have generated docking poses for the FKBP-GPI complex using eight docking programs, and compa

245 ins, and the FK506-binding proteins form the FKBP subfamily of immunophilins.

246 eptidyl-prolyl-isomerase (PPI) function, the FKBP protein family is at the crossroad of several impor

247 X compound and the minimal pharmacore in the FKBP family, shedding new light on the isomerization mec

248 m that missense and nonsense variants in the FKBP-like and tetratricopeptide repeat domains of AIPL1

249 lter phoshorylation of receptors lacking the FKBP domain.

250 domain elements are closely apposed near the FKBP binding site within the RyR1 three-dimensional stru

251 ther Mn or a self-interacting version of the FKBP domain.

252 Recently FK506, an inhibitor of the FKBP family of peptidyl prolyl isomerases, was shown to

253 of the FKBP65 gene and other members of the FKBP multigene family were therefore investigated from a

254 ike 1 (AIPL1) is a distinctive member of the FKBP superfamily in terms of its biochemical properties,

255 e (RyR2-FKBP12.6), however definition of the FKBP-binding site remains elusive.

256 affinities involved in the formation of the FKBP.rapamycin.FRB complex, we used fluorescence polariz

257 cesses that do not necessarily depend on the FKBP domain.

258 (SAR) of small molecules that mimic only the FKBP binding domain portion of FK506 has focused on este

259 l and pipecolyl esters, which mimic only the FKBP binding domain portion of FK506, are proposed and a

260 ogical inhibitors of the PI 3'-kinase or the FKBP 12-rapamycin-associated protein/mammalian target of

261 rotein (FKBP12, also known as FKBP1A) or the FKBP-rapamycin binding (FRB) domain of the mammalian tar

262 al domains of RyR1, thus suggesting that the FKBP binding site is composed of determinants from both

263 These analyses suggest that the FKBP multigene family emerged early in the evolutionary

264 We found that the FKBP-DD confers the PB transposase with a higher transpo

265 In addition, we found that the FKBP-DD regulates transposon activity in a reversible an

266 Binding of FK506 to the FKBP domain causes the target domain to first unfold, th

267 e binding of isoprenyl groups on PDE6 to the FKBP domain of AIPL1.

268 nd have a C-terminal domain belonging to the FKBP fold.

269 t the fragment is positioned adjacent to the FKBP-binding site.

270 binding of the farnesylated-Cys probe to the FKBP-like domain of AIPL1, thus uncovering a novel funct

271 FRAP, one would expect rapamycin to trap the FKBP-fused Golgi protein in the ER if it ever visits the

272 nsight into its biological role, we used the FKBP degradation domain system to generate a fusion prot

273 nrelated Golgi-targeted constructs using the FKBP strategy.

274 so create inducible CASFx (iCASFx) using the FKBP-FRB chemical-inducible dimerization domain, allowin

275 g dimerizes any two proteins tagged with the FKBP and DHFR domains until exposure to light causes its

276 ipid binding that is unparalleled within the FKBP superfamily.

277 e structural and functional diversity of the FKBPs.

278 It has been speculated that these FKBPs are possibly redundant in the immunosuppressant-in

279 lit-tyrosine phosphatases (PTPs) attached to FKBP and FRB, where catalytic activity can be modulated

280 ere prepared and investigated for binding to FKBP and GFP accumulation in transgenic plants.

281 hus ST-FRB cycles artificially by binding to FKBP domain-containing proteins.

282 ular component of whole blood via binding to FKBP.

283 s split into two moieties that were fused to FKBP (FK506-binding protein) and FRB (rapamycin-binding

284 ments of yellow fluorescent protein fused to FKBP and FRB produced detectable BiFC complex fluorescen

285 nt of the Venus fluorescent protein fused to FKBP produced constitutive BiFC complexes with several C

286 s the Q53N mutant was stabilized relative to FKBP(*) with little change in the equilibrium m values.

287 The two FKBP domains differ by an insertion in the second that a

288 shows decreased CaM affinity, but unaltered FKBP 12.6 affinity.

289 vestigate the molecular basis of this unique FKBP-dependence, spontaneous plaque-forming mutants of p

290 Unlike FKBP-FK506, CyPA-CsA interacts with Arg-122 at the activ

291 he affinities of the inducers for unmodified FKBP and FRB.

292 c myocyte environment can be monitored using FKBP biosensors and FRET.

293 These receptor heterocomplexes contain wheat FKBPs, and they bind rabbit cytoplasmic dynein in a PPIa

294 CPS was still triggered by rapamycin when FKBP and FRB occupied one or both of the extein position

295 To test whether FKBP interaction determined localization, we overexpress

296 The comparison of CyPA-CsA-CN with FKBP-FK506-CN significantly contributes to understanding

297 tate of the RyR is intimately connected with FKBP binding affinity.

298 Its predicted binding interface with FKBP consists primarily of electrostatic contacts and co

299 The interaction with FKBPs was found to be surprisingly tolerant to the stere

300 BP) to the N terminus of human Cdc34 yielded FKBP-Cdc34 that was induced to form a dimer upon treatme