ライフサイエンスコーパス: IDP

1 IDP consistently demonstrated the spatiotemporal co-exis

2 IDPs and IDRs constitute a class of proteins and protein

3 IDPs can acquire tertiary structure when bound to their

4 IDPs do not adopt a single dominant structure in isolati

5 IDPs often fold into ordered states upon binding to thei

6 IDPs play important roles in a range of biological funct

7 h was tested using the experimental Rh of 22 IDPs covering a wide range of peptide lengths, net charg

8 , and June 30, 2018, ACF was conducted in 26 IDP camps and 963 host communities in 12 local governmen

9 We created A-IDP puncta using these simple principles, which are capa

10 manipulated by the molecular weight of the A-IDP.

11 native IDPs and designed artificial IDPs (A-IDPs) with different molecular weights and aromatic cont

12 by a confined chiral imidodiphosphoric acid (IDP).

13 ture and crowding agents consequently affect IDPs more than their folded counterparts.

14 ent supports some health interventions among IDPs, locally sourced solutions are lacking.

15 xes (RNCs) of alpha-synuclein (alphaSyn), an IDP associated with Parkinson's disease (PD).

16 n insight into how a small molecule binds an IDP and emphasize the need to examine motions on the low

17 hows high flexibility, characteristic for an IDP, but also a high dynamic range and increasing rigidi

18 Prostate-Associated Gene 4 (PAGE4) is an IDP that acts as a potentiator of the Activator Protein-

19 The phase behavior of an IDP is sensitive to its amino acid sequence.

20 ail the folding-upon-binding mechanism of an IDP segment to its binding partner, as observed in unbia

21 ring the biophysical binding mechanism of an IDP to a structured protein, whereby a local segment of

22 such modifications affect the binding of an IDP to its partner protein?

23 eful NMR experiments to get a snapshot of an IDP/IDR in conditions approaching physiological ones.

24 lity to collect simultaneous snapshots of an IDP/IDR through different two-dimensional spectra provid

25 inantly in-register complex when bound to an IDP domain of the multivalent regulatory protein ASCIZ.

26 Here, we show a mechanism by which an IDP can allosterically control function by simultaneousl

27 ation between government, civil society, and IDP community partners, which also included mapping of I

28 w) membraneless biomolecular condensates and IDPs/IDRs are functionally involved in key cellular proc

29 implicate specific types of condensates and IDPs/IDRs in important cellular level processes and mole

30 ficult to address under such conditions, and IDPs are vulnerable to both.

31 hobic interactions for other SH3 domains and IDPs in general.

32 for the dimensions of unfolded proteins and IDPs in the absence of chemical denaturants.

33 ered ACTR accelerated its binding to another IDP, NCBD of the CREB-binding protein.

34 ed an innovative hybrid sequencing approach, IDP-fusion, to detect fusion genes, determine fusion sit

35 interpret the phase behaviour of archetypal IDP sequences and demonstrate the rational design of a v

36 ribe the dynamic behavior of this archetypal IDP.

37 space of native IDPs and designed artificial IDPs (A-IDPs) with different molecular weights and aroma

38 expands the functional utility of artificial IDPs as well as the available microarchitectures of this

39 (IDI) catalyzes the interconversion between IDP and DMADP.

40 ing its role in optimizing the ratio between IDP and DMADP as precursors for different downstream iso

41 anules composed of a recombinant RNA-binding IDP that exhibits phase behavior in water.

42 conformational landscape of membrane-binding IDPs with multiple binding modes.

43 architectures of this class of biocompatible IDPs, with potential applications in drug delivery and t

44 nge of physicochemical properties encoded by IDP sequences.

45 many of which are organized or regulated by IDPs/IDRs, can enable spatial and temporal regulation of

46 However, in some cases, IDPs such as the ones involved in neurodegenerative dise

47 e crucial for the function of highly charged IDPs presents significant experimental challenges.

48 s particularly helpful for repeat-containing IDPs and low-complexity regions.

49 assignment of challenging, repeat-containing IDPs.

50 We define IDPs as proteins that are disordered along their entire

51 inhibition of translation by using designer IDPs that exhibit tunable phase behavior.

52 discrimination among qualitatively different IDP ensembles for the amyloid-beta peptide.

53 operties can vary strongly between different IDPs.

54 o gas-phase transfer of a range of different IDPs.

55 5C building blocks isopentenyl diphosphate (IDP) and its isomer dimethylallyl diphosphate (DMADP).

56 in that promotes duplex formation of diverse IDP partners.

57 teins with intrinsically disordered domains (IDPs) in the DNA damage response (DDR).

58 Engaging IDP communities, local governments, and civil society or

59 The enzyme IDP isomerase (IDI) catalyzes the interconversion betwee

60 ure to a variety of IDPs and found that even IDPs with low net charge and high hydrophobicity remain

61 addition of Alexa-488 to a normally expanded IDP causes contraction by an additional 15%, a value in

62 l and dynamic information on highly flexible IDPs/IDRs.

63 This results in improved efficiency for IDP analysis and binding studies.

64 importance of conformational flexibility for IDP recognition, it was recently demonstrated that stabi

65 he protein sequence features responsible for IDP phase separation is critical for understanding physi

66 We present design rules for IDPs possessing SLCs that phase separate into diverse as

67 th the most common structural techniques for IDPs: Nuclear Magnetic Resonance (NMR) spectroscopy, Sma

68 inferences based on RG and RE , whereas for IDPs under native conditions, we find substantial deviat

69 Amyloid-forming IDPs, unlike natively folded proteins, have folding traj

70 ch for the unbiased study of amyloid-forming IDPs.

71 NPs and applied to experimental data of four IDP systems with distinctive binding behavior, successfu

72 FRAGFOLD-IDP enables better insight into backbone dynamics in IDP

73 FRAGFOLD-IDP produces very good predictions for 33.5% of cases an

74 e, we present a new de novo method, FRAGFOLD-IDP, which addresses this problem.

75 bles derived from NMR, we show that FRAGFOLD-IDP achieves superior results compared to methods which

76 n in generating and drawing conclusions from IDP conformational ensembles.

77 Furthermore, IDPs/IDPRs are everywhere, and are ubiquitously engaged

78 nalytical description of such types of fuzzy IDP-SNP complexes and may help advance understanding nan

79 e primary error for ranking or creating good IDP ensembles resides in the poor back-calculation from

80 Based on a predictive coarse-grained IDP model, we identified a region of the RGG domain that

81 scale relationships that encode hierarchical IDP assemblies, (2) design rules of such assemblies in c

82 Thus, it is not clear how IDPs, lacking such well-defined structures, can alloster

83 However, IDPs also follow some of the classic paradigms establish

84 s have indicated that relatively hydrophobic IDPs contract significantly in the absence of denaturant

85 demonstrate that even relatively hydrophobic IDPs remain nearly as expanded in water as they are in h

86 ) intervention for TB and testing for HIV in IDP communities and provided linkages to treatment in 3

87 key functional features to be identified in IDP structural ensembles.

88 In this study, we observed a burden of TB in IDP populations of Northeast Nigeria many times higher t

89 les better insight into backbone dynamics in IDPs and opens exciting possibilities for the design of

90 ed, but many disease-associated mutations in IDPs are charge-neutral.

91 of experimental measurement of relaxation in IDPs, the physical origin of the measured relaxation rat

92 odel for the disorder-to-order transition in IDPs termed "templated folding," whereby the binding par

93 f in-register binding in the multivalent LC8-IDP complex assembly and the degree of compositional and

94 important step toward precisely manipulating IDP functions.

95 sed approach is generally applicable to many IDPs/IDRs whose assignment is available in the Biologica

96 ly modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.

97 ere we present a novel computational method, IDP-LZerD, which models the conformation of a disordered

98 as apoenzyme and in complexes with GTP*Mg2+, IDP*PO4, and dGDP*PO4-that highlight conformational swit

99 t tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanis

100 Moreover, IDP-ribose (IDPR) induced currents both in hTRPM2 and Nv

101 The protein NUPR1 is a multifunctional IDP involved in chromatin remodeling and in the developm

102 tically scanned the sequence space of native IDPs and designed artificial IDPs (A-IDPs) with differen

103 Despite the numerous new IDPs that have been identified, progress towards rationa

104 is becoming apparent that among the numerous IDPs that interact with LC8, many contain multiple LC8-b

105 dly webserver that enables rapid analysis of IDP sequences.

106 to methodology development, applications of IDP-ASE to human embryonic stem cells and breast cancer

107 s for deciphering the sequence dependence of IDP phase separation are discussed.

108 An accurate description of IDP conformational ensembles depends crucially on the am

109 However, the details of IDP binding pathways are hard to characterize using expe

110 overall binding affinities, fine details of IDP-SNP affinity profiles, and site-directed mutagenesis

111 nd our knowledge of sequence determinants of IDP phase separation, we characterized variants of the i

112 may modulate thermodynamics and kinetics of IDP interactions.

113 ity partners, which also included mapping of IDP populations and health services, supporting existing

114 ly valuable in elucidating these pathways of IDP folding.

115 n oxide particle demonstrates the ability of IDPs to respond to signals from their surroundings by co

116 R experiments: high solvent accessibility of IDPs promotes water exchange, which disfavors classical

117 aracterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable reso

118 ormation regulates the functional aspects of IDPs remains an open question, however.

119 es new insight into the physical behavior of IDPs, extending our ability to quantitatively investigat

120 tes a deeper fundamental characterization of IDPs and IDRs for discovering new functions and relevant

121 e relevance of our results to condensates of IDPs is discussed.

122 eveal that the residual structure content of IDPs is modulated both by ionic strength and by the type

123 indicate that the hydrodynamic dimensions of IDPs are evidence of considerable sequence-dependent bac

124 ual structure and conformational dynamics of IDPs are crucial for the mechanisms underlying their fun

125 The conformational ensembles of IDPs are encoded by their amino acid sequences.

126 erization of the conformational ensembles of IDPs is of great interest, since their conformational en

127 olds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or reg

128 ins (HRGPs), have characteristic features of IDPs.

129 mational dynamics in free and bound forms of IDPs under conditions approaching physiological, althoug

130 the better understanding of the function of IDPs when encountering inorganic nanomaterials with the

131 nderstanding of the behavior and function of IDPs, adding a new and essential dimension to the descri

132 , which aids discovery of novel functions of IDPs and IDRs.

133 We describe the diverse interactions of IDPs that can have unusual characteristics such as "ultr

134 cromolecular crowding on the interactions of IDPs with their cellular targets.

135 s and solvent quality (self-interactions) of IDPs from a single small-angle x-ray scattering measurem

136 sight into the complex binding mechanisms of IDPs and their regulatory mechanisms.

137 r understanding the functional mechanisms of IDPs.

138 In this study, we propose a simple model of IDPs as associative polymers in poor solvent and explore

139 ption that accurately portrays the motion of IDPs as a function of the intrinsic properties of the cr

140 tion interactions if the polymeric nature of IDPs and crowders is incorporated based on recent theore

141 are consistent with previous observation of IDPs under the influence of synthetic polymers.

142 the coupled folding and binding processes of IDPs.

143 ions for describing the binding reactions of IDPs.

144 can be modified to optimize the recovery of IDPs from other organisms.

145 sses that are dependent on PTM regulation of IDPs.

146 physiological implications given the role of IDPs in signaling, the asymmetric ion profiles of differ

147 eview the prevalence and functional roles of IDPs and IDRs associated with the release and recycling

148 resolution, which were obtained for a set of IDPs by solution NMR relaxation experiments, are explain

149 his sensitivity to the marginal stability of IDPs, which could have physiological implications given

150 tially ordered regions in the bound state of IDPs.

151 o solve the ensemble secondary structures of IDPs in solution, which is important to advance the unde

152 The dynamical and fluctuating structures of IDPs or of disordered regions within proteins result in

153 ts was subsequently developed for studies of IDPs/IDRs and applied to the dilute phase of a 103-resid

154 The study of IDPs is a rapidly growing area as the crucial biological

155 ning the diverse conformational substates of IDPs in their free states, in encounter complexes of bou

156 anding nanotoxicity and in vivo targeting of IDPs by specifically designed nanomaterials.

157 ion of the solution to gas-phase transfer of IDPs and provide a roadmap for future investigations int

158 Tuning of IDPs and IDPRs are mediated through post-translational m

159 We applied this procedure to a variety of IDPs and found that even IDPs with low net charge and hi

160 well as post-translational modifications on IDP structure and interaction.

161 SHACA-HSQC spectra acquired on IDPs provide uncompromised resolution and sensitivity (u

162 en extensively studied, experimental data on IDPs at the air/water (A/W) and water/lipid interfaces a

163 ific structural and dynamical information on IDPs/IDRs, and recent efforts have focused on the develo

164 alesce mechanism, whereby the docking of one IDP segment initiates the process, followed by on-target

165 classes of experiment for studies of IDRs or IDPs in both dilute and phase-separated environments, in

166 y important in explaining signaling in other IDPs.

167 As with many other IDPs, KID undergoes coupled folding and binding to form

168 gh it is established that LC8 forms parallel IDP duplexes with some partners, such as nucleoporin Nup

169 In particular, IDPs that become structured upon binding typically follo

170 semble of intrinsically disordered peptides (IDPs) facilitated by experimental measurements using cir

171 Over 2 million internally displaced persons (IDPs) suffering from lack of basic hygienic conditions,

172 In plants, IDP is synthesized in the cytoplasm from mevalonic acid

173 In plants, IDPs are implicated in plant stress responses, signaling

174 sing the integrative disease predictability (IDP) criterion: if TC-BC association is part of the dise

175 The ability to predict and program IDP-rich assemblies in this fashion offers new insights

176 Intrinsically disordered protein (IDP) conformers occupy large regions of conformational s

177 Intrinsically disordered protein (IDP) duplexes composed of two IDP chains cross-linked by

178 ip1) is an intrinsically disordered protein (IDP) that inhibits cyclin-dependent kinase (Cdk)/cyclin

179 The intrinsically disordered protein (IDP), alpha-synuclein (alphaS), is well-known for phosph

180 ein and an intrinsically disordered protein (IDP), are prevalent in the cell, including important sig

181 tes and an intrinsically disordered protein (IDP), regulates cell division by causing cell cycle arre

182 ily, is an intrinsically disordered protein (IDP).

183 Intrinsically disordaered proteins (IDPs) are a prevalent phenomenon with over 30% of human

184 cognized as intrinsically disorder proteins (IDPs) or partially disordered segments known as intrinsi

185 Intrinsically disordered proteins (IDPs) abound in cellular regulation.

186 These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and intrins

187 acts with intrinsically disordered proteins (IDPs) and influences a wide range of biological processe

188 Intrinsically disordered proteins (IDPs) and intrinsically disordered regions within protei

189 Intrinsically disordered proteins (IDPs) and membrane-less organelles are key examples of t

190 hown that intrinsically disordered proteins (IDPs) and nucleic acids like RNA and other polynucleotid

191 n involve intrinsically disordered proteins (IDPs) and protein binding domains.

192 Many intrinsically disordered proteins (IDPs) and protein regions (IDRs) engage in transient, ye

193 roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent approximately

194 Intrinsically disordered proteins (IDPs) and their conformational transitions play an impor

195 Intrinsically disordered proteins (IDPs) are a set of proteins that lack a definite seconda

196 Intrinsically disordered proteins (IDPs) are a unique class of proteins that have no stable

197 Intrinsically disordered proteins (IDPs) are abundant in eukaryotic proteomes, play a major

198 Intrinsically disordered proteins (IDPs) are characterized by a lack of defined structure.

199 Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structur

200 diseases, intrinsically disordered proteins (IDPs) are dynamic ensembles of interconverting conformer

201 Intrinsically disordered proteins (IDPs) are flexible biomolecules whose essential function

202 Intrinsically disordered proteins (IDPs) are functional proteins that lack a well-defined t

203 Intrinsically disordered proteins (IDPs) are important for health and disease, yet their la

204 Intrinsically disordered proteins (IDPs) are known to undergo a range of posttranslational

205 Intrinsically disordered proteins (IDPs) are ubiquitous in eukaryotes, and they are often a

206 Intrinsically disordered proteins (IDPs) are well known, but correlates in RNA have not bee

207 Intrinsically disordered proteins (IDPs) as well as intrinsically disordered regions (IDRs)

208 Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled foldi

209 ed out by intrinsically disordered proteins (IDPs) binding to their targets.

210 erties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes.

211 study of intrinsically disordered proteins (IDPs) by NMR often suffers from highly overlapped resona

212 Intrinsically disordered proteins (IDPs) can display a broad spectrum of binding modes and

213 Intrinsically disordered proteins (IDPs) can form liquid-like membraneless organelles, gels

214 ration of intrinsically disordered proteins (IDPs) commonly underlies the formation of membraneless o

215 separated intrinsically disordered proteins (IDPs) composed of sequences of low complexity (SLC) have

216 Intrinsically disordered proteins (IDPs) constitute an important class of biomolecules with

217 ampled by intrinsically disordered proteins (IDPs) define their function.

218 havior in intrinsically disordered proteins (IDPs) has not been established.

219 Many intrinsically disordered proteins (IDPs) have been determined to undergo a disorder-to-orde

220 Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, whic

221 Intrinsically disordered proteins (IDPs) have roles in myriad biological processes and nume

222 e (HX) of intrinsically disordered proteins (IDPs) in solutions containing high concentrations of mac

223 ration of intrinsically disordered proteins (IDPs) is a major undergirding factor in the regulated fo

224 ration of intrinsically disordered proteins (IDPs) is a remarkable feature of living cells to dynamic

225 zation of intrinsically disordered proteins (IDPs) is challenging, in part because of a lack of accur

226 zation of intrinsically disordered proteins (IDPs) is very challenging using classical experimental m

227 states in intrinsically disordered proteins (IDPs) is well-established, but many disease-associated m

228 Intrinsically disordered proteins (IDPs) lack stable secondary and tertiary structure under

229 rature on intrinsically disordered proteins (IDPs) led scientists to rethink the structure-function p

230 Intrinsically disordered proteins (IDPs) often fold into stable structures upon specific bi

231 Intrinsically disordered proteins (IDPs) or regions (IDRs) perform diverse cellular functio

232 ration of intrinsically disordered proteins (IDPs) or regions (IDRs).

233 Intrinsically disordered proteins (IDPs) or regions of intrinsic disorder in otherwise fold

234 Intrinsically disordered proteins (IDPs) play central roles in many biological processes.

235 states of intrinsically disordered proteins (IDPs) populate heterogeneous conformational ensembles in

236 Intrinsically disordered proteins (IDPs) present a functional paradox because they lack sta

237 ted to be intrinsically disordered proteins (IDPs) that are induced under conditions of cellular dehy

238 Intrinsically disordered proteins (IDPs) that lack a unique 3D structure and comprise a lar

239 tures for intrinsically disordered proteins (IDPs) that takes full advantage of NMR chemical shifts a

240 including intrinsically disordered proteins (IDPs), adopt in the absence of denaturant remain controv

241 erties of intrinsically disordered proteins (IDPs), or protein regions (IDRs), are modulated by the n

242 s than on intrinsically disordered proteins (IDPs), peptides, and liposomes.

243 rtificial intrinsically disordered proteins (IDPs), we have created complex microparticle geometries,

244 Intrinsically disordered proteins (IDPs), which in isolation do not adopt a well-defined te

245 loited by intrinsically disordered proteins (IDPs).

246 embles of intrinsically disordered proteins (IDPs).

247 lexity or intrinsically disordered proteins (IDPs).

248 e case of intrinsically disordered proteins (IDPs).

249 nction of intrinsically disordered proteins (IDPs).

250 t the D2 domain of p27(Kip1), a prototypical IDP, samples multiple discrete, rapidly exchanging confo

251 We then apply the EISD method to rank IDP ensembles most consistent with the NMR data and show

252 el engineering of self-assembled recombinant IDP-rich materials.

253 trinsically disordered proteins and regions (IDPs) represent a large class of proteins that are defin

254 trinsically disordered proteins and regions (IDPs/IDRs) that do not adopt a dominant well-folded stru

255 lly disordered proteins and protein regions (IDPs and IDRs, respectively) in synaptic vesicle traffic

256 Intrinsically disordered proteins/regions (IDPs/IDRs) are proteins or peptide segments that fail to

257 Intrinsically disordered proteins/regions (IDPs/IDRs) contribute to a diverse array of molecular fu

258 general mechanism of signaling by regulatory IDPs, which can be subverted in human disease.

259 llowed by on-target coalescence of remaining IDP segments.

260 e interaction and subsequently the remaining IDP regions explore and coalesce around the initial bind

261 e conformational ensemble of this 67-residue IDP at both local and global level.

262 of the phase diagram of thermally responsive IDPs within microdroplets.

263 Abp1p SH3 domain (AbpSH3) and a proline-rich IDP, ArkA.

264 However, binding of E3 rRNase(IDP) to Im3 is 4 orders of magnitude weaker than that of

265 spite their simplified amino acid sequences, IDPs/IDPRs are complex entities often resembling chaotic

266 ne the ensemble structures of a set of short IDPs, that mimic the calmodulin binding domain of calciu

267 olymer-intrinsically disordered protein (SOP-IDP) model of Abeta40 and Abeta42.

268 These findings reveal how specific IDPs can phase separate to form permeable, low-density (

269 mputational methods are widely used to study IDPs, however, nearly all treat disorder in a binary fas

270 recently studied and became a model to study IDPs.

271 iscusses biophysical approaches for studying IDPs and illuminates their importance to critical functi

272 dynein intermediate chain (N-IC) is one such IDP that forms a bivalent scaffold with multiple dynein

273 We investigate this question using one such IDP, the kinase inducible domain (KID) of the transcript

274 The results show that IDP-fusion will be useful for unraveling the complexity

275 e characteristics, it is not surprising that IDPs serve as important hubs in signaling networks, scaf

276 of clusters of amino acid residues along the IDP primary sequence, individual residues can adopt a wi

277 gth of TC-BC association was measured by the IDP coefficients and incidence prediction accuracy.

278 at substoichiometric LC8 concentrations, the IDP domain preferentially binds to one of the three LC8

279 An understanding of how the IDP nature of p27 underpins its functional interactions

280 onally generated structural ensembles of the IDP amyloid-beta42 (Abeta42) to an alternative sequence

281 coupling between the dynamic behavior of the IDP and its environment allows us to develop analytical

282 tra into secondary structure features of the IDP ensemble.

283 ured protein, whereby a local segment of the IDP initiates the interaction and subsequently the remai

284 However, it is greatly unknown how the IDPs are involved in DDR.

285 We have shown previously that one of the IDPs RBM14 is required for the canonical nonhomologous e

286 These IDPs form liquid compartments at DNA damage sites in a p

287 iate force fields for MD simulations of this IDP.

288 enables a wide range of analyses relevant to IDP sequences.

289 This approach is applicable to IDPs of varying sizes and complexity, and is particularl

290 nance energy transfer experiments applied to IDPs.

291 d that small molecules bind promiscuously to IDPs, causing expansion of their conformational landscap

292 We developed a tool, IDP-ASE, for full ASE analysis.

293 Phi(b) values of the interaction between two IDP domains: the activation domain from the p160 transcr

294 dered protein (IDP) duplexes composed of two IDP chains cross-linked by bivalent partner proteins for

295 e of crowding on the interaction between two IDPs that fold upon binding, with polyethylene glycol as

296 xample, that the interaction between the two IDPs is less enhanced by crowding than expected for fold

297 The roles of residual structure of unbound IDPs in coupling binding and folding have been under muc

298 To understand IDP function it is critical to determine their configura

299 rom hepatitis C virus (HCV), a typical viral IDP with multiple functions during the viral life cycle.

300 (45.1%) during the intervention period, with IDPs accounting for 46% of these notifications.

301 On a dataset of 22 disordered PPIs with IDPs up to 69 amino acids, successful predictions were m