ライフサイエンスコーパス: intrinsically disordered protein

1 alation of human metallothionein-2A (MT), an intrinsically disordered protein.

2 , a prototypic viral oncoprotein and a model intrinsically disordered protein.

3 rotein is a prime example of a molecular hub intrinsically disordered protein.

4 n the cortactin repeats resemble a coil-like intrinsically disordered protein.

5 )DD) exhibits multiple characteristics of an intrinsically disordered protein.

6 roteins and is prevalent in the sequences of intrinsically disordered proteins.

7 and dynamics of functional de novo designed intrinsically disordered proteins.

8 etics of proteins as well as the dynamics of intrinsically disordered proteins.

9 We apply our analysis to globular and intrinsically disordered proteins.

10 in the denatured state ensemble (DSE) or in intrinsically disordered proteins.

11 used to study the properties of unfolded and intrinsically disordered proteins.

12 s simulations of three different unfolded or intrinsically disordered proteins.

13 e-induced chain collapse of five unfolded or intrinsically disordered proteins.

14 rning the structure-function relationship of intrinsically disordered proteins.

15 l but share overall physical properties with intrinsically disordered proteins.

16 ndicate that rGmUreG belongs to the class of intrinsically disordered proteins.

17 ve used short peptides as a model system for intrinsically disordered proteins.

18 her our understanding of protein folding and intrinsically disordered proteins.

19 nd might have general implications for other intrinsically disordered proteins.

20 en essential for the folding and function of intrinsically disordered proteins.

21 ysis to probe the oligomerization process of intrinsically disordered proteins.

22 ons at the early stage of folding and within intrinsically disordered proteins.

23 her illustrate the regulatory versatility of intrinsically disordered proteins.

24 t exchange at elevated temperatures, such as intrinsically disordered proteins.

25 indicate that L1-CT belongs to the class of intrinsically disordered proteins.

26 lobular conformation with some properties of intrinsically disordered proteins.

27 us and dynamic complexes in the functions of intrinsically disordered proteins.

28 g and for the function of the large group of intrinsically disordered proteins.

29 etheless poorly understood, particularly for intrinsically disordered proteins.

30 WIP is predicted to be an intrinsically disordered protein, a class of polypeptide

31 enaturants on the dimensions of unfolded and intrinsically disordered proteins: A wide range of exper

32 ded state of the spectrin domain R17 and the intrinsically disordered protein ACTR in two different d

33 guanidinium chloride on the structure of the intrinsically disordered protein ACTR, which can be stud

34 Participation of the small, intrinsically disordered protein alpha-synuclein (alpha-

35 Misfolding and aggregation of the intrinsically disordered protein alpha-Synuclein (alphaS

36 Fibrils of the intrinsically disordered protein alpha-synuclein are hal

37 Structural conversion of the presynaptic, intrinsically disordered protein alpha-synuclein into am

38 The formation of amyloid fibrils by the intrinsically disordered protein alpha-synuclein is a ha

39 The aggregation of the intrinsically disordered protein alpha-synuclein to form

40 enhancement experiments were applied to the intrinsically disordered protein alpha-synuclein, the pr

41 Here an intrinsically disordered protein, alpha-synuclein (alpha

42 a similar manner, with one being a bacterial intrinsically disordered protein and the other being a v

43 of functionally and pathologically important intrinsically disordered proteins and disordered regions

44 suitable for both simulations of unfolded or intrinsically disordered proteins and for investigating

45 Crucially, we show that both intrinsically disordered proteins and highly re-wired pr

46 Intrinsically disordered proteins and intrinsically diso

47 Intrinsically disordered proteins and intrinsically diso

48 ferent epitopes within three disease-related intrinsically disordered proteins and peptides (alpha-sy

49 flexibility and binding properties of these intrinsically disordered proteins and probably exemplifi

50 e generally accepted view of the behavior of intrinsically disordered proteins and provide new eviden

51 Intrinsically disordered proteins and regions (IDPs) rep

52 -third of the human proteome is comprised of intrinsically disordered proteins and regions (IDPs/IDRs

53 Intrinsically disordered proteins and regions carry out

54 efore, host cells use numerous advantages of intrinsically disordered proteins and regions to fight f

55 coupled folding and binding reaction of two intrinsically disordered proteins and the conformational

56 light the complexity of interactions between intrinsically disordered proteins and their targets.

57 TaFROG is an intrinsically disordered protein, and it localized to th

58 rding the conformational modulations of this intrinsically disordered protein, and its context-depend

59 rt the identification of MEG-14 as a classic intrinsically disordered protein, and open the possibili

60 LAT is an intrinsically disordered protein, and these data suggest

61 ted to play a key role in the association of intrinsically disordered proteins, and the observed beha

62 Intrinsically disordered proteins are highly abundant in

63 The dimensions of unfolded and intrinsically disordered proteins are highly dependent o

64 Protein-protein interactions involving intrinsically disordered proteins are important for cell

65 Many intrinsically disordered proteins are promiscuous binder

66 Intrinsically disordered proteins are thought to undergo

67 Intrinsically disordered proteins are ubiquitous in natu

68 Intrinsically disordered proteins are very common and me

69 Intrinsically disordered proteins are very common in the

70 tural biology, which include multidomain and intrinsically disordered proteins as well as nucleic aci

71 We show here using NMR that PEP-19 is an intrinsically disordered protein, but with residual stru

72 rates how the promiscuous interactions of an intrinsically disordered protein can produce highly spec

73 Thus, an intrinsically disordered protein can tunnel through the

74 Intrinsically disordered proteins can adopt multiple con

75 ditions has led to the realization that such intrinsically disordered proteins can be functional even

76 e of protein-based inheritance through which intrinsically disordered proteins can drive the emergenc

77 how very small structural motifs present in intrinsically disordered proteins can exert a specific f

78 dings which implicate AP7 as a member of the intrinsically disordered protein class (IDP) and reveal

79 Tau, an intrinsically disordered protein confined to neuronal ax

80 s the activation of nanoscale dynamics of an intrinsically disordered protein, controlling the bindin

81 provide insight into how the environment of intrinsically disordered proteins could dictate their st

82 also the majority of experimental studies of intrinsically disordered protein coupled folding and bin

83 Like other intrinsically disordered proteins, dehydrins can gain st

84 Intrinsically disordered proteins do not form a fixed th

85 In contrast, two intrinsically disordered proteins do not reach the Theta

86 gment of Msm sigma(A), which may comprise an intrinsically disordered protein domain unique to mycoba

87 One of the advantages of intrinsically disordered protein domains is thought to b

88 hese studies were performed on two different intrinsically disordered protein domains, a binding doma

89 ational behavior of the RTX domain and other intrinsically disordered protein domains.

90 The mechanisms by which intrinsically disordered proteins engage in rapid and hi

91 bda serves well to quantify the evolution of intrinsically disordered proteins even though the unstru

92 he case of the Abeta40 peptide, a 40-residue intrinsically disordered protein fragment associated wit

93 probably a common mechanism in molecular hub intrinsically disordered protein function.

94 This novel strategy, based on intrinsically disordered protein, has the potential to i

95 es in modulating structure and dimensions of intrinsically disordered proteins have been limited.

96 allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new

97 We focus on an intrinsically disordered protein, human islet amyloid po

98 other CRIB-family effectors and indeed other intrinsically disordered proteins, hydrophobic residues

99 have identified tumor suppressor PTEN as an intrinsically disordered protein (IDP) and elucidated th

100 Intrinsically disordered protein (IDP) conformers occupy

101 e than an N-terminal, arginine/glycine rich, intrinsically disordered protein (IDP) domain of LAF-1 i

102 Intrinsically disordered protein (IDP) duplexes composed

103 model system to explore general features of intrinsically disordered protein (IDP) folding mechanism

104 The intrinsically disordered protein (IDP), alpha-synuclein

105 Is), those involving a folded protein and an intrinsically disordered protein (IDP), are prevalent in

106 (K(d) approximately 10(-12) M) to become an intrinsically disordered protein (IDP).

107 Here, we show that PAGE4 is a highly (100%) intrinsically disordered protein (IDP).

108 elongs to the BH3-only protein family, is an intrinsically disordered protein (IDP).

109 Intrinsically disordered proteins (IDP) are a broad clas

110 These intrinsically disordered proteins (IDP) are recognized a

111 dration-water dynamics and atomic motions in intrinsically disordered proteins (IDP), a largely unexp

112 Intrinsically disordered proteins (IDPs) adopt heterogen

113 ed amino acid sequences, monomeric proteins, intrinsically disordered proteins (IDPs) and catalytic r

114 These intrinsically disordered proteins (IDPs) and hybrid prot

115 Intrinsically disordered proteins (IDPs) and IDP regions

116 or the deposition of structural ensembles of intrinsically disordered proteins (IDPs) and of denature

117 Many intrinsically disordered proteins (IDPs) and protein reg

118 However, the prevalence of the intrinsically disordered proteins (IDPs) and regions (ID

119 s requires elucidating the critical roles of intrinsically disordered proteins (IDPs) and regions (ID

120 Intrinsically disordered proteins (IDPs) are a newly rec

121 Intrinsically disordered proteins (IDPs) are a set of pr

122 Intrinsically disordered proteins (IDPs) are a unique cl

123 Intrinsically disordered proteins (IDPs) are characteriz

124 Intrinsically disordered proteins (IDPs) are characteriz

125 Intrinsically disordered proteins (IDPs) are frequently

126 Intrinsically disordered proteins (IDPs) are functional

127 Intrinsically disordered proteins (IDPs) are functional

128 Intrinsically disordered proteins (IDPs) are functional

129 The functions of intrinsically disordered proteins (IDPs) are governed by

130 Intrinsically disordered proteins (IDPs) are highly abun

131 Intrinsically disordered proteins (IDPs) are important f

132 Intrinsically disordered proteins (IDPs) are increasingl

133 Intrinsically disordered proteins (IDPs) are involved in

134 Intrinsically disordered proteins (IDPs) are involved in

135 Intrinsically disordered proteins (IDPs) are known to un

136 Intrinsically disordered proteins (IDPs) are now recogni

137 Intrinsically disordered proteins (IDPs) are proteins th

138 Intrinsically disordered proteins (IDPs) are proteins th

139 Many intrinsically disordered proteins (IDPs) are significant

140 Intrinsically disordered proteins (IDPs) are ubiquitous

141 Intrinsically disordered proteins (IDPs) are unfolded un

142 Intrinsically disordered proteins (IDPs) are widespread

143 cant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting th

144 The study of intrinsically disordered proteins (IDPs) by NMR often su

145 A subset of these intrinsically disordered proteins (IDPs) can, upon bindi

146 ular structures that contain phase-separated intrinsically disordered proteins (IDPs) composed of seq

147 Intrinsically disordered proteins (IDPs) containing phen

148 The dynamic modes and time scales sampled by intrinsically disordered proteins (IDPs) define their fu

149 aordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their ro

150 ntitatively reproduce structural behavior in intrinsically disordered proteins (IDPs) has not been es

151 Intrinsically disordered proteins (IDPs) have roles in m

152 Measuring amide hydrogen exchange (HX) of intrinsically disordered proteins (IDPs) in solutions co

153 Liquid-liquid phase separation of intrinsically disordered proteins (IDPs) is a major unde

154 Characterization of intrinsically disordered proteins (IDPs) is challenging,

155 The conformational characterization of intrinsically disordered proteins (IDPs) is complicated

156 Coupled folding and binding of intrinsically disordered proteins (IDPs) is prevalent in

157 Intrinsically disordered proteins (IDPs) lack stable sec

158 Intrinsically disordered proteins (IDPs) lack stable ter

159 A growing body of literature on intrinsically disordered proteins (IDPs) led scientists

160 less organelles form via phase separation of intrinsically disordered proteins (IDPs) or regions (IDR

161 Intrinsically disordered proteins (IDPs) perform their p

162 lasm that collectively we term "assemblage." Intrinsically disordered proteins (IDPs) play an importa

163 Intrinsically disordered proteins (IDPs) play central ro

164 lded states of proteins and native states of intrinsically disordered proteins (IDPs) populate hetero

165 Intrinsically disordered proteins (IDPs) present a funct

166 However, the mechanisms by which such intrinsically disordered proteins (IDPs) recognize their

167 facile specific recognition is essential for intrinsically disordered proteins (IDPs) that are involv

168 Intrinsically disordered proteins (IDPs) that lack a uni

169 ensemble model from candidate structures for intrinsically disordered proteins (IDPs) that takes full

170 Quantitative comparisons of intrinsically disordered proteins (IDPs) with similar se

171 s of naturally unstructured proteins, termed intrinsically disordered proteins (IDPs), demonstrates t

172 chnique for studying complex systems such as intrinsically disordered proteins (IDPs), globular prote

173 dary structure in vitro is characteristic of intrinsically disordered proteins (IDPs), many of which

174 be significantly more heterogeneous than on intrinsically disordered proteins (IDPs), peptides, and

175 rmational fluctuations in the interaction of intrinsically disordered proteins (IDPs), we first combi

176 links structure and function information for intrinsically disordered proteins (IDPs).

177 o characterizing the structural ensembles of intrinsically disordered proteins (IDPs).

178 s six exciting articles on low complexity or intrinsically disordered proteins (IDPs).

179 argely unknown, in particular in the case of intrinsically disordered proteins (IDPs).

180 interest in understanding the properties of intrinsically disordered proteins (IDPs); however, the c

181 ters such as (i) explaining the emergence of intrinsically disordered proteins, (ii) developing compo

182 biophysical studies and show that SilE is an intrinsically disordered protein in its free apo-form bu

183 The inhibitory Pgamma subunit behaves as an intrinsically disordered protein in solution but binds w

184 rs in carbohydrate-active enzymes, which are intrinsically disordered proteins in solution, aid in dy

185 Like some other intrinsically disordered proteins in the solution state

186 hough several well-characterized examples of intrinsically disordered proteins in transcriptional reg

187 P-pRb interactions, or more generally in hub intrinsically disordered protein interaction networks.

188 , a feature we believe could be important in intrinsically disordered protein interactions more gener

189 g dynamic complexes in structural studies of intrinsically disordered protein interactions.

190 Even in unfolded and intrinsically disordered proteins, internal friction has

191 Intrinsically disordered protein is common across the th

192 This intrinsically disordered protein is highly diffusive at

193 -molecule inhibitors that bind covalently to intrinsically disordered proteins is a promising strateg

194 g of the conformational changes exhibited by intrinsically disordered proteins is necessary as we con

195 The function of these intrinsically disordered proteins is the stabilization o

196 A pre-structures motif in the intrinsically disordered proteins is thus important for

197 alpha-Synuclein (alpha-Syn), an intrinsically disordered protein, is associated with Par

198 ollective interactions among multivalent and intrinsically disordered proteins, is thought to mediate

199 Finally, we implicate intrinsically disordered proteins, key components in mRN

200 The number of intrinsically disordered proteins known to be involved i

201 Intrinsically disordered proteins lack a well-defined fo

202 Intrinsically disordered proteins, like tau, are enriche

203 ore the conformations of alpha-synuclein, an intrinsically disordered protein linked to Parkinson's a

204 d binding and folding of alpha-synuclein, an intrinsically disordered protein linked with Parkinson's

205 ifts suggest that new interactions involving intrinsically disordered proteins may evolve via a low-a

206 The low internal friction in expanded intrinsically disordered proteins may have implications

207 Thus, our data suggest that intrinsically disordered proteins might play key roles i

208 nd/or secondary structure in solution (i.e., intrinsically disordered proteins) might be involved in

209 measuring rapid H/D exchange kinetics by an intrinsically disordered protein, murine CBP(2059-2117)

210 hi-psi dihedral angle space, we used a model intrinsically disordered protein, namely, alpha-synuclei

211 prokaryotic ubiquitin-like protein (Pup), an intrinsically disordered protein of 64 residues.

212 mylin (islet amyloid polypeptide, IAPP), two intrinsically disordered proteins of the calcitonin pept

213 Intrinsically disordered proteins often become structure

214 on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist

215 al studies of aggregation of short peptides, intrinsically disordered proteins, or proteins under den

216 As for many intrinsically disordered proteins, order-disorder transi

217 tanding of the molecular mechanisms by which intrinsically disordered proteins perform their diverse

218 Intrinsically disordered proteins play an important role

219 Intrinsically disordered proteins play causative roles i

220 Intrinsically disordered proteins play crucial roles in

221 Intrinsically disordered proteins play important roles t

222 Example dark-matter species include intrinsically disordered proteins, posttranslational sta

223 ) and hybrid proteins containing ordered and intrinsically disordered protein regions (IDPRs) constit

224 s) or partially disordered segments known as intrinsically disordered protein regions (IDPRs).

225 id-liquid phase separations (LLPS) driven by intrinsically disordered protein regions (IDR) of RNA bi

226 Phase transitions driven by intrinsically disordered protein regions (IDRs) have eme

227 Intrinsically disordered protein regions (IDRs) lack a w

228 any cell signaling events are coordinated by intrinsically disordered protein regions (IDRs) that und

229 Intrinsically disordered protein regions are widely dist

230 eveal that the flexibility and plasticity of intrinsically disordered protein regions as well as indu

231 teractions between prion-related domains and intrinsically disordered protein regions found in SG-nuc

232 The results reveal that intrinsically disordered protein regions transition betw

233 orylation sites are very similar to those of intrinsically disordered protein regions.

234 phosphorylation predominantly occurs within intrinsically disordered protein regions.

235 Intrinsically disordered proteins/regions (IDPs/IDRs) ar

236 p27(Kip1) (p27), an intrinsically disordered protein, regulates the various

237 biology, molecular recognition mechanisms in intrinsically disordered proteins remain poorly understo

238 tions that are close in energy, such as many intrinsically disordered proteins, residues distant from

239 hich has acquired a state similar to that of intrinsically disordered proteins, resulting in a predom

240 exes, and the roles in the process played by intrinsically disordered protein segments.

241 Our results revealed that the Cx40CT is an intrinsically disordered protein similar to the Cx43CT a

242 In intrinsically disordered proteins, slow transverse relax

243 Intrinsically disordered proteins such as FlgM play impo

244 Conformational behavior of intrinsically disordered proteins, such as Phe-Gly repea

245 Intrinsically disordered proteins, such as tau protein,

246 Atg29 has the characteristics of an intrinsically disordered protein, suggesting that it und

247 Here we show that tardigrade-specific intrinsically disordered proteins (TDPs) are essential f

248 These intrinsically disordered proteins tend to fold upon bind

249 alpha-Synuclein is an intrinsically disordered protein that appears in aggrega

250 Our results revealed that the Cx32CT is an intrinsically disordered protein that becomes alpha-heli

251 MEG-3 is an intrinsically disordered protein that binds and phase se

252 mutational analyses show APLF is largely an intrinsically disordered protein that binds Ku, Ku/DNA-P

253 PEP-19 is a small, intrinsically disordered protein that binds to the C-dom

254 tems, we introduce a biomimetic, recombinant intrinsically disordered protein that can assemble into

255 The redox switch CP12 is an intrinsically disordered protein that can form two disul

256 with the factors that induce LLPS, tau is an intrinsically disordered protein that complexes with RNA

257 One of them is COR15A, a small, intrinsically disordered protein that contributes to lea

258 In turn, Brh2 is governed by Dss1, an intrinsically disordered protein that forms a tight comp

259 alpha-synuclein is an intrinsically disordered protein that has the capacity t

260 alpha-Synuclein is an intrinsically disordered protein that is associated with

261 ne belonging to the calcitonin family, is an intrinsically disordered protein that is coexpressed and

262 mer that does not bind RNA, human SLBP is an intrinsically disordered protein that is phosphorylated

263 alpha-Synuclein (alphaS) is an intrinsically disordered protein that is water-soluble b

264 the 14-3-3-binding motifs are located, is an intrinsically disordered protein that reduces its flexib

265 oth at high denaturant concentrations and in intrinsically disordered proteins that are expanded due

266 complexes (NPCs) contains a high density of intrinsically disordered proteins that are rich in pheny

267 henylalanine-glycine nucleoporins (FG Nups)--intrinsically disordered proteins that facilitate select

268 Dehydrins are a group of intrinsically disordered proteins that protect plants fr

269 globin, on the conformational ensemble of an intrinsically disordered protein, the N protein of bacte

270 mine the effects of molecular crowding on an intrinsically disordered protein, the N protein of bacte

271 racterize the conformational behavior of two intrinsically disordered proteins, the K18 domain from T

272 s suggested and CD confirmed that P311 is an intrinsically disordered protein, therefore requiring an

273 late folding intermediates but also for some intrinsically disordered proteins-through the eyes of Hs

274 ndings extend the repertoire of functions of intrinsically disordered protein to fine-tuning and vers

275 ese fuzzy interactions are characteristic of intrinsically disordered proteins to achieve liquid-liqu

276 this templated folding mechanism may enable intrinsically disordered proteins to achieve specific an

277 ort the recent notion that the affinities of intrinsically disordered proteins toward their targets a

278 Our study demonstrates that an intrinsically disordered protein undergoing binding-indu

279 Upon analyzing intrinsically disordered proteins, we found a similar pa

280 indicate that allostery is also manifest in intrinsically disordered proteins, which account for a s

281 , such as the increasingly abundant class of intrinsically disordered proteins, which are hard to cha

282 are further strengthened by the finding that intrinsically disordered proteins, which have large hydr

283 energy landscape for interactions involving intrinsically disordered proteins, which is likely a res

284 ndant (LEA) proteins are hydrophilic, mostly intrinsically disordered proteins, which play major role

285 It affects structural properties of intrinsically disordered proteins, which take a consider

286 alpha-Synuclein (alphaS) is an intrinsically disordered protein whose aggregation into

287 alpha-synuclein (alphaS) is an intrinsically disordered protein whose fibrillar aggrega

288 Tau is an intrinsically disordered protein with a central role in

289 Tau is an intrinsically disordered protein with an important role

290 PEP-19 (Purkinje cell protein 4) is an intrinsically disordered protein with an IQ calmodulin (

291 results suggest that the Cel7A linker is an intrinsically disordered protein with and without glycos

292 ing the detailed mechanism of interaction of intrinsically disordered proteins with their partners is

293 nd TMAO on alpha-synuclein in the context of intrinsically disordered proteins, with potential implic

294 g-binding is central to the function of many intrinsically disordered proteins, yet not fully underst