ライフサイエンスコーパス: folding

1 , bistability, and area and volume change by folding).

2 with Zika virus impairs cortical growth and folding.

3 both regionally and temporally with cortical folding.

4 ntially reduced perturbation of G-quadruplex folding.

5 isulfide bonding in the MD models of protein folding.

6 ions with binding partners to support proper folding.

7 se, promote changes to surface curvature and folding.

8 ractility gradients are important for tissue folding.

9 deletion in mouse organoids does not lead to folding.

10 f a beta-sheet, this leads to a pH switch of folding.

11 interactions that is necessary for efficient folding.

12 nherently coupled to cotranslational protein folding.

13 e essential molecular chaperones for protein folding.

14 ormational trapping may also be conducive to folding.

15 between spontaneous and chaperonin-mediated folding.

16 cortex leads to the formation of stereotyped folding.

17 egulate protein complex assembly and protein folding.

18 t the time of initial membrane insertion and folding.

19 aluable in elucidating these pathways of IDP folding.

20 d a nucleosome repeat length (NRL)-dependent folding.

21 ad, they are governed by the kinetics of RNA folding.

22 nin), a complex known to function in protein folding.

23 dulate ribosome speed and facilitate protein folding.

24 (GlucII), and that vIL-6 can promote protein folding.

25 to predictions about each's role in tubulin folding.

26 n to form non-native disulfides during their folding.

27 tion, translation and protein maturation and folding.

28 ds to a marked reorganization of chromosomal folding.

29 molten globules (MG), to understand protein folding.

30 tein reach the transition state and continue folding.

31 ily bind to the nanofibers by triple helical folding, allowing facile display of bioactive molecules

32 l condensation is sufficient to drive tissue folding along programmed trajectories.

33 ut to explore dynamic aspects of twister RNA folding along the cleavage reaction coordinate.

34 we show that sNASP and ASF1A are capable of folding an H3-H4 dimer in vitro under native conditions.

35 strate 'client' proteins, facilitating their folding and activating them for biological function.

36 fold of GPCRs that is important for receptor folding and activation.

37 t of stacking, significantly affect tertiary folding and appear to largely explain previously observe

38 ynechocccus PCC6301 Rubisco, the specialized folding and assembly requirements of Te-Rubisco hinder i

39 s a robust mechanism for heteromeric protein folding and assembly that could also be applied in self-

40 If specific inversions affect folding and assembly, then the sites involved likely are

41 We study the folding and binding of random sequences of hydrophobic (

42 onds to minutes by investigating the coupled folding and binding reaction of two intrinsically disord

43 r demonstrated that DREB2A underwent coupled folding and binding with alpha-helix formation upon inte

44 control sequences to probe contributions to folding and binding, and identified 2,618 high-affinity

45 support endoplasmic reticulum redox protein folding and cell-surface thiol-redox control of thrombos

46 -coding transcription orchestrates chromatin folding and compartmentalization to direct with high pre

47 N-glycosylation (PNG) is crucial for protein folding and enzymatic activities, and has remarkable div

48 ctomyosin bundles through synchronized NM-II folding and filament-assembly activities.

49 own factor that facilitates normal alpha-syn folding and function in vivo.

50 hich can play critical roles in both protein folding and function.

51 ethanolamine is however required for correct folding and function.

52 ained by the consequent challenge to protein folding and function.

53 binding of proteins and modulate the global folding and interactions of double helices with hundreds

54 that provide insights on protein structure, folding and interactions.

55 A fragments have inherited local autonomy of folding and local autonomy of assembly with ribosomal pr

56 ta support an emerging model in which genome folding and misfolding is critically linked to the onset

57 nging career began with the study of protein folding and molecular chaperones, and she went on to sho

58 ocarbon and amide surfaces buried in protein folding and other biopolymer processes and transition st

59 Expression of the cellular protein folding and pro-survival machinery by heat shock transcr

60 ethanolamine lipids, lowers lactose permease folding and reconstitution yields but stabilises the fol

61 nus plays an important role in the efficient folding and regulation of ATP8A2.

62 ikely acts as a hub molecule during collagen folding and secretion by directing other molecules to re

63 this reductive pathway prevents the correct folding and secretion of proteins that are known to form

64 onodisperse macromolecules with programmable folding and self-assembly properties.

65 study the influence of chaperones on protein folding and show that the ribosomal chaperone trigger fa

66 d diverse scaffold libraries with verifiable folding and stability.

67 Toward our mechanistic studies of RNA folding and structures with heterogeneous backbones, we

68 A linkers may control chromatin higher-order folding and thus influence cellular processes such as ge

69 ) systems, the chaperone was shown to assist folding and to prevent degradation of its cognate antito

70 Folding and transporting of P4-ATPases to their cellular

71 nteractions (for example, cleavage, binding, folding and unfolding) and biological targets in in vitr

72 nvestigate the biophysical mechanisms of RNA folding and unfolding, its interactions with ligands, an

73 nks are absolutely required to allow protein folding and, conversely, that protein folding occurs pri

74 multistep catalysis, transient interactions, folding, and allosteric structural transitions.

75 The relationship between protein synthesis, folding, and disulfide formation within the endoplasmic

76 lucII and UGGT1, that vIL-6 promotes protein folding, and that VKORC1v2, UGGT1, and vIL-6 interaction

77 Ps included roles in photosynthesis, protein folding, antioxidant mechanism and metabolic processes,

78 Membrane protein topology and folding are governed by structural principles and topoge

79 es structure and all interactions that drive folding are self-contained within sequence.

80 ps leading to the current concept of protein folding as a highly organized cellular process.

81 lysine abolished PtaA activity and affected folding as well as Tat-dependent transport of the enzyme

82 on show that these mutations perturb protein folding, assembly or polarity of secretion of C1QTNF5 an

83 propeptides, SPI-1 could not substitute as a folding assistant for SBT4.13.

84 der mechanical force during co-translational folding at the ribosome.

85 ops into the target-cell membrane; and (iii) folding back of a cluster of extended trimers into their

86 racterized as resulting from an RNA molecule folding back on itself in cis but could also form in tra

87 ormation defined by the isoprenyl side-chain folding back over the napthoquinone in a U-shape, which

88 e route to enhance the sensor performance by folding back-to-back two pMFCs electrically connected in

89 completely loses its ability to contract by folding, becoming a labile polymer.

90 ns of rProtein uL23 are distinctive in their folding behaviors and the ion dependences of their assoc

91 widely utilized cell shape change linked to folding, bending and invagination of polarized epithelia

92 e process of dissolution in water to protein folding, but its origin at the fundamental level is stil

93 ypeptide's sequence and evaluating impact on folding can be problematic for amyloid aggregates becaus

94 erones, and she went on to show that protein folding can have profound and unexpected biological effe

95 Our results demonstrate that polypeptide folding can occur without complete domain translocation.

96 Insufficient folding capacity of the endoplasmic reticulum (ER) activ

97 Importantly, alteration of the folding capacity of the endoplasmic reticulum (ER) is be

98 d, and oxidative stress, disturb the protein-folding capacity of the endoplasmic reticulum (ER), ther

99 olded protein response (UPR) to increase the folding capacity of the ER.

100 protein response (UPR) increases ER-protein-folding capacity to restore protein-folding homeostasis.

101 proteins when protein load overwhelms the ER folding capacity, which activates the unfolded protein r

102 ptosis due to an enhancement of the cellular folding capacity.

103 cal gyrification of the brain represents the folding characteristic of the cerebral cortex.

104 that quantized native structure and stepwise folding coevolved in ancient repeat proteins and were re

105 during early evolution by addition of small folding-competent RNAs.

106 led structural information on complexes with folding-competent substrates remains lacking.

107 P chaperone activity to cope with suboptimal folding conditions.

108 CPMG-RD captured a low populated protein-folding conformation triggered by the Glu-145 replacemen

109 ated that the two molecules had common rigid folding core and dynamic regions and provided structural

110 complex that coordinates the destruction of folding-defective proteins in the early secretory pathwa

111 hDAT-V158F, hDAT-G327R, and hDAT-L368Q, the folding deficit was remedied with the pharmacochaperone

112 also adjustment of the machinery for protein folding, degradation, and homeostasis.

113 owed by screening for variants whose in vivo folding displays increased or decreased GroEL dependence

114 molecular interactions are not observed, and folding does not compete with duplex formation.

115 CTCF and cohesin control domain location by folding domains into loop structures, which are widely t

116 y choices that have widely varying 'typical' folding energies.

117 The folding energy landscape of an RNA is highly dependent o

118 ding the entropy of crease patterns of given folding energy.

119 e (UPR), to maintain a productive ER protein-folding environment through reprogramming gene transcrip

120 insult or innate genetic deficiency, protein folding environments of the mitochondrial matrix are pro

121 2-mers (AA.DD) where there are no competing folding equilibria.

122 hemical, or mechanical stress to perturb the folding equilibrium for examining protein stability and

123 ork to dissect the coupling of synthesis and folding essential for riboswitch function, revealing the

124 Among the earliest folding events in biogenesis is the formation of a helix

125 for predicting their folding response (e.g., folding force, bistability, and area and volume change b

126 e directly measuring initial cotranslational folding forces.

127 the effect of SAM and magnesium ions on the folding free energy landscape of the SAM-I riboswitch.

128 measurements between such states enabled the folding free-energy landscape to be deduced.

129 the eventual quantitative description of RNA folding from its secondary and tertiary structural eleme

130 xperimental-computational study unravels the folding-functional landscape of a natural thermosensor p

131 The system uses a scalable stacking or folding geometry that generates 110 volts at open circui

132 onding to freezing at -3 degrees C) and that folding gradually increases with decreasing RH.

133 experimental study of cotranscriptional RNA folding has been limited by the lack of easily approacha

134 mplex synthetic nanostructures, unimolecular folding has seen limited progress.

135 y known as the ancient Japanese art of paper folding, has recently inspired a new paradigm of design

136 d Hsp70 chaperone BiP contributes to protein folding homeostasis by engaging unfolded client proteins

137 Secondary effects on protein folding homeostasis likely contribute to UPR activation,

138 -protein-folding capacity to restore protein-folding homeostasis.

139 Finally, our data suggest that RNA folding impact the aggregation behavior of the functiona

140 ntribute to protein stability, activity, and folding in a variety of proteins, including many involve

141 sly present and required for correct protein folding in all proteomes.

142 nstitution hypothesis considers RNA tertiary folding in terms of DeltaGalign, the probability of alig

143 Protein folding in the cell was originally assumed to be a spont

144 eprivation and acidification disturb protein folding in the endoplasmic reticulum (ER) and activate t

145 Proper gp160 folding in the ER requires core glycosylation, disulfide

146 The development of reproducible folding in the gyrencephalic cerebral cortex is a topic

147 BamA has a greater catalytic effect on tOmpA folding in thicker bilayers, suggesting that BAM catalys

148 ending, and random patterns with high-energy folding, in which the sheet bends as much as creases fol

149 ns of cooperativity and stability in protein folding, including the balance between solvent and polyp

150 encoding ER proteins that augment ER protein folding, induced numerous oxidative stress response gene

151 Here, we compile folding information for every base pair of the genome th

152 -termini make physical contact with the PepQ folding intermediate and help retain it deep within the

153 the isolation and purification of a protein folding intermediate in native condition.

154 Here, we investigated the equilibrium (un)folding intermediate state of T4 phage gene product 45 (

155 a particularly challenging problem, because folding intermediates are predicted to be unstable in ei

156 influenced more heavily by specific membrane folding intermediates, and as a result yield different p

157 can dictate gene expression distribution by folding into distinct topological domains.

158 Protein folding is a complex process that can lead to disease wh

159 In many cases, folding is associated with myosin accumulation at the ap

160 to be folded, although it is known that CH1 folding is linked to IgG assembly and secretion.

161 ding environment, the impact of which on RNA folding is poorly understood.

162 ntly, at finite temperatures, the process of folding is probabilistic.

163 the endoplasmic reticulum (ER), where their folding is surveyed by the 170-kDa UDP-glucose:glycoprot

164 ing of the BamA barrel does not affect tOmpA folding kinetics in 1,2-dimyristoyl-sn-glycero-3-phospho

165 study, we have determined the unfolding and folding kinetics of 10 FNIII domains.

166 e central subunit of the BAM complex, on the folding kinetics of a model OMP (tOmpA) using fluorescen

167 Their stability and folding kinetics were similar to those of natural protei

168 d to cross the energy barrier that dominates folding kinetics, known as the transition path time.

169 The structure also demonstrates that the folding landscapes of short DNA single strands is much m

170 data sets, we show that previously reported folding layers appear at different insulation levels.

171 low energy gradients prior to the "downhill" folding leading to fibril formation.

172 ate that although no structurally privileged folding level exists, TADs emerge as a functionally priv

173 zers has emerged as a powerful tool to study folding, ligand binding, and motor enzymes.

174 tructural information for this vital protein-folding machine in humans.

175 erspective that a generalizable model of RNA folding may be developed from understanding of the foldi

176 gested pull and release approach to graphene folding may find applications in the theoretical studies

177 tional free energy landscape and the complex folding mechanism inherent to the pseudoknot motif.

178 tailed mechanistic information regarding the folding mechanism.

179 eins are important for understanding protein-folding mechanisms as well as the interactions of unfold

180 ole of functional constraints in determining folding-mechanistic behaviors, and the design principles

181 To ensure efficient folding, members of different chaperone classes receive

182 nds to acidification by undergoing a coupled folding/membrane insertion process.

183 n bacterial cells, putrescine2+, and how RNA folding might be influenced by the three ions in combina

184 differences between the many-pathway protein folding model derived from theoretical energy landscape

185 mmable stiff sheets with a single low-energy folding motion have been sought in fields ranging from t

186 lenge, we reconstruct a genome-scale protein-folding network for Escherichia coli and formulate a com

187 We found that the residues making up the folding nucleus tend to interact in the denatured state

188 initial events leading to the formation of a folding nucleus.

189 ing incomplete and distorted versions of the folding nucleus.

190 ding nonnative interactions, and most of the folding occurs after the initial binding event.

191 rotein folding and, conversely, that protein folding occurs prior to disulfide formation.

192 or this finding was obtained by showing that folding of an enhanced green fluorescent protein variant

193 Self-folding of an information-carrying polymer into a define

194 hese findings indicate that the higher order folding of chromatin topology may act as a molecular-pat

195 participate in a quality control pathway for folding of EGF repeats in proteins such as Notch.

196 ty of co-replicational or co-transcriptional folding of G-quadruplex inside the polymerase machinery

197 been performed for G-quadruplexes formed by folding of GGG(TTAGGG)3 single strands in buffered solut

198 are believed to be indispensable for proper folding of gp120 and for viral infectivity.

199 s support elevated tensions that promote the folding of interfaces along paths that can be predicted

200 for Tsc1 as a facilitator of Hsp90-mediated folding of kinase and non-kinase clients-including Tsc2-

201 glycosylation of N582, suggesting that rapid folding of local conformation prevents glycosylation of

202 open up potential new avenues to control the folding of macromolecules.

203 disulfide rearrangements required for proper folding of nascent proteins synthesized in the endoplasm

204 The folding of natural proteins typically relies on hydropho

205 labeling modification might affect rates of folding of near-neighbor structural elements, and thus l

206 5-fold, we demonstrate that slow spontaneous folding of PepQ is not caused by aggregation.

207 d anaerobic electron acceptors for oxidative folding of periplasmic proteins.

208 ail how assembly factors regulate the timely folding of pre-18S rRNA.

209 he role of modest free energy changes in the folding of pre-integration forms of a hyperstable outer

210 Folding of proteins entering the secretory pathway in ma

211 atured, transition, and native states in the folding of the activation domain of human procarboxypept

212 BG have been implicated in the expansion and folding of the cerebrum and cerebellum, respectively.

213 n identity-could coordinate co-translational folding of the encoded protein.

214 tions with a protein partner lead to partial folding of the IDR.

215 In contrast, in aromatic solvents folding of the macrocycles with a distinct odd-even effe

216 ap optical tweezers and observe simultaneous folding of the nascent polypeptide chain in real time.

217 rocyclization proceeds efficiently, inducing folding of the o-phenylenes.

218 gp160 chain termination and is dependent on folding of the soluble subunit gp120 to a near-native co

219 analysis mainly detects selection for proper folding of the TCR receptor protein.

220 The folding of the triple-labeled mutant is monitored by the

221 e time required for beta 2-AR activation and folding of the WW domain are greatly diminished using ev

222 lity to resolve fine differences in rates of folding of these elements.

223 n-canonical ER quality control mechanism for folding of thrombospondin type 1 repeats by protein O-fu

224 volves VCP/p97, an AAA ATPase regulating the folding of various cellular substrates including ubiquit

225 An arabinose-inducible, rapidly folding OmpA-GFP chimera was utilized to jam the SecYEG

226 how DNA is folded and the influence of such folding on nuclear processes remain topics of intensive

227 Ps may act on the cell wall, inhibit protein folding or enzyme activity, or act intracellularly.

228 In these structures, folding overcomes intramolecular electrostatic repulsion

229 This finding suggests that the folding path of twister RNA requires proper orientation

230 Here, we effectively map part of the folding pathway for the model large multidomain protein,

231 lasmic conformer involves an export-related, folding pathway not present in E. coli.

232 naturally encode its particular foldon-based folding pathway, and they collectively sum to produce th

233 uggest that they are intermediates along the folding pathway.

234 folding with many intermediate steps in the folding pathway.

235 Long folding pathways are interesting, because they demonstra

236 xplain how the presence of links affects the folding pathways of proteins.

237 me folds inside the 3D nucleus and how these folding patterns are miswired during the onset and progr

238 At a finer scale, we detected distinct folding patterns at the developmentally controlled beta-

239 he physical mechanism of membrane-associated folding, pHLIPs are triggered by the acidic microenviron

240 ic G4 structures, correctly assessing the G4 folding potential of over 700,000 such sequences in the

241 To address this issue, we investigated the folding preferences of oligonucleotides from a chromosom

242 Decades of study of the RNA folding problem have revealed that diverse and complex s

243 ion with a combinatorial approach to the RNA folding problem in order to compute all possible non-pse

244 ir utility for solving the difficult protein folding problem.

245 Proteins with folding problems are trapped in the endoplasmic reticulu

246 In order to protect the delicate protein folding process and ensure the proper cellular delivery

247 int and can be programmed to terminate their folding process at different intermediates.

248 ed intermediate was observed to start the G4 folding process in both salt conditions.

249 Protein folding process involves formation of transiently occurr

250 EFoldMine predictions give insights into the folding process, as illustrated by a qualitative compari

251 ones, notably involved in the gluten-protein folding process, were up-regulated in superior (SP) and

252 examining protein stability and the protein folding process.

253 participates in a broad spectrum of protein folding processes extending from nascent chain folding t

254 and contains all mechanistic information of folding processes of biomolecules such as proteins and n

255 Exploring the tertiary structure folding processes of RNA enables us to understand and co

256 Tissue folding promotes three-dimensional (3D) form during deve

257 nt of PS stem-loops, their number, and their folding propensity.

258 g may be developed from understanding of the folding properties of individual structural motifs.

259 l utilization of these predicted contacts in folding proteins accurately, it is important to study th

260 theory, developed in the context of protein folding, provides, to our knowledge, a new perspective o

261 While GroELS increases the folding rate of PepQ by over 15-fold, we demonstrate tha

262 es primarily with unfolding rate rather than folding rate.

263 We found that the folding rates were relatively similar, approximately 0.1

264 a result, we now know that in vivo, protein folding requires assistance by a complex machinery of mo

265 -based zero-energy patterns, in which crease folding requires no sheet bending, and random patterns w

266 titative proteome scale, the predicted early folding residues tend to become the residues that intera

267 herent foldability, and for predicting their folding response (e.g., folding force, bistability, and

268 An RNA folding/RNA secondary structure prediction algorithm det

269 d by using the strain engineering and a self-folding rolling process.

270 glycoprotein glucosyltransferase 1 (UGT1), a folding sensor in the calnexin/calreticulin quality cont

271 orroborate the structures predicted from the folding simulation and strongly suggest that they are in

272 n naturally occurring protein structures and folding simulations.

273 We also determine possible cotranslational folding sites initiated by hydrophobic collapse for an u

274 ed capture, origamis can be immobilized from folding solution without purification, even in the prese

275 atic effects on the in vitro reconstitution, folding, stability and function of a representative of t

276 e dynamically controllable via switching the folding state of Miura-ori split-ring resonators.

277 el wherein DDX1 can act as an RNA chaperone, folding stem IIB into a proper Rev binding conformation.

278 ranslocation of the C terminus of pHLIP, the folding step more directly relevant to drug delivery, oc

279 tivity, which correlates strongly with helix folding, the system we report here is also highly amenab

280 defining the functions of CTCF in chromosome folding, these results provide new fundamental insights

281 By making a direct connection to protein folding, this analysis provides strong evidence that man

282 lding processes extending from nascent chain folding to protein disaggregation.

283 Several different strand-folding topologies have been reported for Q-quadruplexes

284 IDPs, unlike natively folded proteins, have folding trajectories that frequently involve movements u

285 As force hinders the folding transition, chaperones must play a role in this

286 te structures and a mechanistic model of the folding transitions from native (N) to molten globule (M

287 monitoring the rates of individual subdomain folding transitions in situ, in the context of the whole

288 dopt non-native geometries during synthesis, folding, transport, and turnover.

289 cenario, although their influence on protein folding under force has not been directly monitored yet.

290 as a mechanical foldase by promoting protein folding under force.

291 ighlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the

292 a distributed computing network to study the folding, unfolding, misfolding and conformational plasti

293 functionality that is comparable to protein folding/unfolding.

294 oach to map single-chain nanoparticle (SCNP) folding via high-resolution electrospray ionization mass

295 poral dependence of diffusion anisotropy and folding were distinct from the patterns observed for cer

296 response of the cellular metamaterial during folding were studied to investigate the underlying mecha

297 active model of chaperonin-mediated protein folding, where partial unfolding of misfolded intermedia

298 erstood are the very early stages of protein folding, which are likely defined by intrinsic local int

299 experiments reveal the initial nucleation of folding while simulations corroborate these stable core

300 functional configuration through incremental folding with many intermediate steps in the folding path