ライフサイエンスコーパス: protein folding

1 tions modulate ribosome speed and facilitate protein folding.

2 th translation kinetics, and cotranslational protein folding.

3 o rethink the structure-function paradigm of protein folding.

4 such as those transiently accumulated during protein folding.

5 nse signaling in addition to enhancing viral protein folding.

6 ic, without perturbation of the mechanism of protein folding.

7 on, and TRAP1, which regulates mitochondrial protein folding.

8 he most puzzling and fascinating features of protein folding.

9 dase II (GlucII), and that vIL-6 can promote protein folding.

10 ded by the physical principles that underlie protein folding.

11 d to derive a simplified energy landscape of protein folding.

12 f genes related to programmed cell death and protein folding.

13 drophobic effect is a major driving force in protein folding.

14 to be involved in splicing, translation and protein folding.

15 atic changes in local structure required for protein folding.

16 o called molten globules (MG), to understand protein folding.

17 have evolved to allow efficient and accurate protein folding.

18 at molecular forces drive chaperone-mediated protein folding.

19 e by preventing aggregation and by aiding in protein folding.

20 lpG amenable to in vitro studies of membrane-protein folding.

21 40) cochaperone, assists with Hsp70-mediated protein folding.

22 n genetic codons to regulate cotranslational protein folding.

23 e, the recognition process must also involve protein folding.

24 onformation, besides a moderate loosening of protein folding.

25 rities between molecular crystallization and protein folding.

26 odulate translation rate and thus can affect protein folding.

27 for comparing experiments and simulations of protein folding.

28 condary structure elements in the control of protein folding.

29 es and supports Kauzmann's 1959 mechanism of protein folding.

30 ic ring structures that provide a cavity for protein folding.

31 nclude disulfide bonding in the MD models of protein folding.

32 sis is inherently coupled to cotranslational protein folding.

33 roES, are essential molecular chaperones for protein folding.

34 own to regulate protein complex assembly and protein folding.

35 ribosomes and nascent polypeptides to assist protein folding.

36 re involved in glycan processing and nascent protein folding.

37 chaperonin), a complex known to function in protein folding.

38 conjugation, sporulation, and outer membrane protein folding.

39 may function in protein complex assembly and protein folding.

40 eotide exchange factor (NEF) to regulate the protein folding activity of Hsp70.

41 sts of eight non-identical subunits, and its protein-folding activity is critical for cellular health

42 tablish a sequence-encoded interplay between protein folding, aggregation, and degradation; and highl

43 h as ligand binding, enzymatic catalysis, or protein folding, allosteric regulation of protein confor

44 ffects on modulating the energy landscape of protein folding and (ii) qualitatively predict the kinet

45 needed to understand their contributions to protein folding and amide effects on aqueous processes a

46 ructure to show the residues critical to the protein folding and are available for quick reference.

47 e the consequences of this heterogeneity for protein folding and assembly as well as host-cell adhesi

48 es in using NMR spectroscopy for analysis of protein folding and assembly in cells.

49 Water is essential for protein folding and assembly of amyloid fibrils.

50 roning is a robust mechanism for heteromeric protein folding and assembly that could also be applied

51 ith Hofmeister salts KF and K2SO4 in driving protein folding and assembly.

52 Proteins associated with protein folding and autophagy were the largest group rep

53 out mechanisms and transition states (TS) of protein folding and binding is obtained from solute effe

54 l protein complexes involved in translation, protein folding and carbohydrate metabolism.

55 lated genes in apoptosis, and down-regulated protein folding and cell cycle-related genes.

56 H723R (His723Arg), which leads to defects in protein folding and cell-surface expression.

57 s (PDIs) support endoplasmic reticulum redox protein folding and cell-surface thiol-redox control of

58 simulations of biomolecular dynamics such as protein folding and conformational change.

59 lly "in vitro" experiments, e.g. analysis of protein folding and conformational transitions, be done

60 ion of phenomenological similarities between protein folding and crystallization.

61 olded protein response (UPR), which elevates protein folding and degradation capacity and attenuates

62 quality control by dynamically coordinating protein folding and degradation.

63 However, the generalized protein folding and design problem is unsolved.

64 Hsp70 aids in protein folding and directs misfolded proteins to the ce

65 rotein quality control (PQC) system monitors protein folding and eliminates misfolded proteins throug

66 Protein N-glycosylation (PNG) is crucial for protein folding and enzymatic activities, and has remark

67 ayer is essential for understanding membrane protein folding and for predicting membrane protein stru

68 ins are essential both for the mechanisms of protein folding and for the function of the large group

69 structural information toward understanding protein folding and function.

70 y constrained by the consequent challenge to protein folding and function.

71 tates, which can play critical roles in both protein folding and function.

72 of Cox15 suggests these two mutations affect protein folding and heme binding, respectively.

73 lp to explore certain fundamental aspects of protein folding and is potentially relevant for manufact

74 hus, GPI anchor remodeling is independent of protein folding and leads to efficient ER export of even

75 Disturbances in protein folding and membrane compositions in the endopla

76 The balance between protein folding and misfolding is a crucial determinant

77 wide-ranging career began with the study of protein folding and molecular chaperones, and she went o

78 These events range from protein folding and molecular recognition to the formati

79 position 76 was found to strongly impact on protein folding and oligomerization by altering the hydr

80 Perturbations of protein folding and organelle crosstalk have been implic

81 of hydrocarbon and amide surfaces buried in protein folding and other biopolymer processes and trans

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

83 s may provide an important driving force for protein folding and protein-protein interaction, two ope

84 e protein-disulfide isomerase involved in ER protein folding and quality control, is secreted and int

85 ic reticulum (ER) is closely associated with protein folding and quality control.

86 heterozygous for SOST mutations that impair protein folding and secretion.

87 zers to study the influence of chaperones on protein folding and show that the ribosomal chaperone tr

88 hese results have important implications for protein folding and stability under different environmen

89 Disulfide bonds play an important role in protein folding and stability.

90 ts, which are widely employed to investigate protein folding and stability.

91 for the making proteome-wide measurements of protein folding and stability.

92 ment of new computational methods predicting protein folding and stability.

93 ys showed that the propeptide contributes to protein folding and stability.

94 g is a major contributing factor in membrane protein folding and stability.

95 present evidence that it may participate in protein folding and steroid-binding site formation.

96 a useful reaction coordinate to characterize protein folding and that intrinsic extensions of protein

97 the critical role of secondary structures in protein folding and the dependence of folding propensiti

98 How cotranslational protein folding and the rate of synthesis are linked to

99 ng processing of Hsp70-bound clients through protein folding and translocation pathways.

100 1)H NMR to probe the energy landscape in the protein folding and unfolding process.

101 There are robust trends in the rates of protein folding and unfolding; both modern RNases H evol

102 lfide links are absolutely required to allow protein folding and, conversely, that protein folding oc

103 simulations now allow us to create movies of proteins folding and unfolding.

104 re pivotal modulators of cellular signaling, protein folding, and gene transcription.

105 biological processes such as ligand binding, protein folding, and hydration.

106 EU3 involvement in the cell stress response, protein folding, and intracellular trafficking.

107 but also pathways of conformational change, protein folding, and protein-protein association.

108 x with GlucII and UGGT1, that vIL-6 promotes protein folding, and that VKORC1v2, UGGT1, and vIL-6 int

109 ns of DEPs included roles in photosynthesis, protein folding, antioxidant mechanism and metabolic pro

110 ailed structural studies of co-translational protein folding are now beginning to emerge; such studie

111 ical steps leading to the current concept of protein folding as a highly organized cellular process.

112 ualization of biological networks identified protein folding as the major cellular process affected b

113 ecular molar volume was caused by changes in protein folding, as was revealed by differential deuteri

114 terisation show that these mutations perturb protein folding, assembly or polarity of secretion of C1

115 ral angle fluctuations dictate the course of protein folding, binding, assembly, and function.

116 zyme-substrate active complex formation, and protein folding-binding interactions.

117 The essential biological properties of proteins-folding, biochemical activities, and the capaci

118 HSP90 acts as a protein-folding buffer that shapes the manifestations of

119 after partial hepatectomy (PH) increases the protein folding burden at the endoplasmic reticulum of r

120 bilayers play an important role in membrane protein folding but quantification of the strength of th

121 from the process of dissolution in water to protein folding, but its origin at the fundamental level

122 not only allows us to dissect the process of protein folding, but will also help in the designing of

123 such as trimethylamine N-oxide (TMAO) favor protein folding by being excluded from the vicinity of a

124 e that prevents protein aggregation and aids protein folding by binding to hydrophobic peptide domain

125 anslating codons can enhance cotranslational protein folding by helping to avoid misfolded intermedia

126 Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-dependent mov

127 imental studies have firmly established that protein folding can be described by a funneled energy la

128 sequence, the optimum frustration regime for protein folding can be predicted analytically.

129 lar chaperones, and she went on to show that protein folding can have profound and unexpected biologi

130 ed protein response (UPR) adjusts the cell's protein folding capacity in the endoplasmic reticulum (E

131 tein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (E

132 and lipid biosynthesis enzymes that increase protein-folding capacity in response to demand.

133 ic demand, and oxidative stress, disturb the protein-folding capacity of the endoplasmic reticulum (E

134 To adjust and match the protein-folding capacity of the endoplasmic reticulum (E

135 chloride homeostasis in the ER disrupts the protein-folding capacity of the ER, leading to eventual

136 unfolded protein response (UPR) increases ER-protein-folding capacity to restore protein-folding home

137 ndrance to water and urea, and/or changes in protein folding caused by mismatching of side chains in

138 lved in diverse cellular processes including protein folding, cell wall organisation, sexual reproduc

139 whose activities include an ATP-independent protein folding chaperone.

140 The protein-folding chaperone Hsp90 has been proposed to buf

141 olism, metabolic reprogramming, increases in protein folding competency, and ER expansion/remodeling.

142 CPMG-RD captured a low populated protein-folding conformation triggered by the Glu-145 re

143 mutation, indicating that a model akin to a protein-folding contact order model will not suffice to

144 whether acetylation-dependent mitochondrial protein folding contributes to this regulatory discrepan

145 Enhancing protein folding could be a potential interventional appr

146 an activator of central pathways controlling protein folding, degradation and oxidative stress resist

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

148 y in the endoplasmic reticulum that controls protein folding/degradation in response to high temperat

149 to ion-induced changes in forces that govern protein folding, delineating the underlying mechanism of

150 The UPR also reduces protein folding demands in the ER by degrading mRNAs enc

151 Many protein folding diseases are intimately associated with

152 bserved phenotypes of lipid abnormalities in protein folding diseases.

153 expression of genes that are associated with protein-folding diseases in humans; thus, transcription

154 The amyloidoses are a group of protein-folding disorders in which >/=1 organ is infiltr

155 tions to increase the solution pH and induce protein folding during nanoelectrospray ionization.

156 ional protein modification that can regulate protein folding efficiency and energetics.

157 tion of the fine details and features of the protein folding energy landscape, will fuel this old fie

158 response (UPR), to maintain a productive ER protein-folding environment through reprogramming gene t

159 nmental insult or innate genetic deficiency, protein folding environments of the mitochondrial matrix

160 the nucleus to transcriptionally up-regulate protein-folding enzymes and chaperones.

161 provides a protected environment for initial protein folding events.

162 associations to coordinate co-translational protein folding, facilitate accelerated translation, and

163 ngle publication metric, the activity in the protein folding field has been declining over the past 5

164 territory of its landscape, we find that the protein folding field is still quite active and many imp

165 A longstanding debate in the protein-folding field is whether unfolding rates or fold

166 inding affinities, mutation induced globular protein folding free energy changes, and mutation induce

167 nergy changes, and mutation induced membrane protein folding free energy changes.

168 es that mimicked experimental data of single protein folding from optical tweezers.

169 ular chaperones are responsible for managing protein folding from translation through degradation.

170 A major drive in protein folding has been to develop experimental technol

171 rmediates that are sparsely populated during protein folding have been identified as key players in a

172 o, computational, and theoretical studies of protein folding have converged to paint a rich and compl

173 or folding directly, experimental studies of protein folding have not yielded such structural and ene

174 localized Hsp70 chaperone BiP contributes to protein folding homeostasis by engaging unfolded client

175 Secondary effects on protein folding homeostasis likely contribute to UPR act

176 siological, and pathological insults disrupt protein-folding homeostasis in the endoplasmic reticulum

177 ediated GSR induction to the potentiation of protein-folding homeostasis in the endoplasmic reticulum

178 eases ER-protein-folding capacity to restore protein-folding homeostasis.

179 ne and optimize conditions that favor proper protein folding in a rapid and high-throughput fashion.

180 biquitously present and required for correct protein folding in all proteomes.

181 hanism from fungi to animals that can affect protein folding in eukaryotic organisms.

182 tanding of molecular chaperones in assisting protein folding in living cells.

183 n outgrowth after nervous system injury, and protein folding in neurodegenerative diseases.

184 Da/binding immunoglobulin protein) modulates protein folding in reply to cellular insults that lead t

185 Protein folding in the cell was originally assumed to be

186 nonymous codons provide a secondary code for protein folding in the cell.

187 e equilibrium thermodynamics and kinetics of protein folding in the complex environment of living Esc

188 trient deprivation and acidification disturb protein folding in the endoplasmic reticulum (ER) and ac

189 tein disulfide isomerases (PDI) required for protein folding in the endoplasmic reticulum (ER) should

190 heat shock protein-40 chaperone required for protein folding in the endoplasmic reticulum, resulted i

191 ntext and highlights key differences between protein folding in the ER and refolding of purified prot

192 d modules participated in GroEL(SR)-mediated protein folding in vitro.

193 roEL and GroES and facilitates ATP-dependent protein folding in vivo and in vitro Proteins with very

194 he origins of cooperativity and stability in protein folding, including the balance between solvent a

195 e genes encoding ER proteins that augment ER protein folding, induced numerous oxidative stress respo

196 approaches and focus on the applications to protein folding, interactions, and post-translational mo

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

198 thodology can now determine the structure of protein folding intermediates and their progression in f

199 rly derive the conformations and energies of protein folding intermediates from single-molecule manip

200 ted findings may provide an understanding of protein folding intermediates in general and lead to a p

201 Protein folding is a central problem in biological physi

202 Protein folding is a complex process that can lead to di

203 Protein folding is a fundamental life process with many

204 In the cell, protein folding is carefully regulated; changes in foldi

205 The investigation of the mechanism of protein folding is complicated by the context dependence

206 ect of disease-causing missense mutations on protein folding is difficult to evaluate.

207 Accurate protein folding is essential for proper cellular and org

208 For secreted proteins, proper protein folding is essential not only for biological fun

209 Protein folding is in its early stages largely determine

210 Though the problem of sequence-reversed protein folding is largely unexplored, one might specula

211 Adequate protein folding is necessary for normal cell function an

212 How hydrophobicity (HY) drives protein folding is studied.

213 A fundamental question in protein folding is whether the coil to globule collapse

214 ortant structural information for this vital protein-folding machine in humans.

215 ances the operation in plant cells of the ER protein folding machinery and the PQC system.

216 ranches.Chaperonins (CPNs) are ATP-dependent protein-folding machines.

217 NACHO promotes alpha7 protein folding, maturation through the Golgi complex, a

218 aladies emanate from the failure of a mutual protein folding mechanism?

219 Understanding protein folding mechanisms and their sequence dependence

220 simulations yield unparalleled insight into protein folding mechanisms.

221 ded proteins are important for understanding protein-folding mechanisms as well as the interactions o

222 ompared with chaperones that promote soluble protein folding, membrane protein chaperones require tig

223 ply that a mechanism-based therapy promoting protein folding might also prevent ICH in patients with

224 der the differences between the many-pathway protein folding model derived from theoretical energy la

225 chaperone can use many mechanisms to aid in protein folding, most likely due to the need for most ch

226 his challenge, we reconstruct a genome-scale protein-folding network for Escherichia coli and formula

227 Protein folding occurs as a set of transitions between s

228 allow protein folding and, conversely, that protein folding occurs prior to disulfide formation.

229 fy a new proteostatic mechanism that couples protein folding of channels to forward trafficking in th

230 f what happens first within the ER, that is, protein folding or disulfide formation, we studied foldi

231 rane, AMPs may act on the cell wall, inhibit protein folding or enzyme activity, or act intracellular

232 ates, and can be readily applicable to study protein folding or protein-ligand interactions with forc

233 e binding profiles, suggesting they preserve protein folding or stability.

234 Thus, therapeutic agents ameliorating protein folding or the UPR can be considered as a potent

235 protein mimicking p.Thr185Met has defects in protein folding or trafficking.

236 regulation of protein complex formation, and protein folding, perhaps associated with remodeling of c

237 e to their utility for solving the difficult protein folding problem.

238 In order to protect the delicate protein folding process and ensure the proper cellular d

239 Protein folding process involves formation of transientl

240 d chaperones, notably involved in the gluten-protein folding process, were up-regulated in superior (

241 ell biologists showed little interest in the protein folding process.

242 interest because of their importance to the protein folding process.

243 rium for examining protein stability and the protein folding process.

244 add an additional layer of robustness to the protein-folding process by avoiding the formation of sta

245 Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain f

246 ly affect transcription, protein expression, protein folding, proteasome assembly, and, ultimately, p

247 andscape theory, developed in the context of protein folding, provides, to our knowledge, a new persp

248 even this regime is not fast enough for many protein folding reactions.

249 coupling between allosteric transitions and protein folding reactions.

250 ns isomerization," which plays a key role in protein folding, regulation, and function.

251 How chaperonins accelerate protein folding remains controversial.

252 cells against protein aggregation, assisting protein folding, remodeling protein complexes, and drivi

253 escription of the pathways and mechanisms of protein folding requires a detailed structural and energ

254 As a result, we now know that in vivo, protein folding requires assistance by a complex machine

255 For the tail region of the protein, folding requires rRNA, and association is predo

256 optosis and cell death in the 1 h group, and protein folding, response to unfolded protein and cell c

257 Prediction of protein folding, RNA-shift analysis, and proteomic analy

258 ons (or decoys) are often used for designing protein folding simulation methods and force fields.

259 The characterization of protein folding stability changes on the proteomic scale

260 ionship emerges as a result of selection for protein folding stability in divergent evolution.

261 it was not predicted to significantly alter protein folding stability, it is possible this variant l

262 ughness is an important aspect that controls protein-folding stability and kinetics.

263 aled strong induction of genes responding to protein folding stress in cells devoid of ClpP, but not

264 nication between mitochondria in response to protein folding stress in the nervous system.

265 ctive oxygen species (ROS), or mitochondrial protein folding stress, a percentage of ATFS-1 accumulat

266 Although protein-folding stress at the endoplasmic reticulum (ER)

267 In response to protein-folding stress, compartment-specific unfolded pr

268 Originally developed in the context of protein folding, structure-based models (SBMs) have sinc

269 molecular-dynamics simulations show that the proteins' folding structures are preserved in the single

270 Indeed, quantitative membrane protein folding studies are generally restricted to a ha

271 A major goal of protein folding studies is to understand the structural

272 tural information, but its implementation in protein folding studies using chemical or temperature pe

273 piece (HP35), a model protein widely used in protein folding studies.

274 of the main technical challenges of membrane protein folding studies.

275 pt, have been shown to alter cotranslational protein folding, suggesting that evolution may have shap

276 c and volumetric properties of a three-state protein folding system, comprising a metastable triple m

277 interact as co-chaperones in the Hsp70-based protein-folding system, with target recombinant secreted

278 pt can have a much greater impact on nascent-protein folding than others because they tend to be posi

279 the potential for elucidating key aspects of protein folding that are not revealed by either approach

280 a unique biological scenario associated with protein folding: The diversification of a family of fold

281 onation state of aspartic acid is coupled to protein folding; the apparent pKa of aspartic acid in th

282 By making a direct connection to protein folding, this analysis provides strong evidence

283 The prototypical chaperonin GroEL assists protein folding through an ATP-dependent encapsulation m

284 the physical basis of minimal frustration in protein folding thus remains to be elucidated.

285 , and reaction times are obtained from known protein folding time constants.

286 ing (burst phase) or simultaneously with the protein folding transition.

287 neral theory to describe the distribution of protein-folding transition paths.

288 -kappaB, ubiquitination, cytokine signaling, protein folding, type I interferon production and comple

289 n this scenario, although their influence on protein folding under force has not been directly monito

290 udy low-probability events that occur during protein folding under force.

291 or acts as a mechanical foldase by promoting protein folding under force.

292 of protons exchanged to deuterons (based on protein folding under pressure) could be observed betwee

293 y induce functionality that is comparable to protein folding/unfolding.

294 tact comparison, investigation of individual protein folding using predicted contacts, and analysis o

295 Protein folding varphi-values provide residue-resolved i

296 cal route to promote non-enzymatic oxidative protein folding via disulfide isomerization based on nat

297 Inspired by protein folding, we introduce hydrophobic interactions t

298 pport an active model of chaperonin-mediated protein folding, where partial unfolding of misfolded in

299 he ANE syndrome mutation generates defective protein folding which abrogates protein-protein interact

300 orly understood are the very early stages of protein folding, which are likely defined by intrinsic l