ライフサイエンスコーパス: signal recognition particle

1 nized and targeted co-translationally by the signal recognition particle.

2 teracts directly with Ffh in assembly of the signal recognition particle.

3 acillus subtilis is the RNA component of the signal recognition particle.

4 s 7SL RNA, which is the RNA component of the signal recognition particle.

5 iculum of eukaryotes by interacting with the signal recognition particle.

6 have no effect on the GTPase activity of the signal recognition particle.

7 inding of the nascent signal sequence to the signal recognition particle.

8 ibodies for the barley 54-kDa subunit of the signal recognition particle.

9 sertion of signal peptides recognized by the signal-recognition particle.

10 de novo missense variant in srp54 (encoding signal recognition particle 54 kDa).

11 The signal recognition particle 54-kDa subunit (SRP54) binds

12 shock proteins (Hsp70 and Hsp96 precursor), signal recognition particle 72 (SRP72), and 10 different

13 autoimmune necrotizing myopathies recognize signal recognition particle and 3-hydroxy-3-methylglutar

14 o signal peptides that are recognized by the signal recognition particle and are thereby targeted to

15 did not affect the extent of binding to the signal recognition particle and association with ER memb

16 ly, NSP8 and NSP9 bind to the 7SL RNA in the signal recognition particle and interfere with protein t

17 The signal recognition particle and its receptor (SR) target

18 ncluded ATPase subunits, elongation factors, signal recognition particle and its receptor, three sets

19 A subpopulation of human signal recognition particle and mitochondrial RNA proces

20 chondrial genomes would be recognized by the signal recognition particle and targeted to the endoplas

21 luding yeast snoRNAs, the RNA subunit of the signal recognition particle and the yeast U2 spliceosoma

22 terminal signal peptides for the Sec-, SRP- (signal recognition particle), and Tat (twin arginine tra

23 Ffh (the bacterial protein component of the signal recognition particle), and the SecYEG translocon

24 ) inhibits signal peptide recognition by the signal recognition particle, and we now show that fusion

25 ittle inflammation such as the myopathy with signal recognition particle antibodies; immune myopathie

26 from idiopathic pulmonary fibrosis and anti-signal recognition particle antibody-positive myositis.

27 Although both the SecYEG machinery and signal recognition particle are required for insertion o

28 geting to the ER membrane is directed by the signal recognition particle, as demonstrated in other eu

29 the GTPase activity of the Escherichia coli signal recognition particle, as previously reported, but

30 factor in African American adults with anti-signal recognition particle autoantibodies (OR 7.5, Pcor

31 Patients with anti-signal recognition particle autoantibodies, however, did

32 ed to the presence of antisynthetase or anti-signal recognition particle autoantibodies.

33 ns, showing progressively lower affinity for signal recognition particle binding, were targeted to mi

34 es, including the ribosome, spliceosome, and signal recognition particle, but the role of RNA in guid

35 a gene encoding a component of the bacterial signal recognition particle by screening in vivo for def

36 Addition of saturating levels of signal recognition particle caused only a partial inhibi

37 Signal recognition particles, chaperones, compartmented

38 with weak similarity to the Escherichia coli signal recognition particle component Ffh, are sufficien

39 hey affected housekeeping functions, such as signal recognition particle components and ATP synthase

40 The chloroplast signal recognition particle consists of a conserved 54-k

41 The chloroplast signal recognition particle (cpSRP) and its receptor (cp

42 The chloroplast signal recognition particle (cpSRP) and its receptor, ch

43 complex that interacts with the chloroplast signal recognition particle (cpSRP) and the cpSRP recept

44 etween the 54-kDa subunit of the chloroplast signal recognition particle (cpSRP) and the pCytf nascen

45 Chloroplast signal recognition particle (cpSRP) is a heterodimer com

46 Chloroplast signal recognition particle (cpSRP) is a novel type of S

47 The chloroplast signal recognition particle (cpSRP) is a protein complex

48 l (Chl) b biosynthesis or in the chloroplast signal recognition particle (cpSRP) machinery to study t

49 ion of thylakoid proteins by the chloroplast signal recognition particle (cpSRP) posttranslational tr

50 First, LHCP interacts with a chloroplast signal recognition particle (cpSRP) to form a soluble ta

51 ay in chloroplasts employs the function of a signal recognition particle (cpSRP) to target light harv

52 Chloroplasts contain a unique signal recognition particle (cpSRP).

53 m in which the 38-kDa subunit of chloroplast signal recognition particle (cpSRP43) efficiently revers

54 ded by the 38-kDa subunit of the chloroplast signal recognition particle (cpSRP43), which uses bindin

55 The 43 kDa subunit of the chloroplast signal recognition particle, cpSRP43, is an ATP-independ

56 The signal recognition particle database (SRPDB) is maintain

57 The Signal Recognition Particle Database (SRPDB) provides al

58 The SRPDB (Signal Recognition Particle Database) offers aligned SRP

59 hondrial respiratory chain complex assembly, signal recognition particle-dependent cotranslational pr

60 m via an alternative to the cotranslational, signal recognition particle-dependent mechanism that the

61 cent chain-ribosome complexes during Sec and signal recognition particle-dependent protein translocat

62 artially translated MHC-I heavy chains after signal recognition particle-dependent transfer to the en

63 validated mutations predicted to stabilize a signal recognition particle domain.

64 in African American patients producing anti-signal recognition particle (DQA1*0102) and anti-Mi-2 au

65 The specialised signal recognition particle family guanosine 5c-triphosp

66 ically interacts with YidC and the bacterial signal recognition particle Ffh component.

67 The bacterial Sec and signal recognition particle (ffh-dependent) protein tran

68 that heat shock inhibits the release of the signal recognition particle from the endoplasmic reticul

69 The 54 kDa subunit of the signal recognition particle has to identify a diverse fa

70 mol on an independent test set involving the signal recognition particle, human U1A, PUM1, and FOX-1.

71 Signal recognition particle in chloroplasts (cpSRP) exhi

72 ein 208 (TMEM208), a putative component of a signal recognition particle-independent (SND) ER protein

73 plex plays crucial roles in targeting of the signal recognition particle-independent protein substrat

74 ignal peptides on the GTPase activity of the signal recognition particle is an artifact of the high p

75 Here, we show that the signal recognition particle is required for targeting Ta

76 chloroplast homolog of the 54 kDa subunit of signal recognition particle is required for the in vitro

77 Since the signal recognition particle is required for the insertio

78 helix, the signal sequence recognized by the signal recognition particle, is made by the ribosome.

79 o the RNA component and aggregate the entire signal recognition particle, leading to a loss of its in

80 FlhF is a signal recognition particle-like protein present in mono

81 A homologue of 19 kDa signal recognition particle locus (SRP19) was cloned and

82 gulation of 7SL RNA results in inhibition of signal recognition particle-mediated vesicular protein t

83 such as aminoacyl-transfer RNA synthetases, signal recognition particle, Mi-2, and CADM-140.

84 The second class, designated SIMIBI (after signal recognition particle, MinD, and BioD), consists o

85 stinct autoantibodies recognizing either the signal recognition particle or 3-hydroxy-3-methylglutary

86 involved in targeting and folding, like the Signal Recognition Particle or cytosolic chaperones, mus

87 lw-generated multiple sequence alignments of signal recognition particle or RNaseP orthologs from con

88 ransient, with association occurring via the signal recognition particle pathway and dissociation occ

89 routing of the scFab to the co-translational signal recognition particle pathway combined with reengi

90 The chloroplast signal recognition particle pathway precursor major phot

91 ins interact with members of the chloroplast signal recognition particle pathway through a Lys-rich C

92 own genes encoding components of the E. coli signal recognition particle pathway: ffh, ffs, and ftsY,

93 was found to be only weakly dependent on the signal recognition particle pathway: insertion was weakl

94 with ER localization being conferred by the signal-recognition particle pathway.

95 ty of the nascent protein for binding to the signal recognition particle, preferentially targets CYP2

96 ian ER membrane involves, in addition to the signal recognition particle receptor and the Sec61p comp

97 e and has been proposed to interact with the signal recognition particle receptor during targeting of

98 ith other essential components including the signal recognition particle receptor TRAM and the TRAP c

99 Most dramatically, the alpha subunit of the signal recognition particle receptor was increased over

100 e demonstrate that in Bacillus subtilis, the signal recognition particle receptor, FtsY, transiently

101 uted with purified Sec61p complex, TRAM, and signal recognition particle receptor, some substrates, s

102 ase III transcripts, pre-RNase P RNA and the signal recognition particle RNA (scR1), was more drastic

103 uch as heightened reactivity patterns in the signal recognition particle RNA about 12 nt lengths befo

104 RNA polymerase III (pol III), including the signal recognition particle RNA and an Alu RNA as report

105 n, new results indicate that biosyntheses of signal recognition particle RNA and telomerase RNA invol

106 nal folding pathways of the Escherichia coli signal recognition particle RNA and the Bacillus cereus

107 ssing small cytoplasmic RNA, a member of the signal recognition particle RNA family.

108 In contrast, signal recognition particle RNA was present at the same

109 -coding RNA genes (e.g. Alu RNA, B1 RNA, and signal recognition particle RNA) in macrophages to favor

110 ore than 100 nucleotide residues include the signal recognition particle RNA, group I intron, the Glm

111 ree nucleolus-associated small nuclear RNAs (signal recognition particle RNA, telomerase RNA and U6 R

112 to be plant specific, with the exception of signal recognition particle RNA.

113 ypeptide that associates intimately with the signal-recognition particle RNA (SRP RNA) and serves as

114 ing RNAs from Escherichia coli, RNase P RNA, signal-recognition particle RNA, and tmRNA is facilitate

115 l 44 known transfer RNAs, ribosomal RNAs and signal recognition particle RNAs could be identified.

116 The canonical pathway requires the signal recognition particle (SRP) and its cognate recept

117 ibosome to the endoplasmic reticulum via the signal recognition particle (SRP) and its membrane-assoc

118 The signal recognition particle (SRP) and its membrane-assoc

119 The signal recognition particle (SRP) and its receptor (FtsY

120 Two GTPases in the signal recognition particle (SRP) and its receptor (SR)

121 two guanosine triphosphatase (GTPase) in the signal recognition particle (SRP) and its receptor (SR)

122 The signal recognition particle (SRP) and its receptor (SR)

123 Signal recognition particle (SRP) and its receptor (SR)

124 rotein targeting reaction facilitated by the signal recognition particle (SRP) and its receptor (SR),

125 E. coli homologs of the signal recognition particle (SRP) and its receptor are e

126 The signal recognition particle (SRP) and its receptor compo

127 The mechanism by which a signal recognition particle (SRP) and its receptor media

128 The bacterial homologues of the signal recognition particle (SRP) and its receptor, the

129 rmediate during complex assembly between the Signal Recognition Particle (SRP) and its receptor.

130 major pathways: cotranslational targeting by signal recognition particle (SRP) and posttranslational

131 The universally conserved signal recognition particle (SRP) and SRP receptor (SR)

132 The signal recognition particle (SRP) and SRP receptor compr

133 ous to essential components of the mammalian signal recognition particle (SRP) and SRP receptor, resp

134 n of three GTPases: the SRP54 subunit of the signal recognition particle (SRP) and the alpha- and bet

135 Upon termination of translation, the signal recognition particle (SRP) and the nascent polype

136 We have examined the hypothesis that the signal recognition particle (SRP) and the nascent polype

137 s paradigm is provided by two GTPases in the signal recognition particle (SRP) and the SRP receptor (

138 m is mediated by the concerted action of the signal recognition particle (SRP) and the SRP receptor (

139 The SRP54 and SR alpha subunits of the signal recognition particle (SRP) and the SRP receptor (

140 ted into the endoplasmic reticulum using the signal recognition particle (SRP) and the SRP receptor,

141 membranes is regulated by two GTPases in the signal recognition particle (SRP) and the SRP receptor;

142 ignal sequences by the 54 kDa subunit of the signal recognition particle (SRP) as they emerge from th

143 mutant signal sequences fail to bind to the signal recognition particle (SRP) at the ribosome exit s

144 -> Leu and Tyr-5 --> Leu, which increase the signal recognition particle (SRP) binding, diminished MT

145 The signal recognition particle (SRP) binds to signal sequen

146 ring co-translational protein targeting, the signal recognition particle (SRP) binds to the translati

147 The universally conserved signal recognition particle (SRP) co-translationally del

148 experiments revealed that expression of the signal recognition particle (SRP) complex is essential f

149 The signal recognition particle (SRP) controls the transport

150 The signal recognition particle (SRP) cotranslationally reco

151 ER) occurs in the context of two cycles, the signal recognition particle (SRP) cycle and the ribosome

152 The signal recognition particle (SRP) delivers 30% of the pr

153 The signal recognition particle (SRP) directs integral membr

154 The signal recognition particle (SRP) directs ribosome-nasce

155 The signal recognition particle (SRP) directs translating ri

156 nes encoding the minimal conserved bacterial signal recognition particle (SRP) elements are inactivat

157 signed to identify proteins that utilize the signal recognition particle (SRP) for targeting in Esche

158 Despite conservation of the signal recognition particle (SRP) from bacteria to man,

159 f the signal sequence binding subunit of the signal recognition particle (SRP) from Thermus aquaticus

160 The signal recognition particle (SRP) GTPases Ffh and FtsY p

161 ition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblag

162 is an essential RNA-binding component of the signal recognition particle (SRP) in Archaea and Eucarya

163 The signal recognition particle (SRP) is a conserved cytosol

164 The signal recognition particle (SRP) is a ribonucleoprotein

165 The signal recognition particle (SRP) is a ribonucleoprotein

166 The Escherichia coli signal recognition particle (SRP) is a ribonucleoprotein

167 The signal recognition particle (SRP) is a ribonucleoprotein

168 The signal recognition particle (SRP) is a ribonucleoprotein

169 Signal recognition particle (SRP) is a ribonucleoprotein

170 The signal recognition particle (SRP) is a universally conse

171 The signal recognition particle (SRP) is an essential ribonu

172 The signal recognition particle (SRP) is an RNA-protein comp

173 The universally conserved signal recognition particle (SRP) is essential for the b

174 The signal recognition particle (SRP) is required for co-tra

175 fractionation experiments indicated that the signal recognition particle (SRP) is required for oleosi

176 Recent work has demonstrated that the signal recognition particle (SRP) is required for the ef

177 The RNA component of signal recognition particle (SRP) is transcribed by RNA

178 The RNA component of the signal recognition particle (SRP) is universally require

179 interact with the Alu RNA-binding subunit of signal recognition particle (SRP) known as SRP9/14.

180 The signal recognition particle (SRP) of eukaryotic cells is

181 ses, cancer, and autoantibodies specific for signal recognition particle (SRP) or 3-hydroxy-3-methylg

182 e show here that the Sec translocase and the signal recognition particle (SRP) pathway are required f

183 The signal recognition particle (SRP) pathway in chloroplast

184 The protein targeting signal recognition particle (SRP) pathway in chloroplast

185 is fundamental question, we investigated the signal recognition particle (SRP) pathway in Escherichia

186 The signal recognition particle (SRP) pathway is a universal

187 The signal recognition particle (SRP) pathway mediates co-tr

188 is homologous to the receptor protein of the signal recognition particle (SRP) pathway of membrane pr

189 een shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-transl

190 Protein targeting by the signal recognition particle (SRP) pathway requires the i

191 Using inducible mutants that block the signal recognition particle (SRP) pathway, we find that

192 Using mutations of the signal recognition particle (SRP) pathway, we found that

193 smic protein thioredoxin-1 via the bacterial signal recognition particle (SRP) pathway.

194 drophobicity routes LamB-LacZ Hyb42-1 to the signal recognition particle (SRP) pathway.

195 Signal recognition particle (SRP) plays a central role i

196 Signal recognition particle (SRP) plays a critical role

197 The evolutionarily conserved signal recognition particle (SRP) plays an integral role

198 emonstrated that signal peptides bind to the signal recognition particle (SRP) primarily via hydropho

199 We report that the 72-kDa signal recognition particle (SRP) protein, a rare target

200 The signal recognition particle (SRP) protein-targeting path

201 he disordered linker domain of the mammalian signal recognition particle (SRP) receptor and conserved

202 ants found in the screen have defects in the signal recognition particle (SRP) receptor.

203 The signal recognition particle (SRP) recognizes polypeptide

204 Signal recognition particle (SRP) recognizes signal sequ

205 We present evidence that the signal recognition particle (SRP) recognizes signal sequ

206 ty control of the 7SL ncRNA component of the signal recognition particle (SRP) required for ER-target

207 Cotranslational protein targeting by the signal recognition particle (SRP) requires the SRP RNA,

208 hat A3F specifically interacts with cellular signal recognition particle (SRP) RNA (7SL RNA), which i

209 A fraction of the signal recognition particle (SRP) RNA from human, rat, X

210 nal peptide-binding protein, SRP54, with the signal recognition particle (SRP) RNA in both archaeal a

211 The signal recognition particle (SRP) RNA is a universally c

212 Human signal recognition particle (SRP) RNA is transcribed by

213 we have investigated how the distribution of signal recognition particle (SRP) RNA within the nucleol

214 se rapidly trafficking nucleolar RNAs is the signal recognition particle (SRP) RNA, and further resul

215 ed phylogenies derived from the structure of signal recognition particle (SRP) RNA, the mRNA encoded

216 extended RNA-binding loops upon binding the signal recognition particle (SRP) RNA.

217 evidence indicates that the Escherichia coli signal recognition particle (SRP) selectively targets pr

218 The universally conserved signal recognition particle (SRP) system mediates the ta

219 cons early in translation, by the ubiquitous signal recognition particle (SRP) system.

220 Signal recognition particle (SRP) takes part in protein

221 The signal recognition particle (SRP) targeting pathway is r

222 The prokaryotic signal recognition particle (SRP) targeting system is a

223 Signal recognition particle (SRP) targets proteins for c

224 The signal recognition particle (SRP) targets proteins to th

225 TPase that comprises part of the prokaryotic signal recognition particle (SRP) that functions in co-t

226 zygous mutation in SRP72, a component of the signal recognition particle (SRP) that is responsible fo

227 The binding of signal recognition particle (SRP) to ribosome-bound sign

228 Binding of the signal recognition particle (SRP) to signal sequences du

229 ed to prevent mistargeting due to binding of signal recognition particle (SRP) to signalless ribosome

230 tifs within the ribosome tunnel and lure the signal recognition particle (SRP) to the ribosome, provi

231 ting ribosomes during their targeting by the signal recognition particle (SRP) using a site-specific

232 al dynamics and substrate selectivity of the signal recognition particle (SRP) using a thermodynamic

233 l signal peptide, which is recognized by the signal recognition particle (SRP) when nascent polypepti

234 signal sequences are first recognized by the signal recognition particle (SRP)(3,4) and then moved co

235 Signal recognition particle (SRP), a cytoplasmic ribonuc

236 One important example is the eukaryotic signal recognition particle (SRP), a cytoplasmic RNP con

237 n SRP54 is an integral part of the mammalian signal recognition particle (SRP), a cytosolic ribonucle

238 The signal recognition particle (SRP), a protein-RNA complex

239 (NAC), in regulating substrate selection by signal recognition particle (SRP), a universally conserv

240 tical in all living organisms and involves a signal recognition particle (SRP), an SRP receptor, and

241 These include the Sec, signal recognition particle (SRP), and Delta pH/Tat syst

242 erges from the ribosome, binds the cytosolic signal recognition particle (SRP), and targets the ribos

243 ing membrane proteins to YidC is mediated by signal recognition particle (SRP), and we show by site-d

244 long model protein YohP is recognized by the signal recognition particle (SRP), as indicated by in vi

245 chain complexes (RNCs), associated with the signal recognition particle (SRP), can be targeted to Se

246 in cotranslational protein targeting by the signal recognition particle (SRP), during which the SRP

247 es the binding of the signal sequence to the signal recognition particle (SRP), followed by an intera

248 Consistent with structural analysis of the signal recognition particle (SRP), highly conserved base

249 ing cotranslational protein targeting by the signal recognition particle (SRP), information about sig

250 chia coli and Bacillus subtilis involves the signal recognition particle (SRP), of which the 54-kDa h

251 The signal recognition particle (SRP), responsible for co-tr

252 induction of a dozen genes required for the signal recognition particle (SRP), SRP receptors, the tr

253 ant homology to two GTPases of the mammalian signal recognition particle (SRP), SRP54 and SRalpha.

254 e have analyzed the interactions between the signal recognition particle (SRP), the SRP receptor (SR)

255 y conserved protein-targeting machinery, the signal recognition particle (SRP), which recognizes ribo

256 some, signal sequences are recognized by the signal recognition particle (SRP), which subsequently as

257 e Methionine aminopeptidase (MetAP), and the signal recognition particle (SRP), which targets secreto

258 amB signal peptide (LamB) were targeted in a signal recognition particle (SRP)-dependent manner to ro

259 The signal recognition particle (SRP)-dependent pathway is e

260 r system containing either SecA-dependent or signal recognition particle (SRP)-dependent signal pepti

261 In signal recognition particle (SRP)-dependent targeting of

262 During the signal recognition particle (SRP)-dependent targeting of

263 The signal recognition particle (SRP)-dependent targeting pa

264 f Yarrowia lipolytica is cotranslational and signal recognition particle (SRP)-dependent, whereas tra

265 idence exists, however, for translation- and signal recognition particle (SRP)-independent mRNA local

266 FlhF, a signal recognition particle (SRP)-like GTPase, has been

267 se (GTPase) domains interact directly during signal recognition particle (SRP)-mediated cotranslation

268 a pseudo-transmembrane domain to utilize the signal recognition particle (SRP)-mediated pathway.

269 The signal recognition particle (SRP)-translocation pathway

270 nd number are influenced by FlhF, which is a signal recognition particle (SRP)-type GTPase.

271 translocation pore requires the cytoplasmic signal recognition particle (SRP).

272 ogous to the SRP54 subunit of the eukaryotic signal recognition particle (SRP).

273 e distinguished by their dependence upon the signal recognition particle (SRP).

274 tegral membrane proteins are targeted by the signal recognition particle (SRP).

275 to 4.5S RNA through its M domain to form the signal recognition particle (SRP).

276 e homology with the 7SL RNA component of the signal recognition particle (SRP).

277 sential cotranslational targeting machinery, signal recognition particle (SRP).

278 roteins are targeted cotranslationally via a signal recognition particle (SRP).

279 scent membrane and secretory proteins by the signal recognition particle (SRP).

280 ins is mediated by the universally conserved signal recognition particle (SRP).

281 indow for signal sequence recognition by the signal recognition particle (SRP).

282 The signal-recognition particle (SRP) and its receptor (SR)

283 g from the ribosome are first sampled by the signal-recognition particle (SRP), then targeted to the

284 In signal-recognition particle (SRP)-dependent protein targ

285 Signal recognition particles (SRPs) are universal ribonu

286 Signal recognition particles (SRPs) have been identified

287 Signal recognition particles (SRPs) in the cytosols of p

288 ome profiling that the conserved chloroplast signal recognition particle subunit (cpSRP54) is require

289 Other down-regulated genes included ffh (a signal recognition particle subunit) and brpA (biofilm r

290 ning the secY40 mutation with defects in the signal recognition particle targeting pathway led to syn

291 The conserved signal recognition particle targets ribosomes synthesizi

292 SEC65 gene encodes a 32 kDa subunit of yeast signal recognition particle that is homologous to human

293 In cell fractionation experiments, more signal recognition particle was bound to the endoplasmic

294 brane protein that is normally targeted by a signal recognition particle was observed.

295 Our results confirm that the signal recognition particle weakens TF's interaction wit

296 o signal peptides that are recognized by the signal recognition particle were exported inefficiently.

297 istargeting through recognition by cytosolic signal recognition particle, which preferentially intera

298 e endoplasmic reticulum is controlled by the signal recognition particle, which recognizes a hydropho

299 i homolog of the chloroplast-localized SRP43 signal recognition particle, whose occurrence and functi

300 interaction of protein SRP54M from the human signal recognition particle with SRP RNA was studied by