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

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

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

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

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

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

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

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

8 nized and targeted co-translationally by 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 The signal recognition particle and its receptor (SR) target

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

36 Signal recognition particles, chaperones, compartmented

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

54 The signal recognition particle database (SRPDB) is maintain

55 The Signal Recognition Particle Database (SRPDB) provides al

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

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

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

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

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

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

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

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

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

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

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

67 Signal recognition particle in chloroplasts (cpSRP) exhi

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

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

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

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

72 Since the signal recognition particle is required for the insertio

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

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

75 cteria have a homologue or homologues of the signal recognition particle-like chaperone Ffh.

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

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

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

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

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

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

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

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

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

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

86 The chloroplast signal recognition particle pathway precursor major phot

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

142 The signal recognition particle (SRP) controls the transport

143 The signal recognition particle (SRP) cotranslationally reco

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

145 The signal recognition particle (SRP) delivers 30% of the p

146 The signal recognition particle (SRP) directs integral membr

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

148 The signal recognition particle (SRP) directs translating ri

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

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

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

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

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

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

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

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

157 The signal recognition particle (SRP) is a ribonucleoprotein

158 The signal recognition particle (SRP) is a ribonucleoprotein

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

160 The signal recognition particle (SRP) is a ribonucleoprotein

161 The signal recognition particle (SRP) is a ribonucleoprotein

162 Signal recognition particle (SRP) is a ribonucleoprotein

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

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

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

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

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

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

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

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

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

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

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

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

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

176 The signal recognition particle (SRP) pathway in chloroplast

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

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

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

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

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

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

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

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

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

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

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

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

189 Signal recognition particle (SRP) plays a critical role

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

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

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

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

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

195 The signal recognition particle (SRP) recognizes polypeptide

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

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

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

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

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

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

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

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

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

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

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

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

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

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

210 Signal recognition particle (SRP) takes part in protein

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

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

213 Signal recognition particle (SRP) targets proteins for c

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

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

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

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

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

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

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

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

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

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

224 Signal recognition particle (SRP), a cytoplasmic ribonuc

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

240 the ER membrane require the function of the signal recognition particle (SRP), suggesting that an al

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

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

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

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

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

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

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

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

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

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

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

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

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

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

255 The signal recognition particle (SRP)-translocation pathway

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

271 Signal recognition particles (SRPs) are universal ribonu

272 Signal recognition particles (SRPs) have been identified

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

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

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

276 The conserved signal recognition particle targets ribosomes synthesizi

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

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

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

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

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

282 ti-OJ, anti-EJ, anti-KJ, anti-tRNA, and anti-signal recognition particle) were equally distributed am

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

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

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

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