ライフサイエンスコーパス: mutant protein

1 (/+)) (and thus expresses both wild-type and mutant protein).

2 ty difference score between the wildtype and mutant protein.

3 results in the Doa10-dependent ERAD of this mutant protein.

4 lein, PolyQ protein, and alpha-1-antitrypsin mutant protein.

5 er expression of vIRF1, but not with a vIRF1 mutant protein.

6 ritical signaling pathways downstream of the mutant protein.

7 bly not related to circulating levels of the mutant protein.

8 orrelated with the relative stability of the mutant protein.

9 sease onset relative to mice expressing only mutant protein.

10 ne conferred resistance to triptolide on the mutant protein.

11 site of FANCA rescued the expression of the mutant protein.

12 alization of FUS, regardless of wild-type or mutant protein.

13 (WT) SP6 binds more strongly to it than the mutant protein.

14 onservation and structural properties of the mutant protein.

15 , but rather promoted the degradation of the mutant protein.

16 athway play a role in destabilization of the mutant protein.

17 cs for the treatment of tumors driven by the mutant protein.

18 rescued by overexpression of the p.Lys355Gln mutant protein.

19 potential change in the conformation of the mutant protein.

20 ched and rarely contributed to expression of mutant proteins.

21 ted increased intracellular retention of the mutant proteins.

22 he lifetime of palmitoylated monomers of the mutant proteins.

23 arise primarily from the aggregation of the mutant proteins.

24 ansferases, MMSET and SETD2, by the H3.3K36M mutant proteins.

25 res and dynamics of the ground states of the mutant proteins.

26 absence of neurodegenerative disease-causing mutant proteins.

27 the formation of autophagic vesicles for the mutant proteins.

28 aggregates, which are characteristic of ALS mutant proteins.

29 t also cleared out other misfolded rhodopsin mutant proteins.

30 nonuclear donor cells exposed to recombinant mutant proteins.

31 -throughput basis in vitro for wild-type and mutant proteins.

32 pe cadherin than for cells producing the r15 mutant proteins.

33 o target KRAS have focused on inhibiting the mutant protein; a less explored approach involves target

34 Upon overexpression, the mutant proteins accumulate at the cell surface and are l

35 C mice, suggesting a pathogenic role for the mutant protein accumulation.

36 ein mutants, we propose a model in which the mutant protein acts in a dominant negative manner on the

37 However, overexpression of these mutant proteins also caused profound, non-physiological

38 The mutant proteins also exhibit impaired glutathione bindin

39 Both mutant proteins also interact with HDCAC6 and are degrad

40 ool to study how protein phosphorylation and mutant proteins alter accessibility of myosin binding on

41 ndoplasmic reticulum (ER) degradation of the mutant protein and consequent copper accumulation in hep

42 es containing only Fis or Xis, together with mutant protein and DNA binding studies, support a mechan

43 tation experiments from cells expressing the mutant protein and from human heart tissue from two of t

44 e L176F mutant we expressed and purified the mutant protein and measured key parameters of its activa

45 at severity is increased by a double dose of mutant protein and reduced by the presence of wild-type

46 ease ER stress by inducing misfolding of the mutant protein and subsequently disrupting hypertrophic

47 conformations available to disease-relevant mutant proteins and that comprehensive drug testing of p

48 assembly of the HBV core wild-type and Y132A mutant proteins and thermostabilize the proteins with a

49 mbinase activity of naturally occurring RAG2 mutant proteins and to correlate our results with the se

50 of TBCD, indicating relative instability of mutant proteins, and defective beta-tubulin binding in a

51 d characterization of individual recombinant mutant proteins, and various in vitro and in vivo assays

52 biochemical characteristics of each of these mutant proteins are altered, which in turn could provide

53 n vitro experiments showed that the two CD36 mutant proteins are expressed and trafficked to the plas

54 In case of inherited forms of ataxia, mutant proteins are expressed throughout the brain and i

55 These results suggest that single mutant proteins are incorporated into nonproductive ICP8

56 The mutant proteins are loss-of-function and dominant-negati

57 We show that both mutant proteins are mannose-rich glycosylated proteins t

58 These mutant proteins are misfolded and turnover studies show

59 Although such mutant proteins are prone to aggregation, toxicity is al

60 We show that both recombinant AAC1 mutant proteins are severely impaired in ADP/ATP transpo

61 The study suggests that Cx31 mutant proteins are un/misfolded to cause EKV likely via

62 occluded ground states of the wild-type and mutant proteins are very similar, but the rates of excha

63 ytosolic fractions using an enzyme-dead Mdm2 mutant protein as a substrate for in vitro E3 ligase ass

64 se and a stable myocardial expression of the mutant protein as seen with E193.

65 ere lethal for virus production, because the mutant proteins assembled into tubes or sheets instead o

66 R) gene cluster on chromosome 1q32 and CFHR5 mutant proteins associate with this disease.

67 Furthermore, biochemical analysis of an ACS5 mutant protein bearing an alteration in the C-terminus i

68 perature range 35-45 degrees C, in which the mutant protein began to lose the native conformation of

69 This mutant protein blocks localization of full-length SIGIRR

70 ognizes and marks for degradation not only a mutant protein but also its wild-type variant as long as

71 hSOD1 may indirectly augment the toxicity of mutant protein by competing for protective factors, but

72 ASOs can reduce the levels of mutant proteins by breaking down the targeted transcript

73 Overexpression of these mutant proteins can give rise to disease-associated phen

74 ivity of wild-type IDH1, the R132H and R132C mutant proteins can reduce alpha-ketoglutaric acid (alph

75 of the catalytic carboxylates, we generated mutant proteins catalysing membrane potential-independen

76 Expression of the resultant mutant protein caused coloboma and microphthalmia in zeb

77 QLN2 functions in autophagy and that ALS/FTD mutant proteins compromise this function.

78 Phosphoablative and phosphomimetic FadD32 mutant proteins confirmed both the position and the impo

79 olic and biosynthetic challenges imparted by mutant protein conformers, dysfunctional subcellular org

80 The Leu129Gln CysLT2R mutant protein constitutively activates endogenous Galph

81 toylation properties of native FIV MA with a mutant protein containing a consensus feline myristoylat

82 ast showed that the residual activity of the mutant proteins correlates with the clinical phenotypes

83 ady-state abundance, whereas coexpression of mutant proteins deficient in LMO2 binding compromised LM

84 ER-associated degradation factors to promote mutant protein degradation could be beneficial for the t

85 localized predominantly in the cytoplasm and mutant proteins demonstrate similar protein levels and l

86 Transient transfection assays of the mutant protein demonstrated a 75% reduction in transacti

87 In vitro analysis of the mutant protein demonstrates that--like wild-type Vps1--i

88 cessive gain-of-function or loss-of-function mutant protein, depending on signaling context and prese

89 expressed wild-type ADAMTS9, in contrast to mutant proteins detected in individuals with NPHP-RC, lo

90 evidence supports a proteotoxic role for the mutant protein dictated in part by the specific genetic

91 S52F FOXF1 mutant protein did not bind chromatin and was transcript

92 nucleofilaments, but not RPA or Rad51(T131P) mutant proteins, directly prevent Mre11-dependent DNA de

93 orylation, and transgenic plants bearing the mutant proteins display defective DV asymmetric flower d

94 cluster in and around p97's ATPase domains, mutant proteins display normal or elevated ATPase activi

95 ALIX-1 mutant protein displays reduced interaction with VPS23A

96 The rgh3 mutant protein disrupts colocalization with a known ZRSR

97 e, coupled with functional evidence that the mutant protein disrupts galanin signaling, strongly supp

98 BRCA1 BRCT domain mutant proteins do not fold correctly and are subject to

99 show here that reduced HMGB1 binding by the mutant protein dramatically reduces RAG cutting in vitro

100 ects are conferred by destabilization of the mutant protein due to an increase in proteasomal degrada

101 expression of the acetylation-mimicking p53-mutant protein effectively suppressed K-Ras-induced PDAC

102 We find that both of the mutant proteins exhibit substantial intracellular retent

103 Most PAR3-mutant proteins exhibited a relative reduction in the ab

104 CTE-associated HAI-2 mutant proteins exhibited reduced ability to inhibit mat

105 The mutant protein exhibits even greater RNA specificity tha

106 The level of IFNAR1*557Gluext*46 mutant protein expressed in patient fibroblasts was comp

107 CYP2B6V5-Y317A, -Y380A, and -Y190A mutant proteins expressed in HuH7 cells were less sensit

108 While mutant protein expression is decreased by over 80%, KI/K

109 expressed too highly and methods that reduce mutant protein expression might form the basis for drug

110 iseases have documented the toxic effects of mutant protein expression, misfolding, and aggregation.

111 force spectroscopy, electron microscopy, and mutant protein expression, we demonstrate that phosphory

112 ance of ~250 pS, and was not due to elevated mutant protein expression.

113 Using various mutants, protein expression during spermiogenesis, and R

114 We observed that these SIRT2 mutant proteins fail to restore the replication stress s

115 with beta-catenin, and the resultant ARID1B mutant proteins fail to suppress Wnt/beta-catenin signal

116 We find that most pathogenic TREM2 mutant proteins fail to undergo normal maturation in the

117 The mutant protein failed to reduce food intake and body wei

118 Moreover, the SIRT2 mutant proteins failed to rescue the spontaneous inducti

119 The mutant protein finds its target site in 1,800 RNAs and y

120 Biochemical analyses show that R79A and S83A mutant proteins fold, assemble, and display genome matur

121 ls with pyrin and wild-type and mutated WDR1 Mutant protein formed aggregates that appeared to accumu

122 The mutant protein forms cytoplasmic inclusions when express

123 Like WT ICP8, the QF mutant protein forms filaments in vitro, binds ssDNA coo

124 On the other hand, the mutant protein from a Warsaw breakage syndrome patient f

125 S33A with a proteasome inhibitor rescued the mutant protein from degradation.

126 l surface and with enhanced exclusion of the mutant protein from virions by Nef.

127 Expression of trace amounts of mutant proteins from NMD-competent PTC-containing constr

128 mr-22 could be rescued by expressing a HMR22 mutant protein fused with the transcriptional activation

129 domain in gC and the corresponding purified mutant protein (gCDeltamuc) in cell culture and GAG-bind

130 mRNAs are potent and regulatable sources of mutant protein generation.

131 The resultant mutant protein had increased dimerization, induced eleva

132 lls, the Ail-Deltaloop 2 and Ail-Deltaloop 3 mutant proteins had no cell-binding activity while Ail-D

133 Five mutant proteins had no observable NCKX activity, whereas

134 The mutant protein has a decreased ability to activate conse

135 Transduction experiments suggest that the mutant protein has an effect on B-cell differentiation a

136 The mutant protein has both altered conformation and activit

137 f H3K36 methylation and the purified Set2sup mutant protein has greater enzymatic activityin vitro.

138 es of our preclinical models, the FLCN H255Y mutant protein has lost it tumour suppressive function l

139 However, the production of mutant proteins has not been detected and quantified in

140 Cells expressing these mutant proteins have a dramatically reduced proliferatio

141 Mechanistically, NT5C2 mutant proteins have increased nucleotidase activity as

142 st with previous studies using overexpressed mutant protein in cell lines, FPN1 could still reach the

143 ered after overexpression of Ctnnb1(DeltaE3) mutant protein in corneal keratocytes.

144 Expression of this highly stable mutant protein in Ewing cells while simultaneously deple

145 s, rapid degradation of this large misfolded mutant protein in mouse retina caused little detectable

146 loss of PAX2 and expression of the R273H p53 mutant protein in murine oviductal epithelial (MOE) cell

147 ibrosis transmembrane conductance regulator) mutant protein in the endoplasmic reticulum (ER).

148 Moreover, the nuclear localization of the mutant protein in transfected cells was significantly re

149 Studies of the mutant protein in vitro, in cell lines and in CRISPR-Cas

150 extracellular deficiency, or the presence of mutant proteins in basement membranes represents an impo

151 Transient expression of EBF3 mutant proteins in HEK293T cells revealed mislocalizatio

152 me formation, by comparison of wild-type and mutant proteins in inflammasome reconstitution experimen

153 ically have involved comparative analysis of mutant proteins in the context of reaction network model

154 2a, and Doc2b by reintroducing wild-type and mutant proteins in triple-knock-out neurons, and conclud

155 own model and heterologous expression of the mutant proteins in Xenopus laevis oocytes to measure TRE

156 neurodegenerative proteinopathy, in which a mutant protein (in this case, ATAXIN1) accumulates in ne

157 but not the wildtype claudin-16 or the T303R mutant protein increases the Trpv5 channel conductance a

158 In silico modeling of the mutant proteins indicated all alterations would destabil

159 LS)-associated superoxide dismutase 1 (SOD1) mutant protein induces changes in HSP70 and HSC70 client

160 We reintroduced mutant proteins into this genetically null background to

161 The mutant protein is considerably less active as agglutinin

162 egeneration in G70S/- mice, showing that the mutant protein is essentially non-functional.

163 type and mutant retinas, suggesting that the mutant protein is expressed at some level in mutant reti

164 ic to motor neurons in co-culture, even when mutant protein is expressed only in astrocytes and not i

165 the mutated residue, we could proof that the mutant protein is less abundant when compared with the w

166 We observed that the p53 mutant protein is more sensitive to both PRIMA-1 and MQ

167 At the permissive temperature, the Tor2 mutant protein is partially defective for binding with K

168 A His(nuc) to Ala mutant protein is reportedly inactive, whereas the autos

169 Overexpression studies confirmed that the mutant protein is secreted but neither binds to nor acti

170 isease-associated G319R Gars (G240R in GARS) mutant protein is unable to rescue the above phenotype.

171 I expression in B cells, indicating that the mutant protein is unstable when naturally expressed.

172 ession vectors showed that the PEHO syndrome mutant protein is unstable.

173 tinylation experiments demonstrated that the mutant protein is virtually absent from the plasma membr

174 Accumulation of mutant proteins is a major cause of many diseases (colle

175 isease, but gain-of-function toxicity of the mutant proteins is another possibility.

176 strictive temperature, Kog1 but not the Tor2 mutant protein, is rapidly degraded.

177 riant leads to exon 3 skipping, predicting a mutant protein known to cause human pituitary dwarfism.

178 er with the isolated N-terminal domain and a mutant protein (KpsC D160A) containing a catalytically i

179 KRAS mutations, that which encodes the G13D mutant protein (KRAS(G13D)) behaves differently; for unk

180 Surprisingly, micro1 mutant proteins lacking the basic patch and/or the tyros

181 Simultaneous expression of mutant proteins lacking these residues results in comple

182 The mutant protein lacks a highly conserved helix consisting

183 This mutant protein lacks the FEN, exonuclease (EXO) and gap

184 because of intracellular degradation of the mutant protein, leading to progressive loss of hair bund

185 The presence of mutant protein leads to reduction in endoplasmic reticul

186 Illumination of cells expressing this mutant protein led to a rapid increase in the levels of

187 All mutant proteins maintained their tetrameric conformation

188 For other diseases, a mutant protein may be expressed too highly and methods t

189 nstrated that disease-associated CLC-1 A531V mutant protein may fail to pass the endoplasmic reticulu

190 anifestations of BHD, whereas the FLCN K508R mutant protein may have a dominant negative effect on th

191 lded and toxic superoxide dismutase 1 (SOD1) mutant proteins may find application in attenuating the

192 ctor NADPH, while LBR truncations render the mutant protein metabolically unstable, leading to its ra

193 The resulting mutant protein (mHtt) with extended polyglutamine (polyQ

194 specific expression of an activated TGF-beta mutant protein, mice with heart-specific deletion of Ctg

195 Aberrantly processed or mutant proteins misfold and assemble into a variety of s

196 oligodendrocyte precursor cells showed that mutant proteins mislocalize.

197 Using a dominant-negative mutant protein of the methyl-directed mismatch repair (M

198 ivities using purified wild-type and various mutant proteins of A3F from an Escherichia coli expressi

199 tion is due to a dominant-negative effect of mutant protein on muscle contraction.

200 vels of Nkx3.1 expression and effects of the mutant protein on the prostate.

201 n is widely expressed during adult life, the mutant protein only causes the demise of selective neuro

202 ctious for naive cells expressing either the mutant protein or other PrPs with slightly different del

203 We found that the mutant proteins organized similarly to WT proteins on me

204 -containing mRNAs, indicating that truncated mutant proteins originated primarily in the pioneer roun

205 The mutant protein (p.V258M) is expressed and traffics to th

206 tations in the non-operational sextuplet Asn mutant protein partially restored CaValpha2delta1 functi

207 Our studies of mutant protein posttranslational modification and locali

208 lutamine proteins is that proteolysis of the mutant protein produces a "toxic fragment" that induces

209 single oncogenic driver gene and target its mutant-protein product (for example, EGFR-inhibitor trea

210 Topical application of Hsp90alpha-Delta mutant protein promoted wound closure as effectively as

211 The Rad54-K341R ATPase-deficient mutant protein promotes formation of synaptic complexes

212 We assessed expression of mutant protein, protein activity, and regulation of apop

213 The mutant proteins proved defective in interface 2-specific

214 Loss of these functions by the mutant proteins provides insight into disease mechanisms

215 islocalization of the nonpalmitoylated N-Ras mutant protein, reduced Raf/MEK/ERK signaling, and alter

216 the molecular dynamics trajectories of both mutant proteins relative to the wild-type.

217 These mutant proteins remain enriched at synapses in Caenorhab

218 formational changes in disease-associated or mutant proteins represent a key pathological aspect of H

219 analyzed two mouse models of ADLTE encoding mutant proteins representative of the two groups.

220 adation, and therefore, stabilization of the mutant protein represents an important therapeutic strat

221 ntaining mRNAs evade NMD, and might generate mutant proteins responsible for various diseases, includ

222 quire reduction in the expression of a toxic mutant protein resulting from a gain-of-function allele

223 2W) appeared to be conservative, because the mutant protein retained a highly favorable equilibrium c

224 s depleted of endogenous Lsm4, although this mutant protein retained the ability to assemble with Lsm

225 n and are reversed by expression of a Cyfip1 mutant protein retaining actin regulatory function or by

226 hese functions can be uncoupled, and whether mutant proteins retaining partial activity can complemen

227 ted by H. pylori The nonoligomerizing 88-kDa mutant protein retains the capacity to enter host cells

228 Further analyses of the mutant protein reveal a phosphorylation-independent role

229 Functional analyses of the mutant proteins revealed a partially compromised ability

230 uctures of the wild-type mIDH2 and the K256Q mutant proteins, revealing conformational changes in the

231 One mutant protein showed cytoplasmic accumulation indicatin

232 of the G334R-mutant tetramer, and the G334R-mutant protein showed increased preponderance of mutant

233 However, the mutant proteins showed better binding to Env CTs than th

234 with computational and experimental data on mutant protein stabilities across all types of protein r

235 rather that more subtle changes can lead to mutant proteins stable enough to exert gain-of-function

236 Investigation of mutant proteins supported the importance of this positio

237 Expression of a mutant protein that deletes both regions represses the H

238 f FMRP suppresses, and expression of an FMRP mutant protein that fails to interact with Cdh1 phenocop

239 ja1), resulting in a G60S connexin 43 (Cx43) mutant protein that is dominant negative for Cx43 protei

240 which lead to the expression of full-length mutant proteins that accumulate in cancer cells and may

241 P, like cAMP, can promote the degradation of mutant proteins that cause neurodegenerative diseases.

242 ne-string domain, however the regions of the mutant proteins that drive aggregation have not been det

243 xicity of NPM was assessed using phospho-NPM mutant proteins that either mimic stress-induced or norm

244 Mutant proteins that failed to incorporate contained del

245 ite-directed mutagenesis, we generated FOXM1 mutant proteins that localized to distinct cellular comp

246 pointed to a loss of function for the D252H mutant protein, the D252H homozygous mice were more seve

247 ome insight into the toxic properties of the mutant proteins, their role in pathogenesis remains uncl

248 if a wild-type protein is more stable than a mutant protein, then the same mutant is less stable than

249 ation of EYFP-CENP-A K124R, which allows the mutant protein to bind to HJURP.

250 The feasibility of creating mutant proteins to achieve a protein array capable of de

251 g was demonstrated by the failure of ING3PHD mutant proteins to enhance ING3-mediated DNA damage-depe

252 g and concomitantly abolishes the ability of mutant proteins to mediate antibiotic tolerance.

253 culate, might derive from the ability of the mutant proteins to sequester WT1 into unproductive oligo

254 nity for the essential zinc ion, leaving the mutant protein unable to bind the metal in the low [Zn(2

255 nese hamster ovary AP-1 cells, the Leu515Phe mutant protein was correctly targeted to the TGN/post-Go

256 1 in A-ICs, but basolateral targeting of the mutant protein was preserved.

257 Moreover, the CAV1(Y14F) mutant protein was shown to co-immunoprecipitate with PT

258 eas relaxation mediated by the D40Y and R44H mutant proteins was equal to that with WT protein.

259 in the context of pathogenic aHUS-related FH mutant proteins was investigated.

260 The generation of mutant proteins was promoted by UPF1 depletion, which in

261 mutant PKP2 (c.2203C>T), encoding the R735X mutant protein, was achieved 4 weeks after a single AAV9

262 (SsE(S178A)), an enzymatically inactive SsE mutant protein, was generated.

263 Using genetically altered mice and E2F4 mutant proteins we demonstrate that centriole amplificat

264 Using various MAP65-1 mutant proteins, we demonstrate that efficient cross-lin

265 In the purified mutant proteins, we observed corresponding opposite chan

266 mical studies, live imaging, and analyses of mutant proteins, we propose that Drd3 palmitoylation act

267 By using different Dif1 mutant proteins, we uncover that Dun1 phosphorylates Dif

268 In vitro, the mutant proteins were abnormally processed and sequestere

269 Mutant proteins were analyzed for DNA binding with the u

270 We also found that the mutant proteins were compromised for peptide binding.

271 All mutant proteins were dephosphorylated and incompletely g

272 d to Y290C, T287C, and H83C decreased as the mutant proteins were driven from the inward to the outwa

273 ecreted into the culture medium, whereas all mutant proteins were either not secreted or secreted at

274 1 was found to be easily adapted and several mutant proteins were expressed and characterised.

275 s with idiopathic PAH.Methods: Missense BMP9 mutant proteins were expressed in vitro and the impact o

276 aValpha2delta1 G1061I, suggesting that these mutant proteins were impaired in proteolytic processing.

277 As in yeast, the Bartter mutant proteins were less stable than the WT protein, an

278 tionation experiments demonstrated that EBF3 mutant proteins were less tightly associated with chroma

279 ther alone or together, and the wild type or mutant proteins were purified and tested by replicating

280 We also found that the mutant proteins were significantly less stable than WT R

281 wever, such models generally overexpress the mutant protein, which may give rise to phenotypes not di

282 cumented impaired activity of purified DNMT1 mutant proteins, which in fibroblasts results in increas

283 This expansion encodes a mutant protein whose abnormal function is traditionally

284 disease and suggests that elimination of the mutant protein will be a pre-requisite for any curative

285 the coding sequence of a gene to generate a mutant protein with altered activity or introduce frames

286 he huntingtin (HTT) gene, which results in a mutant protein with an extended polyglutamine tract.

287 f-function JAK1 genetic variant results in a mutant protein with mosaic expression that drives multi-

288 rated that immunization with CspZ-YA, a CspZ mutant protein with no FH-binding activity, protected mi

289 esults show that porB plants expressing PORB mutant proteins with Ala substitutions of Cys276 or Cys3

290 y site-directed mutagenesis that encode PORB mutant proteins with defined Cys-->Ala exchanges.

291 Functional analysis of mutant proteins with missense substitutions revealed red

292 or seizures, and found that both resulted in mutant proteins with significantly reduced but observabl

293 1 decreases the association of the resulting mutant proteins with triads.

294 Cdc42 interface on ACK, creating a panel of mutant proteins with which we can now describe the compl

295 Interaction of Nr2f2(mutant) protein with Fog2 is greater than that with the

296 Additionally, the specificity of mutant proteins, with variants of amino acids that inter

297 ining varphi-values by separately simulating mutant proteins would be computationally demanding and p

298 es point to the areas where stabilization of mutant proteins would have the greatest effect.

299 The structure of a mutant protein (Y100H/V102F) was solved in two different

300 Crystal structures of mutant proteins yielded models of the monomeric pre- and