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 orrelated with the relative stability of the mutant protein.

3 sease onset relative to mice expressing only mutant protein.

4 ne conferred resistance to triptolide on the mutant protein.

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

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

7 l adhesion molecules in cells expressing the mutant protein.

8 inding and transactivational activity of the mutant protein.

9 xpectedly with the glycosphingolipid-binding mutant protein.

10 rkedly increases phosphatase activity of the mutant protein.

11 y interaction assays using an epitope-tagged mutant protein.

12 osis because of increased SUMOylation of the mutant protein.

13 ty difference score between the wildtype and mutant protein.

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

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

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

17 ritical signaling pathways downstream of the mutant protein.

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

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

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

21 absence of neurodegenerative disease-causing mutant proteins.

22 ched and rarely contributed to expression of mutant proteins.

23 the formation of autophagic vesicles for the mutant proteins.

24 aggregates, which are characteristic of ALS mutant proteins.

25 that substantially overexpress wild-type or mutant proteins.

26 by facilitate cytoplasmic mislocalization of mutant proteins.

27 ted increased intracellular retention of the mutant proteins.

28 beta-catenin binding sites remaining in the mutant proteins.

29 ghts pathways of altered contacts within the mutant proteins.

30 by the addition of the wild-type FUS NLS to mutant proteins.

31 he lifetime of palmitoylated monomers of the mutant proteins.

32 arise primarily from the aggregation of the mutant proteins.

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

34 ein targets the plasma membrane, whereas the mutant protein accumulates in cytoplasmic inclusion bodi

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

36 were also recovered; only a minority of the mutant proteins affected rRNA processing, ribosome assem

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 Mutant proteins altered in some of these residues show a

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

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

44 e of three model systems of disease-relevant mutant protein and peptide sequences relates to the IPOD

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 en defective recombination activity of hRAG1 mutant proteins and severity of the clinical and immunol

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

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

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

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

52 teraction in vivo and show that the purified mutant proteins are defective in physical and functional

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

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

55 These mutant proteins are misfolded and turnover studies show

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

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

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

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

60 We then assessed how stable the mutant proteins are, how efficiently they can be cross-l

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

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

63 atics approaches to identify tumour-specific mutant proteins as a major class of T-cell rejection ant

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

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

66 e of clinical relevance for the diverse ALK2 mutant proteins associated with FOP and DIPG.

67 n1, via proteasome-mediated degradation; p63 mutant proteins associated with SHFM or EEC syndromes ar

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

69 The A138T promiscuous mutant protein binds more tightly to the cognate GAATTC

70 This mutant protein blocks localization of full-length SIGIRR

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

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

73 Viable particles containing the mutant protein can be generated at the permissive temper

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

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

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

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

78 ssion of the DNA-binding deficient VP1-K519R mutant protein caused quantitative changes in floral org

79 Full-length versions of both mutant protein chains were expressed in E. coli at level

80 the first time that dominant-negative Clock mutant protein (Clock(Delta19/Delta19)) enhances plasma

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

82 re, we independently predicted the lowest 10 mutant protein conformations for each of the 11 mutants

83 The Leu129Gln CysLT2R mutant protein constitutively activates endogenous Galph

84 Virtually all encoded mutant proteins contain an odd number of cysteines.

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

86 survivin, cellular expression of a survivin mutant protein deficient in its ability to interact with

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

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

89 Biochemical characterization of the mutant protein demonstrated a defect in its ability to s

90 Analysis of different mutant proteins demonstrated that both reactions require

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

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

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

94 to the citZ 5' leader RNA in vitro, but the mutant proteins did not.

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

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

97 The rgh3 mutant protein disrupts colocalization with a known ZRSR

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

99 coupled with physiological evidence that the mutant protein disrupts potassium current inactivation,

100 Intriguingly, these mutant proteins exhibit enhanced stability in strains la

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

102 In addition, this TapA mutant protein exhibited a dominant negative effect on T

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

104 The corresponding CdaS mutant proteins exhibited a significantly increased enzy

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

106 The mutant protein exhibits even greater RNA specificity tha

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

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

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

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

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

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

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

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

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

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

119 essive family, decreased the affinity of the mutant protein for membranes that, together with the spl

120 tion or misfolding hypotheses, which require mutant protein for pathogenicity.

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

122 TWEAK mutant protein formed high molecular weight aggregates u

123 The mutant protein forms cytoplasmic inclusions when express

124 amyotrophic lateral sclerosis (ALS) and the mutant protein forms inclusions that appear to correspon

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

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

127 -adrenergic receptors activate eight Galphas mutant proteins (from a screen of 66 Galphas mutants) th

128 There was a wide range of mutant protein function.

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 However, the mutant proteins had greatly reduced ability to bind 3' a

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

134 Five mutant proteins had no observable NCKX activity, whereas

135 The mutant protein has a decreased ability to activate conse

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

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

138 Characterization of these mutant proteins has provided insights into mechanisms of

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

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

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

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

143 possibility that targeting expression of the mutant protein in skeletal muscle, instead of the nervou

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

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

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

147 However, retention of mutant proteins in podosomes was significantly impaired

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

149 ity and characterized gene regulation by the mutant proteins in transgenic abi3 mutant Arabidopsis pl

150 ote distinct aggregation trends observed for mutant proteins in vitro and in ALS patients.

151 We expressed the ALS-linked profilin 1 mutant proteins in yeast, demonstrating a loss of protei

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

153 Here we show that both mutant proteins, in contrast to the wild-type variants,

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

155 Functional analysis of mutant proteins indicates that myosin-Va works as a tran

156 -like protein tyrosine phosphatase T (PTPRT) mutant proteins induces STAT3 phosphorylation and cell s

157 Even in the presence of wild-type TapA, the mutant protein inhibited fiber assembly in vitro and del

158 The GFI1B mutant protein inhibited nonmutant GFI1B transcriptional

159 Both functional and nonfunctional YscO mutant proteins interacted with SycD, indicating that th

160 Structural Kinetic and Energetic Database of Mutant Protein Interactions (SKEMPI).

161 We reintroduced mutant proteins into this genetically null background to

162 s, like the wild-type SEI protein, the sei-1 mutant protein is able to bind CArG-boxes and can form h

163 The mutant protein is considerably less active as agglutinin

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

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

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

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

175 ating AML and other cancers by targeting IDH mutant proteins, it remains unclear how these mutants af

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

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

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

179 The mutant protein lacks a highly conserved helix consisting

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

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

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

183 All mutant proteins maintained their tetrameric conformation

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

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

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

187 dex patient's fibroblasts suggested that the mutant protein may reduce the efficiency of mitochondria

188 se sarcomere mutations suggests that certain mutant proteins may be more or less stable or incorporat

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

190 l alterations of disk membrane properties by mutant proteins may lead to increased OS rigidity and th

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

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

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

194 oligodendrocyte precursor cells showed that mutant proteins mislocalize.

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

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

197 ous system characterized by the formation of mutant protein oligomers/aggregates.

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

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

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

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

202 The mutant protein possessed undetectable enzymatic activity

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

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

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

206 amyotrophic lateral sclerosis (ALS) make the mutant protein prone to aggregation.

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

208 The mutant proteins proved defective in interface 2-specific

209 tation-specific manner, with the fraction of mutant protein ranging from 30% to 84%.

210 While a majority of the 38 mutant proteins recovered decrease the accuracy of trans

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

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

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

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

215 Murine T-ALLs expressing second site mutant proteins restored full oncogenic Ras activity thr

216 o; however, mutator complexes containing the mutant protein retain the ability to synthesize siRNAs i

217 2W) appeared to be conservative, because the mutant protein retained a highly favorable equilibrium c

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

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

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

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

222 Studies using mutant proteins reveal that the formation of PP5.ERK1 an

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

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

225 disease-causing proteins, due to either the mutant protein's resistance to degradation or overexpres

226 NT5C2 mutant proteins show increased nucleotidase activity in

227 One mutant protein showed cytoplasmic accumulation indicatin

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

229 Enzymatic analysis of mutant proteins showed that base substitutions conferred

230 al analysis of purified loss-of-PBC-function mutant proteins showed that the mutations did not alter

231 We found that the p53(25,26,53,54) mutant protein stabilized and hyperactivated wild-type p

232 The deliberate synthesis of mutant proteins suggests that some of these proteins can

233 Investigation of mutant proteins supported the importance of this positio

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

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

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

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

238 minant-negative (ODN) phenotypes to identify mutant proteins that disrupt function in an otherwise wi

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

240 Mutant proteins that failed to incorporate contained del

241 Proteinopathies such as ALS involve mutant proteins that misfold and activate the heat shock

242 Furthermore, A27 mutant proteins that retained partial activity to intera

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

244 th the short DNAs, binding of the C-terminal mutant protein to M13 ssDNA showed a clear lack of coope

245 PAM-1/H3A, with no detectable return of the mutant protein to secretory granules.

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

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

248 we analyze the binding of the wild-type and mutant proteins to short oligomeric and longer genomic s

249 PLA1 activation and caused a failure of VipD mutant proteins to target to Rab5-enriched endosomal str

250 could be incorporated either during or after mutant protein translation.

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

252 and in stably transfected preadipocytes the mutant protein was associated with smaller lipid droplet

253 Kinase activity of the CLP1 mutant protein was defective, and the tRNA endonuclease

254 Although the mutant protein was efficiently incorporated into virus-l

255 While expression of the PI4P-binding mutant protein was expected to inhibit HCV replication,

256 A C-terminal deletion mutant protein was generated to aid in understanding the

257 1 in A-ICs, but basolateral targeting of the mutant protein was preserved.

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

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

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

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

262 Using a panel of mutant proteins, we identify interactions between active

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

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

265 dies indicated that expression levels of the mutant protein were lower than wild-type protein, and in

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

267 This indicated that monoglucosylated mutant proteins were actively extracted from the calnexi

268 Mutant proteins were analyzed for DNA binding with the u

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

270 All mutant proteins were dephosphorylated and incompletely g

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

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

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

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

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

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

277 Furthermore, the mutant proteins were purified, and the in vitro PIP2 hyd

278 Rac1(S71A) and Rac1(K166R) mutant proteins were resistant to FBXL19-mediated ubiqui

279 brillin-1-binding site intact, none of these mutant proteins were secreted from their producing cells

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

281 Ac-GlcNAc(Hex)2-(SQ-Hex)6 in contrast to the mutant protein, which contained the shorter form GlcNAc2

282 mis, misexpression of the ABA insensitive1-1 mutant protein, which dominantly inhibits ABA signaling,

283 c mice with neuronal dominant-negative A-FOS mutant protein, which has no binding affinity for the AP

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

285 ying these recalcitrant and complex BCR-ABL1 mutant proteins while unveiling unique mechanisms of esc

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

287 y 2 had a missense mutation, which created a mutant protein with an unpaired cysteine residue.

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

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

290 phila RB-related protein Rbf1; surprisingly, mutant proteins with enhanced stability were less, not m

291 Functional analysis of mutant proteins with missense substitutions revealed red

292 e the molecular consequences of such complex mutant proteins with regards to TKI resistance, we deter

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

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