ライフサイエンスコーパス: nucleoprotein

1 Ebola virus proteins, most notably the viral nucleoprotein.

2 senger RNA that encodes Marburg virus (MARV) nucleoprotein.

3 infection by influenza expressing a variant nucleoprotein.

4 er express the same or an altered version of nucleoprotein.

5 ral polymerase, and many copies of the viral nucleoprotein.

6 m Tau protein and N(TAIL) from measles virus nucleoprotein.

7 capsid, but also acts as a chaperone for the nucleoprotein.

8 of VP24 and VP35 to alternate copies of the nucleoprotein.

9 ssays targeting Ebola virus glycoprotein and nucleoprotein.

10 AM134B resulted in 80% of cells positive for nucleoprotein.

11 t peptides belonging to the viral matrix and nucleoproteins.

12 ts, the viral polymerase, and multiple viral nucleoproteins.

13 VHHs uniquely specific for their respective nucleoproteins.

14 ike domains from PRX and its homologue AHNAK nucleoprotein 2 (AHNAK2).

15 vel of nonneutralizing, cross-reactive pH1N1 nucleoprotein Abs following the primary PR8 infection.

16 ng T cells, including cells specific for the nucleoprotein absent from the vaccine, were induced.

17 nza-derived epitopes (D(b)NP(366), influenza nucleoprotein amino acid residues 366-374; D(b)PA(224),

18 allenge, while vaccination with MVA encoding nucleoprotein, an internal viral protein, was not.

19 enza A virus (FLUAV) are encapsidated by the nucleoprotein and associated with RNA polymerase, posing

20 ecognized by the respiratory syncytial virus nucleoprotein and compatible with weak interactions requ

21 ed lower affinity of 627E-containing PB2 for nucleoprotein and is increased by further nucleocapsid i

22 Notably, the rapid accumulation of viral nucleoprotein and matrix (M) gene RNA in chicken and duc

23 novirus or MVA, expressing Influenza A virus nucleoprotein and matrix protein 1, induced antigen-spec

24 a set of diverged homologs of the influenza nucleoprotein and measuring the effects on stability.

25 her RdRP subunits (PB1 and PA) and the viral nucleoprotein and neuraminidase, as well as 171 cellular

26 al studies on isolated DNA, polynucleotides, nucleoprotein and nucleohistone complexes.

27 e-sense RNA genomes that are encapsidated by nucleoprotein and other viral proteins to form a helical

28 M) protein gene is identical to those of the nucleoprotein and phosphoprotein genes except that it co

29 can utilize its viral proteins, such as the nucleoprotein and phosphorylation protein, to subvert th

30 sive human protein interactome of arenavirus nucleoproteins and uncovers a potent antiviral host prot

31 tic diversity in the viral hemagglutinin and nucleoprotein, and (iii) intrahost viral evolution conti

32 utation evolutionary trajectory of influenza nucleoprotein, and also introduced each mutation individ

33 l studies of oligomerized, RNA-encapsidating nucleoprotein, and cryo-electron microscopy of nucleocap

34 matrix protein VP40 to the C terminus of the nucleoprotein, and rigidified by binding of VP24 and VP3

35 n (H3 numbering), I109T in the gene encoding nucleoprotein, and T10I in the gene encoding neuraminida

36 ling during spermiogenesis is not limited to nucleoproteins as part of the nucleoprotein exchange.

37 ze parameters and internal organization of a nucleoprotein assembly formed by the mycobacterial chrom

38 sus (SLE), immune complexes (ICs) containing nucleoprotein autoantigens activate plasmacytoid dendrit

39 n molecule that binds to apoptotic cells and nucleoprotein autoantigens and Fcgamma receptors (Fcgamm

40 fect of CRP on PDC and monocyte responses to nucleoprotein autoantigens and ICs.

41 trated label-free optical detection of viral nucleoprotein binding to a polyvalent anti-influenza apt

42 include cell-cell and cell-matrix adhesions, nucleoprotein bodies, and cell signaling platforms.

43 whereas MDA5 and LGP2 specifically bound MV nucleoprotein-coding region.

44 eeded for molecular assembly of a high-order nucleoprotein complex and for ParB spreading.

45 partitioning mechanism, ParB proteins form a nucleoprotein complex at parS sites.

46 The intasome, a higher-order nucleoprotein complex composed of viral integrase (IN) a

47 rative DNA binding does not require a unique nucleoprotein complex configuration, and that transcript

48 Transposition requires the assembly of a nucleoprotein complex containing all four Tns proteins a

49 some of the models proposed in H-NS-mediated nucleoprotein complex formation.

50 ranscription and in the establishment of the nucleoprotein complex formed at telomeres.

51 ntributes to the formation of the beta-clamp nucleoprotein complex on origin DNA.

52 suggest that a specific DNA geometry of the nucleoprotein complex stabilized on concomitant binding

53 able double-strand breaks and form an active nucleoprotein complex that can nick DNA substrates in tr

54 nals and the DNA is the chromatin, a dynamic nucleoprotein complex that helps to mediate gene regulat

55 Chromatin is the nucleoprotein complex that protects and compacts eukaryo

56 integrase (IN) functions within the intasome nucleoprotein complex to catalyze insertion of viral DNA

57 In this nucleoprotein complex, CTIP2 significantly represses the

58 li chromosome is folded into a self-adherent nucleoprotein complex, or alternately is a confined but

59 nses non-target DNA, forming a tightly bound nucleoprotein complex.

60 enhanced Raman (SERS) spectra of the aptamer-nucleoprotein complex.

61 rB dimers tetramerize to form a higher order nucleoprotein complex.

62 th the protein and DNA components of a large nucleoprotein complex.

63 ules are tightly compacted into a dynamic 3D nucleoprotein complex.

64 ted for knowledge-based design of long-range nucleoprotein complexes and purposeful manipulation of t

65 A more detailed understanding of these nucleoprotein complexes and the host factors with which

66 inspires speculation about the links between nucleoprotein complexes and the origins of viruses.

67 Telomeres are the nucleoprotein complexes at eukaryotic chromosomal ends.

68 croscopic interactions between or throughout nucleoprotein complexes by microscopically altering wrap

69 Telomeres are nucleoprotein complexes comprising telomeric DNA repeats

70 and observed intramolecular condensation of nucleoprotein complexes exceeding expectations based on

71 dinated manner to facilitate assembly of the nucleoprotein complexes into a state that is more access

72 eaction chemistries and architectures of the nucleoprotein complexes involved.

73 al assays, we explored the formation of H-NS nucleoprotein complexes on circular DNA molecules having

74 portant function in serving as a hub to form nucleoprotein complexes on DNA and RNA.

75 t the same way that RecBCD disrupts isolated nucleoprotein complexes on otherwise naked DNA.

76 h the formation of large membrane-associated nucleoprotein complexes physically occludes assembly of

77 nd Fis to assemble two distinct, very large, nucleoprotein complexes that carry out either integrativ

78 Telomeres are specialized nucleoprotein complexes that comprise the ends of linear

79 e novel ATMSI4-associated proteins help form nucleoprotein complexes that determine pleiotropic funct

80 aryotic chromosomes are capped by telomeres, nucleoprotein complexes that prevent chromosome end-to-e

81 Telomeres are macromolecular nucleoprotein complexes that protect the ends of eukaryo

82 Telomeres are nucleoprotein complexes that protect the ends of linear

83 Telomeres are nucleoprotein complexes that reside at the ends of linea

84 er that can mediate either wrapped or looped nucleoprotein complexes to provide the cooperative and c

85 equired for processing protein substrates in nucleoprotein complexes, and that Lon may help regulate

86 s helix is weak and requires the assembly of nucleoprotein complexes, thus establishing a mechanism f

87 ith the formation of larger, poorly defined, nucleoprotein complexes.

88 ring structures that constrict around viral nucleoprotein complexes.

89 structural dynamics and mechanochemistry in nucleoprotein complexes.

90 caps consisting of evolutionarily conserved nucleoprotein complexes.

91 trolled by elaborate, topologically-defined, nucleoprotein complexes.

92 form a conical core that protects the viral nucleoprotein complexes.

93 the cell to separate DNA duplexes or remodel nucleoprotein complexes.

94 nteractions to the combinatorial assembly of nucleoprotein complexes.

95 e the structural dynamics of DNA and diverse nucleoprotein complexes.

96 om the disordered carboxy-terminal region of nucleoprotein-core links nucleoprotein oligomerization,

97 iferase, or influenza virus hemagglutinin or nucleoprotein) could decrease, while the RepRNA structur

98 rg virus shows that the N-terminal region of nucleoprotein defines the inner diameter of the Ebola vi

99 Vaccination with nucleoprotein delivered with a universally used and safe

100 t differences in the polymerase proteins and nucleoprotein determined the altered virulence.

101 one antibody had the capacity to capture the nucleoprotein directly in lysis buffer used for releasin

102 ex translocation-based activities, including nucleoprotein displacement, strand separation (unwinding

103 This work demonstrates that nucleoprotein does not regulate the initiation and termi

104 role in EBOV transcription initiation at the nucleoprotein (eNP) gene, with additional roles in the r

105 (+) T cell response to an H-2D(b)-restricted nucleoprotein epitope (NP366) is characterized by prefer

106 aint a coherent portrait of epistasis during nucleoprotein evolution, with stabilizing mutations perm

107 responses to influenza A matrix protein and nucleoprotein ex vivo in 166 Dutch individuals (mean age

108 not limited to nucleoproteins as part of the nucleoprotein exchange.

109 human RAD51 (HsRAD51) recombinase can form a nucleoprotein filament (NPF) on double-stranded DNA (dsD

110 itiation of HR requires RAD51, which forms a nucleoprotein filament (NPF) that catalyzes homologous p

111 A when bound to single-stranded (ss)DNA as a nucleoprotein filament (RecA*).

112 , which stimulates ATP turnover in the Rad51 nucleoprotein filament and causes dissociation of Rad51

113 tes, implicating the remodelling of the H-NS nucleoprotein filament and the subsequent restoration of

114 DNA breaks, RAD51 recombinase assembles as a nucleoprotein filament around single-stranded DNA to for

115 rationalized in terms of the formation of a nucleoprotein filament followed by a structural rearrang

116 H-NS DNA-stiffening mode caused by nucleoprotein filament formation is able to suppress DNA

117 t interacts with RAD51 and facilitates RAD51 nucleoprotein filament formation on single-stranded DNA

118 two different mechanisms, modifies the RAD51 nucleoprotein filament formation, and allows RAD51 to co

119 versely, when the length of the ssDNA in the nucleoprotein filament is increased, homology is found f

120 timulatory effect is not the result of RAD51 nucleoprotein filament stabilization; rather, we demonst

121 The active form of RAD51 is a nucleoprotein filament that assembles on single-stranded

122 RAD51 can polymerize on DNA to form a nucleoprotein filament that facilitates both the search

123 The nucleoprotein filament then invades homologous DNA to dr

124 es is an ability to stabilize the Rad51/Dmc1 nucleoprotein filament, and we propose that it is this p

125 tion affects FBH1 interaction with the RAD51 nucleoprotein filament, but not its translocase and heli

126 The resulting nucleoprotein filament, known as the presynaptic complex

127 ication fork and its interactions with RAD51 nucleoprotein filament.

128 s of human RAD51 and properties of the RAD51 nucleoprotein filament.

129 ing that a high interaction rate between the nucleoprotein filaments and the dsDNA can be achieved.

130 Disruption of H-NS nucleoprotein filaments by DNA bending is a suggested me

131 This may facilitate the formation of nucleoprotein filaments competent for mtDNA repair.

132 The mechanism by which pre-synaptic RecA nucleoprotein filaments efficiently locate sequence homo

133 mplished by RecA proteins that are active as nucleoprotein filaments formed on single-stranded segmen

134 The yeast Srs2 helicase removes Rad51 nucleoprotein filaments from single-stranded DNA (ssDNA)

135 s been implicated in the disassembly of RecA nucleoprotein filaments in vivo and in vitro.

136 s the RAD51 recombinase, which forms helical nucleoprotein filaments on single-stranded DNA (ssDNA) a

137 Addition of SsoRal3 to SsoRadA nucleoprotein filaments reduces total ATPase activity.

138 Bacterial H-NS forms nucleoprotein filaments that spread on DNA and bridge di

139 The ATPase function of DrRecA nucleoprotein filaments thus exists in an inactive defau

140 G151D forms mixed nucleoprotein filaments with WT RAD51 that have intermed

141 ion of DNA molecules and on the size of RecA nucleoprotein filaments, in agreement with experimental

142 tions alter the physical properties of RAD51 nucleoprotein filaments, with G151D showing the most dra

143 postsynaptic (dsDNA) human recombinase RAD51 nucleoprotein filaments.

144 Hha enhances the silencing activity of H-NS nucleoprotein filaments.

145 tate of RecA determines the stability of its nucleoprotein filaments.

146 During nucleoprotein formation HOP2-MND1 helps to load RAD51 on

147 viral challenge in mice vaccinated with the nucleoprotein from the PR8 strain of influenza A, a prot

148 e) but consistently negative for Ebola virus nucleoprotein gene (not in the vaccine).

149 ntly positive for vesicular stomatitis virus nucleoprotein gene and Ebola virus glycoprotein gene (bo

150 f 20-nt target sequences from the Ebolavirus nucleoprotein gene in a constant-temperature environment

151 was extracted from tissues and amplified for nucleoprotein gene sequencing for phylogenetic compariso

152 oteins from influenza A virus (IAV), such as nucleoprotein, have the potential to provide protection

153 wer the limit of detection of an influenza A nucleoprotein immunoassay by over 50%.

154 lated from plasma samples in which anti-EBOV nucleoprotein immunoglobulin G was detected.

155 However, the precise role of nucleoprotein in viral RNA transcription and replication

156 S165) within the groove of influenza A virus nucleoprotein inhibits oligomerization and, consequently

157 Although a number nucleoprotein interactions involving PAN have been impli

158 nascent transcript, leading to a network of nucleoprotein interactions that define a higher order Nr

159 d, the nature of the catalytically competent nucleoprotein intermediates, and the mechanism describin

160 oprotein complex, the oligomerization of the nucleoprotein is mediated by an interaction between the

161 n a sandwich immunoassay for influenza virus nucleoprotein; it used an enzyme-labeled antibody and a

162 rion forms a left-handed helix with an inner nucleoprotein layer decorated with protruding arms compo

163 rget autoantigens are derived from a protein/nucleoprotein mixture prepared from an inexpensive sourc

164 d nucleic-acid components to form engineered nucleoprotein motors may enable additional sophisticated

165 Our designs include nucleoprotein motors that reversibly change direction in

166 virus is wrapped around the virally encoded nucleoprotein N to form the ribonucleoprotein complex (R

167 capsid (the viral RNA genome packaged by the nucleoprotein N) we present crystallographic structures

168 (Box-2) within the C-terminal domain of the nucleoprotein (N(TAIL)).

169 ) colocalized with viral genomic RNA and the nucleoprotein (N) as early as 6 h postinfection (hpi).

170 The vesicular stomatitis virus (VSV) nucleoprotein (N) associates tightly with the viral geno

171 Here, we show that the hRSV nucleoprotein (N) could be at least partially responsibl

172 The nucleoprotein (N) encapsidates the three viral genomic R

173 ing to certain outbreaks on the basis of the nucleoprotein (N) gene sequence only, as the diversity o

174 tly embedded within a nucleocapsid made of a nucleoprotein (N) homopolymer.

175 localize to cytosolic puncta containing the nucleoprotein (N) of the virus.

176 .3 kb encapsidated by multiple copies of the nucleoprotein (N), giving rise to helical nucleocapsids.

177 In a previous analysis in HEp-2 cells, the nucleoprotein (N), phosphoprotein (P), matrix protein (M

178 -RNA template and acts as a chaperone of the nucleoprotein (N), thereby preventing nonspecific encaps

179 onucleoprotein (RNP) complexes consisting of nucleoprotein (N)-encapsidated viral RNA.

180 rmined the 3D X-ray crystal structure of the nucleoprotein (N)-RNA complex from PIV5 to 3.11-A resolu

181 ), polymerase protein (L), M2-1 protein, and nucleoprotein (N).

182 iral glycoproteins (Gn and Gc) and the viral nucleoprotein (N).

183 w rate and contained the viral M protein and nucleoprotein (N).

184 enome four viral proteins are essential: the nucleoprotein NP, the polymerase L, the polymerase cofac

185 either the hemagglutination (HA [H]) or the nucleoprotein (NP [P]) gene of the influenza A/PR8 virus

186 e, that the HLA-B27 immunodominant influenza nucleoprotein (NP) 383-391 epitope is made as an N-termi

187 A restriction can be achieved when the viral nucleoprotein (NP) acquires the critical human-adaptive

188 (IRF3) activation pathway and that the viral nucleoprotein (NP) alone is responsible for this inhibit

189 expression levels of reporter genes from the nucleoprotein (NP) and glycoprotein precursor (GPC) loci

190 ersal" vaccines targeting the viral antigens nucleoprotein (NP) and matrix 2 (M2), which are conserve

191 We define all epitopes in the nucleoprotein (NP) and matrix protein (M1) with experime

192 ified 32 conserved epitopes derived from the nucleoprotein (NP) and matrix-1 (M1) proteins.

193 hat efficient interaction between arenavirus nucleoprotein (NP) and RNA-dependent RNA polymerase (L p

194 P also interacts with the viral nucleoprotein (NP) and self-associates to form a homotet

195 Interestingly, virus protein 24 (VP24) and nucleoprotein (NP) appear to be major virulence factors

196 show that distinct amino acids of the viral nucleoprotein (NP) are required for packaging of specifi

197 Additional incorporation of Aichi nucleoprotein (NP) but not the hemagglutinin (HA), neura

198 The arenavirus nucleoprotein (NP) can suppress induction of type I inte

199 We recently demonstrated that the viral nucleoprotein (NP) determines resistance of seasonal and

200 T-cell responses to A(H3N2) virus nucleoprotein (NP) dominated and strongly cross-reacted

201 of a ribonucleoprotein complex in which the nucleoprotein (NP) encapsidates the single-stranded RNA

202 We found that nucleoprotein (NP) enhances the phosphorylation of P.

203 Accordingly, the arenavirus nucleoprotein (NP) has been identified as a potent IFN-I

204 ng influenza virus hemagglutinin (HA) and/or nucleoprotein (NP) in cynomolgus macaques.

205 The influenza A virus nucleoprotein (NP) is an essential multifunctional prote

206 IAV nucleoprotein (NP) is known to mediate the nuclear impor

207 Lassa virus (LASV) nucleoprotein (NP) is the only known 3'-5' exoribonuclea

208 lation we demonstrate the reduction of viral nucleoprotein (NP) level and inhibition of influenza vir

209 randed RNA segments that are coated by viral nucleoprotein (NP) molecules.

210 A was able to form stable complexes with the nucleoprotein (NP) of IAV.

211 The nucleoprotein (NP) of influenza A virus is highly conser

212 ion between polymerase basic 2 (PB2) and the nucleoprotein (NP) of influenza A viruses.

213 The nucleoprotein (NP) of influenza viruses is a multifuncti

214 The nucleoprotein (NP) of segmented negative-strand RNA viru

215 We recoded the nucleoprotein (NP) of the prototypic arenavirus lymphocy

216 hemagglutinin (HA), neuraminidase (NA), and nucleoprotein (NP) proteins.

217 irus-derived protein, evidenced by high anti-nucleoprotein (NP) serum antibody titers early, while th

218 viruses in the presence of cycloheximide or nucleoprotein (NP) small interfering RNA (siRNA), which

219 Here, we describe a mutation in IAV nucleoprotein (NP) that enhances replication and transmi

220 RNA synthesis include an interaction of the nucleoprotein (NP) with the viral polymerase.

221 ody fragments (VHHs) against influenza virus nucleoprotein (NP), a viral protein essential for nuclea

222 RNA polymerase, glycoproteins G(n) and G(c), nucleoprotein (NP), and a nonstructural S segment (NSs)

223 s were located in the polymerase complex and nucleoprotein (NP), and all isolates carried mutations i

224 promoter of PIV5, and the first viral gene, nucleoprotein (NP), did not lead to a viable virus.

225 ed viral proteins, primarily ISGylated viral nucleoprotein (NP), in infected cells.

226 l acetylation sites of the influenza A virus nucleoprotein (NP), including the lysine residues K77, K

227 usion bodies (IB), comprised mainly of viral nucleoprotein (NP), similar to those observed in BIBD an

228 We found that viral nucleoprotein (NP), the polymerase cofactor VP35, the ma

229 3 expression cassette that expresses a viral nucleoprotein (NP)-specific artificial microRNA from an

230 n assay, and hemagglutinin (HA)-specific and nucleoprotein (NP)-specific CD4(+) T-cell responses were

231 Nucleoprotein (NP)-specific CD8(+) T cells encountered a

232 lymerase subunits (PB2, PB1, and PA) and the nucleoprotein (NP).

233 ormation through interactions with the viral nucleoprotein (NP).

234 ctors (LV) coexpressing 4-1BBL and influenza nucleoprotein (NP).

235 ently been identified that targets the viral nucleoprotein (NP).

236 ne was both captor and tracer for polyvalent nucleoprotein (NP).

237 viral polymerase, genomic RNA and oligomeric nucleoprotein (NP).

238 he T-to-C substitutions at the 3'-UTR of the nucleoprotein (NP; positions 3008 and 3011), observed in

239 d with Xpert (targets: glycoprotein [GP] and nucleoprotein [NP] genes) and Trombley (target: NP gene)

240 he internal proteins (matrix protein 1 [M1], nucleoprotein [NP], polymerase basic protein 1 [PB1]).

241 cific for the 311-325 peptide from influenza nucleoprotein (NP311-325/IA(b)) to track the Ag-specific

242 The nucleoprotein (NPs) of all arenaviruses carry a unique e

243 e overall fold of PepMV CP resembles that of nucleoproteins (NPs) from the genus Phlebovirus (family

244 entify human proteins that interact with the nucleoproteins (NPs) of the Old World arenavirus lymphoc

245 ctural and functional analyses of arenavirus nucleoproteins (NPs) revealed a conserved DEDDH exoribon

246 etween the disordered domain of Sendai virus nucleoprotein (NT) and the C-terminal domain of the phos

247 rdered C-terminal domain of the Hendra virus nucleoprotein (NTAIL) and compared its interfacial prope

248 full-length viral genes is mediated through nucleoprotein-nucleoprotein homo-oligomerization in a 't

249 Insights into nucleoprotein-nucleoprotein interactions have been deriv

250 ative conditions forms a tetramer, while the nucleoprotein obtained following denaturation and refold

251 Here we show that nucleoprotein of influenza A virus is entirely dispensab

252 hat T cells from TCR transgenic mice for the nucleoprotein of influenza virus NP68 exhibit the distin

253 The nucleoprotein of negative-strand RNA viruses forms a maj

254 ld strengths on the C-terminal domain of the nucleoprotein of Sendai virus, over a large range of tem

255 ncreased binding of unmethylated oligos with nucleoproteins of cells maintained under HG.

256 We propose that nucleoprotein oligomerization in infected cells is regul

257 -terminal region of nucleoprotein-core links nucleoprotein oligomerization, nucleocapsid condensation

258 ecificity for the binding of influenza viral nucleoproteins only to the influenza-specific aptamer.

259 Furthermore, the amount of viral nucleoprotein per focus forming unit differed markedly w

260 r results show that CD8(+) T cells targeting nucleoprotein play an important role in shaping influenz

261 acillus Calmette-Guerin (BCG) expressing RSV nucleoprotein prevented behavioral disorders, corroborat

262 The nucleoprotein purified under native conditions forms a t

263 for ultrasensitive detection of recombinant nucleoprotein, reaching a detection limit of 4 +/- 1 fM

264 ompounds targeting the fusion protein or the nucleoprotein) reduced viral load immediately postinfect

265 RNA-like templates in vivo, suggesting that nucleoprotein represents an elongation factor for the vi

266 ormally subdominant, cross-reactive epitope (nucleoprotein residues 205 to 212, or NP205).

267 avirus LCMV encoding codon-deoptimized viral nucleoproteins (rLCMV/NP(CD)).

268 P positions the viral polymerase onto its nucleoprotein-RNA template and acts as a chaperone of th

269 ading to exposure and aberrant processing of nucleoprotein self antigens, and discuss their role in t

270 s protection correlated with the presence of nucleoprotein specific CD8 T cells in the lungs of infec

271 A substantial proportion of lung nucleoprotein-specific memory CD8(+) T cells expressed C

272 ipheral blood, a high frequency of influenza nucleoprotein-specific memory T cells was detected in th

273 ed on spatial and temporal analyses of viral nucleoprotein staining of lung tissue sections and disso

274 consequently, in generating the appropriate nucleoprotein structure for DNA synthetic reactions requ

275 PA-coated single-stranded DNA (RPA-ssDNA), a nucleoprotein structure induced by DNA damage, promotes

276 ized into chromosomes and capped by a unique nucleoprotein structure, the telomere.

277 r DNA replication, creating a recombinogenic nucleoprotein structure.

278 icity, facilitating the formation of compact nucleoprotein structures by increasing the apparent flex

279 needed to load Gp41 onto D-loops, and other nucleoprotein structures containing clusters of Gp32.

280 Chromosome ends contain nucleoprotein structures known as telomeres.

281 ding sequences in the assembly of long-range nucleoprotein structures remains unknown.

282 charomyces cerevisiae, mtDNA is organized in nucleoprotein structures termed nucleoids, which are dis

283 tion of regulatory proteins with the complex nucleoprotein structures that are found in mammalian cel

284 ngements result in various three-dimensional nucleoprotein structures that differ in their shape and

285 tes and stabilization of distinct long-range nucleoprotein structures.

286 CRISPR-Cas nucleoproteins target foreign DNA via base pairing with

287 ipid nanoparticle (LNP) delivery of a single nucleoprotein-targeting (NP-targeting) siRNA in nonhuman

288 Geminin is a nucleoprotein that can directly bind chromatin regulator

289 S DNA interact together to form a high-order nucleoprotein that is required for the loading of the st

290 at the novel H7N9 bird IAV already carries a nucleoprotein that overcomes the inhibition of viral rep

291 olves under pressure to fix mutations in the nucleoprotein that promote escape from T cells.

292 irely embedded into a helical homopolymer of nucleoproteins that constitutes the nucleocapsid.

293 ssociated with specific amino acids in their nucleoproteins, the target of Mx function.

294 l structure of the bacterially expressed SBV nucleoprotein to a 3.06-A resolution.

295 We also find that the recruitment of nucleoprotein to nascent ribonucleoprotein complexes dur

296 Binding of the nucleoprotein to RNA can assemble a loosely coiled NC-li

297 en commercial antibodies against influenza A nucleoprotein were methodically tested for their reactiv

298 10% of wild-type cells contained detectable nucleoprotein, whereas knockout of FAM134B resulted in 8

299 ts are based upon detection of the influenza nucleoprotein, which are limited in that they are unable

300 neered avian H7N7 influenza virus carrying a nucleoprotein with signature mutations typically found i