ライフサイエンスコーパス: viral protease

1 nd two gamma(1)-proteins (glycoprotein D and viral protease).

2 constraints at specific residues within the viral protease.

3 nits susceptible to aberrant cleavage by the viral protease.

4 ) and had activity comparable to that of the viral protease.

5 recedes the cleavage of these domains by the viral protease.

6 n does not require the presence of an active viral protease.

7 s from coevolution of the substrate with the viral protease.

8 in the ER until selectively released by the viral protease.

9 recombinant (r) TRAIL fusion protein using a viral protease.

10 reduced VLP production in the absence of the viral protease.

11 was more severe in the presence of an active viral protease.

12 ase as part of a fusion with the predominant viral protease.

13 rotein precursor that is cleaved by a single viral protease.

14 2xCL denotes a tandem cleavage site for the viral protease.

15 ral and mechanistic characterization of this viral protease.

16 rmation and irreversible inactivation of the viral protease.

17 ag) is post-translationally processed by the viral protease.

18 binding or on RNA-dependent cleavage by the viral protease.

19 d to inhibit intracellular processing by the viral protease.

20 A likely candidate is the viral protease.

21 ns, the gp41 CT is clipped in virions by the viral protease.

22 lopment of resistance due to mutation of the viral protease.

23 entatively assigned as a storage form of the viral protease.

24 merization and enhancing its cleavage by the viral protease.

25 d hypothesize that cleavage is mediated by a viral protease.

26 Mature RT is released by the action of viral protease.

27 and without drug resistance mutations in the viral protease.

28 main destabilize and inactivate the adjacent viral protease.

29 ubstrate that is subsequently cleaved by the viral protease.

30 cleavage site that can be recognized by the viral protease.

31 ough incomplete Gag processing by the mutant viral protease.

32 e mechanisms, independent of its role as the viral protease.

33 ytoplasmic tail of gp41 to be cleaved by the viral protease.

34 cleavage of the gp41 cytoplasmic tail by the viral protease.

35 oviral drugs that are designed to target the viral protease.

36 polysomes may be preferentially targeted by viral proteases.

37 ication or by inhibiting the nsP2 and capsid viral proteases.

38 s adaptable to other structurally nonrelated viral proteases.

39 identifying novel host proteins targeted by viral proteases.

40 ntly separated into individual components by viral proteases.

41 seful for the design of antivirals targeting viral proteases.

42 at are processed into individual proteins by viral proteases.

43 rvable color change in the presence of other viral proteases.

44 host factor physically interacting with the viral protease 2A.

45 tion factor 4 gamma I (eIF4GI) is cleaved by viral protease 2A.

46 initiation factor eIF4G by sequence-specific viral proteases (2A protease in the case of coxsackievir

47 s unexpected diversity in the genes encoding viral proteases (2A(pro)) that help these viruses achiev

48 s cleavage of a viral precursor by the other viral protease, 2A(pro).

49 he junction of the capsid protein 1D and the viral protease 2Apro.

50 g of the viral protein 3CD (precursor of the viral protease 3C and the viral polymerase 3D) to the cl

51 licated in the viral egress of CVB3, and the viral protease 3C cleaves TFEB during infection.

52 s of a variety of P1 precursor proteins with viral protease 3C demonstrated efficient production of P

53 Remarkably, the viral protease 3C directly targets GSDMD and induces its

54 The viral protease 3C plays an important role in EV71-induce

55 suggest that 2C can negatively regulate the viral protease 3C(pro).

56 Only one protease, viral protease 3C, has been implicated in the nine prote

57 ral RNA-dependent RNA polymerase or the main viral protease, 3CL(pro) 3CL(pro) is an attractive targe

58 uggest that a direct cleavage of CREB by the viral protease 3Cpro leads to inhibition of CREB-activat

59 demonstrate that incubation of TBP with the viral protease (3Cpro) inhibits its ability to bind TATA

60 sis of Pr160(Gag-Pol) polyprotein, hence the viral protease, a predominant expression of Pr55(Gag) de

61 nonstructural proteins (nsps 1 to 16) by two viral proteases, a papain-like protease (PLpro) and a 3C

62 ) cell death through premature intracellular viral protease activation.

63 demonstrate that CARD8 is a broad sensor of viral protease activities and suggests that CARD8 divers

64 ing safe and efficient platforms to evaluate viral protease activities and the efficacy of protease i

65 activation in a manner that is dependent on viral protease activity and largely independent of the N

66 developed here allow for rapid evaluation of viral protease activity and the identification of protea

67 herry fluorescence ratio, reliably predicted viral protease activity in single virions.

68 immature capsids in vitro demonstrates that viral protease activity is sensitive to oxidation-reduct

69 oronavirus papain-like protease, altered the viral protease activity or affected viral replication or

70 Here, monitoring viral protease activity with sensitive techniques, inclu

71 r, the onset of fluorescence correlated with viral protease activity.

72 ral proteins during infection and, like many viral proteases, also targets host proteins to subvert t

73 ral RT/IN processing site are cleaved by the viral protease and (iii) only the cleaved IN protein com

74 ves dissection of the Gag polyprotein by the viral protease and assembly of a conical capsid enclosin

75 odifications of different targets by the VP4 viral protease and by VP2 itself to yield the mature VP2

76 teomics to identify cellular substrates of a viral protease and describe GPx8 as a novel proviral hos

77 a cell type-specific activity profile of the viral protease and its precursors and dose-dependent inh

78 fitness of HIV-1 caused by mutations in the viral protease and may open a new avenue for designing P

79 protects cells in vitro and in vivo from the viral protease and prevents cell death following HIV inf

80 virion membranes, where it is cleaved by the viral protease and protected from digestion by exogenous

81 OS cells presumably allows activation of the viral protease and proteolytic processing of HIV-1 Gag p

82 ) specifically inhibited the function of the viral protease and provide for the first time proof of p

83 oduced and stored, three-drug treatment with viral protease and reverse transcriptase inhibitors mark

84 ons, including inhibitors of the hepatitis C viral protease and RNA polymerase.

85 s not dependent on the presence of an active viral protease and that the NC domain of Pr55(gag) is di

86 uction of less than 10% in the expression of viral protease and viral growth was observed in cells th

87 ontrol apoptosis of tumor cells via specific viral proteases and for use of viral proteases as in viv

88 unctionality of PROFICS is demonstrated with viral proteases and human caspase-2.

89 Here, with the aid of engineered viral proteases and proteolytic signals, we build two se

90 ze the enzymatic function of a wide range of viral proteases and suggests that host mimicry of viral

91 tically analyzed the effect of famotidine on viral proteases and virus replication.

92 al for virion infectivity; inhibitors of the viral protease are potent antivirals, and substitutions

93 To determine which viral proteases are responsible for processing these pro

94 ing for the HAstV polyprotein highlights the viral protease as a promising target for antiviral devel

95 We use SARS-CoV-2 viral protease as a proof-of-concept model system.

96 Here, we identify a viral protease as a target of NO.

97 he nucleocapsid protein and a portion of the viral protease as the only region that influenced the di

98 via specific viral proteases and for use of viral proteases as in vivo reporters for cancer therapy.

99 e emergence of inactivating mutations in the viral protease because the human cathepsin L will not de

100 d into particles, where it is cleaved by the viral protease between amino acids 57 and 58.

101 ze vulnerability to resistance, not only for viral proteases but for other quickly evolving drug targ

102 rocess correlates with the activation of the viral protease by an unknown mechanism, and, as the stru

103 recombinant TBP resistant to cleavage by the viral proteases, called GG rTBP.

104 oxidation-reduction conditions, and that the viral protease can be activated in the absence of viral

105 While other studies have implied that the viral protease can degrade mutant RT proteins, we show h

106 esults are the first proof of principle that viral proteases can directly be imaged in vivo.

107 response on the sequences surrounding the 12 viral protease cleavage sites (PCSs) provided greater th

108 HIV-1 particles from the infected cell, the viral protease cleaves the Gag polyprotein at specific s

109 viral polyprotein amino acid residues where viral protease cleaves the polyprotein as it leaves the

110 brane (TM) subunits in the cell and then the viral protease cleaves the R-peptide from TM in new viru

111 During viral maturation, the viral protease cleaves this tail to release a 16-amino-a

112 inducer reveals that a catalytically active viral protease complex is required to reduce type I IFN

113 d autoproteolytically processed forms of the viral protease containing sequences common to ICP35 (Nb)

114 ent a model for HIV replication in which the viral protease depletes the infected cells of bcl-2, lea

115 nd OFF switch CAR circuits engineered with a viral protease domain.

116 al nature of the coronavirus PLP domain as a viral protease, DUB, and IFN antagonist and suggest that

117 ive target for antiviral therapeutics is the viral protease due to its essential functions throughout

118 and liberated from the viral proteins by the viral protease during particle maturation.

119 ag polyprotein (Pr55(Gag)) is cleaved by the viral protease during the late stages of the virus life

120 e CA-p2 cleavage site from processing by the viral protease during virion maturation, thereby reveali

121 ts highlight the potential for inhibition of viral proteases employing nucleophilic catalysis by beta

122 activated immediately after HIV entry by the viral protease encapsulated in incoming virions.

123 Subsequently, Gag is cleaved by the viral protease enzyme into separate domains, leading to

124 ro by pepsin as well as by the corresponding viral protease enzyme.

125 ARS-CoV-2 main protease, one of two cysteine viral proteases essential for viral replication.

126 findings may be directly applicable in using viral protease expression as a transgene marker in tumor

127 ids by a process involving activation of the viral protease, expulsion of the scaffold proteins, and

128 rpesvirus-like proteases define two distinct viral protease folds that exhibit little sequence or str

129 nserved recognition sequence targeted by the viral protease for cleavage.

130 ytic Cys328, shifting the active site of the viral protease from a closed conformation in the apo for

131 ng was further supported by the finding that viral proteases from picornavirus family specifically ta

132 uses will contribute to our understanding of viral protease function in general, thereby leading to a

133 can be recovered at the normal density when viral protease function is abolished.

134 toration through pharmacologic inhibition of viral protease function.

135 dine and a related analogue, rimantadine, on viral protease, helicase, ATPase, RNA-dependent RNA poly

136 Cleavage was likely orchestrated by a viral protease; however, processing was not required for

137 ein that is cleaved into six proteins by the viral protease in a maturation process that begins durin

138 tions of substoichiometric inhibition of the viral protease in developing herpesviral therapeutics.

139 virus (MLV) transmembrane Env protein by the viral protease in MLV Env-pseudotyped HIV-1 particles be

140 vage intermediates and their cleavage by the viral protease in simian immunodeficiency virus (SIV).

141 ontaining Gag proteins can be cleaved by the viral protease in SIV virions.

142 t was not due to a lack of expression of the viral protease in the form of a Gag-Pol precursor or a l

143 uring infection, the function of this unique viral protease in the pestivirus life cycle remains to b

144 inal mutants occurs in the absence of active viral protease in the virion.

145 Activity of the viral protease in vitro depends on pH, with an increase

146 onally active form of CREB is cleaved by the viral protease in vitro.

147 ing mutations in therapeutic targets such as viral proteases in an unbiased manner.

148 Viral proteases in particular have developed novel regul

149 rmational changes and unique features of the viral protease increase the binding affinity of HIV prot

150 zyme but shows distant similarity to certain viral proteases, indicating the existence of a widely co

151 HIV-infected cells treated with a viral protease inhibitor and their progeny viruses were

152 Indinavir is a viral protease inhibitor used for the treatment of HIV i

153 It represents a novel class of viral protease inhibitor, in which an essential, multifu

154 Viral protease inhibitors are remarkably effective at bl

155 Importance: Evaluating viral protease inhibitors in a small-animal model is a c

156 Hepatitis C viral protease inhibitors increase sustained virologic r

157 nsights led to several strategies to improve viral protease inhibitors to counter resistance, such as

158 Extensive studies on resistance to viral protease inhibitors, particularly those of HIV-1 a

159 erapy dawned with the recent approval of two viral protease inhibitors, used in combination with pegy

160 s a virion protein which is processed by the viral protease into a 20-kDa isoform within the virion p

161 g Gag polyproteins that are processed by the viral protease into individual components, resulting in

162 olves cleavage of the Gag polyprotein by the viral protease into its matrix (MA), capsid (CA), and nu

163 part of a polyprotein that is cleaved by the viral protease into the proteins that form the virus par

164 essing of the nonstructural polyprotein by a viral protease into the viral components required to for

165 eptide chain that subsequently is cleaved by viral proteases into mature protein products, with one p

166 in is processed by a combination of host and viral proteases into structural and non-structural prote

167 Since the viral protease is a homodimer, the rational design of en

168 g PIs due to a wide spectrum of mutations in viral protease is a major factor limiting their broader

169 mination microscopy, we demonstrate that the viral protease is activated within cells prior to the re

170 The viral protease is an attractive target for therapeutics

171 ional cleavage of the Gag polyprotein by the viral protease is associated with striking morphological

172 esolve a long-standing debate as to when the viral protease is initially activated during viral assem

173 In the light of simplicity, our test for viral protease is not limited to an equipped laboratory,

174 results suggest that the presence of active viral protease is not required for the degradation of RT

175 without affecting the activity of the HIV-1 viral protease itself, as demonstrated by in vitro proce

176 ns into functional proteins that include the viral protease itself.

177 Ub-clipping uses an engineered viral protease, Lb(pro)*, to incompletely remove ubiquit

178 Our analysis showed that cleavage by the viral protease liberates Vpr and generates functional he

179 The main viral protease (M(pro)) is an attractive target for anti

180 uents as irreversible inhibitors of the main viral protease (M(pro)).

181 rocessing of Gag and Pol polyproteins by the viral protease, making this enzyme a prime target for an

182 ctural (Gag) polyproteins are cleaved by the viral protease, maturation of the immature virus-like pa

183 Thus, molecules that inhibit the viral protease may have potential therapeutic value.

184 Furthermore, cleavage of autoantigens by viral proteases may target these proteins for the autoim

185 A block in the viral protease-mediated cleavage inhibits the production

186 After the release of the immature virus, a viral protease-mediated cleavage occurs within the cytop

187 sidues, valine 20 and histidine 21, inhibits viral protease-mediated cleavage of the cytoplasmic doma

188 After the release of the immature virus, a viral protease-mediated cleavage of the cytoplasmic tail

189 antiviral activities and susceptibilities to viral protease-mediated cleavage.

190 cule compounds that block a late step in the viral protease-mediated processing of the Gag polyprotei

191 slated via cap-independent mechanisms within viral protease-modified messenger ribonucleoprotein (mRN

192 selected drug-resistant mutants to the main viral protease (Mpro) inhibitor nirmatrelvir.

193 before they can cleave any other substrates, viral proteases need to cleave themselves out of the vir

194 The Zika viral protease NS2B-NS3 is essential for the cleavage of

195 opment is the highly conserved two-component viral protease NS2B-NS3, which plays an essential role i

196 ough Toll-like receptor 3 is mediated by the viral protease NS3/4A, which directs proteolysis of its

197 ght to be mediated, at least in part, by the viral protease (nsP2) which is responsible for processin

198 TUs) are one of the two principal classes of viral proteases observed to reverse posttranslational mo

199 irus Pol precursor protein processing by the viral protease occurs at only one site, releasing a prot

200 ciency virus type 1 (HIV-1), cleavage by the viral protease occurs during viral budding.

201 from the YopE fragment by a T3S-translocated viral protease or fusion to ubiquitin and cleavage by en

202 f NLRP1 by nanobody-mediated ubiquitination, viral proteases, or inhibition of DPP9 was independent o

203 icase polyproteins that are processed by two viral proteases, papain-like protease (PLpro) and 3C-lik

204 of a protease inhibitor, suggesting that the viral protease plays an important role in the degradatio

205 extremely rapid in vitro inactivation of the viral protease, potent antiviral activity against multip

206 ly restored by a second site mutation in the viral protease (PR) gene which prevented proteolytic pro

207 Pro and Pol proteins and to characterize the viral protease (PR) in vitro.

208 In retroviruses, the viral protease (PR) is released as a mature protein by c

209 Proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retrov

210 t the plasma membrane and are cleaved by the viral protease (PR) just before or very soon after parti

211 vage of internal scaffolding proteins by the viral protease (Pr) occurs during HCMV capsid assembly.

212 cell, Gag is cleaved at several sites by the viral protease (PR).

213 is subject to proteolytic processing by the viral protease (Pr).

214 parations of HIV-1 virions which lack active viral protease (PR).

215 1 (CA-SP1) intermediate to mature CA by the viral protease (PR).

216 processed from polyprotein precursors by the viral protease (PR).

217 ently due to the premature activation of the viral protease (PR).

218 tein gp41 that create cleavage sites for the viral protease (PR).

219 Inactivating the viral protease prevents protein cleavage; the resulting

220 (Delta-domain), this domain is eliminated by viral protease prior to subsequent shell maturation and

221 These features of the viral protease provide opportunities to develop specific

222 en MNV strains at multiple loci spanning the viral protease, RdRP, and capsid ORFs and isolated indiv

223 Reporting the activity of a specific viral protease remains an acute need for rapid point-of-

224 d then, in the newly assembled particle, the viral protease removes a 16-residue peptide, the R-pepti

225 tion with an engineered FRET reporter called VIral ProteasE Reporter (VIPER) to investigate heterogen

226 The viral protease represents a key drug target for the deve

227 he HIV-1 gag-pol transframe region, encoding viral protease residues 4 to 8 and a C-terminal Vpr-bind

228 vents catalyzed by a viral recombinase and a viral protease, respectively.

229 MoMuLV TM (the R peptide) are cleaved by the viral protease, resulting in an increased fusogenicity o

230 Cleavage of this fusion protein by the viral protease results in the release and secretion of a

231 sembly, cleavage of the Gag precursor by the viral protease results in the transient appearance of a

232 The main viral protease, SARS 3CLpro, is a validated target for t

233 d understanding of the context dependence of viral protease specificity may aid the development of ne

234 An understanding of viral protease specificity may help the development of f

235 ronavirus Ubl domain as a novel modulator of viral protease stability and reveal manipulating the Ubl

236 sid-like particles by the simple addition of viral protease, suggesting that it is possible in princi

237 ly, Trim7 recognizes the cleavage product of viral proteases, suggesting a novel and broad mechanism

238 ification and virus assembly and, finally, a viral protease suppressing activation of the innate immu

239 action toward 2A(pro) 2A(pro) functions as a viral protease that cleaves a peptide sequence correspon

240 HIV-1 encodes a viral protease that is essential for the maturation of i

241 conclusion, we provide evidence that I7 is a viral protease that is required for AG/X-specific cleava

242 The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into indi

243 We present an assay for viral proteases that relies on the proteolytic cleavage

244 mixing than an inactivating mutation in the viral protease, the target of many successful inhibitors

245 or p2E) are removed from the protein by the viral protease; this cleavage is believed to activate th

246 ach for reporting the activity of a specific viral protease through direct color conversion on a cott

247 y of cGAS-STING evasion enzymes evolved from viral proteases through gain of secondary nuclease activ

248 sting that the PPPY motif is crucial for the viral protease to access the TM tail.

249 SP1 junction and thereby delay access of the viral protease to its substrate.

250 Upon viral budding, Gag is processed by the viral protease to liberate distinct domains as separate

251 rated into virions and then processed by the viral protease to liberate the IN protein.

252 rotein undergoes proteolytic cleavage by the viral protease to release the 16-amino-acid R peptide, a

253 on-associated TM is further processed by the viral protease to remove the C-terminal 16 amino acids o

254 teins which are proteolytically processed by viral proteases to generate mature nonstructural protein

255 le polyprotein, which is cleaved by host and viral proteases to generate viral proteins required for

256 designed protein heterodimers and engineered viral proteases to implement a synthetic protein circuit

257 anslated as a polyprotein that is cleaved by viral proteases to produce the viral structural and nons

258 A and are proteolytically processed by three viral proteases to yield 16 mature nonstructural protein

259 ated into polyproteins that are processed by viral proteases to yield functional intermediate and mat

260 sp1-16), which are subsequently processed by viral proteases to yield mature nsp.

261 Premature intracellular activation of the viral protease triggered CARD8 inflammasome-mediated pyr

262 viral proteins UL6, UL25, and VP19C and the viral protease, VP24, are altered in cells infected with

263 viral proteins UL6, UL25, and VP19C and the viral protease, VP24, were altered in the absence of UL3

264 to determine the substrate specificity of a viral protease, VP4, derived from the blotched snakehead

265 wild-type virus-infected cells, in which the viral protease was active, the cleaved NCp7 copurified w

266 into p6 mutant virions was detected when the viral protease was mutated, suggesting that the interact

267 ombined with a mutation that inactivates the viral protease, we observed a significant reduction in t

268 odel protein that is cleaved by an exogenous viral protease, we show that the new N-terminal sequence

269 ular levels of one virion mRNA, encoding the viral protease, were much lower than those of transcript

270 also flexible enough to be accessible to the viral protease, which cleaves the 6HB during particle ma

271 structural protein 3 (NS3) gene encoding the viral protease, which has been associated with reduced s

272 ag and Gag-Pro-Pol are the substrates of the viral protease, which is responsible for cleaving these

273 eservoir involves prematurely activating the viral protease, which leads to the pyroptotic killing of

274 ts toward targeting SARS-CoV-2 M(pro), a key viral protease, which led to the discovery of compound 1

275 w background that reports on the activity of viral proteases, which are key drug targets.

276 e a family of human pathogens that require a viral protease with a concentration-dependent zymogen ac

277 inhibit processing of Gag polyprotein by the viral protease without affecting the activity of the HIV