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

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

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

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

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

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

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

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

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

11 ral and mechanistic characterization of this viral protease.

12 rmation and irreversible inactivation of the viral protease.

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

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

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

16 d to inhibit intracellular processing by the viral protease.

17 and without drug resistance mutations in the viral protease.

18 main destabilize and inactivate the adjacent viral protease.

19 ubstrate that is subsequently cleaved by the viral protease.

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

21 ough incomplete Gag processing by the mutant viral protease.

22 A likely candidate is the viral protease.

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

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

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

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

27 constraints at specific residues within the viral protease.

28 nits susceptible to aberrant cleavage by the viral protease.

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

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

31 polysomes may be preferentially targeted by viral proteases.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

97 toration through pharmacologic inhibition of viral protease function.

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

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

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

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

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

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

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

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

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

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

108 Viral proteases in particular have developed novel regul

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

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

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

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

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

114 Viral protease inhibitors are remarkably effective at bl

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

116 Hepatitis C viral protease inhibitors increase sustained virologic r

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

162 1 (CA-SP1) intermediate to mature CA by the viral protease (PR).

163 Inactivating the viral protease prevents protein cleavage; the resulting

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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