ライフサイエンスコーパス: proprotein convertase

1 vage of the envelope protein by a furin-like proprotein convertase.

2 y pathway through the activity of furin-like proprotein convertases.

3 th a KD of 0.7 mum but did not bind to other proprotein convertases.

4 of MMPs, cathepsin D and K, kallikrein 4 and proprotein convertases.

5 The proprotein convertases (PCs) furin and proprotein convertase 1/3 (PC1) cleave substrates at dib

6 Proprotein convertase 1/3 (PC1/3) deficiency, an autosom

7 ll mutations in the PCSK1 gene, encoding the proprotein convertase 1/3 (PC1/3), cause recessive monog

8 e that the pKa of the conserved histidine in proprotein convertase 1/3 is acid-shifted compared with

9 The proprotein convertase 1/3 is expressed in the regulated

10 stidines within the propeptides of furin and proprotein convertase 1/3 using a histidine hydrogen-deu

11 olgi network at a pH of 6.5 while a paralog, proprotein convertase 1/3, activates in secretory vesicl

12 ine/kexin type 1 gene (PCSK1), which encodes proprotein convertase 1/3, causes a severe multihormonal

13 vation of the eukaryotic proteases furin and proprotein convertase-1/3.

14 be required for the productive maturation of proprotein convertase 2 (proPC2) to an active enzyme for

15 checkpoint dependent on the serine protease proprotein convertase 7 (PC7) can rescue unstable MHC I,

16 Proprotein convertase 7 (PC7) is a member of the subtili

17 ragments the protein undergoes processing by proprotein convertases, a class of serine proteases that

18 We found that PC2 proprotein convertase activity contributes to this patte

19 In contrast to other zymogen proprotein convertases, all incompletely matured interme

20 results show that MERS-S is a substrate for proprotein convertases and demonstrate that processing b

21 ay involves the self-activated furin and PC2 proprotein convertases and membrane type-6 MMP (MT6-MMP/

22 ed by furin intracellularly and by all three proprotein convertases at the cell surface.

23 t LoVo cells, and an inhibitor of furin-like proprotein convertases blocked cleavage of the first and

24 AIN cleavage event in PC1 at 3048 aa and the proprotein convertase cleavage (PPC) event in fibrocysti

25 h prodomain and GF monomer are linked before proprotein convertase cleavage and how much conformation

26 After cleavage at a canonical proprotein convertase cleavage site ((161)RRKR(164)), th

27 stitution of basic residues at the predicted proprotein convertase cleavage site blocks proprotein pr

28 rmined a structure of pro-TGF-beta1 with the proprotein convertase cleavage site mutated to mimic the

29 ysis, SPPL3 cleaves mutant FVenv lacking the proprotein convertase cleavage site necessary for the pr

30 d Scw have three functional furin/subtilisin proprotein convertase cleavage sites; two between the pr

31 ined endotrophin, was released by furin-like proprotein convertase cleavage.

32 the sequence identity of its unconventional proprotein convertase-cleavage motif that lacks arginine

33 se results suggest that the matriptase-2 and proprotein convertase-cleavage products have different r

34 gests that inhibitors of furin or furin-like proprotein convertases could represent promising lead st

35 However, blockade of proprotein convertases did not impact MERS-S-dependent t

36 PCSK3/furin was identified as the major proprotein convertase expressed by adipocytes that media

37 findings suggest that furin or a furin-like proprotein convertase facilitates DHBV infection by clea

38 The proprotein convertase family of enzymes includes seven e

39 otential cleavage sites for proteases of the proprotein convertase family that match the cleavage pro

40 e 7 (PC7) is a member of the subtilisin-like proprotein convertase family, which is involved in the e

41 PC7 belongs to the proprotein convertase family, whose members are implicat

42 essing at a canonical consensus site for the proprotein convertase Furin (RXXR) between the pro- and

43 Here, we show that the proprotein convertase furin is responsible for pro-OCN m

44 The proprotein convertase furin requires the pH gradient of

45 cell entry of SARS-CoV-2 is preactivated by proprotein convertase furin, reducing its dependence on

46 vage and inactivation by the subtilisin-like proprotein convertase furin.

47 rsor forms, the protoxins, which can use the proprotein convertases Furin and PC7 for activation.

48 Another proprotein convertase, furin, cleaves PCSK9 at Arg(218)-

49 Unlike other proprotein convertases, however, this retention is perma

50 Here, we show that MERS-S is processed by proprotein convertases in MERS-S-transfected and MERS-Co

51 enesis provides insight into the function of proprotein convertases in nervous system development.

52 We highlight the ability of a particular proprotein convertase inhibitor to effectively reduce th

53 ot significantly affected by incubation with proprotein convertase inhibitors for up to 8 h, arguing

54 we demonstrated that the cleavage of LPL by proprotein convertases is an inactivation process, simil

55 Furin, a proprotein convertase, is highly expressed in high-grade

56 Indeed, plasma analyses of single-proprotein convertase-knock-out mice showed that loss of

57 cell-based model using stable shRNA-induced proprotein convertase knockdown indicate that only furin

58 eading to isomerization by cyclophilin B and proprotein convertase-mediated L2 minor capsid protein c

59 GF23 R(176)XXR(179)/S(180)AE subtilisin-like proprotein convertase motif.

60 proforms move to the cell surface where the proprotein convertase PACE4 selectively supports IRB mat

61 The first seven members of the proprotein convertase (PC) family activate protein precu

62 The secretory proprotein convertase (PC) family comprises nine members

63 ire proteolytic activation by members of the proprotein convertase (PC) family.

64 p3 species revealed the presence of two RXXR proprotein convertase (PC) motifs, (48)RDLR(51) and (414

65 FURIN is a proprotein convertase (PC) responsible for proteolytic a

66 Furin is a ubiquitously expressed proprotein convertase (PC) that plays a vital role in nu

67 d to the BM that results in L2 cleavage by a proprotein convertase (PC), furin, and/or PC5/6, followe

68 an engineered serpin family inhibitor of the proprotein convertase (PC), furin, that exhibits high sp

69 c motif, suggesting cleavage by a furin-like proprotein convertase (PC).

70 g events, including cleavage by a furin-like proprotein convertase (PC).

71 Proprotein convertases (PC) activate precursor proteins

72 Proprotein convertases (PCs) are crucial in the processi

73 Proprotein convertases (PCs) are highly specific proteas

74 Proprotein convertases (PCs) comprise a large family of

75 The proprotein convertases (PCs) form a family of nine secre

76 ICM formation depend on PC7 and the related proprotein convertases (PCs) Furin and Pace4 and that th

77 The proprotein convertases (PCs) furin and proprotein conver

78 The proprotein convertases (PCs) furin, PC5, PACE4, and PC7

79 The proprotein convertases (PCs) furin, PC5/6, and PACE4 exh

80 The proprotein convertases (PCs) play an important role in p

81 ologic studies, and mutational analysis that proprotein convertases (PCs) proteolytically process hum

82 The propeptides of proprotein convertases (PCs) regulate activation of cogn

83 t neutral pH and was dependent on furin-like proprotein convertases (PCs).

84 roteolytically cleaved into several forms by proprotein convertases (PCs).

85 The proprotein convertase PCSK9 is a major target in the tre

86 n a two-step cascade of protease activation: proprotein convertases, primarily furin, activate latent

87 Propeptides of proprotein convertases regulate activation of their prot

88 ckdown indicate that only furin is the major proprotein convertase required for HA5 cleavage.

89 ellularly by limited proteolysis mediated by proprotein convertase(s) (PCs) along the secretory pathw

90 e propeptide is also cleaved by a furin-like proprotein convertase(s) (PCs) at KKRSHLKR(199) downward

91 ng of the GP precursor (GPC) by the cellular proprotein convertase site 1 protease (S1P), also known

92 vage at the GPS site in polycystin-1 and the proprotein convertase site in fibrocystin.

93 Subtilisin-like proprotein convertases (SPCs) are a family of calcium-de

94 sor molecules by a family of subtilisin-like proprotein convertases (SPCs).

95 and human cross-reactive, antagonistic anti-proprotein convertase substilisin kexin type 9 (PCSK9) a

96 Serum proprotein convertase subtilisin kexin 9 (PCSK9) binds t

97 Since the discovery of proprotein convertase subtilisin kexin 9 (PCSK9) in 2003

98 The proprotein convertase subtilisin kexin isozyme 1 (SKI-1)

99 The proprotein convertase subtilisin kexin isozyme-1 (SKI-1)

100 be an extracellular endogenous inhibitor of proprotein convertase subtilisin kexin type 9 (PCSK9) ac

101 in LDL receptor, apolipoprotein B (APOB), or proprotein convertase subtilisin kexin type 9 (PCSK9) ge

102 treatment with beta-blockers, ezetimibe, and proprotein convertase subtilisin kexin type 9 (PCSK9) in

103 Proprotein convertase subtilisin kexin type 9 (PCSK9) in

104 Proprotein convertase subtilisin kexin type 9 (PCSK9) le

105 Proprotein convertase subtilisin kexin type 9 (PCSK9) pr

106 Levels of proprotein convertase subtilisin kexin type 9 (PCSK9) va

107 vestigate whether high levels of circulating proprotein convertase subtilisin kexin type 9 (PCSK9) wo

108 act of AMG145, a monoclonal antibody against proprotein convertase subtilisin kexin type 9 (PCSK9), o

109 Monoclonal antibodies against proprotein convertase subtilisin kexin type 9 (PCSK9), s

110 145, a monoclonal antibody directed against proprotein convertase subtilisin kexin type 9 (PCSK9), t

111 PCSK9i (proprotein convertase subtilisin kexin type 9 inhibitors

112 new class of cholesterol-lowering drugs, the proprotein convertase subtilisin kexin-9 inhibitors.

113 cumab is a monoclonal antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) an

114 humanized monoclonal antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) an

115 Pharmacologic inhibitors of proprotein convertase subtilisin-kexin type 9 (PCSK9) ar

116 Proprotein convertase subtilisin-kexin type 9 (PCSK9) bi

117 Monoclonal antibodies directed against proprotein convertase subtilisin-kexin type 9 (PCSK9) ha

118 A new class of drugs that inhibit proprotein convertase subtilisin-kexin type 9 (PCSK9) ha

119 Background Findings from clinical trials of proprotein convertase subtilisin-kexin type 9 (PCSK9) in

120 e is encouraging evidence of the efficacy of proprotein convertase subtilisin-kexin type 9 (PCSK9) in

121 ugh day 210, and data on LDL cholesterol and proprotein convertase subtilisin-kexin type 9 (PCSK9) le

122 apeutic agent that inhibits the synthesis of proprotein convertase subtilisin-kexin type 9 (PCSK9), a

123 rocumab, a monoclonal antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9), h

124 b, a humanized monoclonal antibody targeting proprotein convertase subtilisin-kexin type 9 (PCSK9), r

125 locumab, a monoclonal antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9), s

126 rial of evolocumab, a monoclonal antibody to proprotein convertase subtilisin-kexin type 9 (PCSK9).

127 The impact of lipid lowering by proprotein convertase subtilisin-kexin type 9 inhibition

128 Cholesterol reduction with proprotein convertase subtilisin-kexin type 9 inhibitors

129 Loss-of-function variants in PCSK9 (proprotein convertase subtilisin-kexin type 9) are assoc

130 Previous trials of PCSK9 (proprotein convertase subtilisin-kexin type 9) inhibitor

131 y human monoclonal antibody directed against proprotein convertase subtilisin-kexin type 9, is widely

132 Inclisiran inhibits hepatic synthesis of proprotein convertase subtilisin-kexin type 9.

133 ontrolled the renal epithelial expression of proprotein convertase subtilisin-like kexin type 9, a ke

134 L receptor (LDLR), apolipoprotein B-100, and proprotein convertase subtilisin-like kexin type 9.

135 n selected exons of apolipoprotein B-100 and proprotein convertase subtilisin-like kexin type 9.

136 Proprotein convertase subtilisin-like/kexin type 9 (PCSK

137 PCSK9 (proprotein convertase subtilisin-like/kexin type 9) is a

138 WT (wild type) or PCSK9 (proprotein convertase subtilisin-like/kexin type-9) gain

139 Proprotein convertase subtilisin/kexin (PCSK) enzymes co

140 Serum proprotein convertase subtilisin/kexin 9 (PCSK9) binds t

141 lly methylated region in the promoter of the proprotein convertase subtilisin/kexin 9 (PCSK9) gene th

142 ering the longer-term efficacy and safety of proprotein convertase subtilisin/kexin 9 (PCSK9) inhibit

143 Proprotein convertase subtilisin/kexin 9 (PCSK9) is a ke

144 e have recently reported that >30% of plasma proprotein convertase subtilisin/kexin 9 (PCSK9) is boun

145 Proprotein convertase subtilisin/kexin 9 (PCSK9) is resp

146 Monoclonal antibodies to proprotein convertase subtilisin/kexin 9 (PCSK9) reduce

147 otein (LDL) cholesterol due to inhibition of proprotein convertase subtilisin/kexin 9 (PCSK9) reduces

148 Proprotein convertase subtilisin/kexin 9 (PCSK9) regulat

149 Proprotein convertase subtilisin/kexin 9 (PCSK9), one of

150 PCSK9 (proprotein convertase subtilisin/kexin 9) inhibitors hav

151 y lipoprotein receptor, apolipoprotein B, or proprotein convertase subtilisin/kexin 9.

152 The proprotein convertase subtilisin/kexin enzymes proteolyt

153 lated adipocytes was reduced, and intestinal proprotein convertase subtilisin/kexin type 1 (Pcsk1) ex

154 ive disorder caused by rare mutations in the proprotein convertase subtilisin/kexin type 1 (PCSK1) ge

155 ne and amphetamine regulated transcript, and proprotein convertase subtilisin/kexin type 1 inhibitor.

156 on single nucleotide polymorphisms (SNPs) in proprotein convertase subtilisin/kexin type 1 with modes

157 Proprotein convertase subtilisin/kexin type 2 (PCSK2) is

158 t because of deficiencies in its convertase, proprotein convertase subtilisin/kexin type 5 (PCSK5), c

159 s of the interaction between ANGPTL3, furin, proprotein convertase subtilisin/kexin type 5 (PCSK5), p

160 strongly upregulated upon hypoxia was PCSK6 (proprotein convertase subtilisin/kexin type 6).

161 tion in LDL cholesterol with an inhibitor of proprotein convertase subtilisin/kexin type 9 (PCSK9) af

162 tilin were reported to individually bind the proprotein convertase subtilisin/kexin type 9 (PCSK9) an

163 Proprotein convertase subtilisin/kexin type 9 (PCSK9) an

164 Monoclonal antibodies that inhibit proprotein convertase subtilisin/kexin type 9 (PCSK9) ar

165 Gain-of-function mutations of the proprotein convertase subtilisin/kexin type 9 (PCSK9) ar

166 Proprotein convertase subtilisin/kexin type 9 (PCSK9) bi

167 Proprotein convertase subtilisin/kexin type 9 (PCSK9) bi

168 Plasma proprotein convertase subtilisin/kexin type 9 (PCSK9) bi

169 Proprotein convertase subtilisin/kexin type 9 (PCSK9) bi

170 Proprotein convertase subtilisin/kexin type 9 (PCSK9) bi

171 Proprotein convertase subtilisin/kexin type 9 (PCSK9) de

172 of this study was to determine the effect of proprotein convertase subtilisin/kexin type 9 (PCSK9) de

173 Proprotein convertase subtilisin/kexin type 9 (PCSK9) do

174 Proprotein convertase subtilisin/kexin type 9 (PCSK9) do

175 receptor (LDLR) degradation mediated by the proprotein convertase subtilisin/kexin type 9 (PCSK9) ha

176 Soluble proprotein convertase subtilisin/kexin type 9 (PCSK9) ha

177 The proprotein convertase subtilisin/kexin type 9 (PCSK9) in

178 Proprotein convertase subtilisin/kexin type 9 (PCSK9) in

179 Proprotein convertase subtilisin/kexin type 9 (PCSK9) in

180 ess the long-term safety and efficacy of the proprotein convertase subtilisin/kexin type 9 (PCSK9) in

181 sensus pathways suggest use of ezetimibe and proprotein convertase subtilisin/kexin type 9 (PCSK9) in

182 lable for prescription include ezetimibe and proprotein convertase subtilisin/kexin type 9 (PCSK9) in

183 Proprotein convertase subtilisin/kexin type 9 (PCSK9) in

184 The secreted protein proprotein convertase subtilisin/kexin type 9 (PCSK9) is

185 Proprotein convertase subtilisin/kexin type 9 (PCSK9) is

186 Monoclonal antibodies targeting proprotein convertase subtilisin/kexin type 9 (PCSK9) is

187 Do elevated proprotein convertase subtilisin/kexin type 9 (PCSK9) le

188 y, a recent study has shown that circulating proprotein convertase subtilisin/kexin type 9 (PCSK9) le

189 low-density lipoprotein receptor (LDLR) and proprotein convertase subtilisin/kexin type 9 (PCSK9) me

190 Proprotein convertase subtilisin/kexin type 9 (PCSK9) mo

191 Proprotein convertase subtilisin/kexin type 9 (PCSK9) pl

192 Proprotein convertase subtilisin/kexin type 9 (PCSK9) pl

193 olic study to determine the LDL-ApoB-100 and proprotein convertase subtilisin/kexin type 9 (PCSK9) pr

194 The proprotein convertase subtilisin/kexin type 9 (PCSK9) pr

195 Proprotein convertase subtilisin/kexin type 9 (PCSK9) re

196 Proprotein convertase subtilisin/kexin type 9 (PCSK9) re

197 Proprotein convertase subtilisin/kexin type 9 (PCSK9) se

198 5, a fully human monoclonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9) se

199 Biologic-based strategies to inhibit proprotein convertase subtilisin/kexin type 9 (PCSK9) sh

200 eptor (LDLR) binds to its negative regulator proprotein convertase subtilisin/kexin type 9 (PCSK9) th

201 Proprotein convertase subtilisin/kexin type 9 (PCSK9) wa

202 locumab are monoclonal antibodies that block proprotein convertase subtilisin/kexin type 9 (PCSK9), a

203 DL receptor (LDLR), apolipoprotein B (APOB), proprotein convertase subtilisin/kexin type 9 (PCSK9), a

204 Several mutations in the apoB, proprotein convertase subtilisin/kexin type 9 (PCSK9), a

205 , HCV negatively modulated the expression of proprotein convertase subtilisin/kexin type 9 (PCSK9), a

206 Moreover, in the presence of exogenous proprotein convertase subtilisin/kexin type 9 (PCSK9), a

207 resent study was aimed at evaluating whether proprotein convertase subtilisin/kexin type 9 (PCSK9), a

208 ted the hypothesis that ENaC is regulated by proprotein convertase subtilisin/kexin type 9 (PCSK9), a

209 gmentation index, blood glucose, endothelin, proprotein convertase subtilisin/kexin type 9 (PCSK9), a

210 uent AAV9/CRISPR treatment for repression of proprotein convertase subtilisin/kexin type 9 (PCSK9), a

211 ocumab, a fully human monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), d

212 Alirocumab, a monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), l

213 cumab are monoclonal antibodies that bind to proprotein convertase subtilisin/kexin type 9 (PCSK9), l

214 Evolocumab, a monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), r

215 ductase, Niemann-Pick C1-Like 1 (NPC1L1) and proprotein convertase subtilisin/kexin type 9 (PCSK9), r

216 locumab, a monoclonal antibody that inhibits proprotein convertase subtilisin/kexin type 9 (PCSK9), s

217 mab (AMG 145), a monoclonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9), s

218 b, a fully human monoclonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9), s

219 DENV infection induced expression of proprotein convertase subtilisin/kexin type 9 (PCSK9), w

220 e reduced by monoclonal antibodies targeting proprotein convertase subtilisin/kexin type 9 (PCSK9).

221 ssion, and reduced the circulating levels of proprotein convertase subtilisin/kexin type 9 (PCSK9).

222 th evolocumab, a monoclonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9).

223 r adding nonstatin medications (ezetimibe or proprotein convertase subtilisin/kexin type 9 [PCSK9] in

224 Importantly, reduced proprotein convertase subtilisin/kexin type 9 activity i

225 ng LDL-R ligand-binding activity using human proprotein convertase subtilisin/kexin type 9 and platel

226 Plasma proprotein convertase subtilisin/kexin type 9 and total

227 Using proprotein convertase subtilisin/kexin type 9 as a repre

228 not exhibit altered vascular pathology in a proprotein convertase subtilisin/kexin type 9 gain-of-fu

229 requency coding DNA sequence variants in the proprotein convertase subtilisin/kexin type 9 gene (PCSK

230 3-Hydroxy-3-Methylglutaryl-CoA Reductase and Proprotein Convertase Subtilisin/Kexin type 9 genetic sc

231 Surprisingly the Proprotein Convertase Subtilisin/Kexin type 9 genetic sc

232 case, and the opposite was observed for the Proprotein Convertase Subtilisin/Kexin type 9 genetic sc

233 The Proprotein Convertase Subtilisin/Kexin type 9 genetic sc

234 y lipoprotein clearance (the effect of these Proprotein Convertase Subtilisin/Kexin type 9 genotypes)

235 Proprotein convertase subtilisin/kexin type 9 inhibitor

236 The proprotein convertase subtilisin/kexin type 9 inhibitor

237 Preliminary cost-effectiveness analyses of proprotein convertase subtilisin/kexin type 9 inhibitor

238 Alirocumab, a proprotein convertase subtilisin/kexin type 9 inhibitor,

239 Proprotein convertase subtilisin/kexin type 9 inhibitors

240 , 0.34-0.71) vs 0.61 (95% CI, 0.58-0.65) for proprotein convertase subtilisin/kexin type 9 inhibitors

241 apolipoprotein B-containing lipoproteins and proprotein convertase subtilisin/kexin type 9 inhibitors

242 excluded in sepsis clinical trials involving proprotein convertase subtilisin/kexin type 9 inhibitors

243 Thus, there is interest in leveraging proprotein convertase subtilisin/kexin type 9 inhibitors

244 Proprotein convertase subtilisin/kexin type 9 is a centr

245 accumulates in hepatocytes, and knocks down proprotein convertase subtilisin/kexin type 9 level in m

246 Proprotein convertase subtilisin/kexin type 9 loss-of-fu

247 Proprotein convertase subtilisin/kexin type 9 loss-of-fu

248 In contrast to the adult host, proprotein convertase subtilisin/kexin type 9 loss-of-fu

249 Proprotein convertase subtilisin/kexin type 9 monoclonal

250 s were engineered to encode gain-of-function proprotein convertase subtilisin/kexin type 9 mutants, a

251 e, sitosterol, lathosterol, campesterol, and proprotein convertase subtilisin/kexin type 9 plasma con

252 ls with fully human monoclonal antibodies to proprotein convertase subtilisin/kexin type 9 published

253 Inhibition of proprotein convertase subtilisin/kexin type 9 serine pro

254 Proprotein convertase subtilisin/kexin type 9 single-nuc

255 nd provide comprehensive data that targeting proprotein convertase subtilisin/kexin type 9 very effec

256 Genetic analysis has identified PCSK9 (proprotein convertase subtilisin/kexin type 9) as a cruc

257 development of sdAbs targeting human PCSK9 (proprotein convertase subtilisin/kexin type 9) as an alt

258 PCSK9 (proprotein convertase subtilisin/kexin type 9) has emerg

259 PCSK9 (proprotein convertase subtilisin/kexin type 9) has emerg

260 duals who derive greater benefit from PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitio

261 We set out to determine the effect of PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitio

262 short-term trials have suggested that PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitor

263 tion of those events by alirocumab, a PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitor

264 PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitor

265 The PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitor

266 PCSK9 (proprotein convertase subtilisin/kexin type 9) is a nega

267 l) homeostasis through regulating the PCSK9 (proprotein convertase subtilisin/kexin type 9) levels.

268 a fully human monoclonal antibody to PCSK9 (proprotein convertase subtilisin/kexin type 9), markedly

269 Alirocumab, an antibody that blocks PCSK9 (proprotein convertase subtilisin/kexin type 9), was asso

270 )-KO (knockout), LDLr-KO/APOB100, and PCSK9 (proprotein convertase subtilisin/kexin type 9)-overexpre

271 th AdPCSK9 (adenoviral vector overexpressing proprotein convertase subtilisin/kexin type 9).

272 In contrast, bile acids, proprotein convertase subtilisin/kexin type 9, acetate,

273 olled in Vasopressin and Septic Shock Trial, Proprotein Convertase Subtilisin/Kexin type 9, and 3-Hyd

274 ype 9 single-nucleotide polymorphisms, serum proprotein convertase subtilisin/kexin type 9, and lipid

275 ucleotides to apoB, monoclonal antibodies to proprotein convertase subtilisin/kexin type 9, cholester

276 earance, which can be achieved by inhibiting proprotein convertase subtilisin/kexin type 9, may decre

277 Single injections of proprotein convertase subtilisin/kexin type 9-encoding r

278 expression, and higher levels of circulating proprotein convertase subtilisin/kexin type 9.

279 Proprotein convertase subtilisin/kexin type-9 (PCSK9) is

280 Proprotein convertase subtilisin/kexin type-9 (PCSK9) is

281 Proprotein convertase subtilisin/kexin type-9 (PCSK9, a

282 ised by prior trials, pharmacological PCSK9 (proprotein convertase subtilisin/kexin type-9) inhibitio

283 The archetype proprotein convertase subtilisin/kexin, FURIN, is a dire

284 Here we show that proprotein convertase subtilisin/kexin-6 (PCSK6, also na

285 Recently approved proprotein convertase subtilisin/kexin-type 9 inhibitors

286 udy we report that furin is unique among the proprotein convertases subtilisin/kexin in being highly

287 mature form by members of the family of the proprotein convertases subtilisin/kexin.

288 Congenital deficiency of the proprotein convertase subtilisine/kexin type 1 gene (PCS

289 PCSKs (Proprotein convertase subtilisins/kexins) are a protease

290 These analogs inhibit other proprotein convertases, such as PC1/3, PC4, PACE4, and P

291 Furin is a ubiquitous proprotein convertase that cleaves after basic residues

292 Inhibition of PACE4, a proprotein convertase that is overexpressed in prostate

293 st provided a key clue in the search for the proprotein convertases, the endoproteases that work alon

294 o proteolytic processing by furin/subtilisin proprotein convertases to release the active ligand.

295 ade as proprotein dimers and then cleaved by proprotein convertases to release the C-terminal domain

296 We identified that members of the proprotein convertase were rate-limiting enzymes in the

297 wnward arrowArg cleavage motif of furin-like proprotein convertases, whereas the cleavage motif of FR

298 lecular connection between ANGPTL3, LPL, and proprotein convertases, which may represent a rapid sign

299 HJV can be cleaved by the furin family of proprotein convertases, which releases a soluble form of

300 Site-1 protease (S1P) is a proprotein convertase with essential functions in lipid