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

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

4 y pathway through the activity of furin-like 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 PACE4, a proprotein convertase, activates membrane type matrix me

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 The proprotein convertases are believed to be responsible fo

23 10 zymogen is processed by a subtilisin-like proprotein convertase at two sites (Arg64/Gly and Arg233

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

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

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

27 somes recognize only the luminal products of proprotein convertase cleavage and not the remaining pro

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

29 ino acid position 583 between the furin-like proprotein convertase cleavage site and the transmembran

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

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

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

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

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

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

36 he activation process is then completed by a proprotein convertase cleaving the inhibitory prodomain

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

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

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

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

41 se searches identified a novel member of the proprotein convertase family called proprotein convertas

42 Furin is one of seven proprotein convertase family members that promote proteo

43 The proprotein convertase family of enzymes includes seven e

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

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

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

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

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

49 The proprotein convertase furin requires the pH gradient of

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

51 statin can be cleaved extracellularly by the proprotein convertase furin.

52 ependent on metalloprotease activity and the proprotein convertase furin.

53 the activity of the cellular subtilisin-like proprotein convertase furin.

54 nvelope glycoprotein, prM, is cleaved by the proprotein convertase furin; this cleavage is required f

55 ing secretion, indicating that inhibition of proprotein convertases (furin) represents a viable thera

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

57 ut a third gene (PCSK9), encoding a putative proprotein convertase, has recently been implicated.

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

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

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

61 on-redundant functions of furin versus other proprotein convertases in T cells are unclear.

62 Moreover, cells and medium treated with the proprotein convertase inhibitor decanoyl-Arg-Val-Lys-Arg

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

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

65 Furin, a potent proprotein convertase involved in activation of several

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

67 Cleavage by furin, a cell-encoded proprotein convertase, is known to be required for endos

68 uggests that furin, a ubiquitously expressed proprotein convertase, is the likely processing enzyme.

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

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

71 tion activation of this pool by furin family proprotein convertases may therefore represent a major c

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

73 s a large precursor protein, which undergoes proprotein convertase-mediated proteolytic maturation al

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

75 Blisterase is a subtilisin-like proprotein convertase of nematodes.

76 can be used to determine the specificity of proprotein convertases on recombinant precursors, and (3

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

78 A highly conserved furin/proprotein convertase (PC) cleavage site motif (RSKR247)

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

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

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

82 e RNKR, a known recognition sequence for the proprotein convertase (PC) family.

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

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

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

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

87 Surprisingly, a ubiquitously expressed proprotein convertase (PC), furin, was one of the most c

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

89 requires cleavage of Pmel17 by a furin-like proprotein convertase (PC).

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

91 ine selectivity that defines the prohormone (proprotein) convertase (PC) family.

92 Proprotein convertases (PCs) are crucial in the processi

93 Proprotein convertases (PCs) are highly specific proteas

94 Proprotein convertases (PCs) comprise a large family of

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

96 The proprotein convertases (PCs) furin and proprotein conver

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

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

99 ggest an important role of furin and related proprotein convertases (PCs) in mediating both the activ

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

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

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

103 which allows us to determine the identity of proprotein convertases (PCs) related to the processing o

104 Processing of polypeptide precursors by proprotein convertases (PCs) such as furin typically occ

105 d anthrax toxins, require processing by host proprotein convertases (PCs) to enter host cells and to

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

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

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

109 Proprotein convertases play an important role in tumorig

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

111 Propeptides of proprotein convertases regulate activation of their prot

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

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

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

115 The cellular proprotein convertase site 1 protease (S1P) has been imp

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

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

118 Cleavage at a probable proprotein convertase site produces a large extracellula

119 Furin, a human subtilisin-related proprotein convertase (SPC), is emerging as an important

120 type lubricin, mediated by a subtilisin-like proprotein convertase (SPC).

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

122 , an activity carried out by subtilisin-like proprotein convertases (SPCs) in constitutive or regulat

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

124 e proteolytically removed by subtilisin-like proprotein convertases (SPCs).

125 acellularly active family of subtilisin-like proprotein convertases (SPCs).

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

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

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

129 Proprotein convertase subtilisin kexin 9 (PCSK9) is a me

130 Proprotein convertase subtilisin kexin 9 (Pcsk9) is a su

131 r of the proprotein convertase family called proprotein convertase subtilisin kexin 9 (PCSK9).

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

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

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

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

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

137 Proprotein convertase subtilisin kexin type 9 (PCSK9) in

138 Proprotein convertase subtilisin kexin type 9 (PCSK9) le

139 Proprotein convertase subtilisin kexin type 9 (PCSK9) pr

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

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

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

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

144 145, a monoclonal antibody directed against proprotein convertase subtilisin kexin type 9 (PCSK9), t

145 radation is disrupted by reduced activity of proprotein convertase subtilisin kexin type 9.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

164 Proprotein convertase subtilisin/kexin (PCSK) enzymes co

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

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

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

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

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

170 Proprotein convertase subtilisin/kexin 9 (PCSK9) regulat

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

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

173 The proprotein convertase subtilisin/kexin enzymes proteolyt

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

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

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

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

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

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

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

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

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

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

184 Mutations in proprotein convertase subtilisin/kexin type 9 (PCSK9) ar

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

186 dies have demonstrated an important role for proprotein convertase subtilisin/kexin type 9 (PCSK9) as

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

213 Proprotein convertase subtilisin/kexin type 9 (PCSK9) po

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

215 Proprotein convertase subtilisin/kexin type 9 (PCSK9) pr

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

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

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

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

220 5, a fully human monoclonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9) se

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

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

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

224 Mutations in proprotein convertase subtilisin/kexin type 9 (PCSK9) th

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

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

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

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

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

230 Proprotein convertase subtilisin/kexin type 9 (PCSK9), a

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

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

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

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

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

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

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

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

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

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

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

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

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

244 Plasma proprotein convertase subtilisin/kexin type 9 and total

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

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

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

248 100 gene (APOB), and the recently identified proprotein convertase subtilisin/kexin type 9 gene (PCSK

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

250 The proprotein convertase subtilisin/kexin type 9 inhibitor

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

252 Proprotein convertase subtilisin/kexin type 9 inhibitors

253 , 0.34-0.71) vs 0.61 (95% CI, 0.58-0.65) for proprotein convertase subtilisin/kexin type 9 inhibitors

254 Proprotein convertase subtilisin/kexin type 9 monoclonal

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

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

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

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

259 Selected missense mutations in the proprotein convertase subtilisin/kexin type 9 serine pro

260 sence or absence of sequence variants in the proprotein convertase subtilisin/kexin type 9 serine pro

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

262 Mutations within PCSK9 (proprotein convertase subtilisin/kexin type 9) are assoc

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

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

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

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

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

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

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

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

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

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

273 PCSK9 encodes proprotein convertase subtilisin/kexin type 9a (PCSK9),

274 e of the four genes was PCSK9, which encodes proprotein convertase subtilisin/kexin type 9a, a protei

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

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

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

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

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

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

281 pears to be minimal, although effects of the proprotein convertase subtilisin/kexine type 9 gene (PCS

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

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

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

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

286 reviously showed that EL could be cleaved by proprotein convertases, such as PC5, resulting in loss o

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

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

289 Kex2 and human furin are subtilisin-related proprotein convertases that function in the late secreto

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

291 cellular MT1-MMP is regulated by furin-like proprotein convertases, TIMPs, shedding, autoproteolysis

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

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

294 lytic domain shares high homology with other proprotein convertases, we designed mutations in the cat

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

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

297 tide requires cleavage of pro-myostatin by a proprotein convertase, which is thought to occur constit

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