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1 (4) (cathepsin G) to 7.1 x 10(5) m(-1)s(-1) (subtilisin).
2 en both enzymes, while 37% were exclusive to subtilisin.
3 s targeting the serine proteases trypsin and subtilisin.
4 degrees of hydrolysis (DH) of 3-4-5-6% with subtilisin.
5 s Pronase, proteinase K, pepsin, papain, and subtilisin.
6 ease in its susceptibility to proteolysis by subtilisin.
7 avage of alphaENaC using the serine protease subtilisin.
8 tivity (4.1 microS), and were insensitive to subtilisin.
11 alysis of secretions reveals the presence of subtilisin (a protease) and a 12 kDa protein, termed sib
13 We therefore aimed to protect and maintain subtilisin-A enzyme activity by exploring two pharmaceut
20 ental model of allergic lung inflammation to subtilisin and to determine the immunological mechanisms
21 age of the similarity of SUB1 with bacterial subtilisins and generated P. vivax SUB1 three-dimensiona
22 ophil and pancreatic elastases, cathepsin G, subtilisin, and trypsin) with a stoichiometry of inhibit
24 ixed backbone design, we have redesigned the subtilisin BPN' propeptide structure to generate synthet
26 R spectroscopy experiments were performed on subtilisin Carlsberg colyophilized with several inorgani
27 bute to accelerated catalysis by solubilized subtilisin Carlsberg upon hydration in organic solvents.
29 here that phosphorylation of Tyr-53 inhibits subtilisin cleavage of the D-loop and reduces the rate o
32 t does not inhibit serine peptidases such as subtilisin, elastase, chymotrypsin, thrombin, and plasmi
33 e present how the broad-specificity protease subtilisin enables mapping of previously hidden areas of
34 of all plasmodia and are mapped between the subtilisin-encoding genes SUB1 and SUB3 P. berghei PIMMS
35 t these epitopes can be degraded in vitro by subtilisin enzymes derived from Rothia mucilaginosa, a n
36 entity with fungal serine proteinases of the subtilisin family, indicating that AsES is synthesized a
37 ensitive disulphide bridge, unique among the subtilisin family, that likely acts as a regulator of pr
40 ensitization followed by airway challenge to subtilisin induces prototypic allergic lung inflammation
41 carpus viz., chitinase (CHI4), Alpha-amylase/subtilisin inhibitor (IAAS) and Flavonoid 3_5 hydroxylas
46 Since the discovery of proprotein convertase subtilisin kexin 9 (PCSK9) in 2003, this PC has attracte
47 viral envelope glycoprotein by the cellular subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)
48 glycoprotein precursor (GPC) by the cellular subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)
52 ndogenous inhibitor of proprotein convertase subtilisin kexin type 9 (PCSK9) activity on cell-surface
55 ockers, ezetimibe, and proprotein convertase subtilisin kexin type 9 (PCSK9) inhibitors, are discusse
59 levels of circulating proprotein convertase subtilisin kexin type 9 (PCSK9) would increase cardiovas
61 nal antibodies against proprotein convertase subtilisin kexin type 9 (PCSK9), such as evolocumab, low
62 ibody directed against proprotein convertase subtilisin kexin type 9 (PCSK9), to enable subjects at h
65 inogenesis in some solid tumors, the role of subtilisin-kexin isoenzyme-1 (SKI-1) in this context is
66 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) and lowers low-density l
67 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) and reduces levels of lo
68 acologic inhibitors of proprotein convertase subtilisin-kexin type 9 (PCSK9) are being evaluated in c
70 of drugs that inhibit proprotein convertase subtilisin-kexin type 9 (PCSK9) has been developed to tr
71 odies directed against proprotein convertase subtilisin-kexin type 9 (PCSK9) have been shown to reduc
72 rom clinical trials of proprotein convertase subtilisin-kexin type 9 (PCSK9) inhibitors have led to c
73 nce of the efficacy of proprotein convertase subtilisin-kexin type 9 (PCSK9) inhibitors; however, the
74 on LDL cholesterol and proprotein convertase subtilisin-kexin type 9 (PCSK9) levels were available th
75 ibits the synthesis of proprotein convertase subtilisin-kexin type 9 (PCSK9), a target for the loweri
76 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9), has been shown to reduc
77 nal antibody targeting proprotein convertase subtilisin-kexin type 9 (PCSK9), reduces levels of low-d
78 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9), significantly reduced l
80 t of lipid lowering by proprotein convertase subtilisin-kexin type 9 inhibition in such patients is u
81 esterol reduction with proprotein convertase subtilisin-kexin type 9 inhibitors reduces ischemic even
82 ion variants in PCSK9 (proprotein convertase subtilisin-kexin type 9) are associated with lower lifet
83 vious trials of PCSK9 (proprotein convertase subtilisin-kexin type 9) inhibitors demonstrated reducti
84 ibody directed against proprotein convertase subtilisin-kexin type 9, is widely used in adult patient
86 vertase site 1 protease (S1P), also known as subtilisin-kexin-isozyme 1 (SKI-1), is crucial for cell-
89 in the promoter of the proprotein convertase subtilisin/kexin 9 (PCSK9) gene that was associated with
90 efficacy and safety of proprotein convertase subtilisin/kexin 9 (PCSK9) inhibitors in secondary preve
92 ed that >30% of plasma proprotein convertase subtilisin/kexin 9 (PCSK9) is bound to LDL, thus we pred
94 dy-based inhibitors of preprotein convertase subtilisin/kexin 9 (PCSK9) produce reductions in LDL-C o
95 noclonal antibodies to proprotein convertase subtilisin/kexin 9 (PCSK9) reduce LDL cholesterol in het
96 l due to inhibition of proprotein convertase subtilisin/kexin 9 (PCSK9) reduces cardiovascular events
102 n is unique among the proprotein convertases subtilisin/kexin in being highly expressed in human GIC.
103 educed, and intestinal proprotein convertase subtilisin/kexin type 1 (Pcsk1) expression, the gene enc
104 rare mutations in the proprotein convertase subtilisin/kexin type 1 (PCSK1) gene, has been associate
106 olymorphisms (SNPs) in proprotein convertase subtilisin/kexin type 1 with modest effects on PC1/3 in
108 ies in its convertase, proprotein convertase subtilisin/kexin type 5 (PCSK5), causing inactive GDF11
109 etween ANGPTL3, furin, proprotein convertase subtilisin/kexin type 5 (PCSK5), paired amino acid conve
111 l with an inhibitor of proprotein convertase subtilisin/kexin type 9 (PCSK9) after acute coronary syn
113 individually bind the proprotein convertase subtilisin/kexin type 9 (PCSK9) and regulate its activit
114 ntibodies that inhibit proprotein convertase subtilisin/kexin type 9 (PCSK9) are an emerging therapy
115 ction mutations of the proprotein convertase subtilisin/kexin type 9 (PCSK9) are associated with hype
122 etermine the effect of proprotein convertase subtilisin/kexin type 9 (PCSK9) deficiency on developmen
125 dation mediated by the proprotein convertase subtilisin/kexin type 9 (PCSK9) has been extensively stu
128 ty and efficacy of the proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitor evolocumab in
130 t use of ezetimibe and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors in patients w
133 include ezetimibe and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors, which both r
134 l antibodies targeting proprotein convertase subtilisin/kexin type 9 (PCSK9) is a new lipid-lowering
135 The secreted protein proprotein convertase subtilisin/kexin type 9 (PCSK9) is a promising new targe
138 shown that circulating proprotein convertase subtilisin/kexin type 9 (PCSK9) levels correlate positiv
139 in receptor (LDLR) and proprotein convertase subtilisin/kexin type 9 (PCSK9) messenger ribonucleic ac
144 e the LDL-ApoB-100 and proprotein convertase subtilisin/kexin type 9 (PCSK9) production rate (PR) and
149 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9) serine protease, demonst
150 strategies to inhibit proprotein convertase subtilisin/kexin type 9 (PCSK9) show promise as anti-hyp
151 its negative regulator proprotein convertase subtilisin/kexin type 9 (PCSK9) through the first EGF (e
153 antibodies that block proprotein convertase subtilisin/kexin type 9 (PCSK9), a circulating protein t
154 ment for repression of proprotein convertase subtilisin/kexin type 9 (PCSK9), a gene that, when repre
155 at evaluating whether proprotein convertase subtilisin/kexin type 9 (PCSK9), a key regulator of low-
156 t ENaC is regulated by proprotein convertase subtilisin/kexin type 9 (PCSK9), a protease that modulat
157 ated the expression of proprotein convertase subtilisin/kexin type 9 (PCSK9), a protein that facilita
158 presence of exogenous proprotein convertase subtilisin/kexin type 9 (PCSK9), a protein that reduces
159 d glucose, endothelin, proprotein convertase subtilisin/kexin type 9 (PCSK9), adhesion molecules, and
160 olipoprotein B (APOB), proprotein convertase subtilisin/kexin type 9 (PCSK9), and LDL protein recepto
161 mutations in the apoB, proprotein convertase subtilisin/kexin type 9 (PCSK9), and MTP genes result in
162 monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), demonstrated marked red
163 ntibodies that bind to proprotein convertase subtilisin/kexin type 9 (PCSK9), lowering LDL by about 5
164 monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), lowers plasma low-densi
165 monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), reduced LDL cholesterol
167 antibody that inhibits proprotein convertase subtilisin/kexin type 9 (PCSK9), significantly reduced l
168 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9), significantly reduced l
169 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9), significantly reduced L
170 induced expression of proprotein convertase subtilisin/kexin type 9 (PCSK9), which reduces low-densi
174 ications (ezetimibe or proprotein convertase subtilisin/kexin type 9 [PCSK9] inhibitors) to statin th
175 Importantly, reduced proprotein convertase subtilisin/kexin type 9 activity increases recycling of
176 g activity using human proprotein convertase subtilisin/kexin type 9 and platelet factor-4, whereas t
179 ascular pathology in a proprotein convertase subtilisin/kexin type 9 gain-of-function atherosclerosis
180 quence variants in the proprotein convertase subtilisin/kexin type 9 gene (PCSK9) lower plasma low-de
184 aryl-CoA Reductase and Proprotein Convertase Subtilisin/Kexin type 9 genetic scores should have been
185 e (the effect of these Proprotein Convertase Subtilisin/Kexin type 9 genotypes) may contribute to imp
186 ectiveness analyses of proprotein convertase subtilisin/kexin type 9 inhibitor (PCSK9i) were based on
192 interest in leveraging proprotein convertase subtilisin/kexin type 9 inhibitors as a therapeutic stra
193 ining lipoproteins and proprotein convertase subtilisin/kexin type 9 inhibitors hold promise in reduc
197 cytes, and knocks down proprotein convertase subtilisin/kexin type 9 level in mouse serum down to 20%
200 ast to the adult host, proprotein convertase subtilisin/kexin type 9 loss-of-function is detrimental
202 ncode gain-of-function proprotein convertase subtilisin/kexin type 9 mutants, and mice were given a s
203 erol, campesterol, and proprotein convertase subtilisin/kexin type 9 plasma concentrations and fatty
204 noclonal antibodies to proprotein convertase subtilisin/kexin type 9 published in the last 18 months
207 ve data that targeting proprotein convertase subtilisin/kexin type 9 very effectively reduces LDL-cho
208 has identified PCSK9 (proprotein convertase subtilisin/kexin type 9) as a crucial gene in the regula
209 targeting human PCSK9 (proprotein convertase subtilisin/kexin type 9) as an alternative to anti-PCSK9
212 er benefit from PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibition has not been establi
213 e the effect of PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibition on the risk of VTE,
216 suggested that PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitors are safe and reduce
220 nal antibody to PCSK9 (proprotein convertase subtilisin/kexin type 9), markedly reduces low-density l
221 ody that blocks PCSK9 (proprotein convertase subtilisin/kexin type 9), was associated with reduced ma
222 KO/APOB100, and PCSK9 (proprotein convertase subtilisin/kexin type 9)-overexpressing mice were all si
224 contrast, bile acids, proprotein convertase subtilisin/kexin type 9, acetate, and acetoacetate were
225 nd Septic Shock Trial, Proprotein Convertase Subtilisin/Kexin type 9, and 3-Hydroxy-3-Methylglutaryl-
226 e polymorphisms, serum proprotein convertase subtilisin/kexin type 9, and lipid profiles in patients.
227 noclonal antibodies to proprotein convertase subtilisin/kexin type 9, cholesterol ester transfer prot
228 achieved by inhibiting proprotein convertase subtilisin/kexin type 9, may decrease the systemic infla
229 Single injections of proprotein convertase subtilisin/kexin type 9-encoding recombinant adeno-assoc
234 pharmacological PCSK9 (proprotein convertase subtilisin/kexin type-9) inhibition was not associated w
236 Here we show that proprotein convertase subtilisin/kexin-6 (PCSK6, also named PACE4;) cleaves an
240 acid residues corresponding to the putative subtilisin-like catalytic triad are important but not es
241 chanism and structural characterization of a subtilisin-like collagenolytic protease secreted by a de
243 chonia chlamydosporia belongs to a family of subtilisin-like enzymes that are involved in infection o
244 o V. cholerae in vivo IvaP bears homology to subtilisin-like enzymes, a large family of serine protea
246 cture of MycP1(24-407) to 1.86 A, defining a subtilisin-like fold with a unique N-terminal extension
247 ithelial expression of proprotein convertase subtilisin-like kexin type 9, a key regulator of cholest
250 machinery (including propeptide precursors, subtilisin-like prohormone convertases, amidated product
251 rotein convertase 7 (PC7) is a member of the subtilisin-like proprotein convertase family, which is i
259 identity (<30%) to previously characterized subtilisin-like proteases, and it contains a novel domai
260 tively encoding oxylipin metabolic proteins, subtilisin-like proteases, and other antimicrobial defen
261 s are mediated respectively, by two parasite subtilisin-like proteases, PfSUB1 and PfSUB2, but the fu
263 E activity in seed coat epidermal cells, the subtilisin-like Ser protease SBT1.7, acts on different P
266 dress this issue we have concentrated on the subtilisin-like serine protease encoding gene ABNORMAL L
267 and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretor
269 ng of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 su
271 rtases (PCs) form a family of nine secretory subtilisin-like serine proteases, seven of which cleave
274 convertases (PCs) comprise a large family of subtilisin-like, eukaryotic, serine endoproteases that p
277 (wild type) or PCSK9 (proprotein convertase subtilisin-like/kexin type-9) gain-of-function Ossabaw m
279 resonance (NMR), revealing that it mimics a subtilisin prodomain including a flexible C-terminal pep
283 t the identification and characterization of subtilisin propeptide-like inhibitor 1 (SPI-1) from Arab
284 Gbb and Scw have three functional furin/subtilisin proprotein convertase cleavage sites; two bet
285 that undergo proteolytic processing by furin/subtilisin proprotein convertases to release the active
287 These allergic responses were dependent on subtilisin protease activity, protease-activated recepto
290 onserved regions in a multigene family of 56 subtilisin-related proteolytic enzymes in Arabidopsis th
291 ed and found to be inactive, but exposure to subtilisin resulted in cleavage to the active, 12 kDa fo
292 vide extensive information for understanding subtilisin's substrate binding and catalytic mechanism,
293 mbined with mathematical modeling, show that subtilisin serves to regulate growth of the colony.
297 thways involved in allergic sensitization to subtilisin that potentially contribute to initiate aller
299 haFD retained the ability to be activated by subtilisin to 108.8 +/- 20.9 microS, a level not signifi
300 btained by the combination of three enzymes (subtilisin, trypsin and flavourzyme) employed sequential