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1 (4) (cathepsin G) to 7.1 x 10(5) m(-1)s(-1) (subtilisin).
2 s Pronase, proteinase K, pepsin, papain, and subtilisin.
3 ease in its susceptibility to proteolysis by subtilisin.
4 avage of alphaENaC using the serine protease subtilisin.
5 tivity (4.1 microS), and were insensitive to subtilisin.
6 r throughout the main structural elements of subtilisin.
7 zing 12 amino acid positions in calcium-free subtilisin.
8 en both enzymes, while 37% were exclusive to subtilisin.
9 s targeting the serine proteases trypsin and subtilisin.
10 degrees of hydrolysis (DH) of 3-4-5-6% with subtilisin.
13 alysis of secretions reveals the presence of subtilisin (a protease) and a 12 kDa protein, termed sib
17 l of the C-terminus of only alpha-tubulin by subtilisin after, but not before, photolabeling is block
19 cell-coat material is partially sensitive to subtilisin alone, while horizontal top connectors resist
21 e kinetically controlled folding reaction of subtilisin, although unusual, is explained by the accrue
25 ve to calcium chelation and proteolysis with subtilisin and reappears at the tips of stereocilia as t
26 ental model of allergic lung inflammation to subtilisin and to determine the immunological mechanisms
28 age of the similarity of SUB1 with bacterial subtilisins and generated P. vivax SUB1 three-dimensiona
29 ophil and pancreatic elastases, cathepsin G, subtilisin, and trypsin) with a stoichiometry of inhibit
32 ixed backbone design, we have redesigned the subtilisin BPN' propeptide structure to generate synthet
33 oevolved high activity and hyperstability in subtilisin by sequentially randomizing 12 amino acid pos
35 examine the motion of enzyme-bound water on subtilisin Carlsberg co-lyophilized with inorganic salts
36 R spectroscopy experiments were performed on subtilisin Carlsberg colyophilized with several inorgani
37 bute to accelerated catalysis by solubilized subtilisin Carlsberg upon hydration in organic solvents.
40 here that phosphorylation of Tyr-53 inhibits subtilisin cleavage of the D-loop and reduces the rate o
43 olysis, immunoprecipitation experiments, and subtilisin digestion indicate that C19-BPC-discodermolid
45 methods, that the propeptide domain and the subtilisin domain show distinctive intrinsic stability t
47 the interface between the propeptide and the subtilisin domains play a key role in maintaining the di
48 residue propeptide at the N-terminal end of subtilisin E plays an essential role in subtilisin foldi
49 t does not inhibit serine peptidases such as subtilisin, elastase, chymotrypsin, thrombin, and plasmi
50 h the calcium chelator BAPTA or the protease subtilisin enabled these links to be further distinguish
51 e present how the broad-specificity protease subtilisin enables mapping of previously hidden areas of
52 of all plasmodia and are mapped between the subtilisin-encoding genes SUB1 and SUB3 P. berghei PIMMS
54 the three proteases that fit these criteria, subtilisin, Epr and Vpr, had a defect in CSF production.
55 Subtilisin, Epr and Vpr are members of the subtilisin family of proteases that are widespread in ba
56 entity with fungal serine proteinases of the subtilisin family, indicating that AsES is synthesized a
57 ensitive disulphide bridge, unique among the subtilisin family, that likely acts as a regulator of pr
58 e physical nature of the kinetic barriers to subtilisin folding and to show how the prodomain overcom
59 d of subtilisin E plays an essential role in subtilisin folding as a tailor-made intramolecular chape
60 n protein folding, but its effect in slowing subtilisin folding is amplified because of the instabili
61 opeptide not only plays an essential role in subtilisin folding, but upon completion of folding it be
64 ed phase zero introns across examined fungal subtilisin genes, half of these positions were highly co
66 ensitization followed by airway challenge to subtilisin induces prototypic allergic lung inflammation
73 Since the discovery of proprotein convertase subtilisin kexin 9 (PCSK9) in 2003, this PC has attracte
75 glycoprotein precursor (GPC) by the cellular subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)
77 viral envelope glycoprotein by the cellular subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)
81 ndogenous inhibitor of proprotein convertase subtilisin kexin type 9 (PCSK9) activity on cell-surface
84 ockers, ezetimibe, and proprotein convertase subtilisin kexin type 9 (PCSK9) inhibitors, are discusse
88 levels of circulating proprotein convertase subtilisin kexin type 9 (PCSK9) would increase cardiovas
90 nal antibodies against proprotein convertase subtilisin kexin type 9 (PCSK9), such as evolocumab, low
91 ibody directed against proprotein convertase subtilisin kexin type 9 (PCSK9), to enable subjects at h
94 inogenesis in some solid tumors, the role of subtilisin-kexin isoenzyme-1 (SKI-1) in this context is
95 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) and lowers low-density l
96 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9) and reduces levels of lo
97 acologic inhibitors of proprotein convertase subtilisin-kexin type 9 (PCSK9) are being evaluated in c
99 of drugs that inhibit proprotein convertase subtilisin-kexin type 9 (PCSK9) has been developed to tr
100 rom clinical trials of proprotein convertase subtilisin-kexin type 9 (PCSK9) inhibitors have led to c
101 nce of the efficacy of proprotein convertase subtilisin-kexin type 9 (PCSK9) inhibitors; however, the
102 on LDL cholesterol and proprotein convertase subtilisin-kexin type 9 (PCSK9) levels were available th
103 ibits the synthesis of proprotein convertase subtilisin-kexin type 9 (PCSK9), a target for the loweri
104 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9), has been shown to reduc
105 nal antibody targeting proprotein convertase subtilisin-kexin type 9 (PCSK9), reduces levels of low-d
106 antibody that inhibits proprotein convertase subtilisin-kexin type 9 (PCSK9), significantly reduced l
108 vertase site 1 protease (S1P), also known as subtilisin-kexin-isozyme 1 (SKI-1), is crucial for cell-
111 in the promoter of the proprotein convertase subtilisin/kexin 9 (PCSK9) gene that was associated with
112 efficacy and safety of proprotein convertase subtilisin/kexin 9 (PCSK9) inhibitors in secondary preve
113 ed that >30% of plasma proprotein convertase subtilisin/kexin 9 (PCSK9) is bound to LDL, thus we pred
114 dy-based inhibitors of preprotein convertase subtilisin/kexin 9 (PCSK9) produce reductions in LDL-C o
115 noclonal antibodies to proprotein convertase subtilisin/kexin 9 (PCSK9) reduce LDL cholesterol in het
120 n is unique among the proprotein convertases subtilisin/kexin in being highly expressed in human GIC.
121 educed, and intestinal proprotein convertase subtilisin/kexin type 1 (Pcsk1) expression, the gene enc
122 rare mutations in the proprotein convertase subtilisin/kexin type 1 (PCSK1) gene, has been associate
124 olymorphisms (SNPs) in proprotein convertase subtilisin/kexin type 1 with modest effects on PC1/3 in
126 ies in its convertase, proprotein convertase subtilisin/kexin type 5 (PCSK5), causing inactive GDF11
127 etween ANGPTL3, furin, proprotein convertase subtilisin/kexin type 5 (PCSK5), paired amino acid conve
129 individually bind the proprotein convertase subtilisin/kexin type 9 (PCSK9) and regulate its activit
130 ntibodies that inhibit proprotein convertase subtilisin/kexin type 9 (PCSK9) are an emerging therapy
131 ction mutations of the proprotein convertase subtilisin/kexin type 9 (PCSK9) are associated with hype
133 an important role for proprotein convertase subtilisin/kexin type 9 (PCSK9) as a determinant of plas
139 etermine the effect of proprotein convertase subtilisin/kexin type 9 (PCSK9) deficiency on developmen
142 dation mediated by the proprotein convertase subtilisin/kexin type 9 (PCSK9) has been extensively stu
145 ty and efficacy of the proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitor evolocumab in
147 t use of ezetimibe and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors in patients w
151 l antibodies targeting proprotein convertase subtilisin/kexin type 9 (PCSK9) is a new lipid-lowering
152 The secreted protein proprotein convertase subtilisin/kexin type 9 (PCSK9) is a promising new targe
156 in receptor (LDLR) and proprotein convertase subtilisin/kexin type 9 (PCSK9) messenger ribonucleic ac
161 e the LDL-ApoB-100 and proprotein convertase subtilisin/kexin type 9 (PCSK9) production rate (PR) and
168 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9) serine protease, demonst
169 strategies to inhibit proprotein convertase subtilisin/kexin type 9 (PCSK9) show promise as anti-hyp
171 its negative regulator proprotein convertase subtilisin/kexin type 9 (PCSK9) through the first EGF (e
173 antibodies that block proprotein convertase subtilisin/kexin type 9 (PCSK9), a circulating protein t
175 t ENaC is regulated by proprotein convertase subtilisin/kexin type 9 (PCSK9), a protease that modulat
176 ated the expression of proprotein convertase subtilisin/kexin type 9 (PCSK9), a protein that facilita
177 presence of exogenous proprotein convertase subtilisin/kexin type 9 (PCSK9), a protein that reduces
178 olipoprotein B (APOB), proprotein convertase subtilisin/kexin type 9 (PCSK9), and LDL protein recepto
179 mutations in the apoB, proprotein convertase subtilisin/kexin type 9 (PCSK9), and MTP genes result in
180 monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), demonstrated marked red
181 ntibodies that bind to proprotein convertase subtilisin/kexin type 9 (PCSK9), lowering LDL by about 5
182 monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), lowers plasma low-densi
183 monoclonal antibody to proprotein convertase subtilisin/kexin type 9 (PCSK9), reduced LDL cholesterol
184 antibody that inhibits proprotein convertase subtilisin/kexin type 9 (PCSK9), significantly reduced l
185 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9), significantly reduced l
186 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9), significantly reduced L
189 Importantly, reduced proprotein convertase subtilisin/kexin type 9 activity increases recycling of
190 g activity using human proprotein convertase subtilisin/kexin type 9 and platelet factor-4, whereas t
193 ascular pathology in a proprotein convertase subtilisin/kexin type 9 gain-of-function atherosclerosis
194 quence variants in the proprotein convertase subtilisin/kexin type 9 gene (PCSK9) lower plasma low-de
195 ectiveness analyses of proprotein convertase subtilisin/kexin type 9 inhibitor (PCSK9i) were based on
199 ining lipoproteins and proprotein convertase subtilisin/kexin type 9 inhibitors hold promise in reduc
201 ncode gain-of-function proprotein convertase subtilisin/kexin type 9 mutants, and mice were given a s
202 erol, campesterol, and proprotein convertase subtilisin/kexin type 9 plasma concentrations and fatty
203 noclonal antibodies to proprotein convertase subtilisin/kexin type 9 published in the last 18 months
205 sense mutations in the proprotein convertase subtilisin/kexin type 9 serine protease gene (PCSK9) cau
206 quence variants in the proprotein convertase subtilisin/kexin type 9 serine protease gene (PCSK9) tha
207 ve data that targeting proprotein convertase subtilisin/kexin type 9 very effectively reduces LDL-cho
208 utations within PCSK9 (proprotein convertase subtilisin/kexin type 9) are associated with dominant fo
209 has identified PCSK9 (proprotein convertase subtilisin/kexin type 9) as a crucial gene in the regula
210 targeting human PCSK9 (proprotein convertase subtilisin/kexin type 9) as an alternative to anti-PCSK9
215 nal antibody to PCSK9 (proprotein convertase subtilisin/kexin type 9), markedly reduces low-density l
216 noclonal antibodies to proprotein convertase subtilisin/kexin type 9, cholesterol ester transfer prot
217 achieved by inhibiting proprotein convertase subtilisin/kexin type 9, may decrease the systemic infla
218 Single injections of proprotein convertase subtilisin/kexin type 9-encoding recombinant adeno-assoc
222 pharmacological PCSK9 (proprotein convertase subtilisin/kexin type-9) inhibition was not associated w
224 Here we show that proprotein convertase subtilisin/kexin-6 (PCSK6, also named PACE4;) cleaves an
227 lthough effects of the proprotein convertase subtilisin/kexine type 9 gene (PCSK9) need fuller explor
228 F-A domain resides on the surface of PCSK9's subtilisin-like catalytic domain containing Asp-374, a r
229 acid residues corresponding to the putative subtilisin-like catalytic triad are important but not es
230 chanism and structural characterization of a subtilisin-like collagenolytic protease secreted by a de
232 We conclude that glycoprotein cleavage by subtilisin-like endoproteases is not critical for Ebola
233 chonia chlamydosporia belongs to a family of subtilisin-like enzymes that are involved in infection o
234 cture of MycP1(24-407) to 1.86 A, defining a subtilisin-like fold with a unique N-terminal extension
235 serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and
236 ithelial expression of proprotein convertase subtilisin-like kexin type 9, a key regulator of cholest
239 -islet cells and is processed in parallel by subtilisin-like prohormone convertases prior to secretio
240 rotein convertase 7 (PC7) is a member of the subtilisin-like proprotein convertase family, which is i
248 nclude ABNORMAL LEAF SHAPE1, which encodes a subtilisin-like protease previously shown to have a simi
250 identity (<30%) to previously characterized subtilisin-like proteases, and it contains a novel domai
251 s are mediated respectively, by two parasite subtilisin-like proteases, PfSUB1 and PfSUB2, but the fu
253 E activity in seed coat epidermal cells, the subtilisin-like Ser protease SBT1.7, acts on different P
254 lt stress response in Arabidopsis requires a subtilisin-like serine protease (AtS1P), related to mamm
256 dress this issue we have concentrated on the subtilisin-like serine protease encoding gene ABNORMAL L
258 and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretor
260 ng of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 su
264 convertases (PCs) comprise a large family of subtilisin-like, eukaryotic, serine endoproteases that p
266 sidues, Trp106 and Trp113, on the surface of subtilisin located on one of the two helices that form t
268 of the subtilisin prodomain and a series of subtilisin mutants, which were designed to explore the s
270 died the bimolecular folding reaction of the subtilisin prodomain and a series of subtilisin mutants,
271 resonance (NMR), revealing that it mimics a subtilisin prodomain including a flexible C-terminal pep
275 t the identification and characterization of subtilisin propeptide-like inhibitor 1 (SPI-1) from Arab
276 Gbb and Scw have three functional furin/subtilisin proprotein convertase cleavage sites; two bet
277 that undergo proteolytic processing by furin/subtilisin proprotein convertases to release the active
279 These allergic responses were dependent on subtilisin protease activity, protease-activated recepto
283 onserved regions in a multigene family of 56 subtilisin-related proteolytic enzymes in Arabidopsis th
284 ed and found to be inactive, but exposure to subtilisin resulted in cleavage to the active, 12 kDa fo
285 rdinately slow folding of the mature form of subtilisin results from the accrued effects of two slow
286 t folding intermediates results in part from subtilisin's high dependence on metal binding for stabil
287 vide extensive information for understanding subtilisin's substrate binding and catalytic mechanism,
289 ubtilisin kexin 9 (PCSK9) is a member of the subtilisin serine protease family with an important role
290 mbined with mathematical modeling, show that subtilisin serves to regulate growth of the colony.
292 ene product (BdSUB-1) clearly belongs to the subtilisin superfamily and shows significant homology to
295 thways involved in allergic sensitization to subtilisin that potentially contribute to initiate aller
297 yl peptidases have a fold resembling that of subtilisin, the proton transfer processes during the nuc
298 haFD retained the ability to be activated by subtilisin to 108.8 +/- 20.9 microS, a level not signifi
299 mide protons in free and prodomain-complexed subtilisin were determined in order to understand how th
300 and shows significant homology to Plasmodium subtilisins, with the highest degree of sequence identit
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