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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.
11               Here, we show that addition of subtilisin (50 nm to 2 mum), a serine protease secreted
12 nts but not bovine chymotrypsin or bacterial subtilisin A.
13 alysis of secretions reveals the presence of subtilisin (a protease) and a 12 kDa protein, termed sib
14 vel not significantly different from that of subtilisin activated alphaWT (125.6 +/- 23.9).
15  C-terminal peptide that may insert into the subtilisin active site.
16                                     Finally, subtilisin activity acted as a Th2 adjuvant to an unrela
17 l of the C-terminus of only alpha-tubulin by subtilisin after, but not before, photolabeling is block
18                                     Notably, subtilisin allows reproducible near-complete digestion o
19 cell-coat material is partially sensitive to subtilisin alone, while horizontal top connectors resist
20                       The bacterial protease subtilisin also enhances binding by alphaXbeta2.
21 e kinetically controlled folding reaction of subtilisin, although unusual, is explained by the accrue
22                                      In free subtilisin, amide protons can be categorized according t
23               For example, the half-lives of subtilisin and a Bacillus subtilis lipase were increased
24  PCs are evolutionarily related to bacterial subtilisin and are synthesized as zymogens.
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
27                                     Purified subtilisin and Vpr were shown to be capable of processin
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
30 ions increased the half-life of calcium-free subtilisin at elevated temperature by 15,000-fold.
31                     The propeptide domain of subtilisin BPN' functions as a molecular chaperone for i
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
34                 Finally, we demonstrate that subtilisin can be used for reporter-ion based in-depth q
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.
38                                   The enzyme subtilisin Carlsberg was surfactant-solubilized into two
39       A limit of detection for one protease, Subtilisin carlsberg, was investigated and was establish
40 here that phosphorylation of Tyr-53 inhibits subtilisin cleavage of the D-loop and reduces the rate o
41  alphaFM were activated to similar levels by subtilisin cleavage.
42                                     However, subtilisin considerably improved the coverage of missing
43 olysis, immunoprecipitation experiments, and subtilisin digestion indicate that C19-BPC-discodermolid
44 e propeptide is autoprocessed and removed by subtilisin digestion.
45  methods, that the propeptide domain and the subtilisin domain show distinctive intrinsic stability t
46 ily eliminated without interference from the subtilisin domain.
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
53                                              Subtilisin, Epr and Vpr are members of the subtilisin fa
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
62  prodomain binding affects the energetics of subtilisin folding.
63        An engineered variant of the protease subtilisin from Bacillus amyloliquefaciens, in which the
64 ed phase zero introns across examined fungal subtilisin genes, half of these positions were highly co
65         Because usage of the serine protease subtilisin in the detergent industry resulted in an outb
66 ensitization followed by airway challenge to subtilisin induces prototypic allergic lung inflammation
67 ty for the generation of novel proteinaceous subtilisin inhibitors.
68             Notably, acute administration of subtilisin into the airways increased lung IL-5-producin
69                Like many secreted proteases, subtilisin is kinetically stable in the mature form but
70                      These data suggest that subtilisin is the maturase for tryparedoxin peroxidases
71                                       Native subtilisin is thermodynamically unstable in the absence
72                  Serum proprotein convertase subtilisin kexin 9 (PCSK9) binds to low-density lipoprot
73 Since the discovery of proprotein convertase subtilisin kexin 9 (PCSK9) in 2003, this PC has attracte
74                        Proprotein convertase subtilisin kexin 9 (PCSK9) is a member of the subtilisin
75 glycoprotein precursor (GPC) by the cellular subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P)
76                    The proprotein convertase 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)
78                    The proprotein convertase subtilisin kexin isozyme-1 (SKI-1)/site-1 protease (S1P)
79                                              Subtilisin kexin isozyme-1/site-1 protease (SKI-1/S1P) p
80 (dec-RRLL-cmk), inhibitors of SKI-1 (site 1; subtilisin kexin like-1) protease.
81 ndogenous inhibitor of proprotein convertase subtilisin kexin type 9 (PCSK9) activity on cell-surface
82 poprotein B (APOB), or proprotein convertase subtilisin kexin type 9 (PCSK9) genes.
83                        Proprotein convertase subtilisin kexin type 9 (PCSK9) inhibitors produce incre
84 ockers, ezetimibe, and proprotein convertase subtilisin kexin type 9 (PCSK9) inhibitors, are discusse
85                        Proprotein convertase subtilisin kexin type 9 (PCSK9) levels are frequently fo
86                        Proprotein convertase subtilisin kexin type 9 (PCSK9) promotes the degradation
87              Levels of proprotein convertase subtilisin kexin type 9 (PCSK9) vary markedly across the
88  levels of circulating proprotein convertase subtilisin kexin type 9 (PCSK9) would increase cardiovas
89 lonal antibody against proprotein convertase subtilisin kexin type 9 (PCSK9), on Lp(a).
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
92 by reduced activity of proprotein convertase subtilisin kexin type 9.
93 ol-lowering drugs, the proprotein convertase subtilisin kexin-9 inhibitors.
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
98                        Proprotein convertase subtilisin-kexin type 9 (PCSK9) binds to the low-density
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
107 monoclonal antibody to proprotein convertase subtilisin-kexin type 9 (PCSK9).
108 vertase site 1 protease (S1P), also known as subtilisin-kexin-isozyme 1 (SKI-1), is crucial for cell-
109                        Proprotein convertase subtilisin/kexin (PCSK) enzymes convert proproteins into
110                  Serum proprotein convertase subtilisin/kexin 9 (PCSK9) binds to low-density lipoprot
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
116                        Proprotein convertase subtilisin/kexin 9 (PCSK9) regulates plasma LDL choleste
117                        Proprotein convertase subtilisin/kexin 9 (PCSK9), one of the serine proteases,
118 , apolipoprotein B, or proprotein convertase subtilisin/kexin 9.
119                    The proprotein convertase subtilisin/kexin enzymes proteolytically convert immatur
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
123 ulated transcript, and proprotein convertase subtilisin/kexin type 1 inhibitor.
124 olymorphisms (SNPs) in proprotein convertase subtilisin/kexin type 1 with modest effects on PC1/3 in
125                        Proprotein convertase subtilisin/kexin type 2 (PCSK2) is a prohormone processi
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
128                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) and inducible degrader o
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
132           Mutations in proprotein convertase subtilisin/kexin type 9 (PCSK9) are strongly associated
133  an important role for proprotein convertase subtilisin/kexin type 9 (PCSK9) as a determinant of plas
134                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) binds LDL receptors, tar
135                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) binds low-density lipopr
136                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) binds to LDL receptors,
137                 Plasma proprotein convertase subtilisin/kexin type 9 (PCSK9) binds to low-density lip
138                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) binds to the low-density
139 etermine the effect of proprotein convertase subtilisin/kexin type 9 (PCSK9) deficiency on developmen
140                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) down-regulates surface e
141                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) down-regulates the low-d
142 dation mediated by the proprotein convertase subtilisin/kexin type 9 (PCSK9) has been extensively stu
143                Soluble proprotein convertase subtilisin/kexin type 9 (PCSK9) has been shown to be pre
144                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) increases serum LDL-chol
145 ty and efficacy of the proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitor evolocumab in
146                    The proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitor evolocumab red
147 t use of ezetimibe and proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors in patients w
148                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors substantially
149                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) inhibitors were recently
150                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) is a member of the prote
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
153                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) is a secreted protein th
154                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) is an important factor i
155            Do elevated proprotein convertase subtilisin/kexin type 9 (PCSK9) levels constitute an eve
156 in receptor (LDLR) and proprotein convertase subtilisin/kexin type 9 (PCSK9) messenger ribonucleic ac
157                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) modulates low-density li
158                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) plays a key role in regu
159                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) plays an important role
160                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) posttranslationally regu
161 e the LDL-ApoB-100 and proprotein convertase subtilisin/kexin type 9 (PCSK9) production rate (PR) and
162                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) promotes degradation of
163                    The proprotein convertase subtilisin/kexin type 9 (PCSK9) promotes independently o
164                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) regulates low density li
165                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) regulates low density li
166                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) regulates serum LDL chol
167                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) selectively binds low-de
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
170           Mutations in proprotein convertase subtilisin/kexin type 9 (PCSK9) that are associated with
171 its negative regulator proprotein convertase subtilisin/kexin type 9 (PCSK9) through the first EGF (e
172                        Proprotein convertase subtilisin/kexin type 9 (PCSK9) was shown to have a mutu
173  antibodies that block proprotein convertase subtilisin/kexin type 9 (PCSK9), a circulating protein t
174                        Proprotein convertase subtilisin/kexin type 9 (PCSK9), a member of the protein
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
187 l antibodies targeting proprotein convertase subtilisin/kexin type 9 (PCSK9).
188 lonal antibody against proprotein convertase subtilisin/kexin type 9 (PCSK9).
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
191                 Plasma proprotein convertase subtilisin/kexin type 9 and total cholesterol increased
192                  Using proprotein convertase subtilisin/kexin type 9 as a representative protein targ
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
196                    The proprotein convertase subtilisin/kexin type 9 inhibitor evolocumab has been de
197 95% CI, 0.58-0.65) for proprotein convertase subtilisin/kexin type 9 inhibitors (P = .25).
198                        Proprotein convertase subtilisin/kexin type 9 inhibitors (PCSK9i) are a novel
199 ining lipoproteins and proprotein convertase subtilisin/kexin type 9 inhibitors hold promise in reduc
200                        Proprotein convertase subtilisin/kexin type 9 monoclonal antibodies can reduce
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
204          Inhibition of proprotein convertase subtilisin/kexin type 9 serine protease (PCSK9) resulted
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
211                 PCSK9 (proprotein convertase subtilisin/kexin type 9) has emerged as a novel therapeu
212                 PCSK9 (proprotein convertase subtilisin/kexin type 9) has emerged as an important reg
213             The PCSK9 (proprotein convertase subtilisin/kexin type 9) inhibitor evolocumab reduced lo
214                 PCSK9 (proprotein convertase subtilisin/kexin type 9) is a negative regulator of the
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
219          PCSK9 encodes proprotein convertase subtilisin/kexin type 9a (PCSK9), a member of the protei
220                        Proprotein convertase subtilisin/kexin type-9 (PCSK9) is a secreted protein th
221                        Proprotein convertase subtilisin/kexin type-9 (PCSK9, a hepatic LDL-receptor r
222 pharmacological PCSK9 (proprotein convertase subtilisin/kexin type-9) inhibition was not associated w
223          The archetype proprotein convertase subtilisin/kexin, FURIN, is a direct target gene of the
224      Here we show that proprotein convertase subtilisin/kexin-6 (PCSK6, also named PACE4;) cleaves an
225      Recently approved proprotein convertase subtilisin/kexin-type 9 inhibitors and mipomersen lower
226  of the family of the proprotein convertases subtilisin/kexin.
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
231                                Here, a novel subtilisin-like collagenolytic protease, myroicolsin, wh
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
237 lipoprotein B-100, and proprotein convertase subtilisin-like kexin type 9.
238 olipoprotein B-100 and proprotein convertase subtilisin-like kexin type 9.
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
241 motes FGF23 cleavage and inactivation by the subtilisin-like proprotein convertase furin.
242 0), within the FGF23 R(176)XXR(179)/S(180)AE subtilisin-like proprotein convertase motif.
243                                              Subtilisin-like proprotein convertases (SPCs) are a fami
244  inactive precursor molecules by a family of subtilisin-like proprotein convertases (SPCs).
245 was found to be derived from a member of the subtilisin-like protease (subtilase) family.
246                  We previously showed that a subtilisin-like protease called PfSUB1 regulates egress
247                                          The subtilisin-like protease P69B was identified as a substr
248 nclude ABNORMAL LEAF SHAPE1, which encodes a subtilisin-like protease previously shown to have a simi
249                                              Subtilisin-like proteases and other pathogenesis-related
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
252 ghei protein with structural similarities to subtilisin-like proteins.
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
255 on site for site-1 protease (AtS1P), a plant subtilisin-like serine protease (subtilase).
256 dress this issue we have concentrated on the subtilisin-like serine protease encoding gene ABNORMAL L
257 d inhibit the pathogenesis-related (PR) P69B subtilisin-like serine protease of tomato.
258  and invasion, controlling maturation of the subtilisin-like serine protease SUB1 in exoneme secretor
259                                The essential subtilisin-like serine protease SUB1 of Plasmodium meroz
260 ng of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 su
261                                              Subtilisin-like serine proteases (SBTs) are extracellula
262                           The propeptides of subtilisin-like serine proteinases (subtilases, SBTs) se
263                                   Instead, a subtilisin-like serine-dependent plant protease named ph
264 convertases (PCs) comprise a large family of subtilisin-like, eukaryotic, serine endoproteases that p
265                 PCSK9 (proprotein convertase subtilisin-like/kexin type 9) is an emerging target for
266 sidues, Trp106 and Trp113, on the surface of subtilisin located on one of the two helices that form t
267                                        Thus, subtilisin might be particularly beneficial for system-w
268  of the subtilisin prodomain and a series of subtilisin mutants, which were designed to explore the s
269 ll wall material, or the processing protease subtilisin or Vpr.
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
272       The substrate is based on a stabilized subtilisin prodomain, extended across the active site by
273             Below a threshold concentration, subtilisin promotes colony growth and expansion.
274                                     Purified subtilisin promotes the growth and expansion of P. dendr
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
278                                          The subtilisin protease (SUB; Clan SB, family S8) of Leishma
279   These allergic responses were dependent on subtilisin protease activity, protease-activated recepto
280                                          The subtilisin protease TgSUB1 trims several MICs on the par
281                                         Like subtilisin proteases in other Apicomplexan parasites, Bd
282 tely 80-kDa passenger domain that contains a subtilisin-related domain.
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,
288 mediate as well as why the unfolding of free subtilisin seldom occurs via this intermediate.
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.
291                                        Also, subtilisin stimulated the expression of the proallergic
292 ene product (BdSUB-1) clearly belongs to the subtilisin superfamily and shows significant homology to
293 well studied endopeptidases belonging to the subtilisin superfamily.
294 at purified StmPr1 behaves more similarly to subtilisin than to trypsin.
295 thways involved in allergic sensitization to subtilisin that potentially contribute to initiate aller
296  our knowledge, the first report of a fungal subtilisin that shows eliciting activity in plants.
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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