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1 ysis of catalytic specificity of an aspartic peptidase.
2 cteria by over activating the bacterial ClpP peptidase.
3 genesis studies identify LspA as an aspartyl peptidase.
4 e thioester bond, which covalently traps the peptidase.
5 at contains the cleavage site for the signal peptidase.
6 and the function of mitochondrial processing peptidase.
7 , followed by cleavage by the inner membrane peptidase.
8 at is the first member of a new subfamily of peptidases.
9 bstrate profiling technique to define active peptidases.
10 mmensal bacteria requires them to evade host peptidases.
11 -8) is mediated by the activities of several peptidases.
12 lity 2/high-temperature requirement A serine peptidase 1 (ARMS2/HTRA1), complement component 2 (C2),
13 DGF signaling upregulated ubiquitin-specific peptidase 1 (Usp1) to promote the survival of murine pro
14 nonsense mutations in the TPP1 (tripeptidyl peptidase 1), DMD (dystrophin), SMARCAL1 (SWI/SNF-relate
15 lity 2/high-temperature requirement A serine peptidase 1, complement component 2, complement componen
23 is specific to free human kallikrein-related peptidase 2, an antigen abundant in malignant prostatic
24 tor of the therapeutic effects of dipeptidyl peptidase 4 (DPP-4) inhibition (vildagliptin) by using t
25 c incretin-based drugs, including dipeptidyl peptidase 4 (DPP-4) inhibitors and glucagon-like peptide
26 s such as the tetraspanin CD9 and dipeptidyl peptidase 4 (DPP4) along with multiple endosomal sorting
29 ficient mice receiving background dipeptidyl peptidase 4 (DPP4) inhibitor treatment were characterize
32 o the cell surface entry receptor dipeptidyl peptidase 4 (DPP4) occurs via S1(B) We now demonstrate t
33 fruit bat (Artibeus jamaicensis) dipeptidyl peptidase 4 (DPP4) receptor and MERS-CoV replicated effi
34 S-CoV) binds to cellular receptor dipeptidyl peptidase 4 (DPP4) via the spike (S) protein receptor-bi
35 he MERS-CoV cell surface receptor dipeptidyl peptidase 4 (DPP4), and evolutionary mechanisms that may
36 r MERS-CoV has been identified as dipeptidyl peptidase 4 (DPP4), the mouse DPP4 homologue does not al
37 ogether, our results point toward dipeptidyl peptidase 4 (DPP4)-dependent endosomal uptake and subseq
39 novirus transduction of the human dipeptidyl peptidase 4 (hDPP4) receptor and then analyzed the abili
40 this study, we show that ubiquitin-specific peptidase 4 (USP4) interacts directly with and deubiquit
41 e identified as a major source of dipeptidyl peptidase 4 and we also found that skin mast cells and f
42 trial results have suggested that dipeptidyl peptidase 4 inhibitor (DPP4i) use might increase heart f
43 r events of adding sitagliptin, a dipeptidyl peptidase 4 inhibitor, to usual care in patients with ty
45 nd is critical for the actions of dipeptidyl peptidase 4 inhibitors that enhance GLP-1 levels in pati
46 t match the human sequence in the dipeptidyl peptidase 4 receptor, making mice susceptible to MERS-Co
47 tigen; double immunostaining with dipeptidyl peptidase 4 showed colocalization in scattered pneumocyt
49 etry analysis revealed that DPP4 (dipeptidyl peptidase 4) was selectively expressed on the surface of
50 ng oxopeptides toward cleavage by dipeptidyl peptidase 4, the principal regulator of their in vivo st
58 ceptor agonists and inhibitors of dipeptidyl peptidase-4 (DPP-4) have shown pleiotropic effects on bo
59 group who also had baseline serum dipeptidyl peptidase-4 (DPP-4) higher than the population baseline
63 hiazolidinediones, sulfonylureas, dipeptidyl peptidase-4 (DPP-4) inhibitors, and sodium-glucose cotra
64 art failure (hHF) associated with dipeptidyl peptidase-4 (DPP-4) inhibitors, creating uncertainty abo
65 atic degradation by inhibition of dipeptidyl peptidase-4 (DPP-4) promotes glycemic reduction for the
66 P-1 and GLP-2 are both cleaved by dipeptidyl peptidase-4 (DPP-4); hence, inhibition of DPP-4 activity
68 actions, as well as the effect of dipeptidyl peptidase-4 (DPP4) inhibitor on CD in endothelial-pericy
69 The incretin-based therapies, dipeptidyl peptidase-4 (DPP4) inhibitors and glucagon-like peptide-
71 ared the safety and efficacy of a dipeptidyl peptidase-4 inhibitor (sitagliptin) plus basal insulin w
73 ihyperglycemic medications in the dipeptidyl peptidase-4 inhibitor, glucagon-like peptide-1 receptor
74 6; six trials), intermediate with dipeptidyl peptidase-4 inhibitors (1.25, 1.08-1.45; two trials), an
75 ting the cardiovascular safety of dipeptidyl peptidase-4 inhibitors and some glucagon-like peptide-1
76 e peptide-1 receptor agonists and dipeptidyl peptidase-4 inhibitors are commonly used for glycemic co
77 tem, GLP-1 receptor agonists, and dipeptidyl peptidase-4 inhibitors for 26 +/- 8 months before underg
78 used in 6.6% of HF patients, and dipeptidyl peptidase-4 inhibitors were used in 5.1%, with trends fo
79 ide [GLP]-1 receptor agonists and dipeptidyl peptidase-4 inhibitors) have proven efficacy for the tre
81 me corin and BNP-degrading enzyme dipeptidyl peptidase-4 were reduced in HF versus normal, perhaps co
82 by producing excessive amounts of Dipeptidyl peptidase-4, a protease that is a target of diabetes the
84 racellular protease KLK5 (kallikrein-related peptidase 5) is efficient in promoting the infectivity o
85 e cleavage preferences of Kallikrein-related peptidase 7 (KLK7) have previously been delineated using
88 tified the deubiquitinase ubiquitin-specific peptidase 9X (USP9X) as an intracellular target, using a
90 nts with high-temperature requirement serine peptidase A1 (HtrA1), which is found in the nervous syst
91 ife on Earth, the fundamental details of how peptidases accommodate posttranslational modifications,
94 ayed higher alpha-amylase, endoxylanase, and peptidase activities as well as signs of (incipient) pro
96 ficient proteasomes reduced both their basal peptidase activity and the stimulation by ATPgammaS.
98 aded because the subcellular distribution of peptidase activity has not been investigated systematica
99 at 37 degrees C) correlate with reduced 20 S peptidase activity in proteasomes purified from cell ext
101 le tau was associated with a decrease in the peptidase activity of brain 26S proteasomes, higher leve
102 ion in vitro and in vivo confirming that the peptidase activity of PNT1 is essential for parasite sur
106 e proteasomes lacking Usp14 had higher basal peptidase activity than WT 26S, and this activity was st
108 hat ClpP1 was responsible for nearly all the peptidase activity, whereas both ClpP1 and ClpP2 contrib
110 oplast transit peptide by stromal processing peptidase, additional processing by unidentified peptida
111 ng alpha-amylase, protease and gamma-carboxy peptidase allowing complete sample preparation within a
115 rgely exceeded that of beta-lactones in ClpP peptidase and protease inhibition assays and displayed u
116 entially cleaved by mitochondrial processing peptidase and then by octapeptidyl aminopeptidase 1 (Oct
117 eafloor (8) (mbsf) encode numerous candidate peptidases and carbohydrate-active enzymes ('CAZymes') (
120 compendium of known and putative Arabidopsis peptidases and inhibitors, and compare the distribution
121 s control as it shows resistance to cellular peptidases and its route of transepithelial transport ha
122 ecules for endothelial nanomedicine includes peptidases and other enzymes, cell adhesion molecules an
125 the (near) absence of cysteine and aspartic peptidases and peptidase inhibitors, whereas other pepti
128 c data, and used to infer additional plastid peptidases and to generate a coexpression network for 97
129 ramembrane-cleaving protease, signal peptide peptidase, and is required for cell fusion activities.
130 f HslV, a double-ring self-compartmentalized peptidase, and one or two AAA+ HslU ring hexamers that h
131 es encoding hemicellulose-degrading enzymes, peptidases, and metabolite transporters were more abunda
133 tasis network containing protein chaperones, peptidases, and their substrate recognition factors.
134 Inhibition of aspartic cathepsin D-like peptidases (APDs) has been often discussed as an antipar
136 n be removed from the transcribed peptide by peptidases, artificial and biomachines working in concer
142 e the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Eart
143 c assortment of ancestral characters such as peptidases between Trypanosoma and Leishmania, genomic d
145 re structural elements with clan CD cysteine peptidases but otherwise structurally differs from the o
146 Here we characterize a ubiquitin-activated peptidase called DA1 that limits the duration of cell pr
150 notation based on the MEROPS nomenclature of peptidase clans and families, is incorporated into the P
151 ies indicate that deletion of the colibactin peptidase ClbP, a modification introduced to promote acc
153 erted to genotoxic colibactins by colibactin peptidase (ClbP)-mediated cleavage of an N-acyl-d-Asn si
159 we now show that the mitochondrial unfoldase-peptidase complex ClpXP associates with the oncoprotein
160 ), SRP receptors, the translocon, the signal peptidase complex, and over 100 other genes with many ot
161 rious protein-translocation machineries, the peptidase-containing ATP-binding cassette transporters (
165 Furthermore, the conserved cysteine of the peptidase domain of the Synpcc7942_1133 gene product (du
167 LK-nuclease (a RNase) and multiple distinct peptidase domains, which are predicted to carry their to
169 ng kinetics and thermodynamics of dipeptidyl peptidase (DPP)-4 inhibitors (gliptins) were investigate
171 ion of an inhibitor of the enzyme dipeptidyl-peptidase (DPP4i), which prevents the cleavage of glucag
173 terization of the dual function macrocyclase-peptidase enzyme involved in the biosynthesis of the hig
174 nal anchors, whose cleavage via the prepilin peptidase, essential for pilin membrane extraction and a
175 ases and peptidase inhibitors, whereas other peptidase families were exclusively organellar; reasons
176 and they comprise the largest of all of the peptidase families, their dynamic motions remain obscure
177 discovered that PGM48 is a member of the M48 peptidase family with PGM48 homologs, forming a clade (M
183 efects in PMPCA and mitochondrial processing peptidase have been described in association with a dise
184 We report here that host range restriction peptidase (hrrP), a gene found on one of these plasmids,
186 sttranslational processing requires a signal peptidase II (LspA) that removes the signal peptide.
187 he signal sequence is then cleaved by signal peptidase II (LspA) to give an N-terminal S-diacylglycer
192 f cells producing native OPH with the signal peptidase II inhibitor globomycin resulted in accumulati
193 ffective at visualizing B1R-positive tumors, peptidase inhibition with phosphoramidon greatly enhance
194 previously reported that secretory leukocyte peptidase inhibitor (SLPI) is regulated by the AR in a l
195 We found that four splice variants of the peptidase inhibitor 16 (PI16) mRNA are among the most hi
196 kines (IL-12p40, IL-13, IL-22, CCL17, CCL18, peptidase inhibitor 3 [PI3]/elafin, and S100As) showed c
197 imicrobials (IL-17A, IL-19, CCL20, LL37, and peptidase inhibitor 3/elafin), TH9/IL-9, IL-33, and inna
199 In this study, we identified SPINT2 (serine peptidase inhibitor Kunitz type 2), a proteolytic inhibi
201 mutations were found in the SERPINF1 (Serpin Peptidase Inhibitor, Clade F) gene which encodes PEDF (p
202 8 (MTRNRL8), interleukin-8 (IL8), and serpin peptidase inhibitor, clade H (SERPINH1) and chemokine li
203 ly 180-kDa multidomain membrane-anchored pan-peptidase inhibitor, which is cleaved by host endopeptid
204 along with the known substrate cleavages and peptidase-inhibitor interactions, and a link to the KEGG
205 ses and identified IL-1 cytokines and serine peptidase inhibitors as the most dysregulated esophagus-
206 es to show the involvement of peptidases and peptidase inhibitors in biological pathways have been cr
208 ence of cysteine and aspartic peptidases and peptidase inhibitors, whereas other peptidase families w
211 ing organ growth in Arabidopsis thaliana The peptidase is activated by two RING E3 ligases, Big Broth
212 ensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory and oxygen radical abso
214 s used to optimise the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during hydroly
216 y and histochemical estimation of dipeptidyl-peptidase IV enzyme activity of donor cells in the negat
217 ony stimulating factor (G-CSF), a dipeptidyl peptidase IV inhibitor (DPP-4i), and a proton pump inhib
218 not inhibit close FAP homologues dipeptidyl peptidase IV, dipeptidyl peptidase 9, and prolyl oligope
220 e (37.8%), alpha-amylase (35.6%), dipeptidyl peptidase-IV (34.4%), reactive oxygen species (81.6%), a
221 riety of bioactivities, including dipeptidyl peptidase-IV (DPP-IV) and angiotensin converting enzyme
224 ionate increased DBS, enhanced by dipeptidyl peptidase-IV (DPPIV) inhibition, at the same time as inc
225 d source of natural inhibitors of dipeptidyl peptidase-IV and prolyl endopeptidase and could potentia
226 d clinical variants, for example, dipeptidyl peptidase-IV inhibitor-associated noninflammatory bullou
227 astomyces dermatitidis elaborates dipeptidyl-peptidase IVA (DppIVA), a close mimic of the mammalian e
232 by the intramembrane protease signal peptide peptidase-like (SPPL)2a, a process critical for B cell d
242 rst followed by the successive action of exo-peptidases (mainly, tri- and di-peptidylpeptidases, amin
243 n internal cleavage by the matrix processing peptidase MPP, and in this respect, it differs from all
245 des a systematic insight into the organellar peptidase network in Arabidopsis thaliana We present a c
246 idase, additional processing by unidentified peptidases occurs to avoid unstable or otherwise unfavor
247 Cruzipain, the main papain-like cysteine peptidase of T. cruzi, is an important virulence factor
251 s of membrane proteins are cleaved by signal peptidase once the nascent proteins reach the endoplasmi
252 Among the 480 genes coding for protease/peptidases, only four were found enriched in cortical in
254 te physiological influence of manipulating a peptidase or an inhibitor cannot be always predicted, si
257 an increase in the level of the neprilysin 1 peptidase overcomes memory deficits induced by amyloid p
258 eous process but is governed by a standalone peptidase PepN, which hydrolyzes LBS in a pH-sensitive w
260 ucial for enzymatic activity of the prepilin peptidase PilD and (iii) that pilin subunits with a C-te
263 This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular
264 ed soluble or membrane-anchored multimodular peptidases regularly found in several paralogous copies
266 hibitors of mosquito peptidyl dipeptidase, a peptidase related to mammalian angiotensin-converting en
268 nherited and caused by the inability of SUMO peptidase sentrin/SUMO-specific protease 2 (SENP2) to de
272 steine residue at the junction of the signal peptidase (Spase) cleavage site along with a well conser
274 e describe a general approach for predicting peptidase substrates de novo using protein structure mod
275 metalloprotease HrrP (host range restriction peptidase), suggesting that disulfide bond formation may
277 ata provide evidence that PNT1 is a cysteine peptidase that is required exclusively for maintenance o
278 of a bacterial calpain, a calcium-responsive peptidase that may generate substrates required for the
279 References 912 Subtilases (SBTs) are serine peptidases that are found in all three domains of life.
281 of beta-lactam antibiotics are bacterial DD-peptidases that catalyze the final steps of peptidoglyca
282 peptidases, a structurally related group of peptidases that include mammalian caspases, exhibit a wi
283 further insight into this group of bacterial peptidases that likely represent ancestral versions of m
284 he alpha subunit of mitochondrial processing peptidase, the primary enzyme responsible for the matura
286 is an integrated source of information about peptidases, their substrates and inhibitors, which are o
287 e other well-characterized groups of clan CD peptidases, there are no high-resolution structures of s
288 while, some rhizobial strains have evolved a peptidase to specifically degrade these antimicrobial pe
289 aborate with the self-compartmentalized ClpP peptidase to unfold and degrade specific proteins in bac
292 ynpcc7942_1133 gene product (dubbed PteB for peptidase transporter essential for biofilm) is crucial
296 f the transcripts encoding putative secreted peptidases were assigned to lineages (7,13,14) of uncult
297 s showed that the gene encoding pyroglutamyl peptidase, which removes N-terminal OP residues, cluster
299 s lspB, a gene encoding a lipoprotein signal peptidase whose expression appears detrimental for infec
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