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1 nd Astn2 as the endoplasmic reticulum signal peptidase.
2 , followed by cleavage by the inner membrane peptidase.
3 ysis of catalytic specificity of an aspartic peptidase.
4 ase in complex with a self-compartmentalized peptidase.
5 eophilic attack during catalysis of cysteine peptidases.
6 of proteolysis phenomenon exerted by muscle peptidases.
7 -8) is mediated by the activities of several peptidases.
8 biotics that can be hydrolyzed by wastewater peptidases.
9 active fragments by at least three different peptidases.
10 ast proteostasis is governed by a network of peptidases.
11 ficity of dissolved extracellular wastewater peptidases.
12 s an oral reversible inhibitor of dipeptidyl peptidase 1 (DPP-1), an enzyme responsible for the activ
14 akoid integration of Plastidic type I signal peptidase 1 (Plsp1) using in vitro targeting assays.
16 nonsense mutations in the TPP1 (tripeptidyl peptidase 1), DMD (dystrophin), SMARCAL1 (SWI/SNF-relate
18 the mRNA encoding for the ubiquitin-specific peptidase 11 (USP11), a known modulator of TGF-beta sign
23 xp3 expression, including ubiquitin-specific peptidase 22 (Usp22) and ring finger protein 20 (Rnf20).
24 eaves and inactivates the ubiquitin-specific peptidase 28 (USP28), preventing USP28 from de-ubiquitin
26 produced via cleavage by kallikrein-related peptidase 3 (KLK3), aka prostate-specific antigen (PSA).
28 d miR-148a suppresses the ubiquitin-specific peptidase 33 (USP33) protein expression levels via bindi
29 have demonstrated CV safety of 3 dipeptidyl peptidase 4 (DPP-4) inhibitors but have included limited
30 tide 1 receptor (GLP-1) agonists, dipeptidyl peptidase 4 (DPP-4) inhibitors, peroxisome proliferator-
31 s such as the tetraspanin CD9 and dipeptidyl peptidase 4 (DPP4) along with multiple endosomal sorting
32 ced levels of the virus receptor, dipeptidyl peptidase 4 (DPP4) and higher basal levels of interferon
34 ficient mice receiving background dipeptidyl peptidase 4 (DPP4) inhibitor treatment were characterize
35 e 1 receptor (GLP1R) agonists and dipeptidyl peptidase 4 (DPP4) inhibitors, can also reduce blood pre
36 e-1 (GLP-1) receptor agonists and dipeptidyl peptidase 4 (DPP4) inhibitors, with the risk of Parkinso
37 o the cell surface entry receptor dipeptidyl peptidase 4 (DPP4) occurs via S1(B) We now demonstrate t
38 S-CoV) binds to cellular receptor dipeptidyl peptidase 4 (DPP4) via the spike (S) protein receptor-bi
39 r MERS-CoV has been identified as dipeptidyl peptidase 4 (DPP4), the mouse DPP4 homologue does not al
40 novirus transduction of the human dipeptidyl peptidase 4 (hDPP4) receptor and then analyzed the abili
41 +/+) and heterozygous (+/-) human dipeptidyl peptidase 4 (hDPP4) transgenic mice to study the effect
42 S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respect
43 ulfonylureas, thiazolidinediones, dipeptidyl peptidase 4 [DPP-4] inhibitors, glucagon-like peptide 1
44 e identified as a major source of dipeptidyl peptidase 4 and we also found that skin mast cells and f
45 wo clinically used T2D drugs: the dipeptidyl peptidase 4 inhibitor linagliptin and the sulfonylurea g
48 es, sulfonylurea, glitazones, and dipeptidyl peptidase 4 inhibitors have variable effects on cardiova
49 nd is critical for the actions of dipeptidyl peptidase 4 inhibitors that enhance GLP-1 levels in pati
52 etry analysis revealed that DPP4 (dipeptidyl peptidase 4) was selectively expressed on the surface of
53 ng oxopeptides toward cleavage by dipeptidyl peptidase 4, the principal regulator of their in vivo st
58 an active comparator drug class, dipeptidyl peptidase-4 (DPP-4) inhibitors, in patients with type 2
59 atic degradation by inhibition of dipeptidyl peptidase-4 (DPP-4) promotes glycemic reduction for the
61 s, we identified the exopeptidase dipeptidyl peptidase-4 (DPP4) as a critical glucocorticoid-responsi
64 actions, as well as the effect of dipeptidyl peptidase-4 (DPP4) inhibitor on CD in endothelial-pericy
67 ose-lowering medication-including dipeptidyl peptidase-4 inhibitor (DPP4i), insulin, or thiazolidined
68 ared the safety and efficacy of a dipeptidyl peptidase-4 inhibitor (sitagliptin) plus basal insulin w
69 omparing empagliflozin versus the dipeptidyl peptidase-4 inhibitor class, and comparing sodium-glucos
70 cotransporter-2 inhibitor versus dipeptidyl peptidase-4 inhibitor classes also produced consistent f
71 cardiovascular safety trials, the dipeptidyl peptidase-4 inhibitor linagliptin demonstrated noninferi
72 HF and related outcomes with the dipeptidyl peptidase-4 inhibitor linagliptin versus placebo in CARM
73 apagliflozin with and without the dipeptidyl peptidase-4 inhibitor saxagliptin, and the effect of dap
74 ihyperglycemic medications in the dipeptidyl peptidase-4 inhibitor, glucagon-like peptide-1 receptor
76 sulfonylurea (8.7% versus 6.9%), dipeptidyl peptidase-4 inhibitors (10.6% versus 7.5%), SGLT-2i (10.
77 with thiazolidinediones (TZDs) or dipeptidyl peptidase-4 inhibitors (DPP-4is) as a third antidiabetic
79 by producing excessive amounts of Dipeptidyl peptidase-4, a protease that is a target of diabetes the
80 of PRSS3/mesotrypsin and kallikrein-related peptidase 5 (KLK5) in lung adenocarcinoma malignancy.
81 f existing inhibitors for kallikrein-related peptidase 5 and show that a variant with substitutions a
82 racellular protease KLK5 (kallikrein-related peptidase 5) is efficient in promoting the infectivity o
83 Kv4.2 with its auxiliary subunit dipeptidyl peptidase 6 (DPP6), and thereby modulates neuronal excit
85 e cleavage preferences of Kallikrein-related peptidase 7 (KLK7) have previously been delineated using
88 ely, USP7 (deubiquitinase ubiquitin-specific peptidase 7) opposes the activities of E3 ligases, stabi
89 12)) within the gene that encodes dipeptidyl peptidase 9 (DPP9); and on chromosome 21q22.1 (rs2236757
90 some activation in the context of dipeptidyl peptidase 9 inhibition and could thereby increase asthma
92 that M1184V increases binding to dipeptidyl peptidase 9, which can account for its inhibitory role i
93 ife on Earth, the fundamental details of how peptidases accommodate posttranslational modifications,
96 xperiments in vivo indicate that the PaClpP2 peptidase active site uniquely contributes to biofilm de
98 ayed higher alpha-amylase, endoxylanase, and peptidase activities as well as signs of (incipient) pro
99 se, tripeptidyl peptidase, and acylaminoacyl peptidase activities have been reported previously, here
100 dases as their receptors is unknown, but the peptidase activities of the receptors are dispensable, s
102 te the physiological importance of both CGEP peptidase activity and its autocatalytic processing.
103 ficient proteasomes reduced both their basal peptidase activity and the stimulation by ATPgammaS.
104 The PA28 regulator stimulates 20S proteasome peptidase activity in vitro, but its role in vivo remain
106 e proteasomes lacking Usp14 had higher basal peptidase activity than WT 26S, and this activity was st
107 le-organism catabolic process, regulation of peptidase activity, and negative regulation of cell deat
108 uitin-modified proteins independently of its peptidase activity, consistent with our recently reporte
112 ng alpha-amylase, protease and gamma-carboxy peptidase allowing complete sample preparation within a
114 While the combined action of signal peptide peptidase and endoplasmic reticulum (ER) aminopeptidase
115 entially cleaved by mitochondrial processing peptidase and then by octapeptidyl aminopeptidase 1 (Oct
116 eafloor (8) (mbsf) encode numerous candidate peptidases and carbohydrate-active enzymes ('CAZymes') (
117 compendium of known and putative Arabidopsis peptidases and inhibitors, and compare the distribution
118 the (near) absence of cysteine and aspartic peptidases and peptidase inhibitors, whereas other pepti
119 c data, and used to infer additional plastid peptidases and to generate a coexpression network for 97
120 peptidase, dipeptidyl peptidase, tripeptidyl peptidase, and acylaminoacyl peptidase activities have b
121 f HslV, a double-ring self-compartmentalized peptidase, and one or two AAA+ HslU ring hexamers that h
123 tasis network containing protein chaperones, peptidases, and their substrate recognition factors.
125 ession and hydrolytic activities of cellular peptidases are increased upon TCR-dependent and MHC-pept
127 n be removed from the transcribed peptide by peptidases, artificial and biomachines working in concer
132 pt in the hydrolysate using the non-specific peptidase because of its high free amino acid content.
134 e the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Eart
137 Here we characterize a ubiquitin-activated peptidase called DA1 that limits the duration of cell pr
139 d four laticifer fluids as a novel source of peptidases capable of hydrolyzing proteins in cow's milk
141 oteolytic activity, cell envelope associated peptidase (CEP) profile and LC-MS/MS analysis of peptide
142 (Arabidopsis thaliana) chloroplast glutamyl peptidase (CGEP) is a homo-oligomeric stromal Ser-type (
143 notation based on the MEROPS nomenclature of peptidase clans and families, is incorporated into the P
145 ies indicate that deletion of the colibactin peptidase ClbP, a modification introduced to promote acc
149 composed of a double-ring compartmentalized peptidase (ClpP) and a AAA+ unfoldase (ClpX or ClpA/ClpC
153 e hydrolysate obtained from the non-specific peptidase contained a larger variety of pyrazines, inclu
155 h can be partially fulfilled by a noncognate peptidase-containing transporter component B (PctB).
158 IG BROTHER (BB) and DA2, activate the latent peptidases DA1, DAR1 and DAR2 by mono-ubiquitination at
159 known about the specificity of extracellular peptidases derived from wastewater microbial communities
161 s Alt-EJ through its SOS-response-associated-peptidase domain (SRAPd), a function that requires DNA b
165 ion of chemokines mediated by the dipeptidyl peptidase DPP4 (CD26) has been shown to negatively regul
168 rolyzed (i.e., inactivated) by extracellular peptidases during biological wastewater treatment, there
169 terization of the dual function macrocyclase-peptidase enzyme involved in the biosynthesis of the hig
170 , cerliponase alfa (Brineura), a tripeptidyl peptidase enzyme replacement therapy, became the first g
172 nal anchors, whose cleavage via the prepilin peptidase, essential for pilin membrane extraction and a
173 ases and peptidase inhibitors, whereas other peptidase families were exclusively organellar; reasons
174 and they comprise the largest of all of the peptidase families, their dynamic motions remain obscure
175 sively hydrolysed firstly by endogenous endo-peptidases followed by the successive action of exo-pept
176 conserved activity as an internal processing peptidase for complex mitochondrial precursor proteins.
177 e, chymosine, thermolysin and a non-specific peptidase from Aspergillus melleus), contained a varying
183 by P. gingivalis are the essential cysteine peptidases gingipain K (Kgp) and R (RgpA and RgpB), whic
185 oluble proteins, the H-segment of the leader peptidase helix used in the von Heijne and White biologi
186 were more resistant to proteolysis by latex peptidases; however, heat pretreatment of the whey prote
188 n criteria included the presence of a signal peptidase I cleavage site, a predicted beta-barrel fold,
192 he signal sequence is then cleaved by signal peptidase II (LspA) to give an N-terminal S-diacylglycer
198 cF Thr74Ile, and Asp486Glu in a hypothetical peptidase) in previously unrecognized S. aureus virulenc
202 iation between low circulating plasma serine peptidase inhibitor Kunitz type-1 (SPINT1) concentration
203 coding alpha-1 antitrypsin, SERPINA1 (serpin peptidase inhibitor, clade A, member 1), in determining
204 8 (MTRNRL8), interleukin-8 (IL8), and serpin peptidase inhibitor, clade H (SERPINH1) and chemokine li
206 ses and identified IL-1 cytokines and serine peptidase inhibitors as the most dysregulated esophagus-
208 al microglia or adult microglia treated with peptidase inhibitors into spinal cord lesions of adult m
209 ike peptide 1 (GLP1) mimetics and dipeptidyl peptidase inhibitors that enhance GLP1 receptor activati
210 for enkephalin activity, we applied specific peptidase inhibitors to determine which peptidase(s) reg
211 ress several extracellular and intracellular peptidase inhibitors, as well as other molecules that ar
212 ence of cysteine and aspartic peptidases and peptidase inhibitors, whereas other peptidase families w
214 Amnesiac and Neprilysin 1 (Nep1), a membrane peptidase involved in memory and expressed in the MB.
215 letal muscle cells, insulin-responsive amino peptidase (IRAP) along with glucose transporter 4 (Glut4
216 ing organ growth in Arabidopsis thaliana The peptidase is activated by two RING E3 ligases, Big Broth
217 ctivation protein (FAP), a membrane-anchored peptidase, is highly expressed in cancer-associated fibr
218 otein of L. major, named inhibitor of serine peptidases (ISP) 2, inactivates neutrophil elastase (NE)
219 idly inactivated by the action of dipeptidyl peptidase IV (DPP-4) which limits their use as therapeut
220 sin-I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities, with inhibi
221 ensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory and oxygen radical abso
223 s used to optimise the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during hydroly
226 y and histochemical estimation of dipeptidyl-peptidase IV enzyme activity of donor cells in the negat
229 e (37.8%), alpha-amylase (35.6%), dipeptidyl peptidase-IV (34.4%), reactive oxygen species (81.6%), a
230 riety of bioactivities, including dipeptidyl peptidase-IV (DPP-IV) and angiotensin converting enzyme
231 d clinical variants, for example, dipeptidyl peptidase-IV inhibitor-associated noninflammatory bullou
239 rst followed by the successive action of exo-peptidases (mainly, tri- and di-peptidylpeptidases, amin
240 ses followed by the successive action of exo-peptidases, mainly, tri- and di-peptidylpeptidases, amin
244 n between GRP75 and mitochondrial processing peptidase (MPP), which makes frataxin more accessible to
247 des a systematic insight into the organellar peptidase network in Arabidopsis thaliana We present a c
249 Cruzipain, the main papain-like cysteine peptidase of T. cruzi, is an important virulence factor
250 pact of Aqualysin 1 (Aq1), the thermo-active peptidase of Thermus aquaticus, on wheat albumin, globul
254 an increase in the level of the neprilysin 1 peptidase overcomes memory deficits induced by amyloid p
257 ions of both pilA1 and pilA2 or the prepilin peptidase, PibD, show the reduction in the number of pil
258 ed principles for processing by the prepilin peptidase PilD and for assembly into filaments; (ii) dis
260 This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular
261 hibitors of mosquito peptidyl dipeptidase, a peptidase related to mammalian angiotensin-converting en
263 y a lack of information regarding a protease/peptidase required for the excision of an early, cross-l
265 This indicates neprilysin is the predominant peptidase responsible for degrading enkephalins in the i
266 equencing that mutations in ASPRV1 (aspartic peptidase retroviral-like 1) cause a dominant Mendelian
267 ght the importance of knowing which specific peptidase(s) control opioid actions in the relevant neur
268 ific peptidase inhibitors to determine which peptidase(s) regulate enkephalin signaling in this regio
272 ed crystal structures of the LysM/M23 family peptidase ShyA, the primary EP of the cholera pathogen V
273 lly processed by the cell membrane-localized peptidase sortase A, which cleaves the LPXTG motif.
275 glycoprotein K (gK) binds to signal peptide peptidase (SPP), also known as minor histocompatibility
276 s of the human HMCES SOS response-associated peptidase (SRAP) domain in complex with DNA-damage subst
277 utionarily conserved SOS-response associated peptidase (SRAP) domain of HMCES and its Escherichia col
279 e describe a general approach for predicting peptidase substrates de novo using protein structure mod
280 the specificity of different classes of ClpP peptidase subunits contributes to the biological outcome
282 p1) is an integral thylakoid membrane signal peptidase that requires an intramolecular disulfide bond
283 References 912 Subtilases (SBTs) are serine peptidases that are found in all three domains of life.
287 ase/translocase that functions with the ClpP peptidase to degrade proteins that are damaged or unneed
293 f the transcripts encoding putative secreted peptidases were assigned to lineages (7,13,14) of uncult
295 s showed that the gene encoding pyroglutamyl peptidase, which removes N-terminal OP residues, cluster
296 ivity, but its action is strongly limited by peptidases, which degrade enkephalin into inactive fragm
297 s lspB, a gene encoding a lipoprotein signal peptidase whose expression appears detrimental for infec
299 is a homo-oligomeric stromal Ser-type (S9D) peptidase with both exo- and endo-peptidase activity.