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1 ensitive aminopeptidase (PSA, cytosol alanyl aminopeptidase).
2 manganese as co-factor, including the BB0366 aminopeptidase.
3 1, but lacked the canalicular marker leucine aminopeptidase.
4 designing effective inhibitors of methionine aminopeptidase.
5 lated aminopeptidase (IRAP), a transmembrane aminopeptidase.
6 trometry identified the protease as aspartyl aminopeptidase.
7 anic chemistry of DNPEP and other M18 family aminopeptidases.
8 f preferred amino acid cleavage by cytosolic aminopeptidases.
9 ding over 200 cleavages of blood proteins by aminopeptidases.
10 n of the substrate specificity of individual aminopeptidases.
11 ed by hydrolysis to amino acids by cytosolic aminopeptidases.
12 se as selective inhibitors for this group of aminopeptidases.
13 cursor peptides by the endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 is an important event
14                        Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims peptides for MHC class I
15 mily of M1 aminopeptidases, consisting of ER aminopeptidase 1 (ERAP1), ER aminopeptidase 2 (ERAP2), a
16 ow-activity variant of endoplasmic reticulum aminopeptidase 1 (ERAP1), Hap10, is associated with the
17 hin the aminopeptidase endoplasmic reticulum aminopeptidase 1 (ERAP1), which is essential for trimmin
18 rocessing peptidase and then by octapeptidyl aminopeptidase 1 (Oct1).
19 ses the aggregation of the premature form of aminopeptidase 1 (prApe1) in cytosol and its sequestrati
20  association of ERAP1 (endoplasmic reticulum aminopeptidase 1) with ankylosing spondylitis (AS), whic
21                        Endoplasmic reticulum aminopeptidases 1 and 2 (ERAP1 and ERAP2) cooperate to t
22 llular aminopeptidases endoplasmic reticulum aminopeptidases 1 and 2 (ERAP1 and ERAP2), and as well a
23 ast to cytosolic peptidases, silencing of ER aminopeptidases 1 and 2 strongly impaired pp65(495-503)-
24             Endoplasmic reticulum-associated aminopeptidase-1 (ERAP1) plays a critical role in the pr
25 ates, we determined crystal structures of ER aminopeptidase 2 (ERAP2) in complex with a substrate ana
26 onsisting of ER aminopeptidase 1 (ERAP1), ER aminopeptidase 2 (ERAP2), and insulin-regulated aminopep
27 n the present study we found that methionine aminopeptidase 2 (MetAP2), a critical component of the t
28 459P mirrored those of endoplasmic reticulum aminopeptidase 2, a human enzyme with proline in the var
29  activity due to binding to human methionine aminopeptidase 2.
30 enic activity by binding to human methionine aminopeptidase 2.
31 he in vitro catalytic activity of methionine aminopeptidase-2 (MetAP2) are effective in blocking angi
32                                   Methionine aminopeptidase-2 (MetAP2) processes N-terminal methionin
33                     Inhibition of methionine aminopeptidase-2 (MetAP2) represents a novel approach to
34 ors of the human metalloprotease, methionine aminopeptidase-2 (MetAP2), identified a potent class of
35 ite mutations, respectively, in the X-prolyl aminopeptidase 3 (XPNPEP3) gene.
36 al and cytosolic splice variants of X-prolyl aminopeptidase 3, can cause nephronophthisis-like ciliop
37                                          The aminopeptidase A (APA) ectopeptidase is an integral memb
38                                              Aminopeptidase A (APA) is expressed in glomerular podocy
39 ral renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by sp
40 tamylcyclotransferase (gamma-GCT) as well as aminopeptidase A (APA), which are overexpressed in renal
41                                      Leucine aminopeptidase A (LapA) is a late wound-response gene of
42  to chemical biology, with a platform for Zn-aminopeptidase A inhibitors being constructed here.
43 0)], and 6C3 [ENPEP glutamyl aminopeptidase (aminopeptidase A)].
44 e II/III of development, while inhibitors of aminopeptidase A, dopamine beta-hydroxylase, and the int
45  studies support the existence of protective aminopeptidase A-Ang III-Ang II type 2 receptor and ACE2
46 pha(v)beta5 integrins, aminopeptidase N, and aminopeptidase A.
47 teases, acid proteases, metalloproteases, or aminopeptidases abolished the effects of MET-1.
48 ates the omega-end of LTA4, distant from the aminopeptidase active site, thus providing a molecular b
49 HIV PIs altered not only proteasome but also aminopeptidase activities in PBMCs.
50 bifunctional enzyme with epoxy hydrolase and aminopeptidase activities.
51 hough sparing the enzyme's anti-inflammatory aminopeptidase activity (i.e., degradation and inactivat
52                We hypothesize that the LTA4H aminopeptidase activity alleviates neutrophilic inflamma
53 ne product possesses previously unrecognized aminopeptidase activity but no carboxy- or endopeptidase
54                      The attenuation of CtsH aminopeptidase activity by a specific inhibitor or siRNA
55 potent leukocyte activating agent, while the aminopeptidase activity cleaves and inactivates the chem
56 ated for their ability to detect beta-alanyl aminopeptidase activity in bacteria known to hydrolyze b
57 all yield and were selective for beta-alanyl aminopeptidase activity in bacteria, producing a lighter
58 acological inhibition of puromycin-sensitive aminopeptidase activity in cell lines permissive for IBD
59 e biological contributions made by the LTA4H aminopeptidase activity in CS-induced emphysema, we expo
60         Acrolein modifies LTA4H and inhibits aminopeptidase activity to the same extent as cigarette
61                               When the LTA4H aminopeptidase activity was selectively augmented by 4MD
62                          PGP/AcPGP and LTA4H aminopeptidase activity were detected by mass spectrosco
63 ease inhibitors and chosen metal ions on the aminopeptidase activity were determined.
64        However, restoring the leukotriene A4 aminopeptidase activity with a pharmaceutical agent prot
65                       LTA(4)H also possesses aminopeptidase activity with unknown substrate and physi
66 pment of COPD, selectively inhibited LTA(4)H aminopeptidase activity, which led to the accumulation o
67 GP in the airspaces by suppressing the LTA4H aminopeptidase activity.
68  a lysosomal cysteine protease with a strong aminopeptidase activity.
69 trate a detailed catalytic mechanism for its aminopeptidase activity.
70 significantly lower as compared with Xaa-Pro aminopeptidase activity.
71 rminated winter rape seeds were screened for aminopeptidase activity.
72 ing cytosolic enzyme with both hydrolase and aminopeptidase activity.
73 mino acids cannot compensate for the loss of aminopeptidase activity.
74 mation through selective inhibition of LTA4H aminopeptidase activity.
75  comparable to that of unlabeled Cry11Ba and aminopeptidase AgAPN2(t1) peptide.
76                                              Aminopeptidases also destroy epitopes by trimming them t
77 ifferentiation 90)], and 6C3 [ENPEP glutamyl aminopeptidase (aminopeptidase A)].
78 we report the structure of insulin-regulated aminopeptidase, an enzyme that prepares antigenic epitop
79                In particular, for dipeptidyl aminopeptidase, an SP that is recognized by the SRP for
80 rengthen a biochemical model that interlinks aminopeptidase and DPP4 activities.
81                                 Both Xaa-Pro aminopeptidase and mitochondrial processing activities o
82 (495-503) epitope presentation after leucine aminopeptidase and tripeptidyl peptidase II knockdown.
83 degraded by the cytosolic peptidases leucine aminopeptidase and tripeptidyl peptidase II, as evidence
84 ses (mainly, tri- and di-peptidylpeptidases, aminopeptidases and carboxypeptidases).
85 l secreted proteolytic activities, including aminopeptidases and carboxypeptidases.
86 erwent endosomal and cytosomal processing by aminopeptidases and proteases.
87 c cleavage events associated with methionine aminopeptidases and signal peptide peptidases, as well a
88  DUF4424 domain and individual domains of M1 aminopeptidases and tricorn proteases, which form massiv
89 hree unknown proteins that are homologous to aminopeptidases and xylanases or that contain a putative
90 r trypsin, 14.8% for chymotrypsin, 93.4% for aminopeptidase, and 19.7% for pepsin.
91 seen in the active-site cavity of methionine aminopeptidase, and at least one of the metal ions is di
92 kin (IL)-6, insulin (INS), alanyl (membrane) aminopeptidase (ANPEP), and IL-10 were observed in the P
93                                              Aminopeptidases are key enzymes involved in the regulati
94                            Tetrahedral (TET) aminopeptidases are large polypeptide destruction machin
95 e vascular receptors--alpha(v) integrins and aminopeptidases--are accessible through the circulation
96         Protocols that use microsomal alanyl aminopeptidase as a discovery-enabling agent are describ
97 roteins such as GLUT4 and insulin-responsive aminopeptidase, as well as six proteins not previously r
98 ading complex, and the endoplasmic reticulum aminopeptidase associated with Ag processing (ERAAP) are
99 es in mice lacking the endoplasmic reticulum aminopeptidase associated with Ag processing (ERAAP).
100  in the endoplasmic reticulum (ER) by the ER aminopeptidase associated with Ag processing (ERAAP).
101  in the absence of the endoplasmic reticulum aminopeptidase associated with Ag processing (ERAAP).
102 s, TAP, and endoplasmic reticulum-associated aminopeptidase associated with Ag processing, but not ta
103                    The endoplasmic reticulum aminopeptidase associated with Ag processing, ERAAP, pla
104  are trimmed to appropriate length by the ER aminopeptidase associated with antigen processing (ERAAP
105  peptides for MHC I are customized by the ER aminopeptidase associated with antigen processing and by
106 teolysis by ERAAP, the endoplasmic reticulum aminopeptidase associated with antigen processing.
107 Additionally, with prolyl oligopeptidase and aminopeptidase B we identified two new Ag processing mac
108 ming of N-extended peptides into epitopes by aminopeptidases before loading onto MHC class I molecule
109 of an evolutionary highly conserved aspartyl aminopeptidase called DNPEP.
110                                              Aminopeptidases catalyze N-terminal peptide bond hydroly
111 atin F in different immune cell types is the aminopeptidase cathepsin C, which regulates the activati
112       Each N-terminal modification prevented aminopeptidase cleavage but surprisingly differed in its
113       In this study, we identified cytosolic aminopeptidases cleavage preferences in primary cells an
114              The oxytocinase subfamily of M1 aminopeptidases, consisting of ER aminopeptidase 1 (ERAP
115                       Localization of tagged aminopeptidases, coupled with biochemical analysis of en
116         In contrast, ERAP2, which encodes an aminopeptidase, did not show preferential parent-of-orig
117                                     Aspartyl aminopeptidase (DNPEP) has been implicated in the contro
118                                          The aminopeptidase DPP9 removes dipeptides from N-termini of
119 m of molecular piracy by a broadly conserved aminopeptidase during disease pathogenesis.
120   Single nucleotide polymorphisms within the aminopeptidase endoplasmic reticulum aminopeptidase 1 (E
121                                Intracellular aminopeptidases endoplasmic reticulum aminopeptidases 1
122 e pp65(495-503) epitope, whereas ER-resident aminopeptidases enhance such generation.
123            A counter screen against glutamyl aminopeptidase (ENPEP), an enzyme with substrate specifi
124                                          The aminopeptidase ERAAP is essential for trimming peptides
125 erones calnexin and calreticulin, and the ER aminopeptidase (ERAAP).
126                    The endoplasmic reticulum aminopeptidases (ERAP)1 and ERAP2 play a critical role i
127 trimming process overall and of the major ER aminopeptidase ERAP1 in particular is not well understoo
128                    The endoplasmic reticulum aminopeptidase ERAP1 regulates innate and adaptive immun
129 he strong selectivity compared to homologous aminopeptidases ERAP1 and ERAP2.
130   Members of the oxytocinase subfamily of M1 aminopeptidases (ERAP1, ERAP2, and IRAP) play important
131 noacyl moiety similar to tricorn-interacting aminopeptidase F1.
132 together, these results indicate that the M1 aminopeptidase family is a divergent family with three s
133                        The members of the M1 aminopeptidase family share conserved domains, yet show
134             Removal of N-terminal Met by Met-aminopeptidases frequently leads to Nt-acetylation of th
135 , in the reaction mechanism of the methionyl aminopeptidase from Escherichia coli ( EcMetAP-I), the H
136        We applied this concept to methionine aminopeptidase from Mycobacterium tuberculosis and showe
137           Seven crystal structures of alanyl aminopeptidase from Neisseria meningitides (the etiologi
138                                         PepX aminopeptidase from Streptococcus thermophilus ACA DC 00
139 ction studies were carried out on the dizinc aminopeptidase from Vibrio proteolyticus.
140                            M1 family metallo-aminopeptidases fulfill a wide range of critical and in
141 eady-state kinetic studies revealed that the aminopeptidase has broad activity, with a preference for
142                                              Aminopeptidases have been linked to the editing of pepti
143 the variable residue in the S1 subsite of M1-aminopeptidases have facilitated the evolution of new sp
144                 To perform this function, ER aminopeptidases have to recognize and process a vast var
145  (IEF) suggest the presence of more than one aminopeptidase, having similar molecular mass.
146 gest a new name for this enzyme: human ileal aminopeptidase (HILAP).
147 essing the enzymatic activities of the LTA4H aminopeptidase in lung tissues and accumulating PGP and
148 ates with the absence of puromycin-sensitive aminopeptidase in these cells.
149  activation, indicating the importance of ER aminopeptidases in pp65(495-503) generation.
150 hese peptides can subsequently be trimmed by aminopeptidases in the cytosol and/or the endoplasmic re
151                                              Aminopeptidases in the endoplasmic reticulum (ER) can cl
152 cell line in the presence and absence of the aminopeptidase inhibitor Tosedostat (CHR-2797).
153                   Tosedostat is a novel oral aminopeptidase inhibitor with clinical activity in a pre
154 te-selective delivery of a potent dipeptidyl aminopeptidase inhibitor.
155 er, these results support the development of aminopeptidase inhibitors as novel chemotherapeutics dir
156 inhibitors (e.g., for Polo-like kinase 1 and aminopeptidase), inhibitors of mutated isocitrate dehydr
157 RAP1, which encodes an endoplasmic reticulum aminopeptidase involved in peptide trimming before HLA c
158        Here, we investigated the role of the aminopeptidase IRAP in GLUT4 trafficking.
159                        In the absence of the aminopeptidase IRAP, the trafficking of CpG and TLR9 to
160      Peptide inhibitors of insulin-regulated aminopeptidase (IRAP) enhance fear avoidance and spatial
161                            Insulin-regulated aminopeptidase (IRAP) is an enzyme with several importan
162                        The insulin-regulated aminopeptidase (IRAP) is involved in vesicular trafficki
163 and ERAP2), and as well as insulin-regulated aminopeptidase (IRAP) process antigenic epitope precurso
164                       The insulin-responsive aminopeptidase (IRAP) was recently identified as an S-ac
165 a glucose transporter, and insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase.
166 oss-presented peptides by insulin-responsive aminopeptidase (IRAP), an enzyme localized in a regulate
167 n of GSV cargos, GLUT4 and insulin-regulated aminopeptidase (IRAP), and ACBD3 was required for intrac
168 or cargo proteins: Glut4, insulin-responsive aminopeptidase (IRAP), and sortilin.
169 s nonpeptide inhibitors of insulin-regulated aminopeptidase (IRAP), have previously been shown to enh
170 nopeptidase 2 (ERAP2), and insulin-regulated aminopeptidase (IRAP), plays critical roles in the gener
171 gen was transported across insulin-regulated aminopeptidase (IRAP)-positive early and late endosomes;
172 aled the engagement of the insulin-regulated aminopeptidase (IRAP).
173  domains of Glut4 and the insulin-responsive aminopeptidase (IRAP).
174  enzymatic digestion using microsomal alanyl aminopeptidase is combined with MS characterization.
175                            Insulin-regulated aminopeptidase is found in a semiclosed conformation wit
176                          Puromycin-sensitive aminopeptidase is responsible for the peptidase activity
177                        The specificity of M1-aminopeptidases is dominated by the interaction of the w
178              The proline-specific dipeptidyl aminopeptidase IV (DPP IV, DPP-4, CD26), widely expresse
179 from P. menziesii, whereas potential leucine aminopeptidase (LA) activity was significantly lower for
180 sequencing, conventional methods for leucine aminopeptidase (LAP) and pyrrolidonyl arylamidase (PYR)
181 ne and human APNs, and the reference leucine aminopeptidase (LAP).
182                                    l-Leucine aminopeptidases (LAPs) are implicated in the progress of
183                                      Leucine aminopeptidases (LAPs) are present in animals, plants, a
184 re crossed to mice lacking another cytosolic aminopeptidase, leucine aminopeptidase, the resulting BH
185                                   Dipeptidyl aminopeptidase-like protein 6 (DPP6) was first identifie
186 available for dimetalated enzyme, methionine aminopeptidase likely functions as a monometalated enzym
187          Human leukotriene (LT) A4 hydrolase/aminopeptidase (LTA4H) is a bifunctional enzyme that con
188                Leukotriene (LT) A4 hydrolase/aminopeptidase (LTA4H) is a bifunctional zinc metalloenz
189                         When used to monitor aminopeptidase M activity, this assay produced similar r
190 trated by screening 12,000 compounds against aminopeptidase M in 384-well microtiter plates with Z fa
191                                              Aminopeptidase M1 (APM1) is essential for embryonic, veg
192                                              Aminopeptidase M1 (APM1), a single copy gene in Arabidop
193                                              Aminopeptidase M1 (PfAM1), a zinc metalloprotease, has b
194 y enhancing cleavage of alpha1 by methionine aminopeptidase (MAP), resulting in acetylation of the N-
195  genetically essential P. falciparum metallo-aminopeptidases (MAPs), PfA-M1 and Pf-LAP.
196 These studies show that a bestatin-sensitive aminopeptidase may be critical for the hydrolysis of exo
197                                   Methionine aminopeptidase (MetAP) carries out an important cotransl
198                                   Methionine aminopeptidase (MetAP) catalyzes the hydrolytic cleavage
199                               The methionine aminopeptidase (MetAP) family is responsible for the cle
200                                   Methionine aminopeptidase (MetAP) is a promising target to develop
201 N-terminal-modifying enzymes like Methionine aminopeptidase (MetAP), and the signal recognition parti
202 thionine from nascent proteins by methionine aminopeptidase (MetAP).
203                                   Methionine aminopeptidases (MetAP) are responsible for the proteoly
204  N-terminal methionine removed by methionine aminopeptidases (MetAP1 and MetAP2) prior to action.
205                                   Methionine aminopeptidases (MetAPs) are essential enzymes that make
206 erative activity and target human methionine aminopeptidases (MetAPs) for their cellular effects.
207                                   Methionine aminopeptidases (MetAPs), which remove the initiator met
208 lar characterization of an Anopheles gambiae aminopeptidase N (AgAPN1) as the predominant jacalin tar
209        The midgut-specific anopheline alanyl aminopeptidase N (AnAPN1) is highly conserved across Ano
210 t Phe(3) is a key residue for neprilysin and aminopeptidase N (AP-N) ectoenkephalinase inhibition.
211 ced the levels of the AngIV-degrading enzyme aminopeptidase N (AP-N).
212  angiotensin-I-converting enzyme (ACE I) and aminopeptidase N (AP-N).
213                           Tumor cell surface aminopeptidase N (APN or CD13) has two puzzling function
214             Here we identify membrane alanyl aminopeptidase N (APN) as a receptor for pea enation mos
215                                    Mammalian aminopeptidase N (APN) plays multifunctional roles in ma
216                          Recently, a 100-kDa aminopeptidase N (APN) was isolated from brush border me
217 of this family that has been well studied is aminopeptidase N (APN), a multifunctional protease known
218                                    A 106-kDa aminopeptidase N (APN), called AgAPN2, was previously id
219                  A nonspecific exopeptidase, aminopeptidase N (APN), is inhibited sequence-specifical
220                                              Aminopeptidase N (APN, CD13; EC 3.4.11.2) is a transmemb
221 ptidases, neprilysin (NEP, EC 3.4.24.11) and aminopeptidase N (APN, EC 3.4.11.2).
222                          The metalloprotease aminopeptidase N (APN; CD13) is often overexpressed in t
223 cificity of human, pig, and rat orthologs of aminopeptidase N (CD13), a highly conserved cell surface
224                                        Human aminopeptidase N (hAPN/hCD13) is a dimeric membrane prot
225                                In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sod
226 ide GNGRAHA, a ligand of the surface protein aminopeptidase N and of integrin alphavbeta3.
227    The viruses used the human entry receptor aminopeptidase N and replicated in human hepatoma cells,
228                                              Aminopeptidase N from Escherichia coli is a M1 class ami
229             PEDV recognizes protein receptor aminopeptidase N from pig and human and sugar coreceptor
230 EMV binds to a heavily glycosylated receptor aminopeptidase N in the pea aphid gut and is transcytose
231                                         CD13/aminopeptidase N is a negative regulator of mast cell ac
232                                         CD13/aminopeptidase N is a transmembrane peptidase that is in
233 r with the lack of receptor functionality of aminopeptidase N proteins might account for some of the
234 d hydrophobic character for the S1 pocket of aminopeptidase N that is conserved with aminopeptidase N
235 s residue methionine 260 in Escherichia coli aminopeptidase N were characterized.
236     We have recently demonstrated that CD13 (aminopeptidase N) expressed by nonmalignant host cells o
237                                        CD13 (aminopeptidase N) expression in pericytes was determined
238 ch as alpha(v)beta3/alpha(v)beta5 integrins, aminopeptidase N, and aminopeptidase A.
239 ular adhesion molecule 1 (ICAM-1), anti-LG3, aminopeptidase N, CXCL9, endothelin-1, and gelsolin.
240 f a receptor protein in the aphid gut called aminopeptidase N, which is responsible for entry of the
241                          Lepidopteran midgut aminopeptidases N (APNs) are phylogenetically divided in
242 d with differential alteration of two midgut aminopeptidases N, APN1 and APN6, conferred by a trans-r
243 ta-glucosidase (carbon-cycling) and l-leucin aminopeptidase (nitrogen-cycling), was reduced following
244 t of aminopeptidase N that is conserved with aminopeptidase Ns.
245 k and conclude that DPP9 is a novel integral aminopeptidase of the N-end rule pathway.
246                     No other known cytosolic aminopeptidase or endopeptidase was found to digest thes
247 of catalytically inactive insulin-responsive aminopeptidase/oxytocinase only rescued apm1-2.
248   Overexpression of human insulin-responsive aminopeptidase/oxytocinase rescued all apm1 phenotypes,
249 dase, angiotensin-I-converting enzyme (ACE), aminopeptidase P (APP), and carboxypeptidase N/M (CPN)]
250                                P. falciparum aminopeptidase P (PfAPP) shares with mammalian cytosolic
251 se P (PfAPP) shares with mammalian cytosolic aminopeptidase P a three-domain, homodimeric organizatio
252                            The metalloenzyme aminopeptidase P catalyzes the hydrolysis of amino acids
253 Plasmodium falciparum expresses a homolog of aminopeptidase P during its asexual intraerythrocytic cy
254               Finally, through this approach Aminopeptidase P was identified as a new regulator of be
255  endopeptidase, dipeptidyl peptidase IV, and aminopeptidase P.
256 ed by this system is an exoprotease, leucine aminopeptidase (PA-LAP), which is coexpressed with sever
257 oduct of a putative cell membrane-associated aminopeptidase (PepN).
258 hia coli was nearly entirely dependent on an aminopeptidase, PepN, expression of PepN in periplasm al
259 idue valine 459 in the Plasmodium falciparum aminopeptidase PfA-M1 and of three substitutions of the
260   Here we present evidence that an M1-family aminopeptidase, PfA-M1, has been recruited to specialize
261                    Two Plasmodium falciparum aminopeptidases, PfA-M1 and PfA-M17, play crucial roles
262 te Plasmodium falciparum employs two metallo-aminopeptidases, PfA-M1 and PfA-M17, which are essential
263 ed one of the extracellular enzymes (leucine aminopeptidase), pointing to a specific nanoparticle eff
264 ction of residues that are less cleavable by aminopeptidases predominantly at N-flanking sites, leadi
265 The partially purified enzyme as well as the aminopeptidases present in crude extract cleaved prefere
266                   Endoplasmic reticulum (ER) aminopeptidases process antigenic peptide precursors to
267                                              Aminopeptidases process the N-terminal amino acids of ta
268 r-fold increase in vasopressinase, a cystine aminopeptidase produced by placental trophoblasts, which
269 aminopeptidase, the resulting BH(-/-)leucine aminopeptidase(-/-) progeny show a selective increase in
270                          Puromycin-sensitive aminopeptidase (PSA) is the only cytosolic enzyme able t
271 zyme have suggested that puromycin-sensitive aminopeptidase (PSA) plays a role in creating and destro
272 ngle aminopeptidase, the puromycin-sensitive aminopeptidase (PSA, cytosol alanyl aminopeptidase).
273                          Puromycin-sensitive aminopeptidase (PSA/NPEPPS) is a novel modifier of TAU-i
274  by a host protease, the puromycin-sensitive aminopeptidase (PurSA).
275  variation in domestic cats as Transmembrane aminopeptidase Q (Taqpep), which encodes a membrane-boun
276 e active fractions, and recombinant aspartyl aminopeptidase recapitulated the cleavage pattern observ
277 nflammation is established, changes to LTA4H aminopeptidase remain, even in the absence of ongoing ci
278 nts of beta-casein with elastase and leucine aminopeptidase revealed the release of BCM-7 by competit
279  Pro-Gly-Pro was identified as an endogenous aminopeptidase substrate for LTA4 hydrolase.
280 ins participating in chitin utilization, two aminopeptidases, TagA-related protein, cytolysin, RbmC,
281                                        Since aminopeptidases take part in many physiological processe
282  Dipeptidyl peptidase I (DPPI) is a cysteine aminopeptidase that can activate several serine protease
283 ll surface-anchored and seahorse-shaped zinc-aminopeptidase that forms head-to-head dimers.
284          pam-1 encodes a puromycin sensitive aminopeptidase that regulates centrosome positioning in
285                                              Aminopeptidases that generate antigenic peptides influen
286 egradation at neutral pH was due to a single aminopeptidase, the puromycin-sensitive aminopeptidase (
287 ng another cytosolic aminopeptidase, leucine aminopeptidase, the resulting BH(-/-)leucine aminopeptid
288 amily of metalloproteases called M17 leucine aminopeptidases, the preferred substrate for the T. dent
289 to T cells, such peptides must be trimmed by aminopeptidases to the proper size (typically 8-10 resid
290 of action of the orally available methionine aminopeptidase type 2 inhibitor, [(1R)-1-carbamoyl-2-met
291   PPI-2458, a potent irreversible methionine aminopeptidase type 2 inhibitor, was administered orally
292           To characterize this activity, the aminopeptidase was cloned, overexpressed, and purified.
293 lammation, and selective inhibition of LTA4H aminopeptidase, which ordinarily degrades PGP.
294 found that these enzymes are genuine Xaa-Pro aminopeptidases, which hydrolyze peptides with proline a
295 a membrane, detected using insulin-regulated aminopeptidase with a pH-sensitive GFP tag (pHluorin), p
296 ymes is a self-compartmentalizing tetrameric aminopeptidase with a preference for cysteine and hydrop
297 tidase N from Escherichia coli is a M1 class aminopeptidase with the active-site region related to th
298 t (4MDM) that selectively augments the LTA4H aminopeptidase without affecting the bioproduction of le
299                                    The human aminopeptidase XPNPEP3 is associated with cystic kidney
300 ch, which can be applied in principle to all aminopeptidases, yields useful information for the desig

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