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1 2, but not by cathepsin D, a closely related aspartyl protease.
2 rary of inhibitors of cathepsin D (CatD), an aspartyl protease.
3 nalogs, suggesting gamma-secretase may be an aspartyl protease.
4 in systems: IMPDH, MAP kinase p38, and HIV-1 aspartyl protease.
5 inhibitors directed to the active site of an aspartyl protease.
6 g strong evidence that gamma-secretase is an aspartyl protease.
7 d suggesting that these compounds inhibit an aspartyl protease.
8 -secretase, an autoactivated intramembranous aspartyl protease.
9 he FK506 binding protein (FKBP-12) and HIV-1 aspartyl protease.
10 nes a functional domain for an intramembrane aspartyl protease.
11 butes one aspartate to the active site of an aspartyl protease.
12 (Spp) that encodes a multipass transmembrane aspartyl protease.
13 homologs are related intramembrane-cleaving aspartyl proteases.
14 t disturbing the functions of other cellular aspartyl proteases.
15 ectivity against other biologically relevant aspartyl proteases.
16 the catalytic mechanism of BACE and related aspartyl proteases.
17 omplex and its similarity to other polytopic aspartyl proteases.
18 rger family of polytopic membrane-associated aspartyl proteases.
19 define a new subfamily of membrane-anchored aspartyl proteases.
20 susceptibilities that are characteristic of aspartyl proteases.
21 ecursor Gag (Pr55(Gag)) operated by cellular aspartyl proteases.
22 glycosylphosphatidylinositol (GPI)-anchored aspartyl proteases.
23 0 nM, and >100-fold selectivity over related aspartyl proteases.
24 -embedded enzyme in the presenilin family of aspartyl proteases.
25 cellular glycosylphosphatidylinositol-linked aspartyl proteases.
27 gs of beta-1,3-glucanases (16), metallo- and aspartyl proteases (13), glycerophosphodiesterases (6),
28 Here we establish that Toxoplasma gondii aspartyl protease 3 (ASP3) resides in the endosomal-like
31 (ii) Experiments designed to demonstrate aspartyl protease activity in a phage display system fai
33 do not resemble transition state analogs of aspartyl proteases, also displayed potent, non-competiti
35 cterized mechanism-based inactivators for an aspartyl protease and show promise as novel antimalarial
36 II) is the most extensively studied of these aspartyl proteases and catalyzes the initial step in the
37 ey have a direct bearing on the mechanism of aspartyl proteases and efforts to model beta-secretase.
41 called gamma-secretase) has properties of an aspartyl protease, and mutation of either of the two asp
43 d hydrolases (e.g., lipases, phospholipases, aspartyl proteases, and acid sphingomyelinases) was foun
44 hored protein with clear homology to soluble aspartyl proteases, and alpha-secretase displays charact
45 with a C2 GRAM domain protein (BAGP1) and an aspartyl protease (APCB1), both of which are required fo
47 eptide peptidase (SPP)-related intramembrane aspartyl proteases are a homologous group of polytopic m
48 gene for presenilin 1, a multi-transmembrane aspartyl protease, are known to cause familial Alzheimer
52 by sequential proteolysis, catalysed by the aspartyl protease BACE, followed by presenilin-dependent
57 hough not selective over the closely related aspartyl protease BACE2, verubecestat has high selectivi
58 lectivity for the other structurally related aspartyl proteases BACE2, cathepsin D, renin, and pepsin
59 lectivity for the other structurally related aspartyl proteases BACE2, cathepsinD, renin, and pepsin.
60 rotein (APP) cleaving enzyme 1 (BACE1) is an aspartyl protease best known for its role in generating
61 ge of amyloid precursor protein (APP) by the aspartyl protease beta-secretase and the presenilin-depe
64 otein (APP) in the brain is a membrane-bound aspartyl protease beta-site APP cleaving enzyme (BACE).
66 the consensus sequences found in most known aspartyl proteases, but otherwise has only modest homolo
67 ive diseases involves activation of cysteine aspartyl proteases (caspases), which initiate and execut
68 Increasing evidence suggests that serine-aspartyl proteases-caspases are activated in the AD brai
70 Edr bears both CCHC zinc-finger and putative aspartyl protease catalytic site retroviral-like motifs,
73 ur in functionally interesting situations in aspartyl proteases, citrate synthase, EF hands, haemoglo
74 eta-secretase (BACE), a type-I transmembrane aspartyl protease, cleaves APP first to generate a 99-am
78 of XRN4 and VCS in seeds (PECTIN LYASE-LIKE, ASPARTYL PROTEASE, DWD-HYPERSENSITIVE-TO-ABA3, and YELLO
79 ficiency virus 1 (HIV-1) protease (PR) is an aspartyl protease essential for HIV-1 viral infectivity.
80 zyme 1) is a membrane-tethered member of the aspartyl proteases, essential for the production of beta
83 also efficiently inhibited Sap9p, a secreted aspartyl protease from the human pathogen, Candida albic
86 Unlike beta-secretase, which is a monomeric aspartyl protease, gamma-secretase activity resides as p
87 in the sequence Asp-Thr-Gly, the hallmark of aspartyl proteases, had no effect on viral replication i
88 ases, plasmepsin I, II, and IV and the histo-aspartyl protease (HAP), have been identified in the foo
89 cleaving enzyme) with characteristics of an aspartyl protease has been identified as the beta-secret
91 ase is a multiprotein intramembrane cleaving aspartyl protease (I-CLiP) that catalyzes the final clea
96 talloprotease inhibitor), or pepstatin A (an aspartyl protease inhibitor) but was inhibited by E-64 a
97 anomolar, low-molecular-weight plasmepsin II aspartyl protease inhibitors have been identified using
98 roteasome inhibitors as well as cysteine and aspartyl protease inhibitors stabilize MHC class I compl
100 ysis within autolysosomes with cysteine- and aspartyl-protease inhibitors caused a marked accumulatio
101 teases and gamma-secretase, an intramembrane aspartyl protease involved in Alzheimer's disease, cleav
102 peptidase (SPP) is an intramembrane cleaving aspartyl protease involved in release of leader peptide
104 active site of gamma-secretase, a polytopic aspartyl protease involved in the transmembrane processi
105 sin D is unaffected, showing that this major aspartyl protease is not involved in degradation of Ii o
108 which has little or no homology to any known aspartyl protease) is itself a transmembrane aspartyl pr
109 Cathepsin D (CD), the major intracellular aspartyl protease, is a mediator of IFN-gamma and TNF-al
112 Within lysosomes, cathepsin D (CtsD), an aspartyl protease, is suggested to be the main protease
113 the first cleavage event is a transmembrane aspartyl protease known as beta-site amyloid precursor p
115 tor motif that has not been described in the aspartyl protease literature and may serve as a starting
116 d glycosyl-phosphatidylinositol-linked yeast aspartyl proteases, Mkc7p and Yap3p (collectively termed
118 cursor protein (APP) by an integral membrane aspartyl protease named the beta-site APP-cleaving enzym
119 ecently identified as a novel membrane-bound aspartyl protease, named BACE1, Asp2, or memapsin 2.
120 Here we show that an inhibitor of the HIV aspartyl protease, Nelfinavir, triggers inflammasome for
121 as high selectivity for BACE1 over other key aspartyl proteases, notably cathepsin D, and profoundly
122 but otherwise has only modest homology with aspartyl proteases of known three-dimensional structure
126 aspartyl protease) is itself a transmembrane aspartyl protease or a gamma-secretase cofactor, or help
128 s PS1 might function in Notch cleavage as an aspartyl protease or di-aspartyl protease cofactor.
130 Export is dependent on the activity of the aspartyl protease, plasmepsin V (PMV), which cleaves pro
131 opportunity to examine the role this unique aspartyl protease plays in altering Abeta metabolism and
132 no inhibition of other proteases such as the aspartyl proteases porcine pepsin, human cathepsin D, pl
133 igen, which is homologous to secreted fungal aspartyl proteases, protected mice against pulmonary inf
134 ts associated with strong inhibition of this aspartyl protease raised serious concerns regarding this
138 tanding of the mechanisms whereby BACE1, the aspartyl protease required for the initial cleavage of A
139 Gamma-secretase is an intramembrane-cleaving aspartyl protease required for the normal development of
140 ase enzyme 1 (BACE1), a type I transmembrane aspartyl protease required to cleave amyloid precursor p
141 osomal acidification as well as cysteine and aspartyl proteases resident within these organelles.
142 aving enzyme 1 (BACE1), an integral membrane aspartyl protease responsible for cleavage of amyloid pr
144 eaved within the plane of the membrane by an aspartyl protease, resulting in a soluble MHC class I fr
145 s, including a nucleic acid binding protein, aspartyl protease, reverse transcriptase and integrase.
146 nts in galactose also inhibited secretion of aspartyl protease (Sap) and caused 90-nm secretory vesic
148 Thus, human SPPL3 is the first GxGD-type aspartyl protease shown to be capable of acting like a s
149 cally cleavage by the intramembrane-cleaving aspartyl protease signal peptide peptidase (SPP), is inv
150 activity and inactivation studies, using an aspartyl protease specific suicide inhibitor, demonstrat
152 The assay has also been applied to related aspartyl proteases such as cathepsin D (Cat D) and BACE-
154 ion of a gene encoding a chloroplast-located aspartyl protease that alters its pattern of expression.
155 effected by Presenilin, an unusual polytopic aspartyl protease that apparently cleaves Notch and nume
156 etalloprotease (glycoprotease) and one is an aspartyl protease that belongs to the recently described
157 cleaving enzyme 1 (BACE1) is a transmembrane aspartyl protease that catalyzes the proteolytic process
159 gamma-secretase complex is an intramembrane aspartyl protease that cleaves its substrates along thei
160 peptide peptidase (SPP) is an intramembrane aspartyl protease that cleaves remnant signal peptides a
161 beta-Secretase (BACE) is a membrane-bound aspartyl protease that cleaves the amyloid precursor pro
163 uct is a glycosylphosphatidylinositol-linked aspartyl protease that functions as a yeast secretase.
164 ified substrates of a unique intramembranous aspartyl protease that has presenilin as its active-site
168 (SPP) and gamma-secretase are intramembrane aspartyl proteases that bear similar active site motifs
169 ite of APP suggest that gamma-secretases are aspartyl proteases that catalyze a novel intramembranous
170 lin 2 (PS2) are proposed to be transmembrane aspartyl proteases that cleave amyloid precursor protein
171 se is a founding member of membrane-embedded aspartyl proteases that cleave substrates within transme
172 de peptidase (SPP) are related transmembrane aspartyl proteases that cleave transmembrane substrates.
173 (BACE1) is a membrane-tethered member of the aspartyl proteases that has been identified as beta-secr
174 sess a hydroxyethylene dipeptide isostere of aspartyl protease transition state analogs, suggesting g
175 ed by pepstatin and more potently by a novel aspartyl protease transition-state analog inhibitor that
176 Both proteases are inhibited by the same aspartyl protease transition-state analogue inhibitors,
178 hromatography on pepstatin-A agarose bed the aspartyl proteases were purified and concentrated over 2
179 cleaving enzyme 1 (BACE1), the transmembrane aspartyl protease which initiates Abeta production, is a
180 protease inhibitors (HIV-PIs) target the HIV aspartyl protease, which cleaves the HIV gag-pol polypro
181 results identify a mechanism that couples an aspartyl protease with a molecular cochaperone to trigge
182 gamma-Secretase is an unusual and ubiquitous aspartyl protease with an intramembrane catalytic site t
184 vious suggestions that gamma-secretase is an aspartyl protease with some properties similar to those
185 tor, Y1, of the basic residue-specific yeast aspartyl protease, yapsin 1, was synthesized and charact
186 racellular inhibitory domain of Msb2p by the aspartyl protease Yps1p generated the active form of the
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