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Aspartic Acid Endopeptidases
Known as:
Endopeptidases, Aspartic Acid
, Aspartic Endopeptidases
, aspartic endopeptidase
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A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
National Institutes of Health
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Related topics
Related topics
49 relations
Narrower (40)
AXP protein, Yarrowia lipolytica
Aspergillus oryzae carboxyl proteinase
BACE1 protein, human
Bace protein, rat
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Aspartic Acid Proteases
In Blood
Process of secretion
antagonists & inhibitors
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Broader (1)
Endopeptidases
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2010
Review
2010
Novel research horizons for presenilins and γ-secretases in cell biology and disease.
B. de Strooper
,
W. Annaert
Annual review of cell and developmental biology
2010
Corpus ID: 19830432
Presenilins are the catalytic subunits of larger tetrameric γ-secretase complexes. The degradome of these aspartyl proteases…
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Highly Cited
2007
Highly Cited
2007
A family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata
R. Kaur
,
B. Ma
,
B. Cormack
Proceedings of the National Academy of Sciences
2007
Corpus ID: 36576150
Candida glabrata is a yeast pathogen of humans. We have established a tissue culture model to analyze the interaction of C…
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Highly Cited
2000
Highly Cited
2000
Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1.
Y. M. Li
,
M. Xu
,
+15 authors
S. Gardell
Nature
2000
Corpus ID: 46159686
Cleavage of amyloid precursor protein (APP) by the beta- and gamma-secretases generates the amino and carboxy termini…
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Highly Cited
2000
Highly Cited
2000
Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
H. Steiner
,
M. Kostka
,
+9 authors
C. Haass
Nature Cell Biology
2000
Corpus ID: 10189662
Endoproteolysis of β-amyloid precursor protein (βAPP) and Notch requires conserved aspartate residues in presenilins 1 and 2 (PS1…
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Highly Cited
2000
Highly Cited
2000
Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase.
J. Huse
,
D. S. Pijak
,
G. Leslie
,
V. Lee
,
R. Doms
The Journal of biological chemistry
2000
Corpus ID: 27124708
The amyloidogenic Abeta peptide is liberated from the amyloid precursor protein (APP) by two proteolytic activities, beta…
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Highly Cited
2000
Highly Cited
2000
L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity.
M. Shearman
,
D. Beher
,
+7 authors
J. L. Castro
Biochemistry
2000
Corpus ID: 37210221
Progressive cerebral amyloid beta-protein (A beta) deposition is believed to play a central role in the pathogenesis of Alzheimer…
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Highly Cited
1999
Highly Cited
1999
Peptidomimetic probes and molecular modeling suggest that Alzheimer's gamma-secretase is an intramembrane-cleaving aspartyl protease.
M. Wolfe
,
W. Xia
,
+5 authors
D. Selkoe
Biochemistry
1999
Corpus ID: 10750932
The amyloid beta-protein (Abeta), implicated in the pathogenesis of Alzheimer's disease (AD), is a proteolytic metabolite…
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Highly Cited
1995
Highly Cited
1995
alpha-Hydroxy phosphinyl-based inhibitors of human renin.
D. Patel
,
K. Rielly‐Gauvin
,
+6 authors
E. Petrillo
Journal of medicinal chemistry
1995
Corpus ID: 32560063
The design and application of alpha-hydroxy phosphonates, a new class of transition state analogs, toward the discovery of novel…
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Highly Cited
1991
Highly Cited
1991
Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide.
Z. Zhang
,
R. Poorman
,
L. Maggiora
,
R. Heinrikson
,
F. Kézdy
The Journal of biological chemistry
1991
Corpus ID: 12859671
Highly Cited
1986
Highly Cited
1986
The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
C. Woolford
,
L. B. Daniels
,
F. J. Park
,
E. W. Jones
,
J. V. Van Arsdell
,
M. Innis
Molecular and cellular biology
1986
Corpus ID: 7254040
pep4 mutants of Saccharomyces cerevisiae accumulate inactive precursors of vacuolar hydrolases. The PEP4 gene was isolated from a…
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