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Cysteine Proteases
Known as:
Cysteine Protease
, Proteases, Cysteine
, Proteinases, Cysteine
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An enzyme that contains an unpaired cysteine in the active site which acts as a nucleophilic thiol to catalyze the proteolytic processing of other…
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National Institutes of Health
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Related topics
Related topics
26 relations
Narrower (2)
CASP10 protein, human
eimeripain protein, Eimeria tenella
CTSS protein, human
Cathepsin H
Cathepsin L
Cathepsins B
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2002
Review
2002
Plant seed cystatins and their target enzymes of endogenous and exogenous origin.
S. Arai
,
I. Matsumoto
,
Y. Emori
,
K. Abe
Journal of Agricultural and Food Chemistry
2002
Corpus ID: 44558263
Cystatins are protein inhibitors of cysteine proteinases of the papain family, and those of animal origin have long been studied…
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Highly Cited
1999
Highly Cited
1999
Antisense Inhibition of Expression of Cysteine Proteinases Affects Entamoeba histolytica-Induced Formation of Liver Abscess in Hamsters
S. Ankri
,
T. Stolarsky
,
R. Bracha
,
F. Padilla‐Vaca
,
D. Mirelman
Infection and Immunity
1999
Corpus ID: 6636805
ABSTRACT Trophozoites of virulent Entamoeba histolyticatransfected with the antisense gene encoding cysteine proteinase 5 (CP5…
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Highly Cited
1998
Highly Cited
1998
Isolation and molecular characterization of a surface‐bound proteinase of Entamoeba histolytica
T. Jacobs
,
I. Bruchhaus
,
T. Dandekar
,
E. Tannich
,
M. Leippe
Molecular Microbiology
1998
Corpus ID: 23484868
Major pathogenic functions of Entamoeba histolytica involved in destruction of host tissues are the degradation of extracellular…
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Highly Cited
1995
Highly Cited
1995
Toxicity toChrysomela tremulae (Coleoptera: Chrysomelidae) of transgenic poplars expressing a cysteine proteinase inhibitor
J. Leplé
,
M. Bonadé-Bottino
,
+5 authors
L. Jouanin
Molecular breeding
1995
Corpus ID: 28530206
The aim of this study was to test the potential of proteinase inhibitors to controlChrysomela tremulae, a beetle that causes…
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Highly Cited
1992
Highly Cited
1992
The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes.
O. Campetella
,
J. Henriksson
,
U. Åslund
,
A. Frasch
,
U. Pettersson
,
J. Cazzulo
Molecular and biochemical parasitology (Print)
1992
Corpus ID: 4052763
Highly Cited
1990
Highly Cited
1990
Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II.
H. Kondo
,
K. Abe
,
I. Nishimura
,
H. Watanabe
,
Y. Emori
,
S. Arai
Journal of Biological Chemistry
1990
Corpus ID: 27456419
Oryzacystatin (oryzacystatin-I) is a proteinaceous cysteine proteinase inhibitor (cystatin) in rice seeds and is the first well…
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Highly Cited
1990
Highly Cited
1990
Some kinetic properties of a cysteine proteinase (cruzipain) from Trypanosoma cruzi.
J. Cazzulo
,
M. C. Cazzulo Franke
,
Javier Martínez
,
B. M. Franke de Cazzulo
Biochimica et Biophysica Acta
1990
Corpus ID: 23605641
Highly Cited
1986
Highly Cited
1986
Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.
G. Salvesen
,
C. Parkes
,
M. Abrahamson
,
A. Grubb
,
A. Barrett
Biochemical Journal
1986
Corpus ID: 41810720
We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as had previously been thought…
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Highly Cited
1983
Highly Cited
1983
Two distinct Ca2+ proteases (calpain I and calpain II) purified concurrently by the same method from rat kidney.
N. Yoshimura
,
T. Kikuchi
,
T. Sasaki
,
A. Kitahara
,
M. Hatanaka
,
T. Murachi
Journal of Biological Chemistry
1983
Corpus ID: 1165657
Review
1976
Review
1976
Handbook of Enzymatic Methods of Analysis
G. Guilbault
1976
Corpus ID: 82716564
developing embryos, dipeptidases from Escherichia coli B and from Ehrlich Lettre mouse ascites-tumour cells, and a selection of…
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