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Papain
Known as:
Papain [Chemical/Ingredient]
, papase
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical…
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National Institutes of Health
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Related topics
Related topics
35 relations
Narrower (12)
Citroxain
Papacarie
S-carboxamido-papain
S-methylthio-papain
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ENZYMATIC CLEANER (PAPAIN) TAB,OPH
In Blood
MULTIVITAMIN/MINERALS, HERBAL CHELATION CAP/TAB
NUX VOMICA/PANCREATIN/PAPAIN/PEPSIN/PHENOBARB 16MG/NA BICARB TAB
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Broader (1)
caspase
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
A noncovalent class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication
K. Ratia
,
S. Pegan
,
+10 authors
A. Mesecar
Proceedings of the National Academy of Sciences…
2008
Corpus ID: 27775728
We report the discovery and optimization of a potent inhibitor against the papain-like protease (PLpro) from the coronavirus that…
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Highly Cited
2007
Highly Cited
2007
Regulation of IRF-3-dependent Innate Immunity by the Papain-like Protease Domain of the Severe Acute Respiratory Syndrome Coronavirus
S. Devaraj
,
Nan Wang
,
+8 authors
Kui Li
Journal of Biological Chemistry
2007
Corpus ID: 39191808
Severe acute respiratory syndrome coronavirus (SARS-CoV) is a novel coronavirus that causes a highly contagious respiratory…
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Highly Cited
2006
Highly Cited
2006
Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme.
K. Ratia
,
K. Saikatendu
,
+4 authors
A. Mesecar
Proceedings of the National Academy of Sciences…
2006
Corpus ID: 28848770
Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase…
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Review
2006
Review
2006
Evolutionary genomics of nucleo-cytoplasmic large DNA viruses.
L. Iyer
,
S. Balaji
,
E. Koonin
,
L. Aravind
,
La Scola
Virus Research
2006
Corpus ID: 14756424
Review
2000
Review
2000
Lysosomal cysteine proteases: more than scavengers.
B. Turk
,
D. Turk
,
V. Turk
Biochimica et Biophysica Acta
2000
Corpus ID: 32219808
Highly Cited
1990
Highly Cited
1990
The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.
M. Stubbs
,
B. Laber
,
+4 authors
V. Turk
EMBO Journal
1990
Corpus ID: 24626423
A stoichiometric complex of human stefin B and carboxymethylated papain has been crystallized in a trigonal crystal form. Data to…
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Highly Cited
1986
Highly Cited
1986
Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids.
M. Abrahamson
,
G. Salvesen
,
A. Barrett
,
A. Grubb
Journal of Biological Chemistry
1986
Corpus ID: 837031
Highly Cited
1977
Highly Cited
1977
Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
D. Cleveland
,
S. Fischer
,
M. Kirschner
,
U. Laemmli
Journal of Biological Chemistry
1977
Corpus ID: 20271864
Highly Cited
1969
Highly Cited
1969
Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation.
S. Lowey
,
H. Slayter
,
A. Weeds
,
H. Baker
Journal of Molecular Biology
1969
Corpus ID: 30156844
Highly Cited
1959
Highly Cited
1959
The hydrolysis of rabbit y-globulin and antibodies with crystalline papain.
R. Porter
Biochemical Journal
1959
Corpus ID: 441116
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