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Proteolytic Enzyme
Known as:
proteolytic
, Proteinase
, Protease
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Enzymes acting on peptide bonds. EC 3.4.-
National Institutes of Health
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Related topics
Related topics
40 relations
ATG4C protein, human
Activated Caspase-3
BAP1 protein, human
CAPN1 protein, human
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2002
Highly Cited
2002
1-[2-[(5-Cyanopyridin-2-yl)amino]ethylamino]acetyl-2-(S)-pyrrolidinecarbonitrile: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties.
E. B. Villhauer
,
J. Brinkman
,
+6 authors
T. Hughes
Journal of Medicinal Chemistry
2002
Corpus ID: 8966102
Dipeptidyl peptidase IV (DPP-IV) inhibition has the potential to become a valuable therapy for type 2 diabetes. We report the…
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Highly Cited
1998
Highly Cited
1998
Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli.
J. D. Gier
,
P. Scotti
,
+4 authors
G. Heijne
Proceedings of the National Academy of Sciences…
1998
Corpus ID: 36449765
Assembly of several inner membrane proteins-leader peptidase (Lep), a Lep derivative (Lep-inv) that inserts with an inverted…
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Highly Cited
1991
Highly Cited
1991
Glucocorticoids induce neutral endopeptidase in transformed human tracheal epithelial cells.
D. Borson
,
Dieter C. Gruenert
American Journal of Physiology
1991
Corpus ID: 29406269
Neutral endopeptidase (NEP, also known as enkephalinase, CALLA, or EC 3.4.24.11) is a membrane-bound peptidase present in many…
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Highly Cited
1991
Highly Cited
1991
Dipeptidyl peptidase IV in the immune system. Effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes.
Ekkehard Schön
,
I. Born
,
+5 authors
Siegfried Ansorge
Biological Chemistry Hoppe-Seyler
1991
Corpus ID: 45896571
Dipeptidyl peptidase IV (DP IV) is a membrane peptidase playing a significant role in the process of activation and proliferation…
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Highly Cited
1989
Highly Cited
1989
Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NH2-terminal signal sequence as the membrane-anchoring domain.
S. Ogata
,
Y. Misumi
,
Y. Ikehara
Journal of Biological Chemistry
1989
Corpus ID: 38777224
Highly Cited
1985
Highly Cited
1985
Involvement of plasma membrane dipeptidyl peptidase IV in fibronectin-mediated adhesion of cells on collagen.
C. Hanski
,
T. Huhle
,
W. Reutter
Biological Chemistry Hoppe-Seyler
1985
Corpus ID: 33685303
Dipeptidyl peptidase IV is an exopeptidase found in the serum and in plasma membranes of most animal tissues. The role of this…
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Highly Cited
1984
Highly Cited
1984
Nucleotide sequence of the Escherichia coli prolipoprotein signal peptidase (lsp) gene.
M. Innis
,
M. Tokunaga
,
+4 authors
H. C. Wu
Proceedings of the National Academy of Sciences…
1984
Corpus ID: 23175609
The nucleotide sequence of the prolipoprotein signal peptidase (lsp) gene has been determined. The lsp gene was found to be…
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Highly Cited
1978
Highly Cited
1978
A technique for the removal of pyroglutamic acid from the amino terminus of proteins using calf liver pyroglutamate amino peptidase.
D. Podell
,
George N. Abraham
Biochemical and Biophysical Research…
1978
Corpus ID: 39505578
Highly Cited
1976
Highly Cited
1976
A calcium-activated neutral protease in normal and dystrophic human muscle.
N. Kar
,
C. Pearson
Clinica chimica acta; international journal of…
1976
Corpus ID: 32711561
Highly Cited
1974
Highly Cited
1974
Peptidase Mutants of Salmonella typhimurium
C. Miller
,
K. Mackinnon
Journal of Bacteriology
1974
Corpus ID: 6399577
Six peptidase activities have been distinguished electrophoretically in cell extracts of Salmonella typhimurium with the aid of a…
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