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Procollagen N-Endopeptidase
Known as:
Procollagen N Proteinase
, Procollagen Peptidase
, Procollagen N Endopeptidase
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An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the…
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National Institutes of Health
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Related topics
Related topics
9 relations
ADAMTS2 gene
CHMP1A gene
In Blood
Process of secretion
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2007
Highly Cited
2007
Insights into How CUB Domains Can Exert Specific Functions while Sharing a Common Fold
G. Blanc
,
B. Font
,
+4 authors
C. Moali
Journal of Biological Chemistry
2007
Corpus ID: 21327995
Procollagen C-proteinase enhancers (PCPE-1 and -2) are extracellular glycoproteins that can stimulate the C-terminal processing…
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Highly Cited
2002
Highly Cited
2002
Interaction Properties of the Procollagen C-proteinase Enhancer Protein Shed Light on the Mechanism of Stimulation of BMP-1*
S. Ricard-Blum
,
S. Bernocco
,
+7 authors
D. Hulmes
Journal of Biological Chemistry
2002
Corpus ID: 22701529
Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that binds to the C-propeptide of procollagen I…
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Highly Cited
2000
Highly Cited
2000
Bone Morphogenetic Protein 1 Is an Extracellular Processing Enzyme of the Laminin 5 γ2 Chain*
S. Amano
,
I. Scott
,
+9 authors
R. Burgeson
Journal of Biological Chemistry
2000
Corpus ID: 23682716
Epithelial cells maintained in culture medium containing low calcium proteolytically process laminin 5 (α3β3γ2) within the α3 and…
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Highly Cited
1997
Highly Cited
1997
Cleavage of Type I Procollagen by Human Mast Cell Chymase Initiates Collagen Fibril Formation and Generates a Unique Carboxyl-terminal Propeptide*
M. Kofford
,
L. Schwartz
,
N. Schechter
,
D. Yager
,
R. Diegelmann
,
M. Graham
Journal of Biological Chemistry
1997
Corpus ID: 40492065
The ability of human mast cell chymase and tryptase to process procollagen was examined. Purified human intestinal smooth muscle…
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Highly Cited
1987
Highly Cited
1987
Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical…
K. Kadler
,
Y. Hojima
,
D. J. Prockop
Journal of Biological Chemistry
1987
Corpus ID: 10949264
Highly Cited
1981
Highly Cited
1981
Assembly and processing of procollagen type III in chick embryo blood vessels.
L. Fessler
,
R. Timpl
,
J. Fessler
Journal of Biological Chemistry
1981
Corpus ID: 24814702
Highly Cited
1979
Highly Cited
1979
Separate amino and carboxyl procollagen peptidases in chick embryo tendon.
M. Leung
,
L. Fessler
,
D. Greenberg
,
J. Fessler
Journal of Biological Chemistry
1979
Corpus ID: 30458658
Procollagen synthesized by freshly excised chick enbryo leg tendons is efficiently processed by proteolytic removal of first the…
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1973
1973
Identification of two distinct species of procollagen synthesized by a clonal line of calf dermatosparactic cells.
R. Church
,
M. Tanzer
,
C. Lapière
Nature: New biology
1973
Corpus ID: 42033298
THE heritable connective tissue disease in cattle called dermatosparaxis is characterized by extreme fragility of the skin1,2…
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Highly Cited
1972
Highly Cited
1972
Procollagen: Conversion of the Precursor to Collagen by a Neutral Protease
P. Bornstein
,
H. Ehrlich
,
A. Wyke
Science
1972
Corpus ID: 36099366
An enzymatic activity (procollagen peptidase), capable of converting the biosynthetic precursor procollagen to collagen at…
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Highly Cited
1971
Highly Cited
1971
Procollagen peptidase: an enzyme excising the coordination peptides of procollagen.
C. Lapière
,
A. Lenaers
,
L. Kohn
Proceedings of the National Academy of Sciences…
1971
Corpus ID: 7719949
A heritable connective tissue disorder of cattle, dermatosparaxis, is characterized by an extreme fragility of the skin and the…
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