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CAPN1 gene
Known as:
CANP
, CANPL1
, MU-CANP, LARGE SUBUNIT
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This gene is involved in proteolytic processing.
National Institutes of Health
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Related topics
Related topics
7 relations
CAPN1 protein, human
CAPN13 gene
CAPN2 gene
CAPNS1 gene
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2014
Highly Cited
2014
Melatonin Inhibits mTOR-Dependent Autophagy during Liver Ischemia/Reperfusion
Jung-Woo Kang
,
Hong‐Ik Cho
,
Sun-Mee Lee
Cellular Physiology and Biochemistry
2014
Corpus ID: 11198718
Background: Autophagy is a self-digestion system responsible for maintaining cellular homeostasis and interacts with reactive…
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Highly Cited
2007
Highly Cited
2007
Asymmetric localization of calpain 2 during neutrophil chemotaxis.
P. Nuzzi
,
Melissa A Senetar
,
A. Huttenlocher
Molecular Biology of the Cell
2007
Corpus ID: 5370901
Chemoattractants induce neutrophil polarization through localized polymerization of F-actin at the leading edge. The suppression…
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Highly Cited
2004
Highly Cited
2004
Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin.
M. P. Kent
,
M. Spencer
,
M. Koohmaraie
Journal of Animal Science
2004
Corpus ID: 147197
Using both in vitro and in vivo approaches, numerous studies have provided evidence that mu-calpain is responsible for postmortem…
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Highly Cited
2001
Highly Cited
2001
Disruption of the Mouse μ-Calpain Gene Reveals an Essential Role in Platelet Function
M. Azam
,
Shaida Andrabi
,
K. Sahr
,
Lakshmi Kamath
,
A. Kuliopulos
,
A. Chishti
Molecular and Cellular Biology
2001
Corpus ID: 31436505
ABSTRACT Conventional calpains are ubiquitous calcium-regulated cysteine proteases that have been implicated in cytoskeletal…
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Highly Cited
1994
Highly Cited
1994
Domain structure of calpain: mapping the binding site for calpastatin.
D. E. Croall
,
K. McGrody
Biochemistry
1994
Corpus ID: 34474802
The peptide EKLGERDDTIPPEYRELLEKKTGV was synthesized to mimic the central consensus sequence of calpastatin, the specific…
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Highly Cited
1989
Highly Cited
1989
Properties of erythrocyte membrane binding and autolytic activation of calcium-activated neutral protease.
M. Inomata
,
M. Hayashi
,
Megumi Nakamura
,
Yumiko Saito
,
Seiichi KawashimaS
Journal of Biological Chemistry
1989
Corpus ID: 15841752
Highly Cited
1988
Highly Cited
1988
Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease.
S. Imajoh
,
K. Aoki
,
+4 authors
K. Suzuki
Biochemistry
1988
Corpus ID: 20092411
A nearly full-length cDNA clone for the large subunit of high-Ca2+-requiring Ca2+-activated neutral protease (mCANP) from human…
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Highly Cited
1986
Highly Cited
1986
Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequence
K. Aoki
,
S. Imajoh
,
+4 authors
Koichi Suzuki
FEBS Letters
1986
Corpus ID: 36697759
Highly Cited
1983
Highly Cited
1983
Purification and characterization of two forms of Ca2+-activated neutral protease from calf brain.
Mazhar N. MalikS
,
M. Fenko
,
K. Iqbal
,
H. M. Wisniewski
Journal of Biological Chemistry
1983
Corpus ID: 27442769
Highly Cited
1981
Highly Cited
1981
Autolysis of calcium-activated neutral protease of chicken skeletal muscle.
K. Suzuki
,
S. Tsuji
,
S. Ishiura
,
Y. Kimura
,
S. Kubota
,
K. Imahori
Journal of Biochemistry (Tokyo)
1981
Corpus ID: 23208291
The conditions and process of autolysis of calcium-activated neutral protease (CANP) were examined. Optimal conditions for…
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