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Calpain
Known as:
Papain-Like Cysteine Protease
, Neutral Proteinase, Calcium-Dependent
, Proteinase, Calcium-Dependent Neutral
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Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from…
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National Institutes of Health
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Related topics
Related topics
30 relations
Narrower (14)
CAPN1 protein, human
CAPN11 protein, human
Calpain I
Calpain II
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Cysteine Protease Genes
Enzyme Gene
Hydrolysis
In Blood
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Broader (1)
caspase
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2004
Review
2004
The giant protein titin: a major player in myocardial mechanics, signaling, and disease.
H. Granzier
,
S. Labeit
Circulation Research
2004
Corpus ID: 1635220
The sarcomere contains, in addition to thin and thick filaments, a filament composed of the giant protein titin (also known as…
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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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Review
1993
Review
1993
Medicinal and therapeutic value of the shiitake mushroom.
Shung-Chang Jong
,
J. M. Birmingham
Advances in Applied Microbiology
1993
Corpus ID: 9039582
Highly Cited
1991
Highly Cited
1991
Degradation of Microtubule‐Associated Protein 2 and Brain Spectrin by Calpain: A Comparative Study
G. Johnson
,
J. Litersky
,
R. Jope
Journal of Neurochemistry
1991
Corpus ID: 24540448
Abstract: The in vitro degradation of microtubule‐associated protein 2 (MAP‐2) and spectrin by the calcium‐dependent neutral…
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Highly Cited
1988
Highly Cited
1988
Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits.
Byung Joon Hwang
,
Kee Min Woo
,
A L Goldberg
,
C. H. Chung
Journal of Biological Chemistry
1988
Corpus ID: 27921317
Highly Cited
1987
Highly Cited
1987
Isolation and structural studies of the intact scrapie agent protein.
D. C. Bolton
,
P. Bendheim
,
A. Marmorstein
,
Anna Potempska
Archives of Biochemistry and Biophysics
1987
Corpus ID: 42144123
Highly Cited
1985
Highly Cited
1985
On the association of glycoprotein Ib and actin-binding protein in human platelets
J. Okita
,
D. Pidard
,
P. Newman
,
R. Montgomery
,
T. Kunicki
Journal of Cell Biology
1985
Corpus ID: 7309700
Glycoprotein (GP) Ib was purified from lysates of human platelets prepared in the presence or absence of inhibitors of the…
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Highly Cited
1982
Highly Cited
1982
Characterization of a brain calcium-activated protease that degrades neurofilament proteins.
U. Zimmerman
,
W. Schlaepfer
Biochemistry
1982
Corpus ID: 28042227
A Ca2+-dependent protease was prepared from rat brain by using DEAE-Sephadex, Sephadex G-200, and substrate affinity…
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Highly Cited
1982
Highly Cited
1982
The stimulation of protein degradation in muscle by Ca2+ is mediated by prostaglandin E2 and does not require the calcium-activated protease.
H. Rodemann
,
L. Waxman
,
A L Goldberg
Journal of Biological Chemistry
1982
Corpus ID: 13443512
Highly Cited
1981
Highly Cited
1981
Limited autolysis of Ca2+-activated neutral protease (CANP) changes its sensitivity to Ca2+ ions.
K. Suzuki
,
S. Tsuji
,
S. Kubota
,
Y. Kimura
,
K. Imahori
Journal of Biochemistry (Tokyo)
1981
Corpus ID: 21101612
Ca2+-activated neutral protease (CANP) usually requires mM Ca2+ for activation. The sensitivity of CANP to Ca2+ is greatly…
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