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A Ca(2+) switch aligns the active site of calpain
scientific article published on 8 March 2002
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title
A Ca(2+) switch aligns the active site of calpain
(English)
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author
Tudor Moldoveanu
object named as
Tudor Moldoveanu
series ordinal
1
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author name string
Christopher M Hosfield
series ordinal
2
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Daniel Lim
series ordinal
3
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John S Elce
series ordinal
4
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Zongchao Jia
series ordinal
5
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Peter L Davies
series ordinal
6
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language of work or name
English
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publication date
8 March 2002
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published in
Cell
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volume
108
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issue
5
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page(s)
649-60
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cites work
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Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes
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v-Src-induced modulation of the calpain-calpastatin proteolytic system regulates transformation.
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Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation
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Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain.
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Neurotoxicity induces cleavage of p35 to p25 by calpain
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EF-hand calcium-binding proteins.
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Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding
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Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation
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Dissociation and aggregation of calpain in the presence of calcium
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Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
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Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
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7 January 2021
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C2-domains, structure and function of a universal Ca2+-binding domain
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7 January 2021
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7 January 2021
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The structure of calpain.
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7 January 2021
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inferred from DOI database lookup
Structure and physiological function of calpains
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7 January 2021
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The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
1 reference
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reference URL
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7 January 2021
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Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution
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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
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The calpain cascade. Mu-calpain activates m-calpain
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7 January 2021
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Domain III of calpain is a ca2+-regulated phospholipid-binding domain
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reference URL
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7 January 2021
based on heuristic
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Calpain and caspase: can you tell the difference?
1 reference
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Crossref
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https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900659-1
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7 January 2021
based on heuristic
inferred from DOI database lookup
Calpain inhibition: an overview of its therapeutic potential
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Crossref
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https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900659-1
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7 January 2021
based on heuristic
inferred from DOI database lookup
Calpain dissociates into subunits in the presence of calcium ions
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reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900659-1
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7 January 2021
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inferred from DOI database lookup
The calpain small subunit gene is essential: its inactivation results in embryonic lethality.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2802%2900659-1
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0092-8674(02)00659-1
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PubMed publication ID
11893336
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ResearchGate publication ID
11470741
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