Modulation of the calpain autoproteolysis by calpastatin and phospholipids
about
The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretionsCa2+-dependent regulations and signaling in skeletal muscle: from electro-mechanical coupling to adaptationSpatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activationAsymmetric localization of calpain 2 during neutrophil chemotaxis.Effect of nutrient restriction and re-feeding on calpain family genes in skeletal muscle of channel catfish (Ictalurus punctatus)Vitamin D nuclear receptor deficiency promotes cholestatic liver injury by disruption of biliary epithelial cell junctions in miceDY-9760e, a novel calmodulin inhibitor, exhibits cardioprotective effects in the ischemic heart.Calpain-generated natural protein fragments as short-lived substrates of the N-end rule pathway.PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegenerationRole of calpain in apoptosis.Calpain-1 inhibitors for selective treatment of rheumatoid arthritis: what is the future?Calpain system and its involvement in myocardial ischemia and reperfusion injury.Calpain-dependent proteolysis of merlin occurs by oxidative stress in meningiomas: a novel hypothesis of tumorigenesis.Purification of native p94, a muscle-specific calpain, and characterization of its autolysisRoles of individual EF-hands in the activation of m-calpain by calciumChanges in intracellular localization of calpastatin during calpain activationThe calcium-activated neutral protease calpain I is present in normal foetal skin and is decreased in neonatal harlequin ichthyosis.Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation.Changes in intracellular calpastatin localization are mediated by reversible phosphorylation.Characterization of a new p94-like calpain form in human lymphocytes.Calcium-dependent cleavage of the Na(+)/Ca(2+) exchanger by m-calpain in isolated endoplasmic reticulum.Calpain-mediated breakdown of cytoskeletal proteins contributes to cholecystokinin-induced damage of rat pancreatic acini.Conformational changes of calpain from human erythrocytes in the presence of Ca2+.Dysregulation of the calpain-calpastatin system plays a role in the development of cerulein-induced acute pancreatitis in the rat.Involvement of μ/m-calpain in the proteolysis and meat quality changes during postmortem storage of chicken breast muscle.Rat brain contains multiple mRNAs for calpastatin.Phosphorylation of rat brain calpastatins by protein kinase C.Selective coupling of mu-calpain activation with the NMDA receptor is independent of translocation and autolysis in primary cortical neurons.Molecular and functional properties of a calpain activator protein specific for mu-isoforms.
P2860
Q24628711-F12B4E76-6118-47B3-B3AA-79CEEE7AB88AQ27001582-DFB90B71-8A05-418C-950B-3B3C93E2399FQ30478059-CEE580FC-1998-474C-AFDB-CBBC0393833EQ30479028-DD9491BA-20DF-450F-90C5-DF402F852CFCQ34635153-448FD2D2-7018-4599-9F73-4AF03A7AC102Q34854093-079B7CDC-FF1C-42D1-9353-CC07FFE8FA95Q36589372-AC58605F-D627-4E84-90CC-8502D12E0B70Q37628055-938F9A2C-6EE9-4951-97EC-44D01C4610E1Q37822920-D9332E1E-C444-4B44-A65C-31970FA070F1Q38090928-9E797C9B-9946-43CB-9393-BA08EC23FD68Q38161548-4D447B03-8676-4A6D-A93F-6AB51B0B7B16Q38234563-685CD9CC-B732-420B-9F0F-E49CECBD1F84Q40763254-8C57D304-8CC6-4048-93F0-A1526BE690B4Q41857185-97A480C1-792D-4455-BA6C-F4712CD1B40EQ41981605-1527823C-5E3E-4E49-BBCC-CDE5F658A138Q42158670-8D8C657C-B7D1-4CEB-8113-62F44931D15CQ42481448-2E07BE62-8FE4-425B-AC20-D69773453E4DQ42917910-1CBD0B43-5303-49AE-8593-C9A0FCF48CDBQ42998593-69C4F3BB-5B9F-49D3-A514-1EAD075B8A41Q43003200-F91D038A-1A7D-490E-A00F-98139AFA9774Q43250109-A0936035-31FB-432A-B25E-D796B5A628E9Q43297643-E4F95EB9-7D6A-4FAB-ABEE-5A26D90A2E3BQ44109992-A99E3368-6B49-429D-80EF-D10DF453F94DQ44888020-118606BB-C0C4-4D80-A2FF-AA3D5D98203BQ47823940-88F9B653-1348-46CE-A04B-AAA5761D6A82Q48040198-D428C1E9-6681-4259-B842-1932DAE6DC82Q48197898-687C2863-F526-45F7-BCB8-D2BBDE636663Q48366651-0CF2A318-B4E4-471E-BCB0-B888FB92F3C1Q48462979-59BE6FC2-D3C0-404F-AC85-F6B68D8049DC
P2860
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
description
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1996
@ast
im Dezember 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1996/12/04)
@sk
vědecký článek publikovaný v roce 1996
@cs
wetenschappelijk artikel (gepubliceerd op 1996/12/04)
@nl
наукова стаття, опублікована в грудні 1996
@uk
научни чланак (објављен 1996/12/04)
@sr
name
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@ast
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@en
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@nl
type
label
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@ast
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@en
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@nl
prefLabel
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@ast
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@en
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@nl
P2093
P356
P1476
Modulation of the calpain autoproteolysis by calpastatin and phospholipids
@en
P2093
E. Melloni
F. Salamino
M. Michetti
R. Minafra
S. Pontremoli
P304
P356
10.1006/BBRC.1996.1779
P407
P577
1996-12-04T00:00:00Z