about
The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosisThe major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cellsThe isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphataseThe carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivoAn alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective.Alternative splice variants of doublecortin-like kinase are differentially expressed and have different kinase activitiesCalpain-mediated cleavage of the cyclin-dependent kinase-5 activator p39 to p29Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human plateletsRole of calcium-activated neutral protease (calpain) with diet and exerciseAquaporin-2 downregulation in kidney medulla of aging rats is posttranscriptional and is abolished by water deprivationAltered expression and localization of N-myristoyltransferase in experimentally induced rat model of ischemia-reperfusionCalmodulin protects androgen receptor from calpain-mediated breakdown in prostate cancer cellsDRL1, a homolog of the yeast TOT4/KTI12 protein, has a function in meristem activity and organ growth in plants.Discrete proteolysis of neuronal calcium sensor-1 (NCS-1) by mu-calpain disrupts calcium binding.Molecular cloning and sequencing of the plasma-membrane Ca2+ pump of pig smooth muscle.The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain.Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscleRole of calmodulin-calmodulin kinase II, cAMP/protein kinase A and ERK 1/2 on Aeromonas hydrophila-induced apoptosis of head kidney macrophagesCollapsin response mediator protein-2 is a calmodulin-binding proteinOxidative stress and cytoskeletal alterations.Biomarkers of proteolytic damage following traumatic brain injury.Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-β revealed by a novel fluorescence resonance energy transfer assay.Calmodulin-binding domain of recombinant erythrocyte beta-adducin.Proteolytic processing of endogenous and recombinant beta 4 integrin subunitBiochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosinIn vivo stimulation of I kappa B phosphorylation is not sufficient to activate NF-kappa BRelationship of eukaryotic initiation factor 3 to poliovirus-induced p220 cleavage activityProgrammed autologous cleavage of platelet receptors.MAP2: a sensitive cross-linker and adjustable spacer in dendritic architecture.B-50 (GAP-43): biochemistry and functional neurochemistry of a neuron-specific phosphoprotein.Evidence That the Blood Biomarker SNTF Predicts Brain Imaging Changes and Persistent Cognitive Dysfunction in Mild TBI PatientsEffects of paraquat-induced oxidative stress on the neuronal plasma membrane Ca(2+)-ATPase.Alterations of Ca²⁺-responsive proteins within cholinergic neurons in aging and Alzheimer's disease.Calpain-1 inhibitors for selective treatment of rheumatoid arthritis: what is the future?PEST sequences do not influence substrate susceptibility to calpain proteolysis.Specific cleavage of transcription factors by the thiol protease, m-calpain.Calcium dependent interaction of calmodulin with the GlyT1 C-terminus.The SLAM family member CD84 is regulated by ADAM10 and calpain in platelets.Predictions of Cleavability of Calpain Proteolysis by Quantitative Structure-Activity Relationship Analysis Using Newly Determined Cleavage Sites and Catalytic Efficiencies of an Oligopeptide Array.Identification and characterization of PEBP as a calpain substrate.
P2860
Q22010566-8FA79502-E835-4A83-BCA5-ED9F31E5A0F3Q24311357-1583FB91-2554-42AC-A725-E9B61F14D9F2Q24318660-FA95F28E-5642-404E-8879-53968DBB2E0AQ24336430-9415B85C-CFB6-4224-80C1-2E7CE08D12FBQ24610905-DCABB8B3-ACDB-4572-81C9-6603DBE8FC94Q28205820-D1D822F0-9707-48BD-B2A2-AAF3C8CCDBB9Q28215152-ACB40072-5FC2-4718-9B9C-F4CA4DAF8D7BQ28235484-DE825A91-5AD1-420B-A9B7-0D0DB3ED457EQ28295829-AD1CDCBD-7CB0-4F8A-9F4D-9EF4547AD55BQ28574015-EF4F016F-1E2E-43FB-AEC5-3C778B2AE726Q28579837-CA9C11B8-75D2-48C9-90D3-752B549DB1C1Q30500293-96657783-1193-4BAF-A3FC-3BD144E27EE6Q33338158-C50AB653-2C17-4230-9756-5E4FD9A44B54Q33500422-2BD89397-AE7E-42D6-8A33-FDDA11132F33Q33864419-152099F4-556A-4E01-8F95-EF165D7585FFQ33876994-3C38070E-1228-4E12-98EA-528C6591D9D0Q33935953-444D6519-E5B5-485D-B768-5660FD701B17Q35157054-0CE99E29-290A-4763-B64D-77E1D148A83BQ35597378-1F1C29ED-1866-47EA-99A9-8AEF4854F719Q35656703-BE83F5EA-7E40-4FB6-B6EC-631FD8AF7C37Q35802481-AB1C1241-7BFC-43A1-83D4-86501F5915D3Q35966841-CC70693E-852F-4D7D-B53A-765FDEEE8BAEQ36242358-3E4B27B4-27CD-4854-B86C-864E1420C4B3Q36531714-5333487B-A619-4F84-B73E-D3FF8579F008Q36533238-942BDAEB-59C9-49F1-B4EF-3E871F9DB907Q36549755-BB7397B9-2607-4867-8EDD-C33BC99D2FB8Q36697427-DCBD92FD-9A2B-456B-976D-D4F06284D783Q36884408-66FB1C42-9EA4-436C-B1BA-F45860DB26A0Q36891178-BEA0762A-295B-46EC-97E1-C307BF392DCBQ37164949-453DCD6C-9054-43C5-BDDC-CBC03FA00E8BQ37317257-0B7FBEDA-7E2A-40A8-AC73-0B5A91549ADEQ37462173-B0412B02-9745-48C2-A5C9-70C8927B800FQ37652855-1334C051-03F4-4CC5-9420-91E43ACF9224Q38161548-50BAA0E1-EDD2-4AEE-BA81-B19069EC0842Q38298943-BC39BF34-9944-4EC3-ABA9-67D5BC20F96AQ38314364-4849C345-F227-4AF3-A965-EDFB29D55B37Q38962081-2AA4F9CB-7144-4DDB-9CB8-AA520D51D428Q39268482-22F599E4-83D7-46DD-ACA7-7A6364E92B6AQ39967858-CDA85570-E510-4565-AABC-B2C53F687511Q40224274-061E7A6A-2575-4FB7-8AB6-E55A043A9277
P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Calmodulin-binding proteins as calpain substrates.
@en
type
label
Calmodulin-binding proteins as calpain substrates.
@en
prefLabel
Calmodulin-binding proteins as calpain substrates.
@en
P2860
P356
P1433
P1476
Calmodulin-binding proteins as calpain substrates
@en
P2093
B D Roufogalis
P2860
P304
P356
10.1042/BJ2620693
P407
P577
1989-09-01T00:00:00Z