Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis.
about
Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosisBAG3 deficiency results in fulminant myopathy and early lethalityA novel role for microtubules in apoptotic chromatin dynamics and cellular fragmentationBacterial cell curvature through mechanical control of cell growth.The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.Intermediate filaments: a historical perspectiveCaspase proteolysis of the integrin beta4 subunit disrupts hemidesmosome assembly, promotes apoptosis, and inhibits cell migration.Upregulation of nestin protects podocytes from apoptosis induced by puromycin aminonucleoside.Expression and activation of caspase-6 in human fetal and adult tissuesIntermediate filaments control the intracellular distribution of caspases during apoptosis.Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's diseaseCoxsackievirus-induced miR-21 disrupts cardiomyocyte interactions via the downregulation of intercalated disk components.Cleavage of p53-vimentin complex enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis of rheumatoid arthritis synovial fibroblastsBcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathyUbiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophyDesminopathies: pathology and mechanisms.Serological muscle loss biomarkers: an overview of current concepts and future possibilitiesDesmin mediates TNF-alpha-induced aggregate formation and intercalated disk reorganization in heart failure.Targets of caspase-6 activity in human neurons and Alzheimer disease.Caspase cleavage of GFAP produces an assembly-compromised proteolytic fragment that promotes filament aggregation.Mutation of caspase-digestion sites in keratin 18 interferes with filament reorganization, and predisposes to hepatocyte necrosis and loss of membrane integrity.Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases.Emerging roles of apoptotic microtubules during the execution phase of apoptosis.Dantrolene improves in vitro structural changes induced by serum from Trypanosoma cruzi-infected mice.Overview of the Muscle Cytoskeleton.Viscum album agglutinin-I induces degradation of cytoskeletal proteins in leukaemia PLB-985 cells differentiated toward neutrophils: cleavage of non-muscle myosin heavy chain-IIA by caspases.The differentiation-dependent desmosomal cadherin desmoglein 1 is a novel caspase-3 target that regulates apoptosis in keratinocytes.Primary bovine skeletal muscle cells enters apoptosis rapidly via the intrinsic pathway when available oxygen is removed.Myofibril breakdown during atrophy is a delayed response requiring the transcription factor PAX4 and desmin depolymerization.The expressions of HSP70 and αB-crystallin in myocarditis associated with foot-and-mouth disease virus in lambs.Effect of ouabain on myocardial ultrastructure and cytoskeleton during the development of ventricular hypertrophy.Proteasomal degradation of caspase-6 in 17beta-estradiol-treated neurons.Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases.Dynamic Reorganization of the Cytoskeleton during Apoptosis: The Two Coffins Hypothesis.The Process of Engraftment of Myogenic Cells in Skeletal Muscles of Primates: Understanding Clinical Observations and Setting Directions in Cell Transplantation Research.Caspase-mediated Cleavage of Insulin Receptor Substrate.MRCKα is activated by caspase cleavage to assemble an apical actin ring for epithelial cell extrusion.A mutation in keratin 18 that causes caspase-digestion resistance protects homozygous transgenic mice from hepatic apoptosis and injury.Two coffins and a funeral: early or late caspase activation determines two types of apoptosis induced by DNA damaging agents.Cardiomyocyte-specific disruption of Cathepsin K protects against doxorubicin-induced cardiotoxicity.
P2860
Q24338378-EF289D7B-0025-4E50-8CC1-B948E89BBA02Q28585764-70140C31-29F2-4940-8CAD-19CC96FCE913Q30478057-B57CB38A-CA7F-47B6-A19B-080AB819971BQ30487655-93D6DB7E-5486-4616-BCD7-DCB4BAAA7B83Q30539278-757D7C0D-7290-4C18-9902-5D8F75E8D5E0Q33284286-AD7B2E9C-6DEF-454C-BEE3-A410F2E1F265Q33643674-F5A253EA-6C49-448E-9CAF-48B41239C9F2Q34032857-5A79C70B-4761-4456-A989-D6641A212606Q35050463-D5034998-0354-42D9-9116-96335231DA2BQ35083421-E21775CB-63FD-43E2-ADB7-904A4A9B9630Q35102948-4D60D128-DF16-4F69-9B03-339E1796C722Q35145377-C11B2080-3952-448F-978E-02D5DE530C24Q35221776-133DC545-EF06-4DBC-8274-9F7049983EADQ35554203-7F93D274-1E52-4721-A29C-B85CDD864EF0Q36444247-017980EC-EADD-4CF7-948D-6F00132DC129Q36503373-596596A3-B51D-40B9-A1EC-4D78D52A6D1EQ36636397-1A0384B5-5842-45A3-B796-197C5F0A2006Q36677507-B403E8A4-B288-48A8-A323-10AF53007645Q36818158-6B7C6B1C-44AE-4567-8AC0-DEB2B60722C1Q37323740-53098949-864A-413D-88AE-1DF603667110Q37674669-9985F037-99DB-4FBA-B004-4895AD46AEFCQ37784801-CD79D91E-7909-46CC-97F8-BC7A2D25CB5EQ38588842-74752D00-AFBB-4742-96C3-23E55CBF879CQ39208961-3FECAB8A-4775-4B52-AA56-A9D62DE90AF7Q39391006-4B766879-24DC-43D4-80D3-3BC7169A037DQ40101355-CDBD7F2A-5D89-44D6-A7D0-FC1B506D8F4CQ40351730-3374E486-2705-4334-805F-2235F99F3F04Q41323956-03C92023-7D81-460F-B439-A06F9921B2F5Q41943570-0BA745DF-3CBC-4A65-BCF4-E5074981C02AQ42246286-0A5B3ACA-59FB-4587-95FF-78E1BD3BDF04Q43747128-B60DC909-8B6B-44E3-9533-7AE5E5FBAD2AQ44846023-BCFED754-F626-4851-ADF6-AADB164BB8EFQ45120869-42C29304-F568-40C0-9D76-A83CFB749EAAQ47154984-126208F0-1860-4E09-88DD-9DEF9324F922Q47729696-41212DF0-0F40-4D35-A885-FF2B201A2782Q47804073-C919BB86-87CB-41F2-AB2E-AF33D0AEEBF4Q48259723-6D39FF4C-6280-4FD5-B9C2-7A233217E356Q48290523-75F21CD9-F565-4873-9021-B6667971FF28Q50221540-D98F482D-99F8-41AC-8D19-32F338BED9F6Q55265082-F251949F-C2C9-4A61-86FC-EF2EE82D6D79
P2860
Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Caspase proteolysis of desmin ...... aments and promotes apoptosis.
@en
type
label
Caspase proteolysis of desmin ...... aments and promotes apoptosis.
@en
prefLabel
Caspase proteolysis of desmin ...... aments and promotes apoptosis.
@en
P2093
P2860
P356
P1476
Caspase proteolysis of desmin ...... aments and promotes apoptosis.
@en
P2093
Marcus Trivedi
Roger Chang
Vincent L Cryns
Yassemi Capetanaki
P2860
P304
P356
10.1074/JBC.M212021200
P407
P577
2002-12-10T00:00:00Z