Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments.
about
Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filamentsCellular vimentin regulates construction of dengue virus replication complexes through interaction with NS4A proteinThe Serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein VimentinKeratin 20 serine 13 phosphorylation is a stress and intestinal goblet cell markerTorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeletonAssembling an intermediate filament network by dynamic cotranslation.Abnormal intermediate filament organization alters mitochondrial motility in giant axonal neuropathy fibroblastsVimentin is a novel anti-cancer therapeutic target; insights from in vitro and in vivo mice xenograft studiesWithaferin a alters intermediate filament organization, cell shape and behaviorPKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motilityMyospryn is a calcineurin-interacting protein that negatively modulates slow-fiber-type transformation and skeletal muscle regenerationDNA-PK target identification reveals novel links between DNA repair signaling and cytoskeletal regulationThe serine/threonine kinase 33 is present and expressed in palaeognath birds but has become a unitary pseudogene in neognaths about 100 million years agoPlasticity of intermediate filament subunits.The dynamic properties of intermediate filaments during organelle transportVimentin filaments support extension of tubulin-based microtentacles in detached breast tumor cells.Vimentin organization modulates the formation of lamellipodia.Microtubule-dependent transport of vimentin filament precursors is regulated by actin and by the concerted action of Rho- and p21-activated kinasesVimentin is involved in regulation of mitochondrial motility and membrane potential by Rac1.Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers.Stereotypical chronic lymphocytic leukemia B-cell receptors recognize survival promoting antigens on stromal cells.Proteomic and systems biology analysis of the monocyte response to Coxiella burnetii infection.Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease.Shear stress induced reorganization of the keratin intermediate filament network requires phosphorylation by protein kinase C zeta.Synovial detection and autoantibody reactivity of processed citrullinated isoforms of vimentin in inflammatory arthritides.A novel and efficient gene transfer strategy reduces glial reactivity and improves neuronal survival and axonal growth in vitro.Withaferin A targets intermediate filaments glial fibrillary acidic protein and vimentin in a model of retinal gliosisInterphase phosphorylation of lamin A.Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.Proteome analysis of human Wharton's jelly cells during in vitro expansion.Expression of peptidylarginine deiminase 4 in an alkali injury model of retinal gliosis.Top-down label-free LC-MALDI analysis of the peptidome during neural progenitor cell differentiation reveals complexity in cytoskeletal protein dynamics and identifies progenitor cell markers.Phosphorylation of a novel cytoskeletal protein (RsmP) regulates rod-shaped morphology in Corynebacterium glutamicum.Platform-independent and label-free quantitation of proteomic data using MS1 extracted ion chromatograms in skyline: application to protein acetylation and phosphorylation.Evidence that formation of vimentin mitogen-activated protein kinase (MAPK) complex mediates mast cell activation following FcεRI/CC chemokine receptor 1 cross-talk.Human mesenchymal stem cell expression program upon extended ex-vivo cultivation, as revealed by 2-DE-based quantitative proteomics.Vimentin as an integral regulator of cell adhesion and endothelial sprouting.Full-length synaptonemal complex grows continuously during meiotic prophase in budding yeastUpregulated expression of integrin α1 in mesangial cells and integrin α3 and vimentin in podocytes of Col4a3-null (Alport) miceWithaferin A effectively targets soluble vimentin in the glaucoma filtration surgical model of fibrosis.
P2860
Q24305364-E6051D81-75C4-4BC4-9EB0-FF45C8F0ECE9Q24310514-A1DAA9AE-1698-463B-8766-51B3B4FA8282Q24315125-0D4560BB-5DAA-4020-BBDD-5FD0139FDEE3Q24316577-DC4FBCF2-9FFC-494D-8FD7-CA11908DE932Q24317502-5036E9E3-8799-45D0-876F-80E4FC38EFD4Q24683808-22034DEF-A813-4090-8DD0-C9427347EA29Q27305085-A01AE98F-D7AE-4709-ACFB-5FD800F69FCEQ28473693-0A37E8D5-BF5E-4B03-B854-B163C192B84EQ28480441-3696F3AB-A645-4D29-B85D-435FDD0188F3Q28512303-AD3C2830-5C2B-4CA1-906B-113C46EEC0B8Q28512504-66D874B3-9B32-462B-AF03-F1B5F78C60FBQ28535408-E498DAD2-8CB1-4B75-A955-12B809EC1E62Q28646755-9675DAFA-5C11-46D8-BAEF-4FD1381464CCQ30479682-AEA5FF5B-79FF-4E6C-B04A-18ADB7FB616AQ30489449-06A82E04-6CCA-4BF3-BFFB-0B96111F1D4AQ30494216-2FF7EFFB-6CCB-4355-8DD4-A49B78E7790AQ30499685-B5D6B442-CE8D-4D26-AED0-580E1E1B69C0Q30581023-90D6F4ED-EFF7-43E0-BA51-A46ED679E63FQ30669131-159A5249-BE60-439D-A41D-7E496A24D6F3Q30826123-BF4EA590-2D9C-4FAA-9FE7-A235EA9A590FQ30994095-7524D997-75BB-4323-8EB4-527A10696DC3Q31130533-629630EC-C4D3-4A77-B3B5-E1C4FF0EF372Q33224260-E88463CC-241D-47A3-A853-102D9135EFBBQ33292120-DB3D3212-F212-4D1A-9516-9617EDB07CFDQ33322989-FA01E7B6-C960-45C8-880E-AAB02757D5A4Q33481640-A3E97160-7DD8-4050-BBF1-5F3AD58B12BDQ33748201-99EF1993-D881-40A8-BCB0-4EF9741DB925Q33757351-F4F0F17B-12A5-465A-A2A4-A3BD5DD76EF6Q33832679-0DA2DF9E-EA17-43C2-84A4-E17A67AEFBE9Q33842348-D71B7F10-7603-4D34-BA5F-FE46E09982C1Q33850388-DB684470-EE8B-4C52-9776-09F44475591AQ33962226-B8A6C1C0-FF3A-439D-A84F-8AC7B200E162Q34121598-AA308B4D-ADE4-4C5D-A524-CD8EA0DB1AAAQ34210429-06472B6E-3263-480A-8C44-6F8C8824F789Q34276341-D62440CF-88BC-4F48-A69D-9276233076ECQ34391664-B8F428CC-F6C6-41CB-A19B-8D7969294DF2Q34395548-045C8814-792D-4378-AFC0-1DFDB539C7F4Q34446659-424FCED6-3D2E-4EE7-9B7E-C28E34E29A2EQ34510473-34190490-F877-4D95-B1A1-E8784822924BQ34718470-683A6FBB-47DF-4B3B-9075-272FAD1008C5
P2860
Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Specific in vivo phosphorylati ...... mentin intermediate filaments.
@en
type
label
Specific in vivo phosphorylati ...... mentin intermediate filaments.
@en
prefLabel
Specific in vivo phosphorylati ...... mentin intermediate filaments.
@en
P2093
P356
P1476
Specific in vivo phosphorylati ...... mentin intermediate filaments.
@en
P2093
Amy V Trejo-Skalli
Ann-Sofi Härmälä-Braskén
John E Eriksson
Jukka Hellman
Robert D Goldman
Ying-Hao Chou
P304
P356
10.1242/JCS.00906
P407
P577
2004-02-03T00:00:00Z