Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. - Test2 - elhamkhani - TriplyDB

Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins.

Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins.

http://www.wikidata.org/entity/Q31044872

about

Fluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular Processes Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration The integrin-actin connection, an eternal love affair The F-actin bundler α-actinin Ain1 is tailored for ring assembly and constriction during cytokinesis in fission yeast α-Actinin-4 enhances colorectal cancer cell invasion by suppressing focal adhesion maturation High-resolution quantification of focal adhesion spatiotemporal dynamics in living cells Structural basis for the phototoxicity of the fluorescent protein KillerRed Novel structures for alpha-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton Complementation and reconstitution of fluorescence from circularly permuted and truncated green fluorescent protein Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteins.Force generated by actomyosin contraction builds bridges between adhesive contacts.Regulation of local expression of cell adhesion and motility-related mRNAs in breast cancer cells by IMP1/ZBP1 Integrin-dependent force transmission to the extracellular matrix by α-actinin triggers adhesion maturation Release of cellular tension signals self-restorative ventral lamellipodia to heal barrier micro-wounds.Instantaneous inactivation of cofilin reveals its function of F-actin disassembly in lamellipodia.Optogenetic inhibition of synaptic release with chromophore-assisted light inactivation (CALI).An actomyosin-based barrier inhibits cell mixing at compartmental boundaries in Drosophila embryos.Mechanism of chromophore assisted laser inactivation employing fluorescent proteins.Multiphoton excitation-evoked chromophore-assisted laser inactivation using green fluorescent protein.Fluorophore-assisted light inactivation produces both targeted and collateral effects on N-type calcium channel modulation in rat sympathetic neurons.Vitamin E TPGS-emulsified poly(lactic-co-glycolic acid) nanoparticles for cardiovascular restenosis treatment Electron microscopic visualization of fluorescent signals in cellular compartments and organelles by means of DAB-photoconversion.Chromophore-assisted laser inactivation in cell biology.Regulation of cytoskeleton organization by sphingosine in a mouse cell model of progressive ovarian cancer.Quantification of photosensitized singlet oxygen production by a fluorescent protein.Targeted two-photon chemical apoptotic ablation of defined cell types in vivo.Programmed subcellular release for studying the dynamics of cell detachment.Controlled two-photon photodegradation of PEG hydrogels to study and manipulate subcellular interactions on soft materials Fluorescent proteins and their applications in imaging living cells and tissues.Internet-based image analysis quantifies contractile behavior of individual fibroblasts inside model tissue.Modulation of fibroblast morphology and adhesion during collagen matrix remodeling.Chromophore-assisted laser inactivation in neural development.Microscope-based techniques to study cell adhesion and migration.Shear force at the cell-matrix interface: enhanced analysis for microfabricated post array detectors.Birth, growth and elimination of a single synapse.Collective cell guidance by cooperative intercellular forces Fluorophore assisted light inactivation (FALI) of recombinant 5-HT₃A receptor constitutive internalization and function.Strain-dependent up-regulation of ephrin-B2 protein in periodontal ligament fibroblasts contributes to osteogenesis during tooth movement Light inactivation of water transport and protein-protein interactions of aquaporin-Killer Red chimeras.Growth cone travel in space and time: the cellular ensemble of cytoskeleton, adhesion, and membrane.

P2860

Q22241334-5B215BC5-B96E-40A2-9CDA-D8E9D9231B81 Q24295196-F88DD98B-AABA-4788-8B9C-8090AB4A6F55 Q24676735-1035BFE9-4C90-44A3-8C36-F421B2515698 Q27304782-9D72B182-A283-42B7-99B9-D8A9EACB96BC Q27311366-55282D42-1E73-459B-83EB-D1A9C581D1B3 Q27332337-39D4A2C6-DD32-4682-9CE3-EA1022018E72 Q27656817-E8FCEA83-99C7-4D42-8754-7816ED8C8126 Q28290880-55AA1836-A1FF-4D2B-A507-A3BCFB04AD93 Q30157400-7A4C95DD-5C5E-4E0F-AB94-513F243060BF Q30479466-9E01C575-F743-4E13-9DA9-CEF1B7BD9EBE Q30493871-64FA3A65-9DCB-4AFD-8B84-931D7F897E58 Q30504549-114187DD-5332-49C5-87F2-DE73D4FF42B8 Q30538811-9C29DEE8-989A-4608-B600-72B495E76899 Q30539318-701007BC-87D7-4CAC-8EDB-C5040CE18B7E Q30541354-B2460537-0A79-483D-8729-38420341300D Q30552422-CC2203E3-1300-4121-8274-EF55A9440BF3 Q30577822-FA714563-5A71-4925-905E-985CDB551997 Q30857852-8910DC97-323A-4B22-BA49-F4FEA7166CFC Q33217700-F6143BCD-293F-4660-8914-826C418C2B66 Q33252082-311708E7-3E69-4306-A75B-D38F5A2196E7 Q33306061-A77A6458-4FA5-4E90-9CEF-62A7BAE6F52B Q33332500-34290C9B-71FA-4FB0-8685-D8209F7FA262 Q33360530-623A5837-3773-40EF-9430-C5ECD0674FEA Q33649759-B2B2E0B5-D08C-4A41-BD8F-13BA88AEDF61 Q33791015-7B3838B5-5670-4B1D-8C12-A7B55F7E65C7 Q33883062-E2D1511A-C895-422D-B114-F505911D3547 Q33899302-46035749-7DAD-411A-8006-3715DC4AB64B Q34044799-9FF3AE1E-416A-4972-A7E6-4E054DD1F922 Q34128238-C388E537-FAC3-45BE-9629-53280F3CE7E0 Q34180955-E7EA9B95-E69C-420A-9044-9D7A2DDF66B6 Q34274449-548BB31F-DA32-4D74-983E-EE39AAF9ECB7 Q34351894-EE966ECC-3C9F-418A-BEDF-659E243224EC Q34594627-8A8DE923-11DF-4346-AA10-D9EC9E05A030 Q34686682-B4A5B71F-16DE-4A31-B4F9-24EB67C53E5B Q35056491-38F10DAB-47A2-4511-B0D5-27937908879B Q35103305-9568A8DB-D41D-4894-B8C8-DE1FA3F3DB1A Q35212039-9295494D-AF73-43D6-937D-6E5A5EBD04EF Q35423979-2889ABF6-0974-458A-A63A-72B56C3E45D4 Q35647380-934072DA-BC4D-4A95-BEDA-ED9EECC33D62 Q35870286-B8325E54-16BD-4B6E-8CF8-6C25D12D4369

P2860

Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins.

http://www.wikidata.org/entity/Q31044872

description

2002 nî lūn-bûn

@nan

2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

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

name

Dissecting the link between st ...... ALI with EGFP fusion proteins.

@ast

Dissecting the link between st ...... ALI with EGFP fusion proteins.

@en

type

label

Dissecting the link between st ...... ALI with EGFP fusion proteins.

@ast

Dissecting the link between st ...... ALI with EGFP fusion proteins.

@en

prefLabel

Dissecting the link between st ...... ALI with EGFP fusion proteins.

@ast

Dissecting the link between st ...... ALI with EGFP fusion proteins.

@en

P1433

Q31044872-5F68F157-38E5-450C-B87D-6E17E2D4A154

P1476

Q31044872-F1E6022F-CBE9-4F03-A909-5911B0DC7741

P2093

Q31044872-0FDF0628-81FB-43B7-8A3C-52B08A850F75

Q31044872-5247373B-373B-4D2C-92DF-DAC1B18AACCB

Q31044872-D2A29A52-F89C-4EDF-AD80-1EDF63F63F8C

Q31044872-E3F682EF-38D6-4125-8C00-8FF51F739161

P2860

Q31044872-02B7DEDC-392F-4A3D-A436-495DDB0F42CA

Q31044872-03BE630D-FCBC-41F6-ADC3-3E28F3521FE9

Q31044872-08CFBE2F-ABA1-4358-A672-74354CA813B4

Q31044872-0950F84B-E2B1-47E9-A398-6CC63900FCC8

Q31044872-1094D601-F583-40F8-AFB3-0CECDB031E40

Q31044872-19E815CF-362A-4513-8BA7-F92389EC42A4

Q31044872-1AFB15F3-3CCB-41B1-8034-DB540E0F276A

Q31044872-24CF89B5-0595-40A9-A1DC-2C62A1ED3ACD

Q31044872-307A8F8C-7AB9-47CF-8BEC-D84015FBE763

Q31044872-330640B8-4A06-48E7-93AF-4B2800ADA4FD

P2888

Q31044872-8A263D9A-73A6-46D9-AF9F-FAAE2D685F77

P304

Q31044872-D23609FC-D6F2-45D8-B78F-CBD35C5DD2EF

P31

Q31044872-424CD9C9-B129-4B29-8A65-0B7D38C3A25A

P356

Q31044872-79CD15BE-EDEC-4A70-ABC6-0EEB17963B6C

P433

Q31044872-5786FB4C-6553-453A-85F5-1C32242D78DA

P478

Q31044872-8FD61251-29ED-4EF2-A7C6-20443F964E8A

P50

Q31044872-28E0BAFC-E34C-47FD-BE87-9A5C8E8FF522

P577

Q31044872-C0CBD874-D862-40AF-990C-924A8A67A848

P6179

Q31044872-188F957C-5505-445E-87CC-5B20C56D851C

P698

Q31044872-99BBAEF1-9064-4211-A091-F10D86C05417

P356

P1433

Nature Cell Biology

P1476

Dissecting the link between st ...... CALI with EGFP fusion proteins

@en

P2093

Carol Otey

http://www.w3.org/2001/XMLSchema#string

Ken Jacobson

http://www.w3.org/2001/XMLSchema#string

Lewis Romer

http://www.w3.org/2001/XMLSchema#string

Partha Roy

http://www.w3.org/2001/XMLSchema#string

P2860

Dynamics of alpha-actinin in focal adhesions and stress fibers visualized with alpha-actinin-green fluorescent protein

An interaction between alpha-actinin and the beta 1 integrin subunit in vitro

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation

Biochemical signals and biological responses elicited by the focal adhesion kinase

Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells

Focal adhesions, contractility, and signaling

Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice

Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin

P2888

P304

286-293

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/NCB772

http://www.w3.org/2001/XMLSchema#string

P433

4

http://www.w3.org/2001/XMLSchema#string

P478

4

http://www.w3.org/2001/XMLSchema#string

P50

P577

2002-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P6179

1024266784

http://www.w3.org/2001/XMLSchema#string

P698

11912490

http://www.w3.org/2001/XMLSchema#string