Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway. - Wikidata - awgldk - TriplyDB

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

http://www.wikidata.org/entity/Q40741202

about

S1P differentially regulates migration of human ovarian cancer and human ovarian surface epithelial cells Protein kinase Calpha activates c-Src and induces podosome formation via AFAP-110 Protein kinase Czeta mediates insulin-induced glucose transport through actin remodeling in L6 muscle cells Dynamic adhesions and MARCKS in melanoma cells PI3K activation is required for PMA-directed activation of cSrc by AFAP-110.SRChing for the substrates of Src.Calponin repeats regulate actin filament stability and formation of podosomes in smooth muscle cells.Erk1/2 MAPK and caldesmon differentially regulate podosome dynamics in A7r5 vascular smooth muscle cells.Protein kinase C activation decreases peripheral actin network density and increases central nonmuscle myosin II contractility in neuronal growth cones PKC expression is regulated by dietary K intake and mediates internalization of SK channels in the CCD.CD47 surface stability is sensitive to actin disruption prior to inclusion within the band 3 macrocomplex.Regulation of ROMK (Kir1.1) channels: new mechanisms and aspects.Recovery of PEX1-Gly843Asp peroxisome dysfunction by small-molecule compounds.Importance of RhoGTPases in formation, characteristics, and functions of invadosomes.Keratin 8/18 regulation of cell stiffness-extracellular matrix interplay through modulation of Rho-mediated actin cytoskeleton dynamics.Pregnancy downregulates actin polymerization and pressure-dependent myogenic tone in ovine uterine arteries.Activation of protein kinase C-α and Src kinase increases urea transporter A1 α-2, 6 sialylation.PKCα-Mediated Signals Regulate the Motile Responses of Cochlear Outer Hair Cells Kinase-dependent activation of voltage-gated Ca2+ channels by ET-1 in pulmonary arterial myocytes during chronic hypoxia.Melatonin as a cytoskeletal modulator: implications for cell physiology and disease.Pseudomonas aeruginosa Activates PKC-Alpha to Invade Middle Ear Epithelial Cells.Regulation of L-type calcium channel sparklet activity by c-Src and PKC-α.Suppressive effect of orthovanadate on hepatic stellate cell activation and liver fibrosis in rats.Activity-dependent structural and functional plasticity of astrocyte-neuron interactions.The NADPH oxidase inhibitor diphenyleneiodonium is also a potent inhibitor of cholinesterases and the internal Ca(2+) pump.Angiotensin II stimulates basolateral 50-pS K channels in the thick ascending limb.Concise review: Mechanotransduction via p190RhoGAP regulates a switch between cardiomyogenic and endothelial lineages in adult cardiac progenitors.Dynamics of Gαq-protein-p63RhoGEF interaction and its regulation by RGS2.Protein kinase C Signaling in Adenoviral Infection.SRC-induced disintegration of adherens junctions of madin-darby canine kidney cells is dependent on endocytosis of cadherin and antagonized by Tiam-1.Melatonin inhibits granulocyte adhesion to ICAM via MT3/QR2 and MT2 receptors.Central role of protein kinase Cepsilon in constitutive activation of ERK1/2 and Rac1 in the malignant cells of hairy cell leukemia.Syndecan-4 regulates localization, activity and stability of protein kinase C-alpha."RACK"-ing up the effectors: Receptor for activated C kinase acts downstream of Rac GTPase signaling in growth cone outgrowth.Protein kinase C delta induces Src kinase activity via activation of the protein tyrosine phosphatase PTP alpha.Phosphorylated HSP27 essential for acetylcholine-induced association of RhoA with PKCalpha.Mechanical strain inhibits airway smooth muscle gene transcription via protein kinase C signaling.A Boolean network of the crosstalk between IGF and Wnt signaling in aging satellite cells.Calcium channel and glutamate receptor activities regulate actin organization in salamander retinal neurons.

P2860

Q24646539-F8A071BE-5DDF-40F6-AB92-85BFEAE3DA21 Q28391904-9BFE27B1-1D94-4B80-9E7A-BD87D79A2B05 Q28565306-D8198306-AB16-4BAA-8ED0-16E4B23019EA Q28579253-746071E6-A974-411C-88DB-97096CBE0E1E Q30158027-766089E0-01F0-41C5-B470-18E8D7DC62D1 Q30457060-928EB215-D3F6-4693-BC3A-7F1C44B91499 Q30479883-FC0FFFE8-71A6-4F69-9A4C-A3D987FA64C3 Q30480258-8F581FDE-0DE9-486E-86E6-AEF6C878E814 Q30547068-E9ED35F7-73B7-42D2-97F4-2E97BDFEEE9E Q33655444-0474C9E4-8559-45FB-995F-6D2B565B397A Q33714963-58B5CD0F-A29D-488F-B2B4-B5B7B99782D0 Q33723819-7939DB06-9FDA-496A-AEA9-66388239B6D1 Q33777739-4AA1C900-BA2F-4862-AA6E-B0DFFC5E45E6 Q33968821-3059B40F-E9CC-47A8-961E-69B49473CE79 Q34299746-32B77237-BB0D-4B0E-81F6-F17BF425E171 Q34401687-DEF1B9F8-37C3-466A-B60D-5926038F1233 Q35228540-A92AC94C-66D7-479E-B4CF-F7C766E98138 Q35578843-337A27F6-BAB8-46E4-AC8E-A6C7AF62AFD0 Q35994822-925233CC-86EC-4185-A0C9-1AF1116D8D13 Q36325041-B4B7E7E4-B786-4C00-874A-F672B9C12E0E Q36650036-CA2D2B04-B3CC-44A8-88BF-D00375C5E299 Q37142360-25B00BE1-A7C9-4CC0-BA6C-745DF1C7F1E6 Q37150782-434A8CC6-3526-4646-AC68-298CAF2CF570 Q37216071-252E566C-0823-4067-9AA6-8415507C1EAE Q37395911-1FAD7162-72AE-4525-9906-02D3644DD671 Q37629179-1C47A01F-BCD5-4B98-AE73-958425C2A84C Q38202900-7F1A5FBD-1E2E-4BCA-B956-49EA70A3037A Q38310704-083458B5-2C82-4C41-9E83-580D5DA64AEC Q40517696-34ADF86D-4C30-48D8-9BC7-115CE66C0316 Q40604733-642C38E7-AA44-4E4D-9B5A-A42038546F7F Q41192507-1EE8F63C-A7BC-4A4E-A68F-B669AE539BEE Q41916859-2C6A3645-6CF5-4385-B31C-5BFE5E01CB4C Q42156901-6AC96FDB-8960-4D4C-9886-A5880965C5B7 Q42760738-2EB1D0FA-B016-4E16-BF91-2589205484CC Q44491461-4CA0F677-D97E-4661-B23B-537B3FF08513 Q44639151-5FCDE32B-1F41-4B33-8AF9-4BB1E7777C34 Q47194220-7AE2A345-69F2-4F2C-BA8C-91825EBBDEA4 Q51758439-8997FBAA-ACB2-4A04-A828-5088E1C81EB6 Q52571480-AB650ACC-586B-4FBA-AA38-5F6A151ED649

P2860

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

http://www.wikidata.org/entity/Q40741202

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

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

@en

type

label

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

@en

prefLabel

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

@en

P1433

Q40741202-26605C3F-B796-48CE-8A89-FFC90730758F

P1476

Q40741202-700E3D3E-7461-4ABC-AC1E-EE02A803E769

P2093

Q40741202-01C2422B-A338-40A3-AAC3-670A8535569E

Q40741202-842A7ED0-0F7E-4882-A1BA-90AEB14F9D4B

Q40741202-F0736E97-561A-48A7-9C7B-FCDFA4721FC0

P2860

Q40741202-04527743-42C8-44F4-A148-78DE5F6D551F

Q40741202-047EE83C-ADEC-4AE8-B0F2-35965C21B939

Q40741202-05BB5CEB-2CB0-4C43-BA4D-8257D87C51D6

Q40741202-084D4C20-4B14-4D41-A5E1-6910688366F1

Q40741202-08C0DBB1-2F8D-4FCD-BB94-B85EEA177EFD

Q40741202-14D4F15D-524E-4496-9CF5-267FB44C570A

Q40741202-2BE44109-4F34-4060-85FC-85F8D2CC10DF

Q40741202-3404C94C-6BFC-46CF-BECA-7C66616A2553

Q40741202-3766D240-DD7A-491D-840B-78F298D4CFDC

Q40741202-386ACA4B-5157-4FFE-9C28-E4EFA60C3F3A

P304

Q40741202-530F8FD4-D597-4805-9FC4-BA79B9B81890

P31

Q40741202-307684AB-EEAE-40C0-9034-CDEE953481A4

P356

Q40741202-26495977-C495-457F-A713-EFE394AA14EE

P407

Q40741202-2C9FAE04-B31F-418B-823F-CA750DFD9F6C

P433

Q40741202-878C7C96-5B58-48BA-8214-B08DD327436E

P478

Q40741202-4B76DCD8-4853-48EE-8330-11DA2A657DD1

P50

Q40741202-05475E7C-7AA7-4DC6-A865-7747B2924EFC

Q40741202-FD4EEB6F-7BE0-4A41-A62F-960EFC7105D2

P577

Q40741202-CC89D142-F2E7-451B-B638-478D710C7E69

P698

Q40741202-C08A263E-BE46-4911-821A-DCFD9B45A432

P356

P1433

Journal of Biological Chemistry

P1476

Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway.

@en

P2093

Dominique Brandt

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

Mario Gimona

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

Meike Hillmann

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

P2860

A phosphotyrosine displacement mechanism for activation of Src by PTPalpha

The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1

Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases

RasGRP, a Ras guanyl nucleotide- releasing protein with calcium- and diacylglycerol-binding motifs

Phorbol esters and related analogs regulate the subcellular localization of beta 2-chimaerin, a non-protein kinase C phorbol ester receptor

Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion

Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility

The receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane

p190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation

Requirement for protein kinase C theta for cell cycle progression and formation of actin stress fibers and filopodia in vascular endothelial cells

P304

20903-20910

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

P31

scholarly article

P356

10.1074/JBC.M200946200

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

P407

P433

23

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

P478

277

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

P50

P577

2002-03-29T00:00:00Z

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

P698

11925438

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