Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport. - Wikidata - wikimedia - TriplyDB

Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport.

Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport.

http://www.wikidata.org/entity/Q42833787

about

Virtual Nuclear Envelope Breakdown and Its Regulators in Fission Yeast Meiosis Nuclear lamins and oxidative stress in cell proliferation and longevity Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae Modeling Cellular Noise Underlying Heterogeneous Cell Responses in the Epidermal Growth Factor Signaling Pathway Minireview: progress and challenges in proteomics data management, sharing, and integration Disruption of the ran system by cysteine oxidation of the nucleotide exchange factor RCC1 The interaction of Epac1 and Ran promotes Rap1 activation at the nuclear envelope.How Genetics Has Helped Piece Together the MAPK Signaling Pathway.Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation.An approach for identification of phosphoproteins using the G-electrode-loading method in two-dimensional gel electrophoresis.Phosphoproteomics identifies oncogenic Ras signaling targets and their involvement in lung adenocarcinomas.Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes.ERK as a model for systems biology of enzyme kinetics in cells.Transportin-1 and Transportin-2: protein nuclear import and beyond.Phosphorylation of nucleoporin Tpr governs its differential localization and is required for its mitotic function Monodisperse REPO4 (RE = Yb, Gd, Y) hollow microspheres covered with nanothorns as affinity probes for selectively capturing and labeling phosphopeptides.The nuclear envelope environment and its cancer connections.Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint Necrostatin-1 protects against reactive oxygen species (ROS)-induced hepatotoxicity in acetaminophen-induced acute liver failure Activation of diverse signalling pathways by oncogenic PIK3CA mutations.Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics.Nucleoporin MOS7/Nup88 contributes to plant immunity and nuclear accumulation of defense regulators.Lessons on transcriptional control from the serum response network.BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins Progress in mining the human proteome for disease applications Phosphorylation of Atg31 is required for autophagy A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells.Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Regulation of synaptic MAPK/ERK phosphorylation in the rat striatum and medial prefrontal cortex by dopamine and muscarinic acetylcholine receptors.The human Na(+)/H(+) exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2 The Nup153-Nup50 protein interface and its role in nuclear import.Amphetamine increases phosphorylation of MAPK/ERK at synaptic sites in the rat striatum and medial prefrontal cortex.GRK6 deficiency in mice causes autoimmune disease due to impaired apoptotic cell clearance.Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity.Gain-of-function mutations in transient receptor potential C6 (TRPC6) activate extracellular signal-regulated kinases 1/2 (ERK1/2)Large-scale discovery of ERK2 substrates identifies ERK-mediated transcriptional regulation by ETV3.Protein kinase D regulates positive selection of CD4(+) thymocytes through phosphorylation of SHP-1.

P2860

Q26766323-9F61B97A-7E92-4F03-ACCE-F6960432D416 Q27003105-5160C1C9-7F09-4962-91FC-72E453C0802A Q27677302-296DFB78-7565-4132-BD9E-FD0A0959C989 Q27932275-EEBDF9E1-7453-4F0C-AFBD-CB7114A9972C Q28554588-7A7811CC-8252-4159-8AE6-AE4D9EA625C9 Q28727478-EE6C2040-92E1-40F5-8FF3-09076DC3FAD7 Q30301217-5E5F4264-B65D-439C-AB5C-5EFA22300CB1 Q30433366-1E965001-6F99-497A-83E7-216D61B6199E Q33364397-9E11B15A-9DA3-4E75-B281-9EC71C1415F4 Q33521265-E29A715D-0F01-4299-AC4D-932BDC4CE1E3 Q33661520-DF3C6698-2F12-42CB-B527-6C660F208901 Q33834460-4B588365-9822-4DE7-BD5F-B28ADE36246B Q33921360-423F6C40-724B-406A-A9E3-F994A42BB71A Q34025448-F9FAAD0C-5437-4DFE-A4C9-284716987B48 Q34038931-9C06C45D-E9FD-4261-AEE5-243C294EDCB6 Q34040766-0AE82772-5492-4883-B46D-FCCB06B993A4 Q34076444-0AEA5878-B8E3-4977-BBD9-06EB48599B52 Q34126147-EDCF9C8D-C545-4D79-991D-59771AC2391C Q34254678-F0B8A7BB-F47A-4EA0-AFAC-D725CA691D56 Q34300397-D83BCB26-5A69-441D-81E5-D028213B09E8 Q34368610-06C37A0A-C865-493A-B518-8A0087FF7023 Q34397405-CE84B809-0299-4657-A031-0723A04CB710 Q34408364-7761A1A0-258D-42CA-9ABC-0B43D0B8B22A Q34468439-56FA56AE-FA2B-48BE-B2B3-5A97E4FA7CD4 Q34521532-ADC65A85-6667-4A72-863F-622368AFA55A Q34762281-03D8D878-A363-4791-B6A9-4B50A151E435 Q34991450-26C265B3-CCBD-4BFE-9010-8B5D7733F5CF Q35056154-F043AE63-B09B-4D60-9F80-05D2EC1CBC3B Q35252223-5F6B2C2D-2451-4333-B86B-1852AFF56CA0 Q35692123-588EB45F-DEED-4BED-AEED-8364B338813F Q35693224-567CC2FC-16C1-4584-A231-135078F4C7BA Q35985571-0547874F-9586-4019-BFAF-AAE51C0A6DAC Q35991347-D9511887-8085-4CE9-B742-50F81E3982E6 Q36385778-E385027E-64C4-40B4-85D0-F595942E5A9C Q36536725-CBFB1253-7E7E-49DD-AF6C-5B2D0542F4FA Q36652054-81CB888D-842F-4333-9801-3C8D6A6C9D02 Q36745305-5A8ECA44-D426-427E-9531-A5B2CBF74821 Q36947844-8362AE12-771A-4AE7-8F82-15265F1C7883 Q37189824-5DD4F498-C437-4329-ADE9-49906E979EE4 Q37315012-70E54C45-2D22-4CEE-A2C8-C89A523D5811

P2860

Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport.

http://www.wikidata.org/entity/Q42833787

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@en

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@nl

type

label

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@en

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@nl

prefLabel

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@en

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@nl

P1433

Q42833787-98064321-FA51-4A00-81FB-C488CC711F0D

P1476

Q42833787-F24B42B2-C969-49DC-87F2-4DACDE744A18

P2093

Q42833787-00D8F71D-A19A-409C-8C43-A2DD758CB06E

Q42833787-1F289E7C-5B60-419E-90F9-775F7F898592

Q42833787-24531AD1-D848-4288-B1C3-9824A9D1BD39

Q42833787-58C2D664-6276-4B51-B992-A9924B3C7A8F

Q42833787-58C89462-80EA-43F5-B9D1-62F2C3B284F8

Q42833787-8D3A5E2D-E90C-4C8B-BAEE-19903712AAEF

Q42833787-9377FA96-671F-47BD-80EA-D2FD4ECC3E76

Q42833787-990415B3-882B-48DC-8011-4C08B3A12390

Q42833787-A9602C17-E233-495E-A5D2-62221BF873EC

P2860

Q42833787-039CF210-A4F2-4B93-A571-46F055453297

Q42833787-0433B63D-F5B7-4592-9A99-EF63CB4FFA4B

Q42833787-05CB8DA3-B89C-465D-BD38-6EDCE1ECC250

Q42833787-07F9F310-C968-4B67-B17A-35F8D52D2E02

Q42833787-07FDC56E-AEA2-4FE6-BB76-B5E6BCF60BAA

Q42833787-09984419-EF9D-4C01-A4AD-545CE3D3902D

Q42833787-0A40AE70-BBA0-4A24-B031-8B9C659A8C9D

Q42833787-0BF4752F-0047-4494-AB0D-5E2D39EE8723

Q42833787-17FA8979-9519-4F20-9701-EF80D84EB6DB

Q42833787-1904D1E0-6999-47F3-8560-5D80AF75666E

P2888

Q42833787-F199AC0C-A97C-4170-BE0D-FCE797806D59

P304

Q42833787-4F8B81BF-A07B-453D-BD93-DB6C41A42656

P31

Q42833787-2C024F6A-2534-4499-88EE-772DBABC341A

P356

Q42833787-B77385D8-6C94-4697-B19E-DF6690082383

P433

Q42833787-C28CDFDE-8F4F-4A3F-8D43-AECB3E5669C1

P478

Q42833787-2DFE65C7-0E10-44F5-BA29-C76EA4909493

P577

Q42833787-660DE800-8DF1-4253-A8D8-8BC848C0A6F9

P5875

Q42833787-7F16EFAA-5C6B-4496-AA86-AFE6B5C4A88E

P698

Q42833787-43896844-A617-4F31-9BC7-2F890C820F73

P356

P1433

Nature Structural & Molecular Biology

P1476

Phosphoproteomics reveals new ...... in-mediated nuclear transport.

@en

P2093

Chizuru Aranami

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

Eisuke Nishida

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

Hidetaka Kosako

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

Hisaaki Taniguchi

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

Masato Ushiyama

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

Naoko Imamoto

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

Nozomi Yamaguchi

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

Seisuke Hattori

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

Shingo Kose

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

P2860

Current two-dimensional electrophoresis technology for proteomics

Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 subcomplex

Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage

Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

The Fas-induced apoptosis analyzed by high throughput proteome analysis

Neurofibrillary tangle-associated collapsin response mediator protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518, and Ser-522

Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs

Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import

P2888

P304

1026-1035

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

P31

scholarly article

P356

10.1038/NSMB.1656

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

P433

10

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

P478

16

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

P577

2009-09-20T00:00:00Z

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

P5875

26825203

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

P698

19767751

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