Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling. - Wikidata - wikimedia - TriplyDB

Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling.

Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling.

http://www.wikidata.org/entity/Q39616171

about

Activation of ErbB2 by 2-methyl-1,4-naphthoquinone (menadione) in human keratinocytes: role of EGFR and protein tyrosine phosphatases Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment Computational modeling reveals molecular details of epidermal growth factor binding The LINK-A lncRNA activates normoxic HIF1α signalling in triple-negative breast cancer Evidence for intermolecular interactions between the intracellular domains of the arabidopsis receptor-like kinase ACR4, its homologs and the Wox5 transcription factor Gas6-axl receptor signaling is regulated by glucose in vascular smooth muscle cells Single-molecule analysis of epidermal growth factor binding on the surface of living cells.RETRACTED: The antibody zalutumumab inhibits epidermal growth factor receptor signaling by limiting intra- and intermolecular flexibility.Single-molecule imaging reveals transforming growth factor-beta-induced type II receptor dimerization.Spatio-temporal modeling of signaling protein recruitment to EGFR.Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response The SCHOOL of nature: I. Transmembrane signaling.Affecting Rhomboid-3 function causes a dilated heart in adult Drosophila.Functional characterization of wild-type and 24 CYP2D6 allelic variants on gefitinib metabolism in vitro.Mechanisms of activation of receptor tyrosine kinases: monomers or dimers.EGF receptor exposed to oxidative stress acquires abnormal phosphorylation and aberrant activated conformation that impairs canonical dimerization Asp-960/Glu-961 controls the movement of the C-terminal tail of the epidermal growth factor receptor to regulate asymmetric dimer formation.Investigating extracellular in situ EGFR structure and conformational changes using FRET microscopy.Physical basis behind achondroplasia, the most common form of human dwarfism.Kinase-mediated quasi-dimers of EGFR The tethering arm of the EGF receptor is required for negative cooperativity and signal transduction.Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1.Quantitative assays for the measurement of HER1-HER2 heterodimerization and phosphorylation in cell lines and breast tumors: applications for diagnostics and targeted drug mechanism of action Regulation of the catalytic activity of the EGF receptor.The membrane-proximal intracellular domain of the epidermal growth factor receptor underlies negative cooperativity in ligand binding.Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging.Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy.Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis.Hypoxia promotes ligand-independent EGF receptor signaling via hypoxia-inducible factor-mediated upregulation of caveolin-1 Juxtamembrane contribution to transmembrane signaling.EGF prevents the neuroendocrine differentiation of LNCaP cells induced by serum deprivation: the modulator role of PI3K/Akt Three Recombinant Engineered Antibodies against Recombinant Tags with High Affinity and Specificity Quantitation of the effect of ErbB2 on epidermal growth factor receptor binding and dimerization Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor.The Metastasis Suppressor, N-MYC Downstream-regulated Gene-1 (NDRG1), Down-regulates the ErbB Family of Receptors to Inhibit Downstream Oncogenic Signaling Pathways Intracellular activation of EGFR by fatty acid synthase dependent palmitoylation.Prediction, refinement, and persistency of transmembrane helix dimers in lipid bilayers using implicit and explicit solvent/lipid representations: microsecond molecular dynamics simulations of ErbB1/B2 and EphA1.Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry.Different Epidermal Growth Factor Receptor (EGFR) Agonists Produce Unique Signatures for the Recruitment of Downstream Signaling Proteins

P2860

Q24306579-FAA72B60-991B-4AE2-A01F-8A3DFBA6C321 Q24309071-03C4A5EF-D965-4206-8C59-F006DFDDCACD Q24814137-FC4FC297-9929-47A5-9A36-55276F7F8160 Q28118941-A07C204F-42D4-413B-A547-BABA59F1437F Q28543936-B62D9FDF-ACA6-486C-ACA4-174618FABBA1 Q28576589-300125AD-6883-480C-B331-3FCA3D520D83 Q30478014-8229C34F-9C97-4C7B-8471-53884D9CA4C1 Q30481746-E07DC9C4-CDCE-4355-8155-5263D7D4C7B4 Q30490342-1CEE9372-2AA4-4C50-9121-0D593774CD77 Q30982487-105058BA-5FBE-4ED2-86D2-0952B8841B5D Q33212570-F30B09D4-BBB1-4CF9-9668-D863C45664DE Q33351190-C16F0DA1-C75B-41D1-AC53-729BFD69AB9D Q33594430-0A1C1A0B-049C-4907-95B5-1FD26B1CD72A Q33609979-65EEB911-4378-439A-9D1E-851DCAE03F15 Q33883884-9D9868AA-FCA5-4E3F-8AAC-1D870F2F0375 Q33996985-55052C13-A045-4999-AB61-F77A977F690B Q34025360-DAB41B96-33A4-4511-8D3D-AF7A69100156 Q34133392-0B679DEC-6EAC-424F-9770-74E1B586FFAC Q34144662-0678FA53-439C-4533-B252-6F960D7DE300 Q34352792-183615C4-EB53-4C59-B5C9-EE2B6039CF3F Q34489094-7DF75C55-C372-45A3-9B00-088D9135E2AA Q34525985-F3EDD5A6-FADB-40D0-AF63-011B277D643E Q34538158-4C8A3D20-CF7B-4F29-AB10-1058BE3B3CF6 Q35559032-AEB7F3B1-A609-46C3-B441-41170F7AEE13 Q35597077-934ED666-EB75-4685-A4BF-CDD9C9405D0F Q35639911-DFB1A6F4-82FF-4C52-8BA3-7096B04C425A Q35657617-E3220052-B0AF-4480-B85E-1683A9CD8220 Q35850949-DA135ACA-5702-4887-964B-A0DBB2B3A817 Q35878699-958229D6-30D4-4E60-A9B2-F240840949CC Q35882401-B5F56CE3-FE83-43CF-9BBD-217A62866440 Q35893679-44E9EA51-7F8B-496D-8FFF-37F7EBC356F5 Q35945055-FFD25904-EBAB-4E86-BE34-C09E68C574BE Q35946289-6CB4479B-9CB2-46AE-9C5D-96A00239D81C Q36225710-5F963F58-50F4-41DA-9A1F-773EDFC8BC9B Q36368323-B582B53F-D566-41A1-9CB4-6A33C12FBCA1 Q36466104-ED4D90C3-B472-44D6-9FBB-30F1DB1BB3E2 Q36544282-BFCCD6D9-D8E0-46DA-B433-298EF9538F9C Q36569264-75FF90E1-354B-4845-B881-383B59DEF4F7 Q36588488-3A6BDF92-944E-4200-8060-C2EB2B26A5E6 Q36674591-0BE1DFD9-6B4A-449A-A08E-7AC2A97A3E19

P2860

Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling.

http://www.wikidata.org/entity/Q39616171

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

Ligand-independent dimer forma ...... ligand-induced EGFR signaling.

@en

Ligand-independent dimer formation of epidermal growth factor receptor

@nl

type

label

Ligand-independent dimer forma ...... ligand-induced EGFR signaling.

@en

Ligand-independent dimer formation of epidermal growth factor receptor

@nl

prefLabel

Ligand-independent dimer forma ...... ligand-induced EGFR signaling.

@en

Ligand-independent dimer formation of epidermal growth factor receptor

@nl

P1433

Q39616171-285646AE-47D7-4439-B794-2DEEBC42EB73

P1476

Q39616171-175EC9D6-12A0-4DED-BFDA-F5BE9DD82813

P2093

Q39616171-2EF04ADF-230C-46FB-811E-64E2A9714A53

Q39616171-41D5991B-0232-49D2-97E0-BE984A066356

Q39616171-727F48A0-A309-4898-B4B2-E72293E25095

Q39616171-7A383353-F1F9-43AE-B62E-F31D94BEA8B1

Q39616171-B45C0A60-5206-4CDB-8C0F-6839E70A9EA7

P2860

Q39616171-07757C30-08B4-4422-B3D4-D8E7CA1B6C98

Q39616171-08F7D9B0-D280-4D6A-A273-5AA120B371BB

Q39616171-0D137257-D07A-436C-ACCB-C1AB6BB5B0EA

Q39616171-1630956E-E4FD-43A4-8CA1-FB22DB6B4BF4

Q39616171-1F311136-DD03-425F-B11E-CCAFCA658DF8

Q39616171-267A4C42-6FD1-46B0-A5CB-D5694FCC964D

Q39616171-31D10257-5C11-43B6-9C42-BB44872B7814

Q39616171-33DAE1D3-F6AD-484F-A121-34C087B4B2EF

Q39616171-371F964A-80C3-45D5-9889-06B3EB35B2CD

Q39616171-3E675EC4-811B-4716-A066-895AAC75EEB2

P304

Q39616171-7135EE8B-0514-425C-B557-2D154D2E9EEC

P31

Q39616171-1CE67A71-6DFB-4E06-B425-D2A3B99E04E7

P356

Q39616171-D51BE016-A1EA-4511-9DA0-1603322D9B71

P433

Q39616171-3DFD3668-0294-4E0C-9E0B-5CDD898DBF3B

P478

Q39616171-BB89E0C2-0CEC-49BB-A067-F8BF65809A3F

P577

Q39616171-6170708C-F78D-4F79-8DE4-E502B532048F

P5875

Q39616171-F29041D4-EB7E-424F-A3B8-8C7693F19374

P698

Q39616171-24E3B880-950E-4BE5-B08E-CB8DA3AF2EAE

P932

Q39616171-EB4D532E-02F3-4BF8-9B1E-A71AD860C871

P356

P1433

Molecular Biology of the Cell

P1476

Ligand-independent dimer forma ...... ligand-induced EGFR signaling.

@en

P2093

Eisuke Mekada

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

Kailash D Sharma

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

Ryo Iwamoto

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

Tsuyoshi Takahashi

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

Xiaochun Yu

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

P2860

Structure and function of human amphiregulin: a member of the epidermal growth factor family

Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor

A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF

Epiregulin. A novel epidermal growth factor with mitogenic activity for rat primary hepatocytes

The cellular response to neuregulins is governed by complex interactions of the erbB receptor family

Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity

Receptor signaling: when dimerization is not enough.

Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.

Two EGF molecules contribute additively to stabilization of the EGFR dimer

Single-molecule imaging of EGFR signalling on the surface of living cells.

P304

2547-2557

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

P31

scholarly article

P356

10.1091/MBC.01-08-0411

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

P433

7

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

P478

13

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

P577

2002-07-01T00:00:00Z

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

P5875

11247908

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

P698

12134089

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

P932

117333

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