Fully quantified spectral imaging reveals in vivo membrane protein interactions.
about
VEGFR-2 conformational switch in response to ligand binding.Intracellular Domain Contacts Contribute to Ecadherin Constitutive Dimerization in the Plasma Membrane.Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.Understanding the FRET Signatures of Interacting Membrane Proteins.Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination.Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles.A small peptide promotes EphA2 kinase-dependent signaling by stabilizing EphA2 dimers.Quaternary structures of opsin in live cells revealed by FRET spectrometry.Cooperative interactions between VEGFR2 extracellular Ig-like subdomains ensure VEGFR2 dimerization.Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells.Carbonic Anhydrases Function in Anther Cell Differentiation Downstream of the Receptor-Like Kinase EMS1.A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors.The SAM domain inhibits EphA2 interactions in the plasma membrane.Immunoglobulin-like domain 4-mediated ligand-independent dimerization triggers VEGFR-2 activation in HUVECs and VEGFR2-positive breast cancer cells.The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
P2860
Q36791927-24139F23-3D12-40AB-9557-40B2CD8E84E9Q38702139-1FBE8C83-6769-4C0E-A125-9ED544F347F6Q38797027-B969B1B5-DE1E-45DE-B0F7-55EBCC011562Q38966553-A0D32B2F-7DF6-4698-B8F6-013BAF8ECDE3Q39128587-548384AE-2229-4D4F-9661-1674F666AF6DQ39867428-869238D6-8235-4CAB-AAD7-2C3105441643Q41867076-66468204-3694-4915-86BC-C75B9734AED7Q42723814-79D3D00A-B182-49DC-BA1F-5D248F1FA3B7Q47746275-DA3319BD-631E-46F4-977F-FDBC24710E88Q47892855-8E4D381F-A732-4882-BFF3-FDF2B530E697Q48124748-56310408-9C01-47DE-BF85-D3D2DE83F278Q50293429-0B8EA908-41C4-471F-B15E-1DD80B9493B8Q51123807-100AF295-FBD3-47C7-91C8-28B25DC2BAFEQ52700516-517B1822-CE4C-4ACB-B71F-A87D23EC953CQ57147941-FD7BA17B-7C40-483B-9057-D0BCD5EE1A08
P2860
Fully quantified spectral imaging reveals in vivo membrane protein interactions.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Fully quantified spectral imaging reveals in vivo membrane protein interactions.
@en
type
label
Fully quantified spectral imaging reveals in vivo membrane protein interactions.
@en
prefLabel
Fully quantified spectral imaging reveals in vivo membrane protein interactions.
@en
P2093
P2860
P356
P1433
P1476
Fully quantified spectral imaging reveals in vivo membrane protein interactions.
@en
P2093
Christopher King
Michael Stoneman
Valerica Raicu
P2860
P304
P356
10.1039/C5IB00202H
P577
2016-01-20T00:00:00Z