Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions.
about
Understanding FRET as a research tool for cellular studiesAutomated selection of regions of interest for intensity-based FRET analysis of transferrin endocytic trafficking in normal vs. cancer cellsFörster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells.Progressive accumulation of activated ERK2 within highly stable ORF45-containing nuclear complexes promotes lytic gammaherpesvirus infectionFRET microscopy in 2010: the legacy of Theodor Förster on the 100th anniversary of his birthInvestigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopyThree-color spectral FRET microscopy localizes three interacting proteins in living cellsLipin proteins form homo- and hetero-oligomersCharacterization of an orange acceptor fluorescent protein for sensitized spectral fluorescence resonance energy transfer microscopy using a white-light laser.Additional correction for energy transfer efficiency calculation in filter-based Forster resonance energy transfer microscopy for more accurate resultsCharacterization of an improved donor fluorescent protein for Forster resonance energy transfer microscopy.Förster resonance energy transfer photoacoustic microscopyVisualisation of PCNA monoubiquitination in vivo by single pass spectral imaging FRET microscopy.Comparison between whole distribution- and average-based approaches to the determination of fluorescence resonance energy transfer efficiency in ensembles of proteins in living cellsLigase detection reaction generation of reverse molecular beacons for near real-time analysis of bacterial pathogens using single-pair fluorescence resonance energy transfer and a cyclic olefin copolymer microfluidic chip.FRET characterisation for cross-bridge dynamics in single-skinned rigor muscle fibres.Partial acceptor photobleaching-based quantitative FRET method completely overcoming emission spectral crosstalks.Ma-PbFRET: multiple acceptors FRET measurement based on partial acceptor photobleaching.Assessing FRET using spectral techniques.Quantitative FRET measurement using emission-spectral unmixing with independent excitation crosstalk correction.NKX2-5 mutations causative for congenital heart disease retain functionality and are directed to hundreds of targets.Wide-field microscopic FRET imaging using simultaneous spectral unmixing of excitation and emission spectra.Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cellsNesprin-2G, a Component of the Nuclear LINC Complex, Is Subject to Myosin-Dependent Tension.Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt.Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells.FRET spectrometry: a new tool for the determination of protein quaternary structure in living cells.Quantum dots in cell biologyA Protocol for Using Förster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex.Quantifying macromolecular interactions in living cells using FRET two-hybrid assays.SensorFRET: A Standardless Approach to Measuring Pixel-based Spectral Bleed-through and FRET Efficiency using Spectral Imaging.Multichannel wide-field microscopic FRET imaging based on simultaneous spectral unmixing of excitation and emission spectra.Quantification of protein interaction in living cells by two-photon spectral imaging with fluorescent protein fluorescence resonance energy transfer pair devoid of acceptor bleed-through.Determination of supramolecular structure and spatial distribution of protein complexes in living cells
P2860
Q28088633-06C83CEA-84E3-4789-8EDF-7C8864597A6DQ30407485-58534CC6-5CE1-4776-8CBB-08353525356DQ30410957-0A26E631-56D4-4F18-974E-9084C9EC191CQ30413848-93D12EB0-E636-4B07-BEFB-BB27F5A4A7BBQ30425496-25B2E660-8CE9-40E8-823F-0C38A0680960Q30428161-762D6289-9C26-44B2-B271-BF73BAF7F14FQ30431100-995695DF-B230-44DA-8997-7B34C536B1C5Q30431845-6C7449DA-AB52-47E2-94AF-540AA120A1A9Q30434786-80B73077-B149-4EAC-9753-94F84BAD0900Q30436110-FB6E904A-306F-48CC-AAB2-A1D923842358Q30441360-59B6ACC4-0E19-4F29-8F60-F0C8F1F8CFF3Q30451121-FBE73BB6-449C-47F9-BDB1-9832C5BA0C24Q33528989-F347BBDA-CCC6-4625-A546-424793247994Q33581599-BB509A28-2649-4862-94D9-C1121889E574Q33736943-4A0D4A9A-D98C-4C38-AFC4-43C1901919C7Q34398378-7787BD82-B16D-4682-9D52-787E63638E37Q34425759-EA2B1269-0A79-4396-B45D-C770E2F5EBC6Q34561247-FFC258F4-1969-4CE0-99A9-B7DBCC8400D5Q35219413-F4EDB611-FBDD-4010-A3E4-7E34EF10ED9CQ35375506-4FD483A5-B086-4F96-8D42-AF7092820AA1Q35992694-2D953708-7226-4C65-9FDB-397D38312094Q36076002-B5BA0B5D-42BF-4209-82E5-ED3A07706B77Q36453119-78A4A8BA-4209-45D3-A3AC-C8CB36DFBB3CQ36724244-8DF85775-3ACC-4FB4-ADCC-110941DD3BD7Q37131524-35BE0DCA-ED9F-4EBA-B053-AB0E87FB794DQ37261574-087A2EAE-DEC6-48AE-A05C-7D61E90CB94DQ37299744-796A0A8D-7D29-41F9-BDB5-1E03B27B35ABQ37850214-50F4A98A-0000-4E0E-9CED-A1A1C1A330F1Q38817379-FC486439-2C3A-446E-8A8F-87EEA7309397Q39199394-E5CD975B-7615-4E75-81B3-C7BD14441194Q45073059-5A3E5C8F-F531-4EA4-98D3-996D229A5DA3Q48056894-98BCC69F-0BD7-4F30-B019-A7D94534E37DQ50507967-C94C6253-6BE8-42DA-9AD0-EBBB2D8AEC15Q56336641-A9AACDA9-4B97-46F1-B035-7A37D5E4638D
P2860
Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions.
description
2007 nî lūn-bûn
@nan
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Characterization of spectral F ...... nuclear protein interactions.
@ast
Characterization of spectral F ...... nuclear protein interactions.
@en
type
label
Characterization of spectral F ...... nuclear protein interactions.
@ast
Characterization of spectral F ...... nuclear protein interactions.
@en
prefLabel
Characterization of spectral F ...... nuclear protein interactions.
@ast
Characterization of spectral F ...... nuclear protein interactions.
@en
P2093
P2860
P1476
Characterization of spectral F ...... nuclear protein interactions.
@en
P2093
Ammasi Periasamy
Joshua P Mauldin
Richard N Day
P2860
P304
P356
10.1111/J.1365-2818.2007.01838.X
P577
2007-11-01T00:00:00Z