利用荧光共振能量转移（FRET）和荧光寿命成像显微镜（FLIM）研究内耳蛋白质-蛋白质相互作用。
Studying inner ear protein-protein interactions using FRET and FLIM.
作者信息
Hallworth Richard, Currall Benjamin, Nichols Michael G, Wu Xudong, Zuo Jian
机构信息
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68178, USA.
出版信息
Brain Res. 2006 May 26;1091(1):122-31. doi: 10.1016/j.brainres.2006.02.076. Epub 2006 Apr 13.
Abstract
Molecular genetic studies of the inner ear have recently revealed a large number of previously undescribed proteins, but their functions remain unclear. Optical methods such as FRET and FLIM are just beginning to be applied to the study of functional interactions between novel inner ear proteins. This review discusses the various methods for employing FRET and FLIM in protein-protein interaction studies, their advantages and pitfalls, with examples drawn from inner ear studies.
摘要
内耳的分子遗传学研究最近发现了大量以前未被描述的蛋白质，但其功能仍不清楚。诸如荧光共振能量转移（FRET）和荧光寿命成像（FLIM）等光学方法刚刚开始应用于新型内耳蛋白质之间功能相互作用的研究。本文综述了在蛋白质-蛋白质相互作用研究中应用FRET和FLIM的各种方法、它们的优点和缺陷，并以内耳研究为例进行说明。
相似文献
1
Studying inner ear protein-protein interactions using FRET and FLIM.利用荧光共振能量转移（FRET）和荧光寿命成像显微镜（FLIM）研究内耳蛋白质-蛋白质相互作用。
Brain Res. 2006 May 26;1091(1):122-31. doi: 10.1016/j.brainres.2006.02.076. Epub 2006 Apr 13.
2
Assessment of prestin self-association using fluorescence resonance energy transfer.利用荧光共振能量转移评估预应力蛋白的自缔合。
Brain Res. 2006 May 26;1091(1):140-50. doi: 10.1016/j.brainres.2006.02.084. Epub 2006 Apr 13.
3
Imaging protein molecules using FRET and FLIM microscopy.利用荧光共振能量转移（FRET）和荧光寿命成像显微镜（FLIM）对蛋白质分子进行成像。
Curr Opin Biotechnol. 2005 Feb;16(1):19-27. doi: 10.1016/j.copbio.2004.12.002.
4
Investigating Plant Protein-Protein Interactions Using FRET-FLIM with a Focus on the Actin Cytoskeleton.利用 FRET-FLIM 研究植物蛋白-蛋白相互作用，重点关注肌动蛋白细胞骨架。
Methods Mol Biol. 2023;2604:353-366. doi: 10.1007/978-1-0716-2867-6_29.
5
The use of FLIM-FRET for the detection of mitochondria-associated protein interactions.使用荧光寿命成像-荧光共振能量转移技术检测线粒体相关蛋白相互作用。
Methods Mol Biol. 2015;1264:395-419. doi: 10.1007/978-1-4939-2257-4_34.
6
Rapid Imaging of BCL-2 Family Interactions in Live Cells Using FLIM-FRET.使用荧光寿命成像-荧光共振能量转移技术对活细胞中BCL-2家族相互作用进行快速成像。
Methods Mol Biol. 2019;1877:305-335. doi: 10.1007/978-1-4939-8861-7_19.
7
ShadowY: a dark yellow fluorescent protein for FLIM-based FRET measurement.ShadowY：一种用于基于荧光寿命成像的荧光共振能量转移（FRET）测量的暗黄色荧光蛋白。
Sci Rep. 2017 Jul 28;7(1):6791. doi: 10.1038/s41598-017-07002-4.
8
In Vivo Interaction Studies by Measuring Förster Resonance Energy Transfer Through Fluorescence Lifetime Imaging Microscopy (FRET/FLIM).通过荧光寿命成像显微镜（FRET/FLIM）测量Förster共振能量转移进行的体内相互作用研究。
Methods Mol Biol. 2017;1662:159-170. doi: 10.1007/978-1-4939-7262-3_14.
9
Measuring protein interactions using Förster resonance energy transfer and fluorescence lifetime imaging microscopy.使用Förster共振能量转移和荧光寿命成像显微镜测量蛋白质相互作用。
Methods. 2014 Mar 15;66(2):200-7. doi: 10.1016/j.ymeth.2013.06.017. Epub 2013 Jun 24.
10
FLIM FRET technology for drug discovery: automated multiwell-plate high-content analysis, multiplexed readouts and application in situ.用于药物发现的 FLIM FRET 技术：自动化多孔板高内涵分析、多重读出以及在体应用。
Chemphyschem. 2011 Feb 25;12(3):609-26. doi: 10.1002/cphc.201000874. Epub 2011 Feb 17.
引用本文的文献
1
Large Scale Chemical Cross-linking Mass Spectrometry Perspectives.大规模化学交联质谱分析展望
J Proteomics Bioinform. 2013 Feb 8;6(Suppl 2):001. doi: 10.4172/jpb.S2-001.
2
Interferon-inducible protein Mx1 inhibits influenza virus by interfering with functional viral ribonucleoprotein complex assembly.Mx1 干扰素诱导蛋白通过干扰功能性病毒核糖核蛋白复合物的组装来抑制流感病毒。
J Virol. 2012 Dec;86(24):13445-55. doi: 10.1128/JVI.01682-12. Epub 2012 Sep 26.
3
Going deeper than microscopy: the optical imaging frontier in biology.超越显微镜：生物学中的光学成像前沿。
Nat Methods. 2010 Aug;7(8):603-14. doi: 10.1038/nmeth.1483. Epub 2010 Jul 30.
4
Auditory proteomics: methods, accomplishments and challenges.听觉蛋白质组学：方法、成就与挑战。
Brain Res. 2009 Jun 24;1277:24-36. doi: 10.1016/j.brainres.2009.02.026. Epub 2009 Feb 24.
本文引用的文献
1
Advances in fluorescence imaging with quantum dot bio-probes.量子点生物探针荧光成像的进展
Biomaterials. 2006 Mar;27(9):1679-87. doi: 10.1016/j.biomaterials.2005.11.018. Epub 2005 Nov 28.
2
N-terminal-mediated homomultimerization of prestin, the outer hair cell motor protein.外毛细胞运动蛋白prestin的N端介导的同源多聚化
Biophys J. 2005 Nov;89(5):3345-52. doi: 10.1529/biophysj.105.068759. Epub 2005 Aug 19.
3
Fluorescence lifetime imaging microscopy (FLIM).荧光寿命成像显微镜（FLIM）。
Adv Biochem Eng Biotechnol. 2005;95:143-75. doi: 10.1007/b102213.
4
Have we found the tip link, transduction channel, and gating spring of the hair cell?我们找到毛细胞的纤毛连接、转导通道和门控弹簧了吗？
Curr Opin Neurobiol. 2005 Aug;15(4):389-96. doi: 10.1016/j.conb.2005.06.007.
5
Proteomic analysis of a eukaryotic cilium.真核生物纤毛的蛋白质组学分析。
J Cell Biol. 2005 Jul 4;170(1):103-13. doi: 10.1083/jcb.200504008.
6
Imaging protein molecules using FRET and FLIM microscopy.利用荧光共振能量转移（FRET）和荧光寿命成像显微镜（FLIM）对蛋白质分子进行成像。
Curr Opin Biotechnol. 2005 Feb;16(1):19-27. doi: 10.1016/j.copbio.2004.12.002.
7
Quantum dots for live cells, in vivo imaging, and diagnostics.用于活细胞、体内成像和诊断的量子点。
Science. 2005 Jan 28;307(5709):538-44. doi: 10.1126/science.1104274.
8
Interactions in the network of Usher syndrome type 1 proteins.1型Usher综合征蛋白网络中的相互作用。
Hum Mol Genet. 2005 Feb 1;14(3):347-56. doi: 10.1093/hmg/ddi031. Epub 2004 Dec 8.
9
Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions.用于定位膜受体 - 激酶相互作用的EGFP - mRFP1荧光共振能量转移对的多光子荧光寿命成像定量分析
Biophys J. 2005 Feb;88(2):1224-37. doi: 10.1529/biophysj.104.050153. Epub 2004 Nov 5.
10
TRPA1 is a candidate for the mechanosensitive transduction channel of vertebrate hair cells.瞬时受体电位锚蛋白1（TRPA1）是脊椎动物毛细胞机械敏感转导通道的一个候选者。
Nature. 2004 Dec 9;432(7018):723-30. doi: 10.1038/nature03066. Epub 2004 Oct 13.
Zotero 插件