caa a22 4500 44529857X CHVBK 20180317142550.0 cr unu---uuuuu 170323e20100101xx s 000 0 eng 10.1007/s12013-009-9070-7 doi (NATIONALLICENCE)springer-10.1007/s12013-009-9070-7 Morris May Interactions and Molecular Mechanisms regulating Cell Cycle Progression, Université de Montpellier, CRBM-CNRS UMR5237, 1919 Route de Mende, IFR122, 34293, Montpellier, France aut Fluorescent Biosensors of Intracellular Targets from Genetically Encoded Reporters to Modular Polypeptide Probes [Elektronische Daten] [May Morris] With the escalation of drug discovery programmes, it has become essential to visualize and monitor biological activities in healthy and pathological cells, with high spatial and temporal resolution. To this aim, the development of probes and sensors, which can report on the levels and activities of specific intracellular targets, has become essential. Together with the discovery of the Green Fluorescent Protein (GFP), and the development of GFP-based reporters, recent advances in the synthesis of small molecule fluorescent probes, and the explosion of fluorescence-based imaging technologies, the biosensor field has witnessed a dramatic expansion of fluorescence-based reporters which can be applied to complex biological samples, living cells and tissues to probe protein/protein interactions, conformational changes and posttranslational modifications. Here, we review recent developments in the field of fluorescent biosensor technology. We describe different varieties and categories of fluorescent biosensors together with an overview of the technologies commonly employed to image biosensors in cellulo and in vivo. We discuss issues and strategies related to the choice of synthetic fluorescent probes, labelling, quenching, caging and intracellular delivery of biosensors. Finally, we provide examples of some well-characterized genetically encoded FRET reporter systems, peptide and protein biosensors and describe biosensor applications in a wide variety of fields. Humana Press Inc., 2009 Biosensor nationallicence Fluorescence nationallicence Imaging nationallicence Peptide nationallicence Enzyme nationallicence Cell cycle nationallicence CDK : Cyclin-dependent kinase nationallicence CPP : Cell-penetrating peptide nationallicence CRS : Cytoplasmic retention sequence nationallicence FACS : Fluorescence-activated cell sorting nationallicence FCS : Fluorescence correlation spectroscopy nationallicence FP : Fluorescent protein nationallicence FRET : Fluorescence resonance energy transfer nationallicence FLIM : Fuorescence life-time imaging nationallicence GFP : Green fluorescent protein nationallicence IRFP : Infra-red fluorescent protein nationallicence Mant : Methylanthraniloyl nationallicence MMP : Matrix metalloproteinase nationallicence NIRF : Near-infrared fluorescence nationallicence NLS : Nuclear localization sequence nationallicence PBD : p21-Derived binding domain nationallicence PTD : Protein transduction domain nationallicence RBD : RhoA-Binding domain nationallicence Cell Biochemistry and Biophysics Humana Press Inc 56/1(2010-01-01), 19-37 1085-9195 56:1<19 2010 56 12013 https://doi.org/10.1007/s12013-009-9070-7 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s12013-009-9070-7 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Morris May Interactions and Molecular Mechanisms regulating Cell Cycle Progression, Université de Montpellier, CRBM-CNRS UMR5237, 1919 Route de Mende, IFR122, 34293, Montpellier, France aut NATIONALLICENCE 773 0- Cell Biochemistry and Biophysics Humana Press Inc 56/1(2010-01-01), 19-37 1085-9195 56:1<19 2010 56 12013 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer