Curated Optogenetic Publication Database

Search precisely and efficiently by using the advantage of the hand-assigned publication tags that allow you to search for papers involving a specific trait, e.g. a particular optogenetic switch or a host organism.

Qr: switch:"Dronpa"
Showing 101 - 104 of 104 results
101.

Illuminating cell signalling with optogenetic tools.

blue cyan red Cryptochromes Fluorescent proteins Phytochromes Review
Nat Rev Mol Cell Biol, 16 Jul 2014 DOI: 10.1038/nrm3837 Link to full text
Abstract: The light-based control of ion channels has been transformative for the neurosciences, but the optogenetic toolkit does not stop there. An expanding number of proteins and cellular functions have been shown to be controlled by light, and the practical considerations in deciding between reversible optogenetic systems (such as systems that use light-oxygen-voltage domains, phytochrome proteins, cryptochrome proteins and the fluorescent protein Dronpa) are well defined. The field is moving beyond proof of concept to answering real biological questions, such as how cell signalling is regulated in space and time, that were difficult or impossible to address with previous tools.
102.

Optobiology: optical control of biological processes via protein engineering.

blue cyan red UV Cryptochromes Fluorescent proteins LOV domains Phytochromes UV receptors Review
Biochem Soc Trans, 23 Sep 2013 DOI: 10.1042/bst20130150 Link to full text
Abstract: Enabling optical control over biological processes is a defining goal of the new field of optogenetics. Control of membrane voltage by natural rhodopsin family ion channels has found widespread acceptance in neuroscience, due to the fact that these natural proteins control membrane voltage without further engineering. In contrast, optical control of intracellular biological processes has been a fragmented effort, with various laboratories engineering light-responsive properties into proteins in different manners. In the present article, we review the various systems that have been developed for controlling protein functions with light based on vertebrate rhodopsins, plant photoregulatory proteins and, most recently, the photoswitchable fluorescent protein Dronpa. By allowing biology to be controlled with spatiotemporal specificity and tunable dynamics, light-controllable proteins will find applications in the understanding of cellular and organismal biology and in synthetic biology.
103.

Optogenetic tools for mammalian systems.

blue cyan red BLUF domains Cryptochromes Fluorescent proteins LOV domains Phytochromes Review
Mol Biosyst, 5 Apr 2013 DOI: 10.1039/c3mb25590e Link to full text
Abstract: Light is fundamental to life on earth. Therefore, nature has evolved a multitude of photoreceptors that sense light across all kingdoms. This natural resource provides synthetic biology with a vast pool of light-sensing components with distinct spectral properties that can be harnessed to engineer novel optogenetic tools. These devices enable control over gene expression, cell morphology and signaling pathways with superior spatiotemporal resolution and are maturing towards elaborate applications in basic research, in the production of biopharmaceuticals and in biomedicine. This article provides a summary of the recent advances in optogenetics that use light for the precise control of biological functions in mammalian cells.
104.

Optical control of protein activity by fluorescent protein domains.

cyan Dronpa145K/N Dronpa145N HEK293T HeLa in vitro NIH/3T3 Control of cytoskeleton / cell motility / cell shape
Science, 9 Nov 2012 DOI: 10.1126/science.1226854 Link to full text
Abstract: Fluorescent proteins (FPs) are widely used as optical sensors, whereas other light-absorbing domains have been used for optical control of protein localization or activity. Here, we describe light-dependent dissociation and association in a mutant of the photochromic FP Dronpa, and we used it to control protein activities with light. We created a fluorescent light-inducible protein design in which Dronpa domains are fused to both termini of an enzyme domain. In the dark, the Dronpa domains associate and cage the protein, but light induces Dronpa dissociation and activates the protein. This method enabled optical control over guanine nucleotide exchange factor and protease domains without extensive screening. Our findings extend the applications of FPs from exclusively sensing functions to also encompass optogenetic control.
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