scispace - formally typeset
E

Ernst Bamberg

Researcher at Max Planck Society

Publications -  267
Citations -  26909

Ernst Bamberg is an academic researcher from Max Planck Society. The author has contributed to research in topics: Bacteriorhodopsin & Membrane. The author has an hindex of 74, co-authored 261 publications receiving 24745 citations. Previous affiliations of Ernst Bamberg include Moscow Institute of Physics and Technology & Free University of Berlin.

Papers
More filters
Journal ArticleDOI

Millisecond-timescale, genetically targeted optical control of neural activity.

TL;DR: In this paper, the authors adapted the naturally occurring algal protein Channelrhodopsin-2, a rapidly gated light-sensitive cation channel, by using lentiviral gene delivery in combination with high-speed optical switching to photostimulate mammalian neurons.
Journal ArticleDOI

Channelrhodopsin-2, a directly light-gated cation-selective membrane channel.

TL;DR: It is demonstrated by functional expression, both in oocytes of Xenopus laevis and mammalian cells, that ChR2 is a directly light-switched cation-selective ion channel, and may be used to depolarize small or large cells, simply by illumination.
Journal ArticleDOI

Multimodal fast optical interrogation of neural circuitry

TL;DR: An archaeal light-driven chloride pump from Natronomonas pharaonis is identified and developed for temporally precise optical inhibition of neural activity and forms a complete system for multimodal, high-speed, genetically targeted, all-optical interrogation of living neural circuits.
Journal Article

Multimodal fast optical interrogation of neural circuitry

TL;DR: In this paper, an archaeal light-driven chloride pump (NpHR) was developed for temporally precise optical inhibition of neural activity, allowing either knockout of single action potentials, or sustained blockade of spiking.
Journal ArticleDOI

Channelrhodopsin-1: a light-gated proton channel in green algae.

TL;DR: A complementary DNA sequence in the green alga Chlamydomonas reinhardtiithat encodes a microbial opsin-related protein, which is suggested to be Channelopsin-1, which shows homology to the light-activated proton pump bacteriorhodopsin.