Results 31 to 40 of about 634,170 (178)

Chimeric Microbial Rhodopsins for Optical Activation of Gs-Proteins [PDF]

Biophysics and Physicobiology, 2017
Hideki Kandori, Yoshinori Shichida, Keiichi Inoue   +2 more
exaly   +2 more sources

Microbial Rhodopsins as Multi-functional Photoreactive Membrane Proteins for Optogenetics [PDF]

, 2021
In life science research, methods to control biological activities with stimuli such as light, heat, pressure and chemicals have been widely utilized to understand their molecular mechanisms.
Nakao, Shin, Sudo, Yuki, Kojima, Keiichi
core   +2 more sources

CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments. [PDF]

Sci Adv
Microbial rhodopsins are omnipresent on Earth, however the vast majority of them remain uncharacterized. Here we describe a new rhodopsin clade from cold-adapted organisms and cold environments, such as glaciers, denoted as CryoRhodopsins (CryoRs).
Lamm GHU, Marin E, Alekseev A, Schellbach AV, Stetsenko A, Haro-Moreno JM, Bourenkov G, Borshchevskiy V, Asido M, Agthe M, Engilberge S, Rose SL, Caramello N, Royant A, Schneider TR, Bateman A, Mager T, Moser T, Rodriguez-Valera F, Wachtveitl J, Guskov A, Kovalev K.   +21 more
europepmc   +3 more sources

Global abundance of microbial rhodopsins [PDF]

The ISME Journal, 2012
Abstract Photochemical reaction centers and rhodopsins are the only phototrophic mechanisms known to have evolved on Earth. The minimal cost of bearing a rhodopsin-based phototrophic mechanism in comparison to maintaining a photochemical reaction center suggests that rhodopsin is the more abundant of the two. We tested this hypothesis by
Omri M, Finkel, Oded, Béjà, Shimshon, Belkin   +2 more
openaire   +2 more sources

Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization

Scientific Reports, 2021
Microbial rhodopsins are photoswitchable seven-transmembrane proteins that are widely distributed in three domains of life, archaea, bacteria and eukarya.
Masuzu Kikuchi, Keiichi Kojima, Shin Nakao, Susumu Yoshizawa, Shiho Kawanishi, Atsushi Shibukawa, Takashi Kikukawa, Yuki Sudo   +7 more
doaj   +1 more source

Electronic Couplings and Electrostatic Interactions Behind the Light Absorption of Retinal Proteins

Frontiers in Molecular Biosciences, 2021
The photo-functional chromophore retinal exhibits a wide variety of optical absorption properties depending on its intermolecular interactions with surrounding proteins and other chromophores.
Kazuhiro J. Fujimoto, Kazuhiro J. Fujimoto   +1 more
doaj   +1 more source

E. coli Expression and Purification of Microbial and Viral Rhodopsins

, 2022
Microbial rhodopsins have become an indispensable tool for neurobiology. Of thousands of identified microbial rhodopsins, a minute fraction has been studied so far and they have shown remarkable functional diversity suggesting more great promises that ...
Bratanov, Dmitry, Taras Balandin, Gordeliy, Valentin, Dmitry Bratanov, Balandin, Taras, Alekseev, Alexey, Kirill Kovalev, Kovalev, Kirill, Dmytro Volkov, Volkov, Dmytro, Valentin Gordeliy, Alexey Alekseev   +11 more
core   +1 more source

Chimeric proton-pumping rhodopsins containing the cytoplasmic loop of bovine rhodopsin. [PDF]

PLoS ONE, 2014
G-protein-coupled receptors (GPCRs) transmit stimuli to intracellular signaling systems. Rhodopsin (Rh), which is a prototypical GPCR, possesses an 11-cis retinal.
Kengo Sasaki, Takahiro Yamashita, Kazuho Yoshida, Keiichi Inoue, Yoshinori Shichida, Hideki Kandori   +5 more
doaj   +1 more source

Proton-transporting heliorhodopsins from marine giant viruses

eLife, 2022
Rhodopsins convert light into signals and energy in animals and microbes. Heliorhodopsins (HeRs), a recently discovered new rhodopsin family, are widely present in archaea, bacteria, unicellular eukaryotes, and giant viruses, but their function remains ...
Shoko Hososhima, Ritsu Mizutori, Rei Abe-Yoshizumi, Andrey Rozenberg, Shunta Shigemura, Alina Pushkarev, Masae Konno, Kota Katayama, Keiichi Inoue, Satoshi P Tsunoda, Oded Béjà, Hideki Kandori   +11 more
doaj   +1 more source

Oligomeric states of microbial rhodopsins determined by high-speed atomic force microscopy and circular dichroic spectroscopy. [PDF]

Sci Rep, 2018
Oligomeric assembly is a common feature of membrane proteins and often relevant to their physiological functions. Determining the stoichiometry and the oligomeric state of membrane proteins in a lipid bilayer is generally challenging because of their ...
Shibata M, Inoue K, Ikeda K, Konno M, Singh M, Kataoka C, Abe-Yoshizumi R, Kandori H, Uchihashi T.   +8 more
europepmc   +2 more sources