about
Crystal structure of a light-driven sodium pumpTransient protonation changes in channelrhodopsin-2 and their relevance to channel gatingSpectral characteristics of the photocycle of channelrhodopsin-2 and its implication for channel function.Pre-gating conformational changes in the ChETA variant of channelrhodopsin-2 monitored by nanosecond IR spectroscopy.Enlightening the photoactive site of channelrhodopsin-2 by DNP-enhanced solid-state NMR spectroscopy.Functional Green-Tuned Proteorhodopsin from Modern Stromatolites.Temporal evolution of helix hydration in a light-gated ion channel correlates with ion conductanceChannelrhodopsin-2 is a leaky proton pump.Proteorhodopsin.From Gene to Function: Cell-free Electrophysiological and Optical Analysis of Ion Pumps in Nanodiscs.Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond.Light-induced helix movements in channelrhodopsin-2.Projection structure of channelrhodopsin-2 at 6 Å resolution by electron crystallography.Tuning the primary reaction of channelrhodopsin-2 by imidazole, pH, and site-specific mutationsThe photocycle of channelrhodopsin-2: ultrafast reaction dynamics and subsequent reaction steps.High-temperature solution NMR structure of TmCsp.The DC gate in Channelrhodopsin-2: crucial hydrogen bonding interaction between C128 and D156.The retinal structure of channelrhodopsin-2 assessed by resonance Raman spectroscopy.Microbial rhodopsins in the spotlight.Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2.Conformational changes of channelrhodopsin-2.On-demand optogenetic activation of human stem-cell-derived neurons.Structural insights into ion conduction by channelrhodopsin 2.Light-induced movement of the transmembrane helix B in channelrhodopsin-2.A gene-fusion strategy for stoichiometric and co-localized expression of light-gated membrane proteins.Ultra light-sensitive and fast neuronal activation with the Ca²+-permeable channelrhodopsin CatCh.Photochemical Properties of the Red-shifted Channelrhodopsin Chrimson.Photocycle and vectorial proton transfer in a rhodopsin from the eukaryote Oxyrrhis marina.Resonance Raman and FTIR spectroscopic characterization of the closed and open states of channelrhodopsin-1.Kinetics of proton release and uptake by channelrhodopsin-2.Ultrafast Infrared Spectroscopy on Channelrhodopsin-2 Reveals Efficient Energy Transfer from the Retinal Chromophore to the ProteinCritical Role of Asp227 in the Photocycle of ProteorhodopsinStudying the stoichiometries of membrane proteins by mass spectrometry: microbial rhodopsins and a potassium ion channelSolid-state NMR analysis of the sodium pump Krokinobacter rhodopsin 2 and its H30A mutant
P50
Q27700101-2608EC33-02E6-42C6-9711-13030C306FF2Q34333935-6E7F91F4-05BD-45F8-95F3-14DAACC67B63Q34718037-D725FB2C-D198-4E61-B539-68B857F3091CQ35542160-93CEEDB1-086C-4F3D-8A58-3EE8A78787F8Q35961294-7AEE4A44-8526-4D67-A420-CC93F9D2CB5AQ36020038-AA46999D-6D8D-46E8-B266-00729A0A4C17Q36238311-437C5DF0-B62C-435A-AB52-9FED858CF676Q37282472-0A184E15-9614-49EB-9579-75831FBB33EFQ38141374-53D214C6-4F47-430E-87F9-DEB63262DB8AQ38816133-E78299CF-B582-45F7-8A92-61E2D42EA6E3Q39765113-4A81635F-61C0-4BC4-B626-ECC60023BECBQ41606821-A4D86D5F-2240-4448-9E98-C9576674C1DEQ41614755-84DC6673-B7EC-4F9A-B356-64C2D7F1C2F4Q42141136-F338DBC2-D893-43CA-AED6-AE4ADC9099E1Q42929501-FCE05E90-91BE-47A8-B090-3703D79DFA53Q43105240-33E33AFB-F411-45A1-8758-BEB00A9A0C14Q43176669-B385C258-279A-4665-8B7E-0EF2AA862BD0Q43255613-417A830E-59CC-4F09-A7AB-9FBEB6D7A2D9Q45325013-3AFEB26A-6B38-478D-B3DE-FEDA6F2402A8Q45907451-7F53BF00-47B8-498D-95A1-D598AEAB5321Q46021997-DBF1997C-41D1-4FE1-B393-17874AD669D1Q47114932-2E6B940F-E346-42FB-AEB1-999DDD2D3372Q47783696-D2C6CD4A-E793-4147-81F2-3CB92C087CE6Q47916031-49250CBB-2874-48E5-ACCD-09C0FC51C625Q48054791-41778FC0-2D47-478C-867E-078F586F916FQ48679629-218767D1-3ECE-4ADE-8CCA-FA2DC4812580Q50207381-C571418B-8E05-4963-AAAB-A623B64245C6Q50481799-09E56282-3A81-4D70-AE3A-0C672E56E9FCQ52876686-876119FB-D8C1-4FA4-ABC9-3A93F5A99E89Q52888746-13ECB747-78CB-4061-836D-8291247B7EE0Q57637146-C7E5F71E-2BCB-4AB3-A44A-11F1F8BB1D42Q57955495-36590167-CD7F-441F-8E2A-D332021AA4DAQ57955531-26911DC9-3D02-457F-8244-9BFA8B170EA2Q89026342-2B520F30-7303-4988-BCC7-423D844876A1
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Christian Bamann
@ast
Christian Bamann
@en
Christian Bamann
@es
Christian Bamann
@sl
type
label
Christian Bamann
@ast
Christian Bamann
@en
Christian Bamann
@es
Christian Bamann
@sl
prefLabel
Christian Bamann
@ast
Christian Bamann
@en
Christian Bamann
@es
Christian Bamann
@sl
P106
P1153
23092759400
P21
P31
P496
0000-0001-7473-438X