(Q43025671)

12 November 2017

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title

The structure and mechanism of the family of retinal proteins from halophilic archaea (English)

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12 November 2017

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Oesterhelt D

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12 November 2017

publication date

1 August 1998

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Current Opinion in Structural Biology

12 November 2017

published in

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12 November 2017

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12 November 2017

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12 November 2017

page(s)

489-500

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General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model

12 November 2017

cites work

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7 January 2021

Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin

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7 January 2021

Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps

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7 January 2021

Electron-crystallographic refinement of the structure of bacteriorhodopsin

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7 January 2021

Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

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7 January 2021

X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases

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7 January 2021

Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: counterion effects on the 15N shift anisotropy

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7 January 2021

Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst

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7 January 2021

Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface

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7 January 2021

Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy

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7 January 2021

D38 Is an Essential Part of the Proton Translocation Pathway in Bacteriorhodopsin†

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7 January 2021

Role of water in bacteriorhodopsin's chromophore: resonance Raman study

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7 January 2021

Time-resolved titrations of the Schiff base and of the Asp85 residue in artificial bacteriorhodopsins

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7 January 2021

Interaction of the protonated Schiff base with the peptide backbone of valine 49 and the intervening water molecule in the N photointermediate of bacteriorhodopsin

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7 January 2021

Picosecond molecular motions in bacteriorhodopsin from neutron scattering

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7 January 2021

Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering

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7 January 2021

The Predischarge Chromophore in Bacteriorhodopsin: A 15N Solid-State NMR Study of the L Photointermediate

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7 January 2021

Ultraviolet resonance Raman spectra of Trp-182 and Trp-189 in bacteriorhodopsin: novel information on the structure of Trp-182 and its steric interaction with retinal

1 reference

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7 January 2021

Threonine-89 participates in the active site of bacteriorhodopsin: evidence for a role in color regulation and Schiff base proton transfer

1 reference

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7 January 2021

Chemical dynamics in proteins: the photoisomerization of retinal in bacteriorhodopsin

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7 January 2021

Light-induced changes of the pH gradient and the membrane potential inH. halobium

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7 January 2021

Photoproducts of bacteriorhodopsin mutants: a molecular dynamics study

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7 January 2021

Structure at 0.85 A resolution of an early protein photocycle intermediate

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7 January 2021

A cold break for photoreceptors

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7 January 2021

The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Evidence for charge-controlled conformational changes in the photocycle of bacteriorhodopsin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

The last phase of the reprotonation switch in bacteriorhodopsin: the transition between the M-type and the N-type protein conformation depends on hydration

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction

1 reference

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7 January 2021

A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin

1 reference

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7 January 2021

1 reference

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7 January 2021

Changes in the protonation state of bacterio-opsin during reconstitution of bacteriorhodopsin

1 reference

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7 January 2021

Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier-transform infrared spectroscopy

1 reference

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7 January 2021

Fourier transform infrared double-flash experiments resolve bacteriorhodopsin's M1 to M2 transition

1 reference

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7 January 2021

Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin

1 reference

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7 January 2021

Spin-labeling studies of the conformational changes in the vicinity of D36, D38, T46, and E161 of bacteriorhodopsin during the photocycle

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Transient channel-opening in bacteriorhodopsin: an EPR study.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Molecular mechanism of protein-retinal coupling in bacteriorhodopsin

1 reference

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7 January 2021

Electron diffraction studies of light-induced conformational changes in the Leu-93 --> Ala bacteriorhodopsin mutant.

1 reference

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7 January 2021

Time-resolved fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin

1 reference

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7 January 2021

A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins

1 reference

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7 January 2021

Proton uptake and release are rate-limiting steps in the photocycle of the bacteriorhodopsin mutant E204Q

1 reference

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7 January 2021

Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin

1 reference

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7 January 2021

Time-resolved titrations of ASP-85 in bacteriorhodopsin: the multicomponent kinetic mechanism

1 reference

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7 January 2021

The role of water in the extracellular half channel of bacteriorhodopsin

1 reference

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7 January 2021

Interaction between Asp-85 and the proton-releasing group in bacteriorhodopsin. A study of an O-like photocycle intermediate

1 reference

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7 January 2021

Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Mutation of arginine 134 to lysine alters the pK(a)s of key groups involved in proton pumping by bacteriorhodopsin.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Investigation of the proton release channel of bacteriorhodopsin in different intermediates of the photo cycle. A molecular dynamics study

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Evidence for the first phase of the reprotonation switch of bacteriorhodopsin from time-resolved photovoltage and flash photolysis experiments on the photoreversal of the M-intermediate

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Voltage dependence of proton pumping by bacteriorhodopsin is regulated by the voltage-sensitive ratio of M1 to M2

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Infrared Difference Spectra of the Intermediates L, M, N, and O of the Bacteriorhodopsin Photoreaction Obtained by Time-Resolved Attenuated Total Reflection Spectroscopy

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Modeling of halorhodopsin and rhodopsin based on bacteriorhodopsin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Comparative studies on ion pumps of the bacterial rhodopsin family

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Chemical reconstitution of a chloride pump inactivated by a single point mutation.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Specific arginine and threonine residues control anion binding and transport in the light-driven chloride pump halorhodopsin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

The photocycle of the chloride pump halorhodopsin. II: Quantum yields and a kinetic model.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Femtosecond Spectroscopy of Halorhodopsin and Rhodopsin in a Broad Spectral Range of 400−1000 nm

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Nano- and microsecond time-resolved FTIR spectroscopy of the halorhodopsin photocycle

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

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https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

The primary structures of the Archaeon Halobacterium salinarium blue light receptor sensory rhodopsin II and its transducer, a methyl-accepting protein

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Three-dimensional model of sensory rhodopsin I reveals important restraints between the protein and the chromophore

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Asp76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Protonation changes during the photocycle of sensory rhodopsin II from Natronobacterium pharaonis

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Constitutive signaling by the phototaxis receptor sensory rhodopsin II from disruption of its protonated Schiff base-Asp-73 interhelical salt bridge

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Residue replacements of buried aspartyl and related residues in sensory rhodopsin I: D201N produces inverted phototaxis signals

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

His166 is critical for active-site proton transfer and phototaxis signaling by sensory rhodopsin I.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

Bacteriorhodopsin is involved in halobacterial photoreception

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2898%2980128-0

7 January 2021

10.1016/S0959-440X(98)80128-0

Identifiers

DOI

1 reference

release_geoy3gq5u5g7fkul55ralbfh2u

12 November 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/geoy3gq5u5g7fkul55ralbfh2u

24 November 2022

mapped directly with Wikidata item

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