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Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

Science (American Association for the Advancement of Science), 1996-11, Vol.274 (5288), p.768-770

1996

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A Collision Gradient Method to Determine the Immersion Depth of Nitroxides in Lipid Bilayers: Application to Spin-Labeled Mutants of Bacteriorhodopsin

Proceedings of the National Academy of Sciences - PNAS, 1994-03, Vol.91 (5), p.1667-1671

1994

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Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function

The Journal of biological chemistry, 1992-01, Vol.267 (1), p.1-4

Khorana, H G

1992

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Solution NMR Spectroscopy of [α-15N]Lysine-Labeled Rhodopsin: The Single Peak Observed in Both Conventional and TROSY-Type HSQC Spectra is Ascribed to Lys-339 in the Carboxyl-Terminal Peptide Sequence

Proceedings of the National Academy of Sciences - PNAS, 2002-03, Vol.99 (6), p.3452-3457

2002

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Glutamic Acid-113 Serves as the Retinylidene Schiff Base Counterion in Bovine Rhodopsin

Proceedings of the National Academy of Sciences - PNAS, 1989-11, Vol.86 (21), p.8309-8313

1989

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Structure and Function in Rhodopsin: The Role of Asparagine-Linked Glycosylation

Proceedings of the National Academy of Sciences - PNAS, 1994-04, Vol.91 (9), p.4024-4028

1994

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Structure and Function in Rhodopsin: Mapping Light-Dependent Changes in Distance between Residue 316 in Helix 8 and Residues in the Sequence 60−75, Covering the Cytoplasmic End of Helices TM1 and TM2 and Their Connection Loop CL1

Biochemistry (Easton), 2001-12, Vol.40 (51), p.15493-15500

2001

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Structure and Function in Rhodopsin: High-Level Expression of Rhodopsin with Restricted and Homogeneous N-Glycosylation by a Tetracycline-Inducible N-Acetylglucosaminyltransferase I-Negative HEK293S Stable Mammalian Cell Line

Proceedings of the National Academy of Sciences - PNAS, 2002-10, Vol.99 (21), p.13419-13424

2002

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Mechanism of light-dependent proton translocation by bacteriorhodopsin

Journal of Bacteriology, 1993-03, Vol.175 (6), p.1555-1560

1993

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Bacteriorhodopsin, a membrane protein that uses light to translocate protons

The Journal of biological chemistry, 1988-06, Vol.263 (16), p.7439-7442

Khorana, H G

1988

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Structure and Function in Rhodopsin: High Level Expression of a Synthetic Bovine Opsin Gene and Its Mutants in Stable Mammalian Cell Lines

Proceedings of the National Academy of Sciences - PNAS, 1996-10, Vol.93 (21), p.11487-11492

1996

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Aspartic Acid-96 is the Internal Proton Donor in the Reprotonation of the Schiff Base of Bacteriorhodopsin

Proceedings of the National Academy of Sciences - PNAS, 1989-12, Vol.86 (23), p.9228-9232

1989

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Two Light-Transducing Membrane Proteins: Bacteriorhodopsin and the Mammalian Rhodopsin

Proceedings of the National Academy of Sciences - PNAS, 1993-02, Vol.90 (4), p.1166-1171

Khorana, H. Gobind

1993

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Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187

The Journal of biological chemistry, 1990-10, Vol.265 (29), p.17520-17524

1990

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Rapid Long-Range Proton Diffusion Along the Surface of the Purple Membrane and Delayed Proton Transfer Into the Bulk

Proceedings of the National Academy of Sciences - PNAS, 1995-01, Vol.92 (2), p.372-376

1995

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Structure and Function in Rhodopsin: Correct Folding and Misfolding in Two Point Mutants in the Intradiscal Domain of Rhodopsin Identified in Retinitis Pigmentosa

Proceedings of the National Academy of Sciences - PNAS, 1996-05, Vol.93 (10), p.4554-4559

1996

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Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin

The Journal of biological chemistry, 1991-03, Vol.266 (7), p.4269-4275

1991

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Identification of Core Amino Acids Stabilizing Rhodopsin

Proceedings of the National Academy of Sciences - PNAS, 2004-05, Vol.101 (19), p.7246-7251

2004

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Structure and Function in Rhodopsin: Replacement by Alanine of Cysteine Residues 110 and 187, Components of a Conserved Disulfide Bond in Rhodopsin, Affects the Light-Activated Metarhodopsin II State

Proceedings of the National Academy of Sciences - PNAS, 1994-04, Vol.91 (9), p.4029-4033

1994

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Structure and Function in Rhodopsin: A Tetracycline-Inducible System in Stable Mammalian Cell Lines for High-Level Expression of Opsin Mutants

Proceedings of the National Academy of Sciences - PNAS, 2002-10, Vol.99 (21), p.13413-13418

2002

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Protonation State of Asp (Glu)-85 Regulates the Purple-to-Blue Transition in Bacteriorhodopsin Mutants Arg-82 → Ala and Asp-85 → Glu: The Blue Form is Inactive in Proton Translocation

Proceedings of the National Academy of Sciences - PNAS, 1990-02, Vol.87 (3), p.1013-1017

1990

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Expression of a Synthetic Bovine Rhodopsin Gene in Monkey Kidney Cells

Proceedings of the National Academy of Sciences - PNAS, 1987-12, Vol.84 (24), p.8874-8878

1987

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Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212

Biochemistry (Easton), 1988-11, Vol.27 (23), p.8516-8520

1988

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Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin

The Journal of biological chemistry, 1992-07, Vol.267 (21), p.14767-14774

1992

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Cysteine Residues 110 and 187 are Essential for the Formation of Correct Structure in Bovine Rhodopsin

Proceedings of the National Academy of Sciences - PNAS, 1988-11, Vol.85 (22), p.8459-8463

1988

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Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

A Collision Gradient Method to Determine the Immersion Depth of Nitroxides in Lipid Bilayers: Application to Spin-Labeled Mutants of Bacteriorhodopsin

Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function

Solution NMR Spectroscopy of [α-15N]Lysine-Labeled Rhodopsin: The Single Peak Observed in Both Conventional and TROSY-Type HSQC Spectra is Ascribed to Lys-339 in the Carboxyl-Terminal Peptide Sequence

Glutamic Acid-113 Serves as the Retinylidene Schiff Base Counterion in Bovine Rhodopsin

Structure and Function in Rhodopsin: The Role of Asparagine-Linked Glycosylation

Structure and Function in Rhodopsin: Mapping Light-Dependent Changes in Distance between Residue 316 in Helix 8 and Residues in the Sequence 60−75, Covering the Cytoplasmic End of Helices TM1 and TM2 and Their Connection Loop CL1

Structure and Function in Rhodopsin: High-Level Expression of Rhodopsin with Restricted and Homogeneous N-Glycosylation by a Tetracycline-Inducible N-Acetylglucosaminyltransferase I-Negative HEK293S Stable Mammalian Cell Line

Mechanism of light-dependent proton translocation by bacteriorhodopsin

Bacteriorhodopsin, a membrane protein that uses light to translocate protons

Structure and Function in Rhodopsin: High Level Expression of a Synthetic Bovine Opsin Gene and Its Mutants in Stable Mammalian Cell Lines

Aspartic Acid-96 is the Internal Proton Donor in the Reprotonation of the Schiff Base of Bacteriorhodopsin

Two Light-Transducing Membrane Proteins: Bacteriorhodopsin and the Mammalian Rhodopsin

Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187

Rapid Long-Range Proton Diffusion Along the Surface of the Purple Membrane and Delayed Proton Transfer Into the Bulk

Structure and Function in Rhodopsin: Correct Folding and Misfolding in Two Point Mutants in the Intradiscal Domain of Rhodopsin Identified in Retinitis Pigmentosa

Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin

Identification of Core Amino Acids Stabilizing Rhodopsin

Structure and Function in Rhodopsin: Replacement by Alanine of Cysteine Residues 110 and 187, Components of a Conserved Disulfide Bond in Rhodopsin, Affects the Light-Activated Metarhodopsin II State

Structure and Function in Rhodopsin: A Tetracycline-Inducible System in Stable Mammalian Cell Lines for High-Level Expression of Opsin Mutants

Protonation State of Asp (Glu)-85 Regulates the Purple-to-Blue Transition in Bacteriorhodopsin Mutants Arg-82 → Ala and Asp-85 → Glu: The Blue Form is Inactive in Proton Translocation

Expression of a Synthetic Bovine Rhodopsin Gene in Monkey Kidney Cells

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212

Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin

Cysteine Residues 110 and 187 are Essential for the Formation of Correct Structure in Bovine Rhodopsin

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