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Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin

Published in: Proceedings of the National Academy of Sciences of the United States of America

Date of publication: February 1, 1993

Language: English

Main subject: membrane protein

Bibliographic databases:

Cites articles 36

Date

Title

Authors

August 1, 1968

The Molecular Basis of Visual Excitation
September 1, 1975

Three-dimensional model of purple membrane obtained by electron microscopy
January 1, 1978

Molecular mechanisms for proton transport in membranes
March 1, 1979

Bacteriorhodopsin and the purple membrane of halobacteria
June 1982

Bacteriorhodopsin and related pigments of halobacteria
September 1, 1982

Light-induced interaction between rhodopsin and the GTP-binding protein. Metarhodopsin II is the major photoproduct involved,Light-Induced Interaction between Rhodopsin and the GTP-Binding Protein. Metarhodopsin II Is the Major Photoproduct Involved
February 1, 1986

Total synthesis of a gene for bovine rhodopsin
March 1986

Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments
August 1, 1987

Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation
December 1, 1987

Expression of a synthetic bovine rhodopsin gene in monkey kidney cells
July 1, 1987

Structure-function studies on bacteriorhodopsin. V. Effects of amino acid substitutions in the putative helix F.
June 1, 1988

Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
November 1, 1988

Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin
June 1, 1988

Bacteriorhodopsin, a membrane protein that uses light to translocate protons
November 1, 1988

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
August 1, 1989

Molecular genetics of human blue cone monochromacy
September 1, 1989

Three cytoplasmic loops of rhodopsin interact with transducin
April 1, 1989

Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement
November 1, 1989

Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
December 1, 1989

Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
June 1, 1989

Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump

,
February 1, 1989

Two pumps, one principle: light-driven ion transport in halobacteria
November 1, 1989

Effect of carboxylic acid side chains on the absorption maximum of visual pigments
August 1, 1989

Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation
August 1, 1989

Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin
August 1, 1989

Structure-function studies on bacteriorhodopsin. VIII. Substitutions of the membrane-embedded prolines 50, 91, and 186: the effects are determined by the substituting amino acids
July 1, 1990

Role of the intradiscal domain in rhodopsin assembly and function
June 20, 1990

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
February 1, 1990

Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base
October 1, 1990

Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187
October 1, 1990

Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin
March 1, 1991

The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates

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