Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. (Q27638895)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11972040%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

title

Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography (English)

1 reference

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10 December 2019

main subject

X-ray crystallography

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author

Yoshinori Fujiyoshi

2

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10 December 2019

J Navarro

4

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10 December 2019

author name string

Tetsuji Okada

1

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10 December 2019

Maria Silow

3

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10 December 2019

Ehud M Landau

5

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10 December 2019

Yoshinori Shichida

6

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10 December 2019

language of work or name

English

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publication date

23 April 2002

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Proceedings of the National Academy of Sciences of the United States of America

10 December 2019

published in

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10 December 2019

volume

99

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10 December 2019

issue

9

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10 December 2019

page(s)

5982-5987

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Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs)

10 December 2019

cites work

1 reference

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20 March 2017

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High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle

20 March 2017

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20 March 2017

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Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family.

29 September 2017

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X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles.

29 September 2017

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Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: expression of 15N-lysine- and 13C-glycine-labeled opsin in a stable cell line

29 September 2017

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Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin

29 September 2017

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Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F.

29 September 2017

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Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin

29 September 2017

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Functional equivalence of metarhodopsin II and the Gt-activating form of photolyzed bovine rhodopsin

29 September 2017

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The road to color vision: structure, evolution and function of chicken and gecko visual pigments

29 September 2017

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Constitutively active mutants of rhodopsin

29 September 2017

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Resonance Raman microprobe spectroscopy of rhodopsin mutants: effect of substitutions in the third transmembrane helix.

29 September 2017

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29 September 2017

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Identification of the Cl(-)-binding site in the human red and green color vision pigments

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Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin

21 January 2018

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A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor

21 January 2018

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The photobleaching sequence of a short-wavelength visual pigment

21 January 2018

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Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

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21 January 2018

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27 November 2018

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21 January 2018

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12 December 2020

An aspartate conserved among G-protein receptors confers allosteric regulation of alpha 2-adrenergic receptors by sodium

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12 December 2020

Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function

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12 December 2020

Low-temperature spectrophotometry of intermediates of rhodopsin

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12 December 2020

Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin

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12 December 2020

Water and peptide backbone structure in the active center of bovine rhodopsin

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Pivotal role of an aspartate residue in sodium sensitivity and coupling to G proteins of neurotensin receptors

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12 December 2020

Identifiers

DOI

10.1073/PNAS.082666399

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11972040%20AND%20SRC:MED&resulttype=core&format=json

OpenCitations bibliographic resource ID

10 December 2019

ADS bibcode

2002PNAS...99.5982O

0 references

2549037

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11972040%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

1 reference