Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains (Q74316985)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10988291%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

title

Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains (English)

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10 November 2019

author name string

Abdulaev NG

1

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10 November 2019

Ngo T

2

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10 November 2019

Chen R

3

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10 November 2019

Lu Z

4

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10 November 2019

Ridge KD

5

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10 November 2019

language of work or name

English

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publication date

1 December 2000

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Journal of Biological Chemistry

10 November 2019

published in

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10 November 2019

volume

275

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10 November 2019

page(s)

39354-39363

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10 November 2019

issue

50

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Light-induced conformational changes in the extradiscal regions of bovine rhodopsin

10 November 2019

cites work

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Photoactivated conformational changes in rhodopsin: a time-resolved spin label study

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Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin

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Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study.

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

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Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study

21 January 2018

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Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: a site-directed spin-labeling study

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C-terminal peptides of rhodopsin. Determination of the optimum sequence for recognition of retinal transducin

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Three cytoplasmic loops of rhodopsin interact with transducin

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Rhodopsin mutants discriminate sites important for the activation of rhodopsin kinase and Gt

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Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation

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Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: sulfhydryl reactivity and transducin activation reveal a tertiary structure

21 January 2018

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The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction

21 January 2018

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Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin alpha and gamma subunits.

21 January 2018

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Mechanistic studies on rhodopsin kinase. Light-dependent phosphorylation of C-terminal peptides of rhodopsin

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In vitro assay for trans-phosphorylation of rhodopsin by rhodopsin kinase

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Structure and function in rhodopsin: peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase

21 January 2018

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Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin

21 January 2018

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21 January 2018

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Binding of arrestin to cytoplasmic loop mutants of bovine rhodopsin

21 January 2018

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Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin

21 January 2018

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Transducin-alpha C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin

21 January 2018

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Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal

21 January 2018

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21 January 2018

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Constitutive activation of opsin: influence of charge at position 134 and size at position 296.

21 January 2018

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Opsins with mutations at the site of chromophore attachment constitutively activate transducin but are not phosphorylated by rhodopsin kinase

21 January 2018

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21 January 2018

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21 January 2018

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Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M005642200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10988291%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

1 reference